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Vishva Dixit
Vishva Mitra Dixit (born ) is a Kenyan-American physician who is currently Vice President and Senior Fellow of Physiological Chemistry and Research Biology at Genentech. Early life and education Vishva Dixit was born in Kenya in 1956. His parents were both physicians, working for the British colonial authorities. Dixit was interested in science from an early age, and his parents encouraged him to pursue a career in medicine. He graduated in 1980 from the University of Nairobi with a Bachelor of Medicine and Bachelor of Surgery, becoming a medical doctor. Career Academia Following medical school, Dixit completed a residency in the Department of Pathology at the Washington University School of Medicine. He decided to pursue pathology because he had been interested in the process of death since childhood and pathology offered more research options across medical disciplines. Encouraged to train in research as part of the residency program, Dixit found a position in the l ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Molecular Biology
Molecular biology is a branch of biology that seeks to understand the molecule, molecular basis of biological activity in and between Cell (biology), cells, including biomolecule, biomolecular synthesis, modification, mechanisms, and interactions. Though cells and other microscopic structures had been observed in living organisms as early as the 18th century, a detailed understanding of the mechanisms and interactions governing their behavior did not emerge until the 20th century, when technologies used in physics and chemistry had advanced sufficiently to permit their application in the biological sciences. The term 'molecular biology' was first used in 1945 by the English physicist William Astbury, who described it as an approach focused on discerning the underpinnings of biological phenomena—i.e. uncovering the physical and chemical structures and properties of biological molecules, as well as their interactions with other molecules and how these interactions explain observ ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
MYD88
Myeloid differentiation primary response 88 (MYD88) is a protein that, in humans, is encoded by the ''MYD88'' gene. originally discovered in the laboratory of Dan A. Liebermann (Lord et al. Oncogene 1990) as a Myeloid differentiation primary response gene. Function The MYD88 gene provides instructions for making a protein involved in signaling within immune cells. The MyD88 protein acts as an adapter, connecting proteins that receive signals from outside the cell to the proteins that relay signals inside the cell. In innate immunity, the MyD88 plays a pivotal role in immune cell activation through Toll-like receptor Toll-like receptors (TLRs) are a class of proteins that play a key role in the innate immune system. They are single-pass membrane protein, single-spanning receptor (biochemistry), receptors usually expressed on sentinel cells such as macrophages ...s (TLRs), which belong to large group of pattern recognition receptors (PRR). In general, these receptors sense ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RIPK3
Receptor-interacting serine/threonine-protein kinase 3 is an enzyme that is encoded by the ''RIPK3'' gene in humans. The product of this gene is a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases. It contains a C-terminal domain unique from other RIP family members. The encoded protein is predominantly localized to the cytoplasm, and can undergo nucleocytoplasmic shuttling dependent on novel nuclear localization and export signals. It is a component of the tumor necrosis factor (TNF) receptor-I signaling complex, and can induce necroptosis by interaction with RIPK1 and MLKL in a protein complex termed the necrosome. Interactions between RIPK1 and RIPK3 also form a necrosome, which triggers apoptosis. Interactions RIPK3 has been shown to interact with RIPK1 to form an amyloid spine The RIP Homotypic Interaction Motifs (RHIM) of RIPK3 allows it to form a necrosome with RIPK1. This interaction makes heterotypic β sheets, which bind ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RIPK2
Receptor-interacting serine/threonine-protein kinase 2 is an enzyme that in humans is encoded by the ''RIPK2'' gene. This gene encodes a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases. The encoded protein contains a C-terminal caspase recruitment domain (CARD), and is a component of signaling complexes in both the innate and adaptive immune pathways. It is a potent activator of NF-κB and inducer of apoptosis in response to various stimuli. Interactions RIPK2 has been shown to interact with BIRC2 Baculoviral IAP repeat-containing protein 2 (also known as cIAP1) is a protein that in humans is encoded by the ''BIRC2'' gene. Function cIAP1 is a member of the Inhibitor of apoptosis, Inhibitor of Apoptosis family that inhibit apoptosis by .... References Further reading * * * * * * * * * * * * * * * * * * * {{gene-8-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sanford Burnham Prebys Medical Discovery Institute
Sanford Burnham Prebys is a nonprofit biomedical research institute located in La Jolla, California. The institute conducts basic research and translational research focused on human disease. Research at the institute focuses on cancer, neurodegeneration, diabetes, infectious diseases, inflammatory diseases, and Pediatrics, pediatric conditions. Additional areas include stem cell research and drug discovery technologies. Sanford Burnham Prebys includes a National Cancer Institute-designated Cancer Center and other specialized programs in genomics, stem cell research, and pediatric health. The institute employs more than 500 scientists, staff, and trainees, and collaborates with academic and industry partners. History Sanford Burnham Prebys originated in 1976 as the La Jolla Cancer Research Foundation, founded by William H. Fishman, Dr. William H. Fishman and Lillian Waterman Fishman after his retirement from Tufts University School of Medicine. The institute was renamed the B ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phosphorylation
In biochemistry, phosphorylation is described as the "transfer of a phosphate group" from a donor to an acceptor. A common phosphorylating agent (phosphate donor) is ATP and a common family of acceptor are alcohols: : This equation can be written in several ways that are nearly equivalent that describe the behaviors of various protonated states of ATP, ADP, and the phosphorylated product. As is clear from the equation, a phosphate group per se is not transferred, but a phosphoryl group (PO3-). Phosphoryl is an electrophile. This process and its inverse, dephosphorylation, are common in biology. Text was copied from this source, which is available under a Creative Commons Attribution 4.0 International License. Protein phosphorylation often activates (or deactivates) many enzymes. During respiration Phosphorylation is essential to the processes of both anaerobic and aerobic respiration, which involve the production of adenosine triphosphate (ATP), the "high-energy" exc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ion Channel
Ion channels are pore-forming membrane proteins that allow ions to pass through the channel pore. Their functions include establishing a resting membrane potential, shaping action potentials and other electrical signals by Gating (electrophysiology), gating the flow of ions across the cell membrane, controlling the flow of ions across secretion, secretory and epithelial cells, and regulating cell (biology), cell volume. Ion channels are present in the membranes of all cells. Ion channels are one of the two classes of ionophore, ionophoric proteins, the other being ion transporters. The study of ion channels often involves biophysics, electrophysiology, and pharmacology, while using techniques including voltage clamp, patch clamp, immunohistochemistry, X-ray crystallography, fluoroscopy, and RT-PCR. Their classification as molecules is referred to as channelomics. Basic features There are two distinctive features of ion channels that differentiate them from other types of ion ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cell Surface Receptor
Cell surface receptors (membrane receptors, transmembrane receptors) are receptors that are embedded in the plasma membrane of cells. They act in cell signaling by receiving (binding to) extracellular molecules. They are specialized integral membrane proteins that allow communication between the cell and the extracellular space. The extracellular molecules may be hormones, neurotransmitters, cytokines, growth factors, cell adhesion molecules, or nutrients; they react with the receptor to induce changes in the metabolism and activity of a cell. In the process of signal transduction, ligand binding affects a cascading chemical change through the cell membrane. Structure and mechanism Many membrane receptors are transmembrane proteins. There are various kinds, including glycoproteins and lipoproteins. Hundreds of different receptors are known and many more have yet to be studied. Transmembrane receptors are typically classified based on their tertiary (three-dimens ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protease
A protease (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalysis, catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks Covalent bond, bonds. Proteases are involved in numerous biological pathways, including Digestion#Protein digestion, digestion of ingested proteins, protein catabolism (breakdown of old proteins), and cell signaling. In the absence of functional accelerants, proteolysis would be very slow, taking hundreds of years. Proteases can be found in all forms of life and viruses. They have independently convergent evolution, evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Classification Based on catalytic residue Proteases can be classified into seven broad ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cell Death
Cell death is the event of a biological cell ceasing to carry out its functions. This may be the result of the natural process of old cells dying and being replaced by new ones, as in programmed cell death, or may result from factors such as diseases, localized injury, or the death of the organism of which the cells are part. Apoptosis or Type I cell-death, and Autophagy (cellular), autophagy or Type II cell-death are both forms of programmed cell death, while necrosis is a non-physiological process that occurs as a result of infection or injury. The term "cell necrobiology" has been used to describe the life processes associated with morphological, biochemical, and molecular changes which predispose, precede, and accompany cell death, as well as the consequences and tissue response to cell death. The word is derived from the Greek language, Greek νεκρό meaning "death", βìο meaning "life", and logos, λόγος meaning "the study of". The term was initially coined to bro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tumor Necrosis Factor
Tumor necrosis factor (TNF), formerly known as TNF-α, is a chemical messenger produced by the immune system that induces inflammation. TNF is produced primarily by activated macrophages, and induces inflammation by binding to its receptors on other cells. It is a member of the tumor necrosis factor superfamily, a family of transmembrane proteins that are cytokines, chemical messengers of the immune system. Excessive production of TNF plays a critical role in several inflammatory diseases, and TNF-blocking drugs are often employed to treat these diseases. TNF is produced primarily by macrophages but is also produced in several other cell types, such as T cells, B cells, dendritic cells, and mast cells. It is produced rapidly in response to pathogens, cytokines, and environmental stressors. TNF is initially produced as a type II transmembrane protein (tmTNF), which is then cleaved by TNF alpha converting enzyme (TACE) into a soluble form (sTNF) and secreted from the cell ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Scientific American
''Scientific American'', informally abbreviated ''SciAm'' or sometimes ''SA'', is an American popular science magazine. Many scientists, including Albert Einstein and Nikola Tesla, have contributed articles to it, with more than 150 Nobel Prize-winners being featured since its inception. In print since 1845, it is the oldest continuously published magazine in the United States. ''Scientific American'' is owned by Springer Nature, which is a subsidiary of Holtzbrinck Publishing Group. History ''Scientific American'' was founded by inventor and publisher Rufus Porter (painter), Rufus Porter in 1845 as a four-page weekly newspaper. The first issue of the large-format New York City newspaper was released on August 28, 1845. Throughout its early years, much emphasis was placed on reports of what was going on at the United States Patent and Trademark Office, U.S. Patent Office. It also reported on a broad range of inventions including perpetual motion machines, an 1860 devi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
