Henry Wallman

Henry "Hank" Wallman (1915–1992) was an American mathematician, known for his work in lattice theory, dimension theory, topology, and electronic circuit design.
A native of Brooklyn and a 1933 graduate of Brooklyn College, Wallman received his Ph.D. in mathematics from Princeton University in 1937, under the supervision of Solomon Lefschetz and became a faculty member at the Massachusetts Institute of Technology, where he was associated with the Radiation Laboratory. During World War II he did classified work at MIT, possibly involving radar. In 1948, he left MIT to become a professor of electrotechnics at the Chalmers University of Technology in Gothenburg, Sweden, which awarded him the Chalmers medal in 1980 and where he eventually retired. In 1950 he was elected as a foreign member to the Swedish Royal Academy. He was elected a member of the Royal Swedish Academy of Engineering Sciences in 1960 and of the Royal Swedish Academy of Engineering Sciences in 1970.
The disjunction property of Wallman is named after Wallman, as is the Wallman compactification, and he co-authored an important monograph on dimension theory with Witold Hurewicz. Wallman was also a radio enthusiast, and in the postwar period co-authored a book comprehensively documenting what was known at the time about vacuum tube amplification technology, including new developments such as showing how the central limit theorem could be used to describe the rise time of cascaded circuits. At Chalmers, Wallman helped build the Electronic Differential Analyser, an early example of an analog computer, and performed pioneering research in biomedical engineering combining video displays with X-ray imaging.


Cyano-2 RNA motif

The Cyano-2 RNA motif is a conserved RNA structure identified by bioinformatics. Cyano-2 RNAs are found in Cyanobacterial species classified within the genus "Synechococcus". Many terminal loops in the two conserved stem-loops contain the nucleotide sequence GCGA, and these sequences might in some cases form stable GNRA tetraloops. Since the two stem-loops are somewhat distant from one another it is possible that they represent two independent non-coding RNAs that are often or always co-transcribed. The region one thousand base pairs upstream of predicted Cyano-2 RNAs is usually devoid of annotated features such as RNA or protein-coding genes. This absence of annotated genes within one thousand base pairs is relatively unusual within bacteria.


Peter Plett

Peter Plett (29 December 1766 – 29 March 1823) was a German teacher and pioneer of smallpox vaccine from Schleswig-Holstein. His work with smallpox vaccine, undertaken in the early 1790s before similar studies by Edward Jenner, was not acknowledged until many years later.
Life.
Plett was born on 29 December 1766 in Klein Rheide. In 1790, Plett was employed as a home tutor in Schönweide where he learnt from milkmaids about cowpox preventing humans from being infected with smallpox. In 1791, he moved to the Meierhof at Hasselburg in Gut Wittenberg/East-Holstein where he vaccinated its owner Martini's three children with cowpox lymph which protected them against smallpox. Only five years later, Edward Jenner discovered this very method which made him world-famous.
In 1790 and again in 1791/92, Plett reported his success to the medical faculty of the University of Kiel, but they favoured the older method of variolation so they did not act on the reports. In 1802 after Jenner's method had reached Germany, Plett was interviewed by Friedrich Adolf von Heinze on behalf of Christoph Heinrich Pfaff from the Medical Faculty of the University of Kiel. His report was published by Pfaff and Heinze and later forwarded to the German Office of the government in Copenhagen.
From 1793 on, Plett attended the teachers' seminar led by Heinrich Müller in Kiel. He was encouraged by his principal pastor Johann Georg Schmidt who considered him "one of Müller's most promising seminar attendees" and engaged him as a teacher in Laboe in 1796 in Stakendorf in 1808.
Franz Hermann Hegewisch, who became a professor of the University of Kiel in 1809, discovered Plett's reports about his success with cowpox vaccination and the university's ignorance. He recommended publishing an article about Plett's discoveries to the editor of the "Neue Schleswig-Holsteinische Provinzialberichte" (New provincial reports of Schleswig-Holstein), Georg Peter Petersen. In 1815, Petersen published the previous year's interview with Plett, so he confirmed Heinze's report of 1802.
In 1820, Plett was forced to retire from teaching due to his alcoholism. Pastor Schmidt and his superior, provost Cay Wilhelm von Ahlefeldt, negotiated a modest pension and accommodation with the citizens of Stakendorf. Three years later, Plett died at the age of 56.
Honours.
In 1956, the community of Stakendorf erected a boulder in honour of Peter Plett in front of the school where he formerly worked. Its inscription was corrected in 2006 and augmented by an information board.


Glutathione dehydrogenase (ascorbate)

In enzymology, a glutathione dehydrogenase (ascorbate) () is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are glutathione and dehydroascorbate, whereas its two products are glutathione disulfide and ascorbate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a quinone or similar compound as acceptor. The systematic name of this enzyme class is glutathione:dehydroascorbate oxidoreductase. Other names in common use include dehydroascorbic reductase, dehydroascorbic acid reductase, glutathione dehydroascorbate reductase, DHA reductase, dehydroascorbate reductase, GDOR, and glutathione:dehydroascorbic acid oxidoreductase. This enzyme participates in 3 metabolic pathways: ascorbate and aldarate metabolism, glutamate metabolism, and glutathione metabolism.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .


Isopentenyl pyrophosphate

Isopentenyl pyrophosphate (IPP, isopentenyl diphosphate, or IDP) is an isoprenoid precursor. IPP is an intermediate in the classical, HMG-CoA reductase pathway (commonly called the mevalonate pathway) and in the "non-mevalonate" MEP pathway of isoprenoid precursor biosynthesis. Isoprenoid precursors such as IPP, and its isomer DMAPP, are used by organisms in the biosynthesis of terpenes and terpenoids.
Biosynthesis.
IPP is formed from acetyl-CoA via the mevalonate pathway (the "upstream" part), and then is isomerized to dimethylallyl pyrophosphate by the enzyme isopentenyl pyrophosphate isomerase.
IPP can be synthesised via an alternative non-mevalonate pathway of isoprenoid precursor biosynthesis, the MEP pathway, where it is formed from ("E")-4-hydroxy-3-methyl-but-2-enyl pyrophosphate (HMB-PP) by the enzyme HMB-PP reductase (LytB, IspH). The MEP pathway is present in many bacteria, apicomplexan protozoa such as malaria parasites, and in the plastids of higher plants.


Phytoglobin-NO cycle

The phytoglobin-nitric oxide cycle is a metabolic pathway induced in plants under hypoxic conditions which involves nitric oxide (NO) and phytoglobin (Pgb). It provides an alternative type of respiration to mitochondrial electron transport under the conditions of limited oxygen supply. Phytoglobin in hypoxic plants acts as part of a soluble terminal nitric oxide dioxygenase system, yielding nitrate ion from the reaction of oxygenated phytoglobin with NO. Class 1 phytoglobins are induced in plants under hypoxia, bind oxygen very tightly at nanomolar concentrations, and can effectively scavenge NO at oxygen levels far below the saturation of cytochrome c oxidase. In the course of the reaction, phytoglobin is oxidized to metphytoglobin which has to be reduced for continuous operation of the cycle. Nitrate is reduced to nitrite by nitrate reductase, while NO is mainly formed due to anaerobic reduction of nitrite which may take place in mitochondria by complex III and complex IV in the absence of oxygen, in the side reaction of nitrate reductase, or by electron transport proteins on the plasma membrane. The overall reaction sequence of the cycle consumes NADH and can contribute to the maintenance of ATP level in highly hypoxic conditions.


Purple bacteria

Purple bacteria or purple photosynthetic bacteria are Gram-negative proteobacteria that are phototrophic, capable of producing their own food via photosynthesis. They are pigmented with bacteriochlorophyll "a" or "b", together with various carotenoids, which give them colours ranging between purple, red, brown, and orange. They may be divided into two groups – purple sulfur bacteria (Chromatiales, in part) and purple non-sulfur bacteria (Rhodospirillaceae). Purple bacteria are anoxygenic phototrophs widely spread in nature, but especially in aquatic environments, where there are anoxic conditions that favor the synthesis of their pigments.
Taxonomy.
Purple bacteria belong to phylum of "Proteobacteria." This phylum was established by Carl Woese in 1987 calling it “purple bacteria and their relatives” even if this is not appropriate because most of them are not purple or photosynthetic. Phylum "Proteobacteria" is divided into six classes:"Alphaproteobacteria, Betaproteobacteria, Gammaproteobacteria, Deltaproteobacteria, Epsilonproteobacteria" and "Zetaproteobcateria". Purple bacteria are distributed between 3 classes:"Alphaproteobacteria", "Betaproteobacteria, Gammaproteobacteria" each characterized by a photosynthetic phenotype. Alpha subdivision contains different photosynthetic purple bacteria species (for instance: "Rhodospirillum, Rhodopseudomonas" and "Rhodomicrobium") but include also some non-photosyntetic purple ones of genera with nitrogen metabolism ( "Rhizobium , Nitrobacter") whereas in "betaproteobacteria" subdivision there are few photosynthetic species.
Purple sulfur bacteria are included in the gamma subgroup. Gammaproteobacteria is divided into 3 subgroups: gamma-1, gamma-2, gamma-3. In gamma-1 subgroup there are the purple photosynthetic bacteria that produce molecular sulfur ("Chromatiaceae" group and "Ectothiorhodospiraceae" group) and also the non-photosyntetic species (as "Nitrosococcus oceani"). The similarity between the photosynthetic machinery in these different lines indicates that it had a common origin, either from some common ancestor or passed by lateral transfer. Purple sulfur bacteria and purple nunsulfur bacteria were distinguished on the basis of physiological factors of their tolerance and utilization of sulfide: was considered that purple sulfur bacteria tolerate millimolar levels of sulfide and oxidized sulfide to sulfur globules stored intracellulary while purple nonsulfur bacteria species did neither. This kind of classification was not absoluted. It was refuted with classic chemostat experiments by Hansen and Van Gemerden (1972) that demonstrate the growing of many purple nonsulfur bacteria species at low levels of sulfide (0.5mM) and in so doing, oxidize sulfide to S0, S4O62-, or SO42-. The important distinction that remains from these two different metabolisms is that: any S0 formed by purple nonsulfur bacteria is not stored intracellularly but is deposited outside the cell (even if there are exception for this as "Ectothiorhodospiraceae"). So if grown on sulfide it is easy to differentiate purple sulfur bacteria from purple non sulfur bacteria because the microscopically globules of S0 are formed.
Metabolism.
Purple Bacteria are able to perform different metabolisms that allow them to adapt to different and even extreme environmental conditions. They are mainly photoautotrophs, but are also known to be chemoautotrophic and photoheterotrophic. Since pigments synthesis does not take place in presence of oxygen, phototrophic growth only occurs in anoxic and light conditions. Howerver purple bacteria can also grow in dark and oxic environments. In fact they can be mixotrophs, capable of anaerobic and aerobic respiration or fermentation basing on the concentration of oxygen and availability of light.
Photosynthesis.
Photosynthetic unit
Purple bacteria use bacteriochlorophyll and carotenoids to obtain the light energy for photosynthesis. Electron transfer and photosynthetic reactions occur at the cell membrane in the photosynthetic unit which is composed by the light-harvesting complexes LHI and LHII and the photosynthetic reaction centre where the charge separation reaction occurs. These structures are located in the intracytoplasmic membrane, areas of the cytoplasmic membrane invaginated to form vesicle sacs, tubules, or single-paired or stacked lamellar sheets which have increased surface to maximize light absorption. Light-harvesting complexes are involved in the energy transfer to the reaction centre. These are integral membrane protein complexes consisting of monomers of α- and β- apoproteins, each one binding molecules of bacteriochlorophyll and carotenoids non-covalently. LHI is directly associated with the reaction centre forming a polymeric ring-like structure around it. LHI has an absorption maximum at 870 nm and it contains most of the bacteriochlorophyll of the photosynthetic unit. LHII contains less bacteriochlorophylls, has lower absorption maximum (850 nm) and is not present in all purple bacteria. Moreover, the photosynthetic unit in Purple Bacteria shows great plasticity, being able to adapt to the constantly changing light conditions. In fact these microorganisms are able to rearrange the composition and the concentration of the pigments, and consequently the absorption spectrum, in response to light variation.
Mechanism.
Purple bacteria use cyclic electron transport driven by a series of redox reactions. Light-harvesting complexes surrounding a reaction centre (RC) harvest photons in the form of resonance energy, exciting chlorophyll pigments P870 or P960 located in the RC. Excited electrons are cycled from P870 to quinones QA and QB, then passed to cytochrome bc1, cytochrome c2, and back to P870. The reduced quinone QB attracts two cytoplasmic protons and becomes QH2, eventually being oxidized and releasing the protons to be pumped into the periplasm by the cytochrome bc1 complex. The resulting charge separation between the cytoplasm and periplasm generates a proton motive force used by ATP synthase to produce ATP energy.
Electron donors for anabolism.
Purple bacteria are anoxygenic because they do not use water as electron donor to produce oxygen. Purple sulfur bacteria (PSB), use sulfide, sulfur, thiosulfate or hydrogen as electron donors. In addition, some species use ferrous iron as electron donor and one strain of "Thiocapsa" can use nitrite. Finally, even if the purple sulfur bacteria are typically photoautotroph, some of them are photoheterotroph and use different carbon sources and electron donor such as organic acids and fatty acids. On the other hand, purple non-sulfur bacteria, typically use hydrogen as an electron donor, but can also use sulfide at lower concentrations compared to PSB and some species can use thiosulfate or ferrous iron as electron donor. In contrast to the purple sulfur bacteria, the purple non sulfur bacteria are mostly photoheterotrophic and can use as electron donor and carbon sources such as sugars, amino acids, organic acids, and aromatic compounds like toluene or benzoate.
Purple bacteria lack external electron carriers to spontaneously reduce NAD(P)+ to NAD(P)H, so they must use their reduced quinones to endergonically reduce NAD(P)+. This process is driven by the proton motive force and is called reverse electron flow.
Ecology.
Distribution.
Purple bacteria inhabit illuminated anoxic aquatic and terrestrial environments. Even if sometimes the two major groups of purple bacteria, purple sulfur bacteria and purple nonsulfur bacteria, coexist in the same habitat, they occupy different niches. Purple sulfur bacteria are strongly photoautotrophs and are not adapted to an efficient metabolism and growth in the dark. A different speech applies to purple nonsulfur bacteria that are strongly photoheterotrophs, even if they are capable of photoautotrophy, and are equipped for living in dark environments. Purple sulfur bacteria can be found in different ecosystems with enough sulfate and light, some examples are shallow lagoons polluted by sewage or deep waters of lakes, in which they could even bloom. Blooms can both involve a single or a mixture of species. They can also be found in microbial mats where the lower layer decomposes and sulfate-reduction occurs.
Purple non sulfur bacteria can be found in both illuminated and dark environments with lack of sulfide. However, they hardly form blooms with sufficiently high concentration to be visible without enrichment techniques.
Purple bacteria have evolved effective strategies for photosynthesis in extreme environments, in fact they are quite successful in harsh habitats. In the 1960s the first halophiles and acidophiles of the genus "Ectothiorhodospira" were discovered. In the 1980s "Thermochromatium tepidum", a thermophilic purple bacterium that can be found in North American hot springs, was isolated for the first time.
Biogeochemical cycles.
Purple bacteria are involved in the biogeochemical cycles of different nutrients. In fact they are able to photoautotrophically fix carbon, or to consume it photoheterotrophically; in both cases in anoxic conditions. However the most important role is played by consuming hydrogen sulphide: a highly toxic substance for plants, animals and other bacteria. In fact, the oxidation of hydrogen sulphide by purple bacteria produces non-toxic forms of sulfur, such as elemental sulfur and sulphate.
In addition, almost all non-sulfur purple bacteria are able to fix nitrogen (N2+8H+--->2NH3+H2), and "Rba Sphaeroides", an alpha proteobacter, is capable of reducing nitrate to molecular nitrogen by denitrification.
Ecological niches.
Quantity and quality of light.
Several studies have shown that a strong accumulation of phototrophic sulfur bacteria has been observed between 2 and 20 meters deep (in some cases even 30 m) of pelagic environments. This is due to the fact that in some environments the light transmission for various populations of phototrophic sulfur bacteria varies with a density from 0.015 to 10% Furthermore, "Chromatiaceae" have been found in chemocline environments over 20 m depths. The correlation between anoxygenic photosynthesis and the availability of solar radiation suggests that light is the main factor controlling all the activities of phototrophic sulfur bacteria. The density of pelagic communities of phototrophic sulfur bacteria extends beyond a depth range of 10 cm, while the less dense population (found in the Black Sea (0.068–0.94 μg BChle/dm−3), scattered over an interval of 30 m. Communities of phototrophic sulfur bacteria located in the coastal sediments of sandy, saline or muddy beaches live in an environment with a higher light gradient, limiting growth to the highest value between 1.5–5 mm of the sediments. At the same time, biomass densities of 900 mg bacteriochlorophyll/dm−3 can be attained in these latter systems.
Temperature and salinity.
Purple sulfur bacteria (like green sulfur bacteria) typically form blooms in non-thermal aquatic ecosystems, some members have been found in hot springs. For example "Chlorobaculum tepidum" can only be found in some hot springs in New Zealand at a ph value between 4.3 and 6.2 and at a temperature above 56 °C. Another example are "Thermochromatium tepidum", has been found in several hot springs in western North America at temperatures above 58 °C and may represent the most thermophilic proteobacteria existent. Of the purple sulfur bacteria, many members of the Chromatiaceae family are often found in fresh water and marine environments. About 10 species of Chromatiaceae are halophilic.
Syntrophy and symbioses.
Like green sulfur bacteria, purple sulfur bacteria are also capable of symbiosis and can rapidly create stable associations between other purple sulfur bacteria and sulfur- or sulfate-reducing bacteria. These associations are based on a cycle of sulfur but not carbon compounds. Thus, a simultaneous growth of two bacteria partners takes place, which are fed by the oxidation of organic carbon and light substrates. Experiments with "Chromatiaceae" have pointed out that cell aggregates consisting of sulfate-reducing Proteobacterium "Desulfocapsa Thiozymogenes" and small cells of "Chromatiaceae" have been observed in the chemocline of an alpine mermocitic lake.
History.
Purple bacteria were the first bacteria discovered to photosynthesize without having an oxygen byproduct. Instead, their byproduct is sulfur. This was demonstrated by first establishing the bacteria's reactions to different concentrations of oxygen. It was found that the bacteria moved quickly away from even the slightest trace of oxygen. Then a dish of the bacteria was taken, and a light was focused on one part of the dish, leaving the rest dark. As the bacteria cannot survive without light, all the bacteria moved into the circle of light, becoming very crowded. If the bacteria's byproduct was oxygen, the distances between individuals would become larger and larger as more oxygen was produced. But because of the bacteria's behavior in the focused light, it was concluded that the bacteria's photosynthetic byproduct could not be oxygen.
In a 2018 article, it has been suggested that purple bacteria can be used as a biorefinery.
Evolution.
Researchers have theorized that some purple bacteria are related to the mitochondria, symbiotic bacteria in plant and animal cells today that act as organelles. Comparisons of their protein structure suggests that there is a common ancestor.


Sonuk Mikko

Sonuk Mikko (unknown—ca. 1864), commonly known as Billy Bowlegs and also known as So-Nuk-Mek-Ko, was a Seminole who gained recognition as a captain in the American Civil War. Mikko adopted the name of Chief Billy Bowlegs from (Holato Micco), who had fought in the Second and Third Seminole wars, following Holato Micco's death in 1859.
Civil War.
With the secession of eleven Southern states in 1861, both the Union and Confederacy vied for control of the Indian Territory. Old tribal rivalries were renewed, with some aligning with the North and others with the South. Sonuk Mikko sided with the Union. When a Confederate force under Col. Douglas H. Cooper attacked Unionist tribes in the Indian Territory, Mikko aligned his followers with Opothleyahola's Upper Creeks and resisted. Together, they fought Cooper in a series of losing battles in the winter of 1861–62 that led to the withdrawal of the Union sympathizers to Kansas in a bitter trek known as the "Trail of Blood on Ice." Mikko's band covered the rear after the Battle of Chustenahlah against Cherokee chief Stand Watie. They eventually settled near Fort Belmont, where a number of his Seminoles perished of exposure and starvation during the winter.
Mikko formally enlisted in the Union Army as a captain in May 1862 and was assigned command of Company A of the First Indian Home Guards. He saw action in a number of battles that year and was commended by Col. William Cloud, commander of the Third Brigade, Army of the Frontier, for his actions at the Battle of Cane Hill in December. The First Indian Home Guards arrived on the battlefield, dismounted, and entered a patch of woods on the left-center, flanked by two white regiments from Kansas and Iowa. When the Iowans gave way under a heavy volley, the entire Union line wavered and fell back. Rallying, the Indians and Kansans pushed forward and gained the position. Colonel Cloud wrote, "Of the Indian officers, Captain Jon-neh, of the Uches, and Captain Billy Bowlegs, of the Seminoles, and Captain Tus-te-nup-chup-ko, of Company A (Creek), are deserving of the highest praise."
Eventually being reassigned to command of Company F, Billy Bowlegs remained prominent in the fighting in Kansas and Indian Territory. At a skirmish with Confederates at Rhea Mills, he lost two revolvers, saddle, bridle and his horse, but emerged unscathed.
Mikko died in 1864 of smallpox and was buried in the Fort Gibson National Cemetery. Indian Agent G.C. Snow lamented, "His loss is very much regretted, as he was an influential man among (the Seminoles) and I believe generally beloved by all."
See also.
Seminole tribe


5-MeO-NMT

5-MeO-NMT (5-methoxy-"N"-methyltryptamine) is an organic chemical compound, being the 5-methoxy analog of "N"-methyltryptamine (NMT). It was first isolated from "Phalaris arundinacea" (reed canary grass). It has also been synthesized by Alexander Shulgin and reported in his book "TiHKAL". Like other members of the "N"-methyltryptamine family of compounds, 5-MeO-NMT is believed to produce few or no psychedelic effects, although very little data exists about its pharmacological properties or toxicity.


Tamara Galloway

Tamara Susan Galloway is a British marine scientist and Professor of Ecotoxicology at the University of Exeter. She was appointed an Officer of the Order of the British Empire in the 2019 Birthday Honours.
Early life and education.
Galloway studied biochemistry at the University of Glasgow. She graduated with first-class honours in 1983, and was awarded the Norman Davidson Memorial medal. Galloway moved to the University of Edinburgh for her graduate studies, and earned her PhD in 1986.
Research and career.
Galloway's research considers the biological impact of environmental change on human populations. Since 2003, Galloway has worked with Richard Thompson at the University of Plymouth on the impact of plastics in the environment. Together they worked to quantify the contamination of microplastics.
She became interested in the impacts of plastics on health and moved to the University of Exeter in 2007. Here she worked with the University of Exeter Medical School on Bisphenol A, which is a compound that is found in food and drink packaging. She used the National Health and Nutrition Examination Survey (NHANES), which was the first to collect information on urinary BPA concentrations. Galloway identified that Bisphenol A, which is detectable in 90% of adults, can cause increased risk of heart disease, diabetes and liver disease. She continued to investigate Bisphenol A, demonstrating that urinary concentrations are independently associated with cardiovascular disease. She conducted a study with the British Heart Foundation that involved over 1,600 patients, which confirmed that Bisphenol A accelerates the progression of heart disease by ten years. Galloway's work on Bisphenol A was covered in "The Naked Scientists", "Chemistry World" and in "USA Today".
Galloway is an expert in microplastics. Galloway predicted that microplastics would have an impact on the marine food chain. She has primarily looked at the impact of micro- and nano-plastics, finding that they can stop animals from feeding on their natural prey. Galloway demonstrated that this likely impacts the rest of the food chain, estimating that shellfish consumed by humans contained around 50 particles of plastic. She found that one shower could result in 100,000 microbeads ending up in the ocean. The work was used for the basis of the United Kingdom law that bans microbeads, which protects the environment from several thousand tonnes of microbeads every year. So far, she has found microplastics in every seawater sample that she has analysed.
Galloway provided evidence to a cross-party committee on the environment. Her research was used in the Government of the United Kingdom report "A Green Future: Our 25 Year Plan to Improve the Environment". Galloway worked with Zero Plastic Waste and Policy Connect to investigate how it would be possible to eliminate plastic waste from the United Kingdom. She is a member of the Science Advice for Policy by European Academies group on microplastics in nature. Galloway served on the advisory board of Blue Planet II.
She is on the editorial board of Chemosphere.


Operation Big Buzz

Operation Big Buzz was a U.S. military entomological warfare field test conducted in the U.S. state of Georgia in 1955. The tests involved dispersing over 300,000 mosquitoes from aircraft and through ground dispersal methods.
Operation.
Operation Big Buzz occurred in May 1955 in the U.S. state of Georgia. The operation was a field test designed to determine the feasibility of producing, storing, loading into munitions, and dispersing from aircraft the yellow fever mosquito (though these were not infected for the test) ("Aedes aegypti"). The second goal of the operation was to determine whether the mosquitoes would survive their dispersion and seek meals on the ground. Around 330,000 uninfected mosquitoes were dropped from aircraft in E14 bombs and dispersed from the ground. In total about one million female mosquitoes were bred for the testing; remaining mosquitoes were used in munitions loading and storage tests. Those mosquitoes that were air-dispersed were dropped from airplanes above the ground, spreading out on their own and due to the wind.
Results.
Mosquitoes were collected as far away as from the release site. They were also active in seeking blood meals from humans and guinea pigs.


Protein metabolism

Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids (anabolism), and the breakdown of proteins by catabolism.
The steps of protein synthesis include transcription, translation, and post translational modifications. During transcription, RNA polymerase transcribes a coding region of the DNA in a cell producing a sequence of RNA, specifically messenger RNA (mRNA). This mRNA sequence contains codons: 3 nucleotide long segments that code for a specific amino acid. Ribosomes translate the codons to their respective amino acids. In humans, non-essential amino acids are synthesized from intermediates in major metabolic pathways such as the Citric Acid Cycle. Essential amino acids must be consumed and are made in other organisms. The amino acids are joined by peptide bonds making a polypeptide chain. This polypeptide chain then goes through post translational modifications and is sometimes joined with other polypeptide chains to form a fully functional protein.
Dietary proteins are first broken down to individual amino acids by various enzymes and hydrochloric acid present in the gastrointestinal tract. These amino acids are absorbed into the bloodstream to be transported to the liver and onward to the rest of the body. Absorbed amino acids are typically used to create functional proteins, but may also be used to create energy.
Proteins can be broken down by enzymes known as peptidases or can break down as a result of denaturation. Proteins can denature in environmental conditions the protein is not made for.
Protein synthesis.
Protein anabolism is the process by which proteins are formed from amino acids. It relies on five processes: amino acid synthesis, transcription, translation, post translational modifications, and protein folding. Proteins are made from amino acids. In humans, some amino acids can be synthesized using already existing intermediates. These amino acids are known as non-essential amino acids. Essential amino acids require intermediates not present in the human body. These intermediates must be ingested, mostly from eating other organisms.
Polypeptide synthesis.
Transcription.
In transcription, RNA polymerase reads a DNA strand and produces an mRNA strand that can be further translated. In order to initiate transcription, the DNA segment that is to be transcribed must be accessible (i.e. it cannot be tightly packed). Once the DNA segment is accessible, the RNA polymerase can begin to transcribe the coding DNA strand by pairing RNA nucleotides to the template DNA strand. During the initial transcription phase, the RNA polymerase searches for a promoter region on the DNA template strand. Once the RNA polymerase binds to this region, it begins to “read” the template DNA strand in the 3’ to 5’ direction. RNA polymerase attaches RNA bases complementary to the template DNA strand (Uracil will be used instead of Thymine). The new nucleotide bases are bonded to each other covalently. The new bases eventually dissociate from the DNA bases but stay linked to each other, forming a new mRNA strand. This mRNA strand is synthesized in the 5’ to 3’ direction. Once the RNA reaches a terminator sequence, it dissociates from the DNA template strand and terminates the mRNA sequence as well.
Transcription is regulated in the cell via transcription factors. Transcription factors are proteins that bind to regulatory sequences in the DNA strand such as promoter regions or operator regions. Proteins bound to these regions can either directly halt or allow RNA polymerase to read the DNA strand or can signal other proteins to halt or allow RNA polymerase reading.
Translation.
During translation, ribosomes convert a sequence of mRNA (messenger RNA) to an amino acid sequence. Each 3-base-pair-long segment of mRNA is a codon which corresponds to one amino acid or stop signal. Amino acids can have multiple codons that correspond to them. Ribosomes do not directly attach amino acids to mRNA codons. They must utilize tRNAs (transfer RNAs) as well. Transfer RNAs can bind to amino acids and contain an anticodon which can hydrogen bind to an mRNA codon. The process of bind an amino acid to a tRNA is known as tRNA charging. Here, the enzyme aminoacyl-tRNA-synthetase catalyzes two reactions. In the first one, it attaches an AMP molecule (cleaved from ATP) to the amino acid. The second reaction cleaves the aminoacyl-AMP producing the energy to join the amino acid to the tRNA molecule.
Ribosomes have two subunits, one large and one small. These subunits surround the mRNA strand. The larger subunit contains three binding sites: A (aminoacyl), P (peptidyl), and E (exit). After translational initiation (which is different in prokaryotes and eukaryotes), the ribosome enters the elongation period which follows a repetitive cycle. First a tRNA with the correct amino acid enters the A site. The ribosome transfers the peptide from the tRNA in the P site to the new amino acid on the tRNA in the A site. The tRNA from the P site will be shifted into the E site where it will be ejected. This continually occurs until the ribosome reaches a stop codon or receives a signal to stop. A peptide bond forms between the amino acid attached to the tRNA in the P site and the amino acid attached to a tRNA in the A site. The formation of a peptide bond requires an input of energy. The two reacting molecules are the alpha amino group of one amino acid and the alpha carboxyl group of the other amino acids. A by-product of this bond formation is the release of water (the amino group donates a proton while the carboxyl group donates a hydroxyl).
Translation can be downregulated by miRNAs (microRNAs). These RNA strands can cleave mRNA strands they are complementary to and will thus stop translation. Translation can also be regulated via helper proteins. For example, a protein called eukaryotic initiation factor-2 (eIF-2) can bind to the smaller subunit of the ribosome, starting translation. When elF-2 is phosphorylated, it cannot bind to the ribosome and translation is halted.
Post-translational Modifications.
Once the peptide chain is synthesized, it still must be modified. Post-translational modifications can occur before protein folding or after. Common biological methods of modifying peptide chains after translation include methylation, phosphorylation, and disulfide bond formation. Methylation often occurs to arginine or lysine and involves adding a methyl group to a nitrogen (replacing a hydrogen). The R groups on these amino acids can be methylated multiple times as long as the bonds to nitrogen does not exceed 4. Methylation reduces the ability of these amino acids to form hydrogen bonds so arginine and lysine that are methylated have different properties than their standard counterparts. Phosphorylation often occurs to serine, threonine, and tyrosine and involves replacing a hydrogen on the alcohol group at the terminus of the R group with a phosphate group. This adds a negative charge on the R groups and will thus change how the amino acids behave in comparison to their standard counterparts. Disulfide bond formation is the creation of disulfide bridges (covalent bonds) between two cysteine amino acids in a chain which adds stability to the folded structure.
Protein folding.
A polypeptide chain in the cell does not have to stay linear; it can become branched or fold in on itself. Polypeptide chains fold in a particular manner depending on the solution they are in. The fact that all amino acids contain R groups with different properties is the main reason proteins fold. In a hydrophilic environment such as cytosol, the hydrophobic amino acids will concentrate at the core of the protein, while the hydrophilic amino acids will be on the exterior. This is entropically favorable since water molecules can move much more freely around hydrophilic amino acids than hydrophobic amino acids. In a hydrophobic environment, the hydrophilic amino acids will concentrate at the core of the protein, while the hydrophobic amino acids will be on the exterior. Since the new interactions between the hydrophilic amino acids are stronger than hydrophobic-hydrophilic interactions, this is enthalpically favorable. Once a polypeptide chain is fully folded, it is called a protein. Often many subunits will combine to make a fully functional protein although physiological proteins do exist that contain only one polypeptide chain. Proteins may also incorporate other molecules such as the heme group in hemoglobin, a protein responsible for carrying oxygen in the blood.
Protein breakdown.
Protein catabolism is the process by which proteins are broken down to their amino acids. This is also called proteolysis and can be followed by further amino acid degradation.
Protein catabolism via enzymes.
Proteases.
Originally thought to only disrupt enzymatic reactions, proteases (also known as peptidases) actually help with catabolizing proteins through cleavage and creating new proteins that were not present before. Proteases also help to regulate metabolic pathways. One way they do this is to cleave enzymes in pathways that do not need to be running (i.e. gluconeogenesis when blood glucose concentrations are high). This helps to conserve as much energy as possible and to avoid futile cycles. Futile cycles occur when the catabolic and anabolic pathways are both in effect at the same time and rate for the same reaction. Since the intermediates being created are consumed, the body makes no net gain gains. Energy is lost through futile cycles. Proteases prevent this cycle from occurring by altering the rate of one of the pathways, or by cleaving a key enzyme, they can stop one of the pathways. Proteases are also nonspecific when binding to substrate, allowing for great amounts of diversity inside the cells and other proteins, as they can be cleaved much easier in an energy efficient manner.
Because many proteases are nonspecific, they are highly regulated in the cell. Without regulation, proteases will destroy many essential proteins for physiological processes. One way the body regulates proteases is through protease inhibitors. Protease inhibitors can be other proteins, small peptides, or molecules. There are two types of protease inhibitors: reversible and irreversible. Reversible protease inhibitors form non-covalent interactions with the protease limiting its functionality. They can be competitive inhibitors, uncompetitive inhibitors, and noncompetitive inhibitors. Competitive inhibitors compete with the peptide to bind to the protease active site. Uncompetitive inhibitors bind to the protease while the peptide is bound but do not let the protease cleave the peptide bond. Noncompetitive inhibitors can do both. Irreversible protease inhibitors covalently modify the active site of the protease so it cannot cleave peptides.
Exopeptidases.
Exopeptidases are enzymes that can cleave the end of an amino acid side chain mostly through the addition of water. Exopeptidase enzymes exist in the small intestine. These enzymes have two classes: aminopeptidases are a brush border enzyme and carboxypeptidases which is from the pancreas. Aminopeptidases are enzymes that remove amino acids from the amino terminus of protein. They are present in all lifeforms and are crucial for survival since they do many cellular tasks in order to maintain stability. This form of peptidase is a zinc metalloenzyme and it is inhibited by the transition state analog. This analog is similar to the actual transition state, so it can make the enzyme bind to it instead of the actual transition state, thus preventing substrate binding and decreasing reaction rates. Carboxypeptidases cleave at the carboxyl end of the protein. While they can catabolize proteins, they are more often used in post-transcriptional modifications.
Endopeptidases.
Endopeptidases are enzymes that add water to an internal peptide bond in a peptide chain and break that bond. Three common endopeptidases that come from the pancreas are pepsin, trypsin, and chymotrypsin. Chymotrypsin performs a hydrolysis reaction that cleaves after aromatic residues. The main amino acids involved are serine, histidine, and aspartic acid. They all play a role in cleaving the peptide bond. These three amino acids are known as the catalytic triad which means that these three must all be present in order to properly function. Trypsin cleaves after long positively charged residues and has a negatively charged binding pocket at the active site. Both are produced as zymogens, meaning they are initially found in their inactive state and after cleavage though a hydrolysis reaction, they becomes activated. Non-covalent interactions such as hydrogen bonding between the peptide backbone and the catalytic triad help increase reaction rates, allowing these peptidases to cleave many peptides efficiently.
Protein catabolism via environmental changes.
pH.
Cellular proteins are held in a relatively constant pH in order to prevent changes in the protonation state of amino acids. If the pH drops, some amino acids in the polypeptide chain can become protonated if the pka of their R groups is higher than the new pH. Protonation can change the charge these R groups have. If the pH raises, some amino acids in the chain can become deprotonated (if the pka of the R group is lower than the new pH). This also changes the R group charge. Since many amino acids interact with other amino acids based on electrostatic attraction, changing the charge can break these interactions. The loss of these interactions alters the proteins structure, but most importantly it alters the proteins function, which can be beneficial or detrimental. A significant change in pH may even disrupt many interactions the amino acids make and denature (unfold) the protein.
Temperature.
As the temperature in the environment increases, molecules move faster. Hydrogen bonds and hydrophobic interactions are important stabilizing forces in proteins. If the temperature rises and molecules containing these interactions are moving too fast, the interactions become compromised or even break. At high temperatures, these interactions cannot form, and a functional protein is denatured. However, it relies on two factors; the type of protein used and the amount of heat applied. The amount of heat applied determines whether this change in protein is permanent or if it can be transformed back to its original form.


Formyltetrahydrofolate dehydrogenase

In enzymology, a formyltetrahydrofolate dehydrogenase () is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are 10-formyltetrahydrofolate, NADP+, and H2O, whereas its 4 products are tetrahydrofolate, CO2, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 10-formyltetrahydrofolate:NADP+ oxidoreductase. Other names in common use include 10-formyl tetrahydrofolate:NADP oxidoreductase, 10-formyl-H2PtGlu:NADP oxidoreductase, 10-formyl-H4folate dehydrogenase, N10-formyltetrahydrofolate dehydrogenase, and 10-formyltetrahydrofolate dehydrogenase. This enzyme participates in one carbon pool by folate.
Structural studies.
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .


DME (psychedelic)

DME (3,4-dimethoxy-beta-hydroxyphenethylamine) is a lesser-known psychedelic drug. It is the beta-hydroxy derivative of 3,4-dimethoxyphenethylamine. DME was first synthesized by Alexander Shulgin. In his book "PiHKAL", the minimum dosage is listed as 115 mg, and the duration unknown. DME produces few to no effects. Very little data exists about the pharmacological properties, metabolism, and toxicity of DME.
Legality.
United Kingdom.
This substance is a Class A drug in the Drugs controlled by the UK Misuse of Drugs Act.


Viera Scheibner

Viera Scheibner (Slovak: "Viera Scheibnerová"; born 27 March 1935, Bratislava) is a Slovak-Australian anti-vaccination activist and retired geologist. From 1958 until 1968 she was assistant professor in the department of geology at Comenius University, Bratislava. Since her retirement from the Department of Mineral Resources, New South Wales, Australia in 1987, Scheibner has been active in the anti-vaccination field, writing and giving lectures opposing vaccines and vaccinations.
A number of critics have questioned her qualifications, research abilities, and honesty.
Education and career.
Viera Scheibner was born in Bratislava (formerly Czechoslovakia, now Slovak Republic).
In 1953, Scheibner studied medicine for one year at Masaryk University in Brno (Faculty of Medicine). She did not complete her studies, and obtained no medical qualifications. She then enrolled in the Faculty of Sciences (Geology), and in 1954 transferred to the Comenius University in Bratislava where she graduated in 1958 under prof. D. Andrusov. During 1958–1961, she became a lecturer in the Department of Geology and Palaeontology of the Comenius University, Bratislava and was also a Senior Lecturer 1962–1967, at the Department of Geology and Palaeontology at Comenius University. Scheibner was awarded a doctorate in Natural Sciences (RNDr.) from the Comenius University in Bratislava in 1964. In 1967–1968 she served as Senior Associate Professor (Docent) at the Department of Geology and Palaeontology of Jan Amos Comenius University, Bratislava.
In 1968, Scheibner together with her husband Ervin Scheibner emigrated to Australia and assumed a position as a micro-palaeontologist with the Geological Survey of New South Wales, Department of Mines, later becoming the Department of Mineral Resources.
The primary emphasis of Scheibner's work in Australia with the NSW Department of Mines was the study of the Cretaceous and Permian Foraminifera of the Great Australian Basin in New South Wales. She also studied the South Australian and Carnarvon Basins in Western Australia, South Africa and the Indian Peninsula, and the Permian Foraminifera of the Sydney Basin. From 1972 to 1976 Scheibner was invited to participate in the Deep Sea Drilling Project (DSDP) conducted under the auspices of the Scripps Institution of Oceanography, in the Atlantic and Indian Oceans. The results of these studies were published in the Initial Reports of the Deep Sea Drilling Project (DSDP).
Views on vaccines.
Sudden infant death syndrome.
Scheibner began claiming that there is a link between vaccination and SIDS in the early 1990s, and in a book "Vaccination..." published in 1993. In the book and subsequently, she has speculated that "vaccination is the single biggest cause of SIDS". However data shows that since she began making her claims, vaccination rates for "Birth to 2-years" component of the Immunisation Schedule in Australia increased from 53% in 1990 to 92% in 2006, while SIDS deaths fell by 81% over the same period. A 2007 meta-analysis found that vaccines halve the risk of SIDS.
Scheibner claimed that when Japan paused their Pertussis vaccination program in 1974, SIDS deaths disappeared in the country. However, Victorian medical practitioner Stephen Basser said that the studies Scheibner cited did not support her statements and that she had omitted information [from the studies] which did not support her position, including data showing pertussis mortality in Japan increased 800% in the five years following the pause in Pertussis vaccination.
Shaken baby syndrome.
Scheibner claims that injuries and death attributed to shaken baby syndrome, including retinal bleeding, broken bones, fractured skulls and detached retinas are actually caused by vaccination although no science supports this claim.
Criticisms.
Dr Stephen Basser has written an extensive critical review of "the quality of the science of ... Scheibner" entitled "Anti-immunisation scare: The inconvenient facts". One of his criticisms involves a conclusion Scheibner makes regarding a potential correlation between SIDS and immunisation in Japan. After review of her principal sources and her resultant conclusion, he states that her analysis of the sources "is at best sloppy, and at worst blatantly dishonest." Overall, he found that her claims - in particular in regard to measles vaccinations and the DPT vaccine - are not supported by scientific evidence, and concludes that "the gaps in her research in this area call into question her objectivity and cast doubts on her ability to speak as an expert witness". In addition, an extensive critique of her claims and qualifications has been published in a 2005 article in the "Journal of Manipulative and Physiological Therapeutics". Two of the authors of that article had also previously described Scheibner's book "Vaccination: 100 years of orthodox research shows that vaccines represent an assault on the immune system" as "highly inaccurate" in a 2000 article in the journal "Pediatrics".
Commissioner William Carter, Q.C., who was hearing a Human Rights and Equal Opportunity Commission enquiry in which Viera Scheibner was called as a witness, dismissed her claims on the subject of vaccines, finding that he was unsatisfied with her formal qualifications and professional experience, which he found did not "properly equip her to provide a valid professional opinion on the complex subject of immunology". As a result, he was unwilling to accept her evidence in the enquiry.
In 2001, Brian Pezzutti criticised Viera's anti-vaccination campaigning in the NSW Legislative Council, describing Scheibner as providing "misleading information", and highlighting her March letter to the "Medical Observer" which "makes claims that are not supported by the documentation she referred to". Pezzutti stated that it was "very important for people to realise that the information provided by Dr Scheibner is not accurate".
In 1997, the Australian Skeptics awarded her the "Bent Spoon Award". This award is presented annually to the Australian "perpetrator of the most preposterous piece of pseudoscientific piffle":


Gertrud Rask

Gertrud Rask (167321 December 1735) was the first wife of the Danish-Norwegian missionary to Greenland Hans Egede and was the mother of the missionary and translator Paul Egede.
Life in Norway.
Gertrud Rask (the parish register records her as Gjertrud Nilsdatter Rasch) was born at Kvæøya, Troms, Norway, the third of six children of Niels Nielsen Rasch (1641–1704) and Nille Nilsdatter (d. 1716). Growing up in the harsh climate of northern Norway, she was 34 when she married Hans Egede, the 21-year-old pastor of Vågan in the Lofoten archipelago. They had four children - Poul (1709–1789), Niels (1710–1782), Kirstine Matthea (1715–1786) and Petronelle (1716–1805).
Her husband's determination to establish a Greenland mission had become firm by 1710 at the latest; Gertrud Rask Egede strongly resisted his plan initially, but eventually she bent to his will after he promised not to go to Greenland without her.
Mission to Greenland.
In 1718, the couple and their children moved to Bergen, whence – at the conclusion of the Great Northern War – they set sail for Greenland on 12 May 1721, arriving at Baal's River (the modern Nuup Kangerlua) on the southwest coast on 3 July. Hope Colony ("Haabets Koloni") was established on Kangeq Island at the mouth of the fjord; the remains of the house where the family lived together with (initially) about 25 other people are still preserved. The settlement was moved to the mainland and renamed Godthaab by the royal governor Claus Paarss in 1728.
Despite her strong Pietist bias, Gertrud supported her husband's missionary work among the Inuit, working among them as a nurse. In 1733, the Moravian missionaries Christian Stach, Matthias Stach, and Christian David arrived and began the settlement that would become first New Herrnhut and then Nuuk. Also with them, however, was one of Hans Egede's child converts who had been sent to Denmark to participate in the festivities around the coronation of Christian VI: the child had contracted smallpox and spread the disease to the defenseless Inuit, thousands of whom died over the next two years. Gertrud Egede worked among them, but finally succumbed herself in 1735.
In 1736, her husband left the island in the care of his son Poul and returned her body to Denmark for burial at the St. Nikolai Church in Copenhagen (now Kunsthallen Nikolaj) where Egede himself was buried upon his death in 1758.
Legacy.
Roads in both Greenland and Denmark, a church in Qaqortoq (then known as Julianehåb), a children's home and a restaurant in Nuuk have all been named after Gertrud Rask.
An icebreaking steamship, the "Gertrude Rask", was launched in Nakskov, Denmark in 1923. The 47-metre ship was used for Greenlandic trade and for several exploration trips from Copenhagen to Greenland, but sank off Nova Scotia in 1942.


Prince Lee Boo

Prince Lee Boo (1764 – 27 December 1784) was the second son of Ibedul (Abba Thule), the ruler of Koror in the Pelew Islands, now called Palau. Prince Lee Boo was one of the first people from the Pacific Islands to visit Great Britain. When the China trader "Antelope", on a voyage to China for the East Indian Company, was wrecked on the island of Oroolong in Western Palau in 1783, its survivors, including Captain Henry Wilson, spent three months on Palau. When the survivors were finally rescued, Captain Wilson agreed to take Lee Boo to London to acquire more knowledge about Europe. He arrived about a decade after the Tahitian Omai, on 14 July 1784, in Portsmouth, aboard the "Morse", and was quickly dubbed "The Black Prince" by London society, who were charmed by his poise and intelligence. The Wilson family took him into their home in London, where he attended church ceremonies, dinner parties and European school for several months. However, he died of smallpox on 27 December 1784, some six months after his arrival in London. He was 20 years old.
He was buried at St Mary the Virgin Rotherhithe.
Prince Lee Boo's story appeared in a book by George Keate (1729–97), titled: "An Account of the Pelew Islands, Situated in the Western Part of the Pacific Ocean. Composed from the Journals and Communications of Captain Henry Wilson, and some of his Officers, who, in August 1783, were there Shipwrecked, in the Antelope, a Packet belonging to the Hon. East India Company." The author's daughter, Georgiana Jane Keate (1770–1850, later Mrs. Georgiana Henderson), painted the portrait of Prince Lee Boo in the book. It was painted from memory, fifteen months after Prince Lee Boo's death.
This book was quite popular. It was translated into over 20 languages between 1789 and 1850.
An abridged version, titled: "The Interesting History of Prince Lee Boo, Brought to England from the Pelew Islands", is available online.


Marinobacter psychrophilus

Marinobacter psychrophilus is a Gram-negative, rod-shaped, psychrophilic and motile bacterium from the genus of Marinobacter which has been isolated from sea-ice of the Canadian Basin.


Ditt Apotek

Ditt Apotek is a chain of 80 pharmacies owned and run by independent pharmacists on franchise from Norsk Medisinaldepot, a subsidiary of McKesson Europe. The chain is the fourth largest, and thus smallest, in Norway. The chain was established in 2001 after the deregulation of the pharmacy market in Norway. The sister company Vitusapotek operates 133 pharmacies owned by the mother company.
Among the members are the four state owned pharmaceutical trusts that operate the pharmacies at the hospitals: Southern and Eastern Norway Pharmaceutical Trust, Western Norway Pharmaceutical Trust, Central Norway Pharmaceutical Trust, and Northern Norway Pharmaceutical Trust.


MMP9

Matrix metallopeptidase 9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), is a matrixin, a class of enzymes that belong to the zinc-metalloproteinases family involved in the degradation of the extracellular matrix. In humans the "MMP9" gene encodes for a signal peptide, a propeptide, a catalytic domain with inserted three repeats of fibronectin type II domain followed by a C-terminal hemopexin-like domain.
Function.
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, angiogenesis, bone development, wound healing, cell migration, learning and memory, as well as in pathological processes, such as arthritis, intracerebral hemorrhage, and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens and other extracellular matrix proteins. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.
Thrombospondins, intervertebral disc proteins, regulate interaction with matrix metalloproteinases (MMPs) 2 and 9, which are key effectors of ECM remodeling.
Neutrophil action.
MMP9, along with elastase, appears to be a regulatory factor in neutrophil migration across the basement membrane.
MMP9 plays several important functions within neutrophil action, such as degrading extracellular matrix, activation of IL-1β, and cleavage of several chemokines. In a mouse model, MMP9 deficiency resulted in resistance to endotoxin shock, suggesting that MMP9 is important in sepsis.
Angiogenesis.
MMP9 may play an important role in angiogenesis and neovascularization. For example, MMP9 appears to be involved in the remodeling associated with malignant glioma neovascularization. It is also a key regulator of growth plate formation- both growth plate angiogenesis and the generation of hypertrophic chondrocytes. Knock-out models of MMP9 result in delayed apoptosis, vascularization, and ossification of hypertrophic chondrocytes. Lastly, there is significant evidence that Gelatinase B is required for the recruitment of endothelial stem cells, a critical component of angiogenesis
Wound repair.
MMP9 is greatly upregulated during human respiratory epithelial healing. Using a MMP9 deficient mouse model, it was seen that MMP9 coordinated epithelial wound repair and deficient mice were unable to remove the fibrinogen matrix during wound healing. When interacting with TGF-ß1, Gelatinase B also stimulates collagen contraction, aiding in wound closure.
Structure.
MMP9 is synthesized as preproenzyme of 707 amino-acid residues, including a 19 amino acid signal peptide and secreted as an inactive pro-MMP. The human MMP9 proenzyme consists of five domains. The amino-terminal propeptide, the zinc-binding catalytic domain and the carboxyl-terminal hemopexin-like domain are conserved. Its primary structure comprises several domain motifs. The propeptide domain is characterized by a conserved PRCGVPD sequence. The Cys within this sequence is known as the “cysteine switch”. It ligates the catalytic zinc to maintain the enzyme in an inactive state.
Activation is achieved through an interacting protease cascade involving plasmin and stromelysin 1 (MMP-3). Plasmin generates active MMP-3 from its zymogen. Active MMP-3 cleaves the propeptide from the 92-kDa pro-MMP-9, yielding an 82-kDa enzymatically active enzyme. In the active enzyme a substrate, or a fluorogenic activity probe., replaces the propetide in the enzyme active site where it is cleaved. The catalytic domain contains two zinc and three calcium atoms. The catalytic zinc is coordinated by three histidines from the conserved HEXXHXXGXXH binding motif. The other zinc atom and the three calcium atoms are structural. A conserved methionine, which forms a unique “Met-turn” structure categorizes MMP9 as a metzincin. Three type II fibronectin repeats are inserted in the catalytic domain, although these domains are omitted in most crystallographic structures of MMP9 in complex with inhibitors. The active form of MMP9 also contains a C-terminal hemopexin-like domain. This domain is ellipsoidal in shape, formed by four β-propeller blades and an α-helix. Each blade consists of four antiparallel β-strands arranged around a funnel-like tunnel that contains two calcium and two chloride ions. The hemopexin domain is important to facilitate the cleavage of triple helical interstitial collagens.
Clinical significance.
MMP9 has been found to be associated with numerous pathological processes, including cancer, placental malaria, immunologic and cardiovascular diseases.
Arthritis.
Elevated MMP9 levels can be found in the cases of rheumatoid arthritis and focal brain ischemia.
Cancer.
One of MMP9's most widely associated pathologies is the relationship to cancer, due to its role in extracellular matrix remodeling and angiogenesis. For example, its increased expression was seen in a metastatic mammary cancer cell line. Gelatinase B plays a central role in tumor progression, from angiogenesis, to stromal remodeling, and ultimately metastasis. However, because of its physiologic function, it may be difficult to leverage Gelatinase B inhibition into cancer therapy modalities. However, Gelatinase B has been investigated in tumor metastasis diagnosis- Complexes of Gelatinase B/Tissue Inhibitors of Metalloproteinases are seen to be increased in gastrointestinal cancer and gynecologic malignancies
MMPs such as MMP9 can be involved in the development of several human malignancies, as degradation of collagen IV in basement membrane and extracellular matrix facilitates tumor progression, including invasion, metastasis, growth and angiogenesis.
Cardiovascular.
MMP9 levels increase with the progression of idiopathic atrial fibrillation.
MMP9 has been found to be associated with the development of aortic aneurysms, and its disruption prevents the development of aortic aneurysms. Doxycycline suppresses the growth of aortic aneurysms through its inhibition of MMP9.
Pregnancy-associated malaria (Placental malaria).
A study on Ghanaian population showed that MMP-9 single nucleotide polymorphism 1562 C > T (rs3918242) was protective against placental malaria which suggests a possible role of MMP-9 in susceptibility to malaria.
Dry eye.
Dry eye patients, especially with meibomian gland dysfunction exhibit higher levels of MMP-9.


Equine arteritis virus leader TRS hairpin (LTH)

The equine arteritis virus leader transcription-regulating sequence hairpin (LTH) is as RNA element that is thought to be a key structural element in discontinuous subgenomic RNA synthesis and is critical for leader transcription-regulating sequences (TRS) function. Similar structures have been predicted in other arteriviruses and coronaviruses.


4-Acetoxy-DiPT

4-Acetoxy-DiPT (4-acetoxy-"N","N"-diisopropyltryptamine, ipracetin) is a synthetic psychedelic tryptamine. It is relatively uncommon and has only a short history of human use.
Chemistry.
4-AcO-DiPT is a tryptamine structurally similar to 4-HO-DiPT and psilocin.
Drug prohibition laws.
Denmark.
4-AcO-DiPT is added to the list of Schedule B controlled substances.
Japan.
4-Acetoxy-DiPT is a controlled substance in Japan
Sweden.
"Sveriges riksdags" health ministry classified 4-AcO-DiPT as "health hazard" under the act (translated "Act on the Prohibition of Certain Goods Dangerous to Health") as of Mar 1, 2005, in their regulation SFS 2005:26 listed as 4-acetoxi-N,N-diisopropyltryptamin (4-AcO-DIPT), making it illegal to sell or possess.
United States.
4-Acetoxy-DiPT is an unscheduled substance in the United States. Due to similarities to other scheduled tryptamines such as psilocin and DiPT, possession may be prosecuted under the Federal Analog Act in the United States.


Wellsoft

Wellsoft Corporation is an Electronic Medical Record software vendor specializing in Emergency Department Information Systems (EDIS).
Wellsoft EDIS v11 is certified as an ONC-ACB 2014 Edition EHR Module (CC-2014-527400-1). This certification does not represent an endorsement by the U.S. Department of Health and Human Services or guarantee the receipt of incentive payments. The system complies with The Joint Commission and CMS requirements.


Robert Blair (VC)

Robert Blair VC (13 March 1834 – 28 March 1859) was a Scottish recipient of the Victoria Cross, the highest and most prestigious award for gallantry in the face of the enemy that can be awarded to British and Commonwealth forces.
He was 23 years old, and a lieutenant in the 2nd Dragoon Guards (Queen's Bays), British Army, attached to 9th Lancers (The Queen's Royal) during the Indian Mutiny when the following deed took place on 28 September 1857 at Bolandshahr, India, for which he was awarded the VC.
Blair was a graduate of University of Glasgow and a Snell exhibitioner at Balliol College, Oxford. Blair joined the army in 1855 in the service of the 9th Lancers and later transferred to the 2nd Dragoon Guards. He later achieved the rank of captain and died of smallpox in Cawnpore, India, on 28 March 1859. He was the cousin of another Indian Mutiny VC recipient James Blair.
His Victoria Cross is displayed at the Queen's Dragoon Guards Regimental Museum in Cardiff Castle, Wales.


Cinamolol

Cinamolol is a beta blocker.


Octadecanoid pathway

The octadecanoid pathway is a biosynthetic pathway for the production of the phytohormone jasmonic acid (JA), an important hormone for induction of defense genes. JA is synthesized from alpha-linolenic acid, which can be released from the plasma membrane by certain lipase enzymes. For example, in the wound defense response, phospholipase C will cause the release of alpha-linolenic acid for JA synthesis.
In the first step, alpha-linolenic acid is oxidized by the enzyme lipoxygenase. This forms 13-hydroperoxylinolenic acid, which is then modified by a dehydrase and undergoes cyclization by allene oxide cyclase to form 12-oxo-phytodienoic acid. This undergoes reduction and three rounds of beta oxidation to form jasmonic acid.


Giuseppina Bozzacchi

Giuseppina Bozzacchi (23 November 1853 – 23 November 1870) was an Italian ballerina, noted for creating the role of Swanhilda in Léo Delibes' ballet "Coppélia" at the age of 16 while dancing for the Paris Opera Ballet.
Bozzacchi, who was born in Milan, had come to Paris to study with Mme Dominique. The choreographer Arthur Saint-Léon and the director of the Académie Royale de Musique, Émile Perrin, had been searching for a suitable Swanhilda, after deciding that none of the ballerinas previously considered – Léontine Beaugrand and Angelina Fioretti – were suitable, while , the favorite ballerina of Saint-Léon, had started to prepare the role with choreography in 1868 but then fell seriously ill. In 1869 they even asked the composer, Léo Delibes, to seek out a suitable Swanhilda on his trip to Italy. He returned empty-handed; in the meantime, Saint-Léon and Perrin had discovered 16-year-old Bozzacchi.
She created the Swanhilda role on 25 May 1870 in the presence of Emperor Napoleon III. She repeated her success in the following weeks. In July an international dispute broke out between France and Prussia over the succession to the Spanish throne, and on 19 July France declared war. Bozzacchi danced Swanhilda for the 18th and last time on 31 August, when the Paris Opéra closed for the duration of the Franco-Prussian War. The Opéra had stopped paying salaries, and Bozzacchi, weakened by lack of food, became ill. She contracted smallpox and fever, and died on the morning of her 17th birthday. She was buried at Cimetière de Montmartre in Paris.


Louis Armand I, Prince of Conti

Louis Armand de Bourbon (30 April 1661 – 9 November 1685) was Prince of Conti from 1666 to his death, succeeding his father, Armand de Bourbon. His mother was Anne Marie Martinozzi, the daughter of Girolamo Martinozzi and Laura Margherita Mazzarini, elder sister of Cardinal Mazarin. As a member of the reigning House of Bourbon, he was a Prince du Sang. He was a son-in-law of King Louis XIV of France, who was his namesake.
Biography.
Louis Armand was born at the Hôtel de Conti (quai Malaquais) in Paris, France.
In August 1679 he acted as the groom in the proxy marriage where Marie Louise d'Orléans married Charles II of Spain. In 1680 he married Marie Anne de Bourbon, the illegitimate daughter of King Louis XIV and his first mistress, Louise de La Vallière. The bride and groom were respectively thirteen and eighteen years old at the time. Since neither of them had been instructed on what to expect on their first night together, it ended up in disaster, with Marie Anne fleeing in despair and the prince not wanting to share the bed of a woman again.
He served with distinction in Flanders in 1683, and, against the wish of the King, went to Hungary, where he helped the Imperialists defeat the Turks at Gran in the same year. He died at the Palace of Fontainebleau from smallpox, which he contracted from his wife. While she recovered after some time, the Prince succumbed after five days.
Having no descendants, he was succeeded as Prince of Conti by his younger brother, François Louis de Bourbon (1664–1709).


GC box

In molecular biology, a GC box, also known as a GSG box, is a distinct pattern of nucleotides found in the promoter region of some eukaryotic genes. The GC box is upstream of the TATA box and approximately 110 bases upstream from the transcription initiation site. It has a consensus sequence GGGCGG which is position-dependent and orientation-independent. The GC elements are bound by transcription factors and have similar functions to enhancers. Some known GC box-binding proteins include Sp1, Krox/Egr, Wilms' tumor, MIGI, and CREA.
The GC box is commonly the binding site for Zinc finger proteins. An Alpha helix section of the protein corresponds with a major groove in the DNA. Zinc-fingers bind to triplet base pair sequences, with residue 21 binding to the first base pair, residue 18 binding to the second base pair, and residue 15 binding to the third base pair. The triplet base pairs can either be a GGG or a GCG. If residue 18 is a histidine, it will bind to a G, and if residue 18 is a glutamic acid, it will bind to a C. GC box-binding zinc-finger have between 2 and 4 fingers, making them interact with base pair sequences that are 6 to 8 base pairs in length.


Ethyldichloroarsine

Ethyldichloroarsine, sometimes abbreviated "ED" and also known as ethyl Dick, is an organoarsenic compound with the formula CH3CH2AsCl2. This colourless volatile liquid is a highly toxic obsolete vesicant or blister agent that was used during World War I in chemical warfare. The molecule is pyramidal with the Cl-As-Cl and C-As-Cl angles approaching 90° (see image). Ethyldichloroarsine has high chronic toxicity, similar to lewisite.


Carteolol

Carteolol is a non-selective beta blocker used to treat glaucoma.
It has been found to act as a serotonin 5-HT1A and 5-HT1B receptor antagonist in addition to being a beta blocker.
It was patented in 1972 and approved for medical use in 1980.
Brand names.
Brand names include Cartrol, Ocupress, Teoptic, Arteolol, Arteoptic, Calte, Cartéabak, Carteol, Cartéol, Cartrol, Elebloc, Endak, Glauteolol, Mikelan, Poenglaucol, and Singlauc.


Mycena polygramma

Mycena polygramma, commonly known as the grooved bonnet, is a species of mushroom in the family Mycenaceae. The inedible fruit bodies are small, pale gray-brown mushrooms with broadly conical caps, pinkish gills. They are found in small troops on stumps and branches of deciduous and occasionally coniferous trees. The mushroom is found in Asia, Europe, and North America, where it is typically found on twigs or buried wood, carrying out its role in the forest ecosystem by decomposing organic matter, recycling nutrients, and forming humus in the soil. "M. polygramma" contains two uncommon hydroxy fatty acids and is also a bioluminescent fungus whose intensity of light emission follows a diurnal pattern.
Taxonomy.
First called "Agaricus polygrammus" by French mycologist Jean Bulliard in 1789, the species was later sanctioned under that name by Elias Magnus Fries in his "Systema Mycologicum". It was soon after transferred into the genus "Mycena" in 1821 by Samuel Frederick Gray, who raised many of Fries' sub-generic divisions to the genus level. "Agaricus chloroticus", described by Friedrich Franz Wilhelm Junghuhn in 1830, is the only known taxonomic synonym. The specific epithet is derived from the Greek πολύς meaning "many" and γραμμή, or "line". It is commonly known as the "grooved bonnet".
Description.
The cap of the "M. polygramma" fruit body is in diameter, and initially egg- to cone-shaped, but expands to become conic to bell-shaped or nearly convex with an abrupt small umbo, or at times plane with a conic umbo. On young fruit bodies, the cap margin is slightly curved inward, and frequently has scalloped edges; in maturity the margin flares out, or is recurved and wavy. The surface of the cap is initially covered with short, fine whitish or grayish hairs that often persist until near maturity. With age, the cap surface becomes smooth, the color dark brownish-gray to black beneath the bloom, fading slowly to a pale gray, and nearly pinkish-buff at times. The cap margin is opaque and frequently has narrow, deep furrows or grooves, with the surface often more or less uneven and appearing as if streaked with glistening lines. The flesh is very hard and cartilaginous, watery grayish to white, rather thin, and with no distinctive odor and a mild taste.
The gills are narrowly adnate (attached squarely to the stem) or have a short decurrent tooth, and are packed close together, with 30–38 gills reaching the stem. They are broad anteriorly (4–7 mm), white or whitish, in age flushed with pink, often with sordid-brownish stains, and with edges pallid and even. The stem is long, thick, very brittle and cartilaginous, equal, and tubular. It sometimes has a well-developed pseudorrhiza that resembles white cotton, and the base is covered with stiff white hairs, and often it stains reddish brown. The surface has fine straight or sometimes twisted longitudinal striations. The surface is ashy-gray or paler grayish-brown beneath the silvery covering, at times nearly smooth, with the apex pallid and faintly powdered.
 "Mycena polygramma" is a bioluminescent mushroom, although the extent of luminescence can vary considerably. The mushroom is inedible, and has a mild to slightly acrid taste and a "pleasant" odor.
Microscopic features.
Collected in deposit, such as in a spore print, the spores appear white. Viewed with a light microscope, the spores are broadly ellipsoid in shape, smooth, amyloid, with dimensions of 7.5–10 by 5–6 µm. Occasionally the spores contain oil droplets. The basidia (pore-bearing cells) are four-spored, 26–30 by 7–8 µm. The cheilocystidia are scattered to abundant, aciculate or with the midportion somewhat enlarged and the apex forked or branched, and give rise to two or several contorted finger-like projections. Pleurocystidia are not differentiated.
Similar species.
Tall and slender forms of "Mycena polygramma" somewhat resemble "M. pullata" or "M. praelonga". The former species is distinguished by its color, and the latter by its relationship to "M. alcalina" and its habitat on sphagnum.
Ecology, habitat and distribution.
The fruit bodies of "M. polygramma" grow in groups or sub-clusters under hardwoods, particularly deciduous trees such as oak, maple, and basswood. In North America, it has been collected from North Carolina, Massachusetts, New York, and Michigan, where it fruits from June to October. The fruit bodies are susceptible to attack by the parasitic fungi "Spinellus fusiger" and "S. macrocarpus".
Typically found on twigs or buried wood, the fungus is known to be a vigorous decomposer of lignin and cellulose in leaf litter. "Mycena polygramma" is a saprobic fungus, and is one of many fungi that contribute to plant litter decomposition in forest ecosystems through nutrient recycling and humus formation in soil. It is a lignocellulose decomposer of larch litter, and can break down both lignin and carbohydrates, although it has a preference for carbohydrates. In an experiment testing the ability of several litter-decomposing fungi to remove lignin from leaves of the perennial grass "Miscanthus sinensis", under pure culture conditions, "M. polygramma" showed limited ability to cause the mass loss of lignin.
Rare in North America, the fungus is common in Europe, including Great Britain. They have been collected on the Falkland Islands, and Japan.
Chemistry and bioluminescence.
"Mycena polygramma" contains the unusual hydroxy fatty acids 7-hydroxy-8,14-dimethyl-9-hexadecenoic acid (0.05% of the total fatty acids) and 7-hydroxy-8,16-dimethyl-9-octadecenoic acid (0.01%).
The fungus is one of several dozen "Mycena" species that are bioluminescent. Unlike most luminescent organisms, "M. polygramma" has a diurnal rhythm of luminescence intensity, and has rises and falls of light intensity as high as 35 percent. However, this light emission is not typically noticed, as it can not be detected visually by the dark-adapted eye; sensitive photomultipliers or long exposure times are required to measure the phenomenon. The wavelength of spectral emissions from the fungus grown in pure culture is in the range 470–640 mμ.


Intron-mediated enhancement

Intron-mediated enhancement (IME) is the ability of an intron sequence to enhance the expression of a gene containing that intron. In particular, the intron must be present in the transcribed region of the gene for enhancement to occur, differentiating IME from the action of typical transcriptional enhancers. Descriptions of this phenomenon were first published in cultured maize cells in 1987, and the term "intron-mediated enhancement" was subsequently coined in 1990. A number of publications have demonstrated that this phenomenon is conserved across eukaryotes, including humans, mice, "Arabidopsis", rice, and "C. elegans." However, the mechanism(s) by which IME works are still not completely understood.
When testing to see whether any given intron enhances the expression of a gene, it is typical to compare the expression of two constructs, one containing the intron and one without it, and to express the difference between the two results as a "fold increase" in enhancement. Further experiments can specifically point to IME as the cause of expression enhancement - one of the most common is to move the intron upstream of the transcription start site, removing it from the transcript. If the intron can no longer enhance expression, then inclusion of the intron in the transcript is important, and the intron probably causes IME.
Not all introns enhance gene expression, but those that do can enhance expression between 2– and >1,000–fold relative to an intronless control. In "Arabidopsis" and other plant species, the IMEter has been developed to calculate the likelihood that an intron sequence will enhance gene expression. It does this by calculating a score based on the patterns of nucleotide sequences within the target sequence. The position of an intron within the transcript is also important - the closer an intron is to the start (5' end) of a transcript, the greater its enhancement of gene expression.


Sabine Werner

Sabine Werner (born 5 September 1960) is a German biochemist and professor.
Biography.
Sabine Werner was born on 5 September 1960 in Tübingen, Germany. She attended Universities of Tubingen and Munich where she studied Biochemistry. Her PhD was in cancer research at the Max Planck Institute of Biochemistry, completed in 1989. Werner then went to the University of California San Francisco working on growth factor action and tissue repair. Werner took a position as group leader at the Max-Planck-Institute from 1993 to 1999 while also working as an Associate Professor in the Ludwig-Maximilians-University of Munich. In 1999 Werner became the Professor of Cell Biology at ETH Zürich. She is also a member of the European Academy of Sciences, the European Molecular Biology Organization and the German Academy of Sciences. Werner was awarded the Pfizer Academic Award in 1998.
Sources.


Resumption of meiosis

Resumption of meiosis occurs as a part of oocyte meiosis after meiotic arrest has occurred. In females, meiosis of an oocyte begins during embryogenesis and will be completed after puberty. A primordial follicle will arrest, allowing the follicle to grow in size and mature. Resumption of meiosis will resume following an ovulatory surge (ovulation) of luteinising hormone (LH).
Meiotic arrest.
Meiosis was initially discovered by Oscar Hertwig in 1876 as he examined the fusion of the gametes in sea urchin eggs. In 1890, August Weismann, concluded that two different rounds of meiosis are required and defined the difference between somatic cells and germ cells.
Studies regarding meiotic arrest and resumption have been difficult to attain because, within females, the oocyte is inaccessible. The majority of research was conducted by removing the follicles and artificially maintaining the oocyte in meiotic arrest. Despite this allowing the gain of knowledge on meiosis in oocytes, the results of this methodology may be difficult to interpret and apply to humans.
During oogenesis, meiosis arrests twice. The main arrest occurs during the diplotene stage of prophase 1, this arrest lasts until puberty. The second meiotic arrest then occurs after ovulation during metaphase 2 and lasts for a much shorter time than the first arrest. Meiotic arrest occurs mainly due to increased cAMP levels in the oocyte, which regulates key regulator cyclin kinase complex maturation promoting factor (MPF). cGMPs produced by somatic follicular cells further regulate cAMP concentration in the oocyte.
Meiotic resumption in mammals.
Meiotic resumption is visually manifested as “germinal vesicle breakdown” (GVBD), referring to the primary oocyte nucleus. GVBD is the process of nuclear envelope dissolution and chromosome condensation similar to mitotic prophase.
In females, the process of folliculogenesis begins during fetal development. Folliculogenesis is the maturation of ovarian follicles. Primordial germ-cells (PGC’S) undergo meiosis leading to the formation of primordial follicles. At birth, meiosis arrests at the diplotene phase of prophase I. Oocytes will remain in this state until the time of puberty. At the time of ovulation a surge of LH initiates the resumption of meiosis and oocytes enter the second cycle, which is known as oocyte maturation. Meiosis is then arrested again during metaphase 2 until fertilisation. At fertilisation meiosis then resumes which results in the disassociation from the 2nd polar body, meaning maturation of the oocyte is now complete.
Meiotic resumption signalling.
Cyclic adenosine monophosphate levels (cAMP).
Elevated concentrations of intra-oocyte cAMP regulates meiotic arrest and prevents meiotic resumption. Intracellular cAMP constantly activates PKA, which then activates nuclear kinase Weel/MtyI. Weel/Mtyl inhibits cell division cycle 25B (CDC25B) which is a main activator for Cyclin-dependent kinase (CDK). This leads to the inactivation of maturation promoting factor (MPF) as MPF comprises CDK and Cyclin B.
MPF is an essential regulator for M-phase transition and plays a key role in meiotic resumption in oocytes and its post-GVBD activities. Hence, a high level of cAMP indirectly inactivates MPF, preventing meiotic resumption.
GPCR3-Gs-ADCY Cascade.
The production of cAMP is maintained by the intra-oocyte GPCR-GS-ADCY cascade.
Inhibition of Gs protein in mouse oocyte leads to meiotic resumption. Gs protein-coupled receptor 3 (GPCR3) KO mice was found to present with spontaneous meiotic resumption as well, which was preventable with the administration of GPCR3 RNA into the oocyte. GPCR3 can be found to be present in the oocyte membrane and functions to sustain a minimal level of cAMP, preventing meiotic resumption.
In the oocyte, the effector enzyme of GPR is adencylate cyclase (ADCY). It acts as a catalyst converting adenosine triphosphate (ATP) to cAMP, maintaining cAMP levels within the oocyte, preventing meiotic resumption.
Somatic follicular cells and cyclic guanosine monophosphate (cGMP).
The removal of oocyte from the follicle results in spontaneous meiotic resumption which implicates the role of somatic follicular cells in meiotic arrest.
cGMP is produced by guanylyl cyclase present the granulosa cells, in particular, natriuretic peptide receptor 2 (NPR2) and natriuretic peptide precursor-C (NPPC) that can be found in the cumulus and mural granulosa cells respectively (in mice, pigs and human).
cGMP produced by these granulosa cells rapidly diffuse into the oocyte through gap junctions and inhibits cAMP-phosphodiesterase 3A (cAMP-PDE3A). cAMP-PDE3A functions as a catalyst for the breakdown of cAMP to AMP within the oocyte. Hence, somatic follicular cells produce cGMP inhibit cell resumption via maintain intra-oocyte cAMP levels.
Inosine 5’ monophosphate (IMP) dehydrogenase (IMPDH).
Previous studies have demonstrated that treatment of mouse oocytes with IMPDH  inhibitors induced gonadotropin-independent meiotic resumption in vivo.
IMPDH is a rate limiting enzyme that catalyses IMP to xanthosine monophosphate (XMP). It can induce meiotic resumption as XMP produced is ultimately be converted to cGMP through a series of enzymatic activities.
In addition, IMPDH maintains hypoxanthine (HX) levels in the follicular fluid. The HX concentration inhibits cAMP-PDE activity in vitro.
Lutensing Hormone (LH).
It is commonly known that monthly surge of preovulatory LH from the pituitary gland promotes meiotic resumption.
First, LH signaling dephosphorylates and inactivates NPR2 guanylyl cyclase. This results in a rapid decrease in cGMP levels in the granulosa cells and the oocytes through the gap junctions. PDE5 is also activated, increasing cGMP hydrolysis. In mouse follicles, the concentration of cGMP drops from ~2-5 μM to ~100nM within a minute from exposure to LH.
The decreasing cGMP concentration occurs in a sequential fashion, from the mural granulosa cells, the cumulus granulosa cells and finally the oocyte. The diffusion of cGMP out of the oocyte promotes meiotic resumption. It proposed that the diffusion of cGMP away from the oocyte occurs before LH-induced closure of gap junctions between somatic cells, could be an “augment step to further guarantee a low level of cGMP within the oocyte or cumulus granulosa”.
It is also believed that LH-induced cGMP decrease in granulosa cells is only part of the mechanism, with the full mechanism remaining unexplained.


Eremitalpa


N-Methylserotonin

"N"-Methylserotonin is a tryptamine alkaloid. Chemically, it is a derivative of serotonin in which a methyl group resides at its alkyl amine. It is also called "N"ω-methylserotonin ("N"ω-methyl-5-hydroxytryptamine) to distinguish it from tryptamine-derived compounds in which a methyl group is bonded to the nitrogen atom of the indole group.
"N"-Methylserotonin is found in plants, animals, and fungi. These include the plants, "Actaea racemosa" (black cohosh) and "Zanthoxylum piperitum", the Green and Golden Bell Frog, "Litoria aurea", and "Amanita" mushrooms. The compound binds to several serotonin receptors, including the 5-HT7 and 5-HT1A receptors, with high affinity (IC50 ≤ 2 nM) and selectivity, and displays agonist activity; besides its direct interaction with the serotonin receptors, "N"-methylserotonin also acts as a selective serotonin reuptake inhibitor.
Legal Status.
United States.
"N"-Methylserotonin is not scheduled at the federal level in the United States, but could be considered an analog (of bufotenin), in which case, sales or possession intended for human consumption could be prosecuted under the Federal Analog Act.
Florida.
"N"-Methylserotonin is a Schedule I controlled substance in the state of Florida making it illegal to buy, sell, or possess in Florida.


Burkholderia

Burkholderia is a genus of Proteobacteria whose pathogenic members include the "Burkholderia cepacia" complex, which attacks humans and "Burkholderia mallei", responsible for glanders, a disease that occurs mostly in horses and related animals; "Burkholderia pseudomallei", causative agent of melioidosis; and "Burkholderia cepacia", an important pathogen of pulmonary infections in people with cystic fibrosis (CF).
The "Burkholderia" (previously part of "Pseudomonas") genus name refers to a group of virtually ubiquitous Gram-negative, obligately aerobic, rod-shaped bacteria that are motile by means of single or multiple polar flagella, with the exception of "Burkholderia mallei", which is nonmotile. Members belonging to the genus do not produce sheaths or prosthecae and are able to use poly-beta-hydroxybutyrate (PHB) for growth. The genus includes both animal and plant pathogens, as well as some environmentally important species. In particular, "B. xenovorans" (previously named "Pseudomonas cepacia" then "B. cepacia" and "B. fungorum") is renowned for being catalase positive (affecting patients with chronic granulomatous disease) and its ability to degrade chlororganic pesticides and polychlorinated biphenyls. The conserved RNA structure anti-hemB RNA motif is found in all known bacteria in this genus.
Due to their antibiotic resistance and the high mortality rate from their associated diseases, "B. mallei" and "B. pseudomallei" are considered to be potential biological warfare agents, targeting livestock and humans.
History.
The genus was named after Walter H. Burkholder, plant pathologist at Cornell University. The first species placed in the genus were transfers from "Pseudomonas", on the basis of various biochemical tests.
Until recently, the genus "Burkholderia" was inclusive of all "Paraburkholderia" species. However, the genus "Paraburkholderia" is phylogenetically distinct, and can be distinguished from all "Burkholderia" species on the basis of molecular signatures that are uniquely found for each genus.
Taxonomy.
"Burkholderia" species form a monophyletic group within the Burkholderiales order of the Betaproteobacteria. Currently, the 48 validly named species can be distinguished from related genera (i.e. "Paraburkholderia") and all other bacteria by conserved signature indels in a variety of proteins. These indels represent exclusive common ancestry shared among all "Burkholderia" species.
The genus has three distinct monophyletic clusters. One group consists of all species belonging to the "Burkholderia cepacia" complex, another clade comprises "B. pseudomallei" and closely related species, and the last clade encompasses of most of the phytogenic species within the genus, including "B. glumae" and "B. gladioli ". Conserved signature indels are specific for each of these subgroups within the genus that aid in demarcating members of this extremely large and diverse genus.
Research.
Recently, research in "Burkholderia" species has investigated a range of topics and characteristics including metabolomic response to antibiotics, contact-dependent interactions between bacterial communities, and genomic potential to yield beneficial products.
In "Burkholderia" species, certain antibiotics such as trimethoprim has been shown to induce and upregulate a large amount of the metabolome, inducing over 100 silent secondary metabolite gene clusters in "Burkholderia thailandensis." These global activators can be used as a source of investigation into how the metabolomes of pathogenic bacterial species respond to antibiotic stress and how bacterial species can vary in response to them. It has been shown that closely related cystic fibrosis-associated "Burkholderia" species respond to trimethoprim with differing levels of expression of various secondary metabolites, highlighting the personalized nature of metabolomics in related bacterial strains.
Research focused on interbacterial signaling using "Burkholderia" has shown that contact-dependent growth inhibition plays a significant role in mediating cell to cell communication specifically in "B. thailandensis". In this interaction, cells release protein toxins to the surrounding environment, and only those with a corresponding protective protein (usually bacteria of the same strain) will not have its growth inhibited or die. Furthermore, recipient cells that have the corresponding protein then undergo changes to gene expression and phenotype that promotes community formation in the form of biofilms. This occurs even if the recipient cell was not of the same bacterial strain which highlights the importance of this system. The genes that encode the protein toxins and the rest of the contact-dependent inhibition system can become mobile in the form of a transposon that can transfer between cells and is critical to communal aspect of the system. Thus, contact-dependent signaling plays a significant role in bacterial self recognition and community formation.
"Burkholderia" species have been shown to be a potential source of beneficial products such as antimicrobials and biosurfactants. Along with the related genus "Pseudomonas", "Burkholderia" can synthesize a particular class of biosurfactant called rhamnolipids. Rhamnolipids synthesized by "Burkholderia" have differing chemical characteristics (compared to those synthesized by "Pseudomonas") and thus have the potential for novel applications.
Species.
List of species:


Jolen (comics)

Jolen is a fictional character and a superhero appearing in American comic books published by Marvel Comics. He is a member of the Inhumans and was part of the delegation sent to Earth.
Fictional character biography.
No background history is known about Jolen, except that he is an Inhuman. In his first appearance, he is seen passing through the Terrigen Mist and gaining his superhuman abilities. He is then selected alongside a number of other youths to be sent to Earth on a sort of foreign exchange program at the University of Wisconsin–Madison. He adjusts quickly to the conditions of Earth, but appears to have trouble understanding the nature of his peers, often overreacting to them.
After hearing from one of his friends that Nahrees, a former love interest, has been captured by Mister Chase, he quickly drives to Chicago where she is being held prisoner. Jolen confronts Mister Chase, a hired hitman, and is shot in the head. After a bit of scuffle, Jolen revives and uses a root to murder the hitman. From here, Jolen appears to take a darker moral path, threatening and killing several other people.
In response to a report of Terrigen crystals in New York City, Jolen is assembled with a team and leads an assault on the reported owner of the crystals. During the assault, the team is confronted by the Fantastic Four and are quickly defeated. The Fantastic Four turned the Inhuman team over to the Office of National Security (ONE), where they were detained.
After being freed by Mala the Diviner and Dewoz, they retrieve the Terrigen crystals as well as capture the holder of the crystals, Dr. Cartwrite. Having accomplished their mission, they return to their moon base.
Powers and abilities.
Due to his race, he is gifted with a number of abilities in addition to that of a normal human. Included in these abilities is an above-average lifespan, 150 years average, physical strength and speed greater than that of a peak-condition human athlete, above-average reflexes, and above-average endurance.
After passing through the Terrigen mists, he is granted plant-related abilities. Among these are the ability to control plants with his mind, grow plants by linking with them, and transform into a plant himself. He is also able to use plants as a means of travel by shrinking, then traveling through the plant's root system. He is also sometimes shown recovering from fatal wounds by transforming into a plant and letting the wound heal.
Appearances.
A likely incomplete list of his appearances, credits included:


Oligopeptide

An oligopeptide, often just called peptide ("oligo-", "a few"), consists of two to twenty amino acids and can include dipeptides, tripeptides, tetrapeptides, and pentapeptides. Some of the major classes of naturally occurring oligopeptides include aeruginosins, cyanopeptolins, microcystins, microviridins, microginins, anabaenopeptins, and cyclamides. Microcystins are best studied, because of their potential toxicity impact in drinking water. A review of some oligopeptides found that the largest class are the cyanopeptolins (40.1%), followed by microcystins (13.4%).
Production.
Oligopeptide classes are produced by nonribosomal peptides synthases (NRPS), except cyclamides and microviridins are synthesized through ribosomic pathways.
Examples.
Examples of oligopeptides include:


List Biological Laboratories

List Biological Laboratories, (List Labs) is a US biotechnology company producing bacterial toxins. Their products are involved in vaccine development, toxin research and infectious disease research worldwide.
History.
List Labs was founded in 1978 by Linda Shoer, and is headquartered in Campbell, California.
Starting with cholera, the firm developed bacterial proteins for research. When thefirm was founded and for many years after, it was the only manufacturer and supplier for several bacterial exotoxins and lipopolysaccharides (LPS).
In 2015 the firm performed a technology transfer of botulinum toxin manufacturing process to Allergan (for the product now known as Botox). It manufactured the first human grade lipopolysaccaride product for clinical trial use, commissioned by the NIH. It was one of the first companies worldwide to manufacture live microbiomes for clinical trial starting in 2012.