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Brenda Schulman
Brenda Schulman is an American biochemist and structural biologist who is a Director at the Max Planck Institute of Biochemistry, Martinsried, Bavaria. Schulman's research interests focus on a class of proteins known as ubiquitin-like proteins. Education and academic career Schulman is a native of Tucson, Arizona. Schulman received her bachelor's degree in biology from Johns Hopkins University in 1989 and her PhD in biology from the Massachusetts Institute of Technology in 1996, advised by Peter S. Kim. She then worked as a postdoctoral fellow with Ed Harlow at the Massachusetts General Hospital Cancer Center and later with Nikola Pavletich at the Memorial Sloan Kettering Cancer Center. Schulman joined the faculty at the St. Jude Children's Research Hospital in 2001 and assumed the Joseph Simone Endowed Chair of Basic Research there in 2014. She became a Howard Hughes Medical Institute Investigator in 2005. She was elected to the American Academy of Arts and Sciences in 2012 an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tucson, Arizona
, "(at the) base of the black ill , nicknames = "The Old Pueblo", "Optics Valley", "America's biggest small town" , image_map = , mapsize = 260px , map_caption = Interactive map outlining Tucson , image_map1 = File:Pima County Incorporated and Unincorporated areas Tucson highlighted.svg , mapsize1 = 250px , map_caption1 = Location within Pima County , pushpin_label = Tucson , pushpin_map = USA Arizona#USA , pushpin_map_caption = Location within Arizona##Location within the United States , subdivision_type = Country , subdivision_type1 = State , subdivision_type2 = County , subdivision_name = United States , subdivision_name1 = Arizona , subdivision_name2 = Pima , established_title = Founded , established_date = August 20, 1775 , established_title1 = Incorporated , e ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
National Academy Of Sciences
The National Academy of Sciences (NAS) is a United States nonprofit, non-governmental organization. NAS is part of the National Academies of Sciences, Engineering, and Medicine, along with the National Academy of Engineering (NAE) and the National Academy of Medicine (NAM). As a national academy, new members of the organization are elected annually by current members, based on their distinguished and continuing achievements in original research. Election to the National Academy is one of the highest honors in the scientific field. Members of the National Academy of Sciences serve '' pro bono'' as "advisers to the nation" on science, engineering, and medicine. The group holds a congressional charter under Title 36 of the United States Code. Founded in 1863 as a result of an Act of Congress that was approved by Abraham Lincoln, the NAS is charged with "providing independent, objective advice to the nation on matters related to science and technology. ... to provide scien ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
1967 Births
Events January * January 1 – Canada begins a year-long celebration of the 100th anniversary of Confederation, featuring the Expo 67 World's Fair. * January 5 ** Spain and Romania sign an agreement in Paris, establishing full consular and commercial relations (not diplomatic ones). ** Charlie Chaplin launches his last film, ''A Countess from Hong Kong'', in the UK. * January 6 – Vietnam War: United States Marine Corps, USMC and Army of the Republic of Vietnam, ARVN troops launch ''Operation Deckhouse Five'' in the Mekong Delta. * January 8 – Vietnam War: Operation Cedar Falls starts. * January 13 – A military coup occurs in Togo under the leadership of Étienne Eyadema. * January 14 – The Human Be-In takes place in Golden Gate Park, San Francisco; the event sets the stage for the Summer of Love. * January 15 ** Louis Leakey announces the discovery of pre-human fossils in Kenya; he names the species ''Proconsul nyanzae, Kenyapithecus africanus''. ** American footbal ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Louis-Jeantet Prize For Medicine
Established in 1986, the Louis-Jeantet Prizes are funded by the ''Fondation Louis-Jeantet'' and awarded each year to experienced researchers who have distinguished themselves in the field of biomedical research in one of the member states of the Council of Europe. They are not intended solely as the recognition of work that has been completed, but also to encourage the continuation of innovative research projects. The prizes are awarded to fully active researchers whose scientific efforts are focused on biomedical research. When the research being recognised is close to practical applications for combating illnesses affecting humankind, one of the Louis-Jeantet Prizes converts into a Jeantet-Collen Prize for Translational Medicine, supported by generous donations from the Désiré Collen Stichting. The particular research domains in which prizes have been awarded are physiology, biophysics, structural biology, biochemistry, cellular and molecular biology, developmental biology ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
German Academy Of Sciences Leopoldina
The German National Academy of Sciences Leopoldina (german: Deutsche Akademie der Naturforscher Leopoldina – Nationale Akademie der Wissenschaften), short Leopoldina, is the national academy of Germany, and is located in Halle (Saale). Founded on January 1, 1652, based on academic models in Italy, it was originally named the ''Academia Naturae Curiosorum'' until 1687 when Emperor Leopold I raised it to an academy and named it after himself. It was since known under the German name ''Deutsche Akademie der Naturforscher Leopoldina'' until 2007, when it was declared to be Germany's National Academy of Sciences. History ' The Leopoldina was founded in the imperial city of Schweinfurt on 1 January 1652 under the Latin name sometimes translated into English as "Academy of the Curious as to Nature." It was founded by four local physicians- Johann Laurentius Bausch, the first president of the society, Johann Michael Fehr, Georg Balthasar Metzger, and Georg Balthasar Wohlfarth; and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gottfried Wilhelm Leibniz Prize
The Gottfried Wilhelm Leibniz Prize (german: link=no, Förderpreis für deutsche Wissenschaftler im Gottfried Wilhelm Leibniz-Programm der Deutschen Forschungsgemeinschaft), in short Leibniz Prize, is awarded by the German Research Foundation to "exceptional scientists and academics for their outstanding achievements in the field of research". Since 1986, up to ten prizes are awarded annually to individuals or research groups working at a research institution in Germany or at a German research institution abroad. It is considered the most important research award in Germany. The prize is named after the German polymath and philosopher Gottfried Wilhelm Leibniz (1646–1716). It is one of the highest endowed research prizes in Germany with a maximum of €2.5 million per award. Past prize winners include Stefan Hell (2008), Gerd Faltings (1996), Peter Gruss (1994), Svante Pääbo (1992), Theodor W. Hänsch (1989), Erwin Neher (1987), Bert Sakmann (1987), Jürgen Habermas (1986), ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ernst Jung Prize
The Ernst Jung Prize is a prize awarded annually for excellence in biomedical sciences. The Ernst Jung Foundation, funded by Hamburg merchant Ernst Jung in 1967, has awarded the Ernst Jung Prize in Medicine, now €300,000, since 1976, and the lifetime achievement Ernst Jung Gold Medal for Medicine since 1990. Ernst Jung Prize for Medicine SourceJung Foundation *1976: Donald Henderson and Lorenz Zimmerman *1977: and John B. West *1979: Karl Lennert and *1980: , Alan Parks and *1981: David E. Kuhl *1982: Hartmut Wekerle and Rolf M. Zinkernagel *1983: and Richard Lower *1984: , Werner Franke and Klaus Weber *1985: Hendrik Coenraad Hemker, Rudolf Pichlmayr and Peter K. Vogt *1986: Albrecht Fleckenstein *1987: Peter Richardson and *1988: Helmut Sies and Charles Weissmann *1989: and Jon van Rood *1990: Gerhard Giebisch and *1991: David Ho and *1992: Roy Yorke Calne and *1993: Charles A. Dinarello and Robert Machemer *1994: and Wolf Singer *1995: Anthony Fauci and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
E3 Ubiquitin Ligase
A ubiquitin ligase (also called an E3 ubiquitin ligase) is a protein that recruits an E2 ubiquitin-conjugating enzyme that has been loaded with ubiquitin, recognizes a protein substrate, and assists or directly catalyzes the transfer of ubiquitin from the E2 to the protein substrate. In simple and more general terms, the ligase enables movement of ubiquitin from a ubiquitin carrier to another thing (the substrate) by some mechanism. The ubiquitin, once it reaches its destination, ends up being attached by an isopeptide bond to a lysine residue, which is part of the target protein. E3 ligases interact with both the target protein and the E2 enzyme, and so impart substrate specificity to the E2. Commonly, E3s polyubiquitinate their substrate with Lys48-linked chains of ubiquitin, targeting the substrate for destruction by the proteasome. However, many other types of linkages are possible and alter a protein's activity, interactions, or localization. Ubiquitination by E3 ligases regu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Substrate (biochemistry)
In chemistry, the term substrate is highly context-dependent. Broadly speaking, it can refer either to a chemical species being observed in a chemical reaction, or to a surface on which other chemical reactions or microscopy are performed. In the former sense, a reagent is added to the ''substrate'' to generate a product through a chemical reaction. The term is used in a similar sense in synthetic and organic chemistry, where the substrate is the chemical of interest that is being modified. In biochemistry, an enzyme substrate is the material upon which an enzyme acts. When referring to Le Chatelier's principle, the substrate is the reagent whose concentration is changed. ;Spontaneous reaction : :*Where S is substrate and P is product. ;Catalysed reaction : :*Where S is substrate, P is product and C is catalyst. In the latter sense, it may refer to a surface on which other chemical reactions are performed or play a supporting role in a variety of spectroscopic and microscop ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
NEDD8
NEDD8 is a protein that in humans is encoded by the ''NEDD8'' gene. (in ''saccharomyces cerevisiae'' this protein is known as Rub1) This ubiquitin-like (UBL) protein becomes covalently conjugated to a limited number of cellular proteins, in a process called NEDDylation similar to ubiquitination. Human NEDD8 shares 60% amino acid sequence identity to ubiquitin. The primary known substrates of NEDD8 modification are the cullin subunits of cullin-based E3 ubiquitin ligases, which are active only when NEDDylated. Their NEDDylation is critical for the recruitment of E2 to the ligase complex, thus facilitating ubiquitin conjugation. NEDD8 modification has therefore been implicated in cell cycle progression and cytoskeletal regulation. Activation and conjugation As with ubiquitin and SUMO, NEDD8 is conjugated to cellular proteins after its C-terminal tail is processed. The NEDD8 activating E1 enzyme is a heterodimer composed of APPBP1 and UBA3 subunits. The APPBP1/UBA3 enzyme has homolog ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ubiquitin
Ubiquitin is a small (8.6 kDa) regulatory protein found in most tissues of eukaryotic organisms, i.e., it is found ''ubiquitously''. It was discovered in 1975 by Gideon Goldstein and further characterized throughout the late 1970s and 1980s. Four genes in the human genome code for ubiquitin: UBB, UBC, UBA52 and RPS27A. The addition of ubiquitin to a substrate protein is called ubiquitylation (or, alternatively, ubiquitination or ubiquitinylation). Ubiquitylation affects proteins in many ways: it can mark them for degradation via the proteasome, alter their cellular location, affect their activity, and promote or prevent protein interactions. Ubiquitylation involves three main steps: activation, conjugation, and ligation, performed by ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin ligases (E3s), respectively. The result of this sequential cascade is to bind ubiquitin to lysine residues on the protein substrate via an isopeptide bond, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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