The SRC Homology 3 Domain is a small protein domain of about 60 amino acid residues. Initially, SH3 was described as a conserved sequence in the viral adaptor protein v-Crk. This domain is also present in the molecules of phospholipase and several cytoplasmic tyrosine kinases such as Abl and Src. It has also been identified in several other protein families such as: PI3 Kinase, Ras GTPase-activating protein, CDC24 and cdc25. SH3 domains are found in proteins of signaling pathways regulating the cytoskeleton, the Ras protein, and the Src kinase and many others. The SH3 proteins interact with adaptor proteins and tyrosine kinases. Interacting with tyrosine kinases, SH3 proteins usually bind far away from the active site. Approximately 300 SH3 domains are found in proteins encoded in the human genome. In addition to that, the SH3 domain was responsible for controlling protein-protein interactions in the signal transduction pathways and regulating the interactions of proteins involved in the cytoplasmic signaling.
Bacteriophage T7 is a bacteriophage, a virus that infects bacteria. It infects most strains of Escherichia coli and relies on these hosts to propagate. Bacteriophage T7 has a lytic life cycle, meaning that it destroys the cell it infects. It also possesses several properties that make it an ideal phage for experimentation: its purification and concentration have produced consistent values in chemical analyses; it can be rendered noninfectious by exposure to UV light; and it can be used in phage display to clone RNA binding proteins.
Mitochondrial carriers are proteins from solute carrier family 25 which transfer molecules across the membranes of the mitochondria. Mitochondrial carriers are also classified in the Transporter Classification Database. The Mitochondrial Carrier (MC) Superfamily has been expanded to include both the original Mitochondrial Carrier (MC) family and the Mitochondrial Inner/Outer Membrane Fusion (MMF) family.
EF-G is a prokaryotic elongation factor involved in protein translation. As a GTPase, EF-G catalyzes the movement (translocation) of transfer RNA (tRNA) and messenger RNA (mRNA) through the ribosome.
Mutation Frequency Decline (mfd) is the gene which encodes the protein Mfd. Mfd functions in transcription-coupled repair to remove a stalled RNA polymerase that has encountered DNA damage and is unable to continue translocating.
In biochemistry, a protein dimer is a macromolecular complex formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word dimer has roots meaning "two parts", di- + -mer. A protein dimer is a type of protein quaternary structure.
Protein moonlighting is a phenomenon by which a protein can perform more than one function. Ancestral moonlighting proteins originally possessed a single function but through evolution, acquired additional functions. Many proteins that moonlight are enzymes; others are receptors, ion channels or chaperones. The most common primary function of moonlighting proteins is enzymatic catalysis, but these enzymes have acquired secondary non-enzymatic roles. Some examples of functions of moonlighting proteins secondary to catalysis include signal transduction, transcriptional regulation, apoptosis, motility, and structural.
Ruth Lehmann is a developmental and cell biologist. She is the Director of the Whitehead Institute for Biomedical Research, succeeding David Page. She previously was affiliated with the New York University School of Medicine, where she was the Director of the Skirball Institute of Biomolecular Medicine, the Laura and Isaac Perlmutter Professor of Cell Biology, and the Chair of the Department of Cell Biology. Her research focuses on germ cells and embryogenesis.
The ATP:ADP Antiporter (AAA) Family is a member of the major facilitator superfamily. Members of the AAA family have been sequenced from bacteria and plants.
Pseudoenzymes are variants of enzymes that are catalytically-deficient, meaning that they perform little or no enzyme catalysis. They are believed to be represented in all major enzyme families in the kingdoms of life, where they have important signaling and metabolic functions, many of which are only now coming to light. Pseudoenzymes are becoming increasingly important to analyse, especially as the bioinformatic analysis of genomes reveals their ubiquity. Their important regulatory and sometimes disease-associated functions in metabolic and signalling pathways are also shedding new light on the non-catalytic functions of active enzymes, of moonlighting proteins, the re-purposing of proteins in distinct cellular roles. They are also suggesting new ways to target and interpret cellular signalling mechanisms using small molecules and drugs. The most intensively analyzed, and certainly the best understood pseudoenzymes in terms of cellular signalling functions are probably the pseudokinases, the pseudoproteases and the pseudophosphatases. Recently, the pseudo-deubiquitylases have also begun to gain prominence.
Mary Bernadette Kennedy is an American biochemist and neuroscientist. She is a member of the American Academy of Arts and Sciences, and is the Allen and Lenabelle Davis Professor of Biology at the California Institute of Technology, where she has been a member of the faculty since 1981. Her research focuses on the molecular mechanisms of synaptic plasticity, the process underlying formation of memory in the central nervous system. Her lab uses biochemical and molecular biological methods to study the protein machinery within a structure called the postsynaptic density. Kennedy has published over 100 papers with over 20,000 total citations.
Paul Hargrave is an American biochemist whose laboratory work established key features of the structure of rhodopsin.
Katherine A. Jones is a professor of regulatory biology and the Edwin K. Hunter Chair at the Salk Institute for Biological Studies. She uses proteomics to study transcription elongation and molecular biology to understand protein coordination. Jones identified elongation factors, a class of proteins which are important in viral gene expression.
Kim Orth is a microbiologist and biochemist. She is currently the Earl A. Forsythe chair in biomedical science and professor of molecular biology and biochemistry at UT Southwestern. She is a Howard Hughes Medical Institute investigator and a member of the National Academy of Sciences. Her research focuses on bacterial pathogenesis.
Anne Ephrussi is a French developmental and molecular biologist. Her research is focused on the study of post-transcriptional regulations such as mRNA localization and translation control in molecular biology as well as the establishment of polarity axes in cell and developmental biology. She is head of the Developmental Biology Unit and director of the EMBL International Centre for Advanced Training (EICAT) program at the European Molecular Biology Laboratory (EMBL).
Deborah Beth Zamble was a Canadian chemist and Canada Research Chair in Biological Chemistry at the University of Toronto. Her research considered how bacteria processed metal nutrients.
Yimon Aye is an American chemist and molecular biologist. Currently she is an Associate Professor of chemistry at EPFL.
Richard B. Gaynor is an American physician specializing in hematology-oncology, educator, drug developer, and business executive. He served as an Associate Professor of Medicine at UCLA School of Medicine for nearly a decade, and subsequently as an endowed Professor of Medicine and Microbiology at the University of Texas Southwestern Medical School prior to joining the pharmaceutical industry in 2002. His research on NF-κB, IκB kinase, and other mechanisms regulating viral and cellular gene expression has been covered in leading subject reviews. He has been a top executive at several pharmaceutical companies, with respect to the development and clinical testing of novel anticancer drugs and cell therapies. For over a decade and a half, he worked at Eli Lilly and Company, where he became the Senior Vice President of Oncology Clinical Development and Medical Affairs in 2013. Gaynor was President of R&D at Neon Therapeutics from 2016 to 2020, when he became the President of BioNTech US, both pharmaceutical companies headquartered in Cambridge, MA. His honors include being elected a member of the American Society for Clinical Investigation, and the Association of American Physicians.
Linda Columbus is an American chemist who is Professor of Chemistry and Molecular Physiology at the University of Virginia. Her research considers the structure-function properties of membrane proteins.
