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Jennifer L. Martin
Professor Jennifer Louise "Jenny" Martin is an Australian scientist, academic, and was recently the Deputy Vice-Chancellor (Research and Innovation) at the University of Wollongong, in New South Wales. She is a former Director of thGriffith Institute for Drug Discoveryat Griffith University. and a former Australian Research Council Laureate Fellow at the Institute for Molecular Bioscience, University of Queensland. Her research expertise lies in the areas of structural biology, protein crystallography, protein interactions and their applications in drug design and discovery. Education Martin completed a Bachelor of Pharmacy at the Victorian College of Pharmacy in Melbourne from 1979–1981, receiving the Gold Medal for the best student in the B Pharm course. After spending a year as a trainee pharmacist, she completed a Masters in Pharmacy, supervised by Professor Peter Andrews, on the application of computational chemistry to opioid analgesics, which piqued her interes ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Drug Discovery
In the fields of medicine, biotechnology and pharmacology, drug discovery is the process by which new candidate medications are discovered. Historically, drugs were discovered by identifying the active ingredient from traditional remedies or by serendipitous discovery, as with penicillin. More recently, chemical libraries of synthetic small molecules, natural products or extracts were screened in intact cells or whole organisms to identify substances that had a desirable therapeutic effect in a process known as classical pharmacology. After sequencing of the human genome allowed rapid cloning and synthesis of large quantities of purified proteins, it has become common practice to use high throughput screening of large compounds libraries against isolated biological targets which are hypothesized to be disease-modifying in a process known as reverse pharmacology. Hits from these screens are then tested in cells and then in animals for efficacy. Modern drug discovery i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
National Health And Medical Research Council
The National Health and Medical Research Council (NHMRC) is the main statutory authority of the Australian Government responsible for medical research. It was the eighth largest research funding body in the world in 2016, and NHMRC-funded research is globally recognised for its high quality. Around 45% of all Australian medical research from 200812 was funded by the federal government, through the NHMRC. As an independent arm of the Department of Health, the NHMRC funds high quality health and medical research, builds research capability in Australia, support the translation of health and medical research into better health outcomes, and promote the ethics and integrity in research. Non-health research is funded by the Australian Research Council. Activities The National Health and Medical Research Council Act 1992' provides for NHMRC to pursue activities designed to: * raise the standard of individual and public health throughout Australia * foster the development of consi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DsbA Crystal
DsbA is a bacterial thiol disulfide oxidoreductase (TDOR). DsbA is a key component of the Dsb (disulfide bond) family of enzymes. DsbA catalyzes intrachain disulfide bond formation as peptides emerge into the cell's periplasm. Structurally, DsbA contains a thioredoxin domain with an inserted helical domain of unknown function. Like other thioredoxin-based enzymes, DsbA's catalytic site is a CXXC motif (CPHC in ''E. coli'' DsbA). The pair of cysteines may be oxidized (forming an internal disulfide) or reduced (as free thiols), and thus allows for oxidoreductase activity by serving as an electron pair donor or acceptor, depending on oxidation state. This reaction generally proceeds through a mixed-disulfide intermediate, in which a cysteine from the enzyme forms a bond to a cysteine on the substrate. DsbA is responsible for introducing disulfide bonds into nascent proteins. In equivalent terms, it catalyzes the oxidation of a pair of cysteine residues on the substrate protein. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nature (journal)
''Nature'' is a British weekly scientific journal founded and based in London, England. As a multidisciplinary publication, ''Nature'' features peer-reviewed research from a variety of academic disciplines, mainly in science and technology. It has core editorial offices across the United States, continental Europe, and Asia under the international scientific publishing company Springer Nature. ''Nature'' was one of the world's most cited scientific journals by the Science Edition of the 2019 '' Journal Citation Reports'' (with an ascribed impact factor of 42.778), making it one of the world's most-read and most prestigious academic journals. , it claimed an online readership of about three million unique readers per month. Founded in autumn 1869, ''Nature'' was first circulated by Norman Lockyer and Alexander Macmillan as a public forum for scientific innovations. The mid-20th century facilitated an editorial expansion for the journal; ''Nature'' redoubled its efforts in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DsbA
DsbA is a bacterial thiol disulfide oxidoreductase (TDOR). DsbA is a key component of the Dsb (disulfide bond) family of enzymes. DsbA catalyzes intrachain disulfide bond formation as peptides emerge into the cell's periplasm. Structurally, DsbA contains a thioredoxin domain with an inserted helical domain of unknown function. Like other thioredoxin-based enzymes, DsbA's catalytic site is a CXXC motif (CPHC in ''E. coli'' DsbA). The pair of cysteines may be oxidized (forming an internal disulfide) or reduced (as free thiols), and thus allows for oxidoreductase activity by serving as an electron pair donor or acceptor, depending on oxidation state. This reaction generally proceeds through a mixed-disulfide intermediate, in which a cysteine from the enzyme forms a bond to a cysteine on the substrate. DsbA is responsible for introducing disulfide bonds into nascent proteins. In equivalent terms, it catalyzes the oxidation of a pair of cysteine residues on the substrate protein. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Escherichia Coli
''Escherichia coli'' (),Wells, J. C. (2000) Longman Pronunciation Dictionary. Harlow ngland Pearson Education Ltd. also known as ''E. coli'' (), is a Gram-negative, facultative anaerobic, rod-shaped, coliform bacterium of the genus '' Escherichia'' that is commonly found in the lower intestine of warm-blooded organisms. Most ''E. coli'' strains are harmless, but some serotypes ( EPEC, ETEC etc.) can cause serious food poisoning in their hosts, and are occasionally responsible for food contamination incidents that prompt product recalls. Most strains do not cause disease in humans and are part of the normal microbiota of the gut; such strains are harmless or even beneficial to humans (although these strains tend to be less studied than the pathogenic ones). For example, some strains of ''E. coli'' benefit their hosts by producing vitamin K2 or by preventing the colonization of the intestine by pathogenic bacteria. These mutually beneficial relationships between ''E. co ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Disulfide Bond
In biochemistry, a disulfide (or disulphide in British English) refers to a functional group with the structure . The linkage is also called an SS-bond or sometimes a disulfide bridge and is usually derived by the coupling of two thiol groups. In biology, disulfide bridges formed between thiol groups in two cysteine residues are an important component of the secondary and tertiary structure of proteins. '' Persulfide'' usually refers to compounds. In inorganic chemistry disulfide usually refers to the corresponding anion (−S−S−). Organic disulfides Symmetrical disulfides are compounds of the formula . Most disulfides encountered in organo sulfur chemistry are symmetrical disulfides. Unsymmetrical disulfides (also called heterodisulfides) are compounds of the formula . They are less common in organic chemistry, but most disulfides in nature are unsymmetrical. Properties The disulfide bonds are strong, with a typical bond dissociation energy of 60 kcal/mol ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
John Kuriyan
John Kuriyan is the Dean of Basic Sciences and a Professor of Biochemistry at Vanderbilt University School of Medicine. He was formerly the Chancellor's Professor at the University of California, Berkeley in the departments of Molecular and Cell Biology (MCB) and Chemistry, a Faculty Scientist in Berkeley Lab's Physical Biosciences Division, and a Howard Hughes Medical Institute investigator. He is a member of the National Academy of Sciences and he has also been on the Life Sciences jury for the Infosys Prize in 2009, 2019 and 2020. Education Kuriyan received his B.S. in chemistry from Juniata College in Pennsylvania, followed by his PhD in physical chemistry at the Massachusetts Institute of Technology supervised by Gregory Petsko and Martin Karplus. Research and career Kuriyan did postdoctoral research work for one year supervised by Karplus at Harvard before becoming an assistant professor at the Rockefeller University. Kuriyan's laboratory studies the structure and mecha ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycogen Phosphorylase
Glycogen phosphorylase is one of the phosphorylase enzymes (). Glycogen phosphorylase catalyzes the rate-limiting step in glycogenolysis in animals by releasing glucose-1-phosphate from the terminal alpha-1,4-glycosidic bond. Glycogen phosphorylase is also studied as a model protein regulated by both reversible phosphorylation and allosteric effects. Mechanism Glycogen phosphorylase breaks up glycogen into glucose subunits (see also figure below): (α-1,4 glycogen chain)n + Pi ⇌ (α-1,4 glycogen chain)n-1 + α-D-glucose-1-phosphate. Glycogen is left with one fewer glucose molecule, and the free glucose molecule is in the form of glucose-1-phosphate. In order to be used for metabolism, it must be converted to glucose-6-phosphate by the enzyme phosphoglucomutase. Although the reaction is reversible in vitro, within the cell the enzyme only works in the forward direction as shown below because the concentration of inorganic phosphate is much higher than that of gluco ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Royal Commission For The Exhibition Of 1851
The Royal Commission for the Exhibition of 1851 is an institution founded in 1850 to administer the international exhibition of 1851, officially called the Great Exhibition of the Works of Industry of all Nations. The Great Exhibition was held in The Crystal Palace in Hyde Park London, England. The enormous building was designed by Joseph Paxton for the Exhibition and construction was supervised by William Cubitt using a cast iron space frame for the glass panes, with wooden beams for flooring. The founding President of the Commission was Prince Albert of Saxe-Coburg and Gotha and its chief administrator was Henry Cole. The current President is Anne, Princess Royal. The exhibition was a great popular and financial success, and made a huge surplus of 186,000 pounds,or about 22 million pounds in today's money). An unusual decision was made to maintain the Royal Commission as a permanent administrative body and to use the profits for charitable purposes. Its revised Charter ch ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
