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ADAM9
Disintegrin and metalloproteinase domain-containing protein 9 is an enzyme that in humans is encoded by the ''ADAM9'' gene. Function This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. The protein encoded by this gene interacts with SH3 domain-containing proteins, binds mitotic arrest deficient 2 beta protein, and is also involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. Two alternative splice variants have been identified, encoding distinct isoforms. Interactions ADAM9 has been shown to interact with: * MAD2L2, * SH3GL2, and * SNX9 Sorting nexin-9 is a protein that in humans is encoded by the ''SNX9'' gene. ...
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A Disintegrin And Metalloprotease
ADAMs (short for a disintegrin and metalloproteinase) are a family of single-pass transmembrane and secreted metalloendopeptidases. All ADAMs are characterized by a particular domain organization featuring a pro-domain, a metalloprotease, a disintegrin, a cysteine-rich, an epidermal-growth factor like and a transmembrane domain, as well as a C-terminal cytoplasmic tail. Nonetheless, not all human ADAMs have a functional protease domain, which indicates that their biological function mainly depends on protein–protein interactions. Those ADAMs which are active proteases are classified as sheddases because they cut off or shed extracellular portions of transmembrane proteins. For example, ADAM10 can cut off part of the HER2 receptor, thereby activating it. ADAM genes are found in animals, choanoflagellates, fungi and some groups of green algae. Most green algae and all land plants likely lost ADAM proteins. ADAMs are categorized under the enzyme group, and in the MEROPS peptidas ...
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MAD2L2
Mitotic spindle assembly checkpoint protein MAD2B is a protein that in humans is encoded by the ''MAD2L2'' gene. Function MAD2L2 is a component of the mitotic spindle assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. MAD2L2 is a homolog of MAD2L1. Interactions MAD2L2 has been shown to interact with: * ADAM9, * MAD2L1, * REV1, and * REV3L Protein reversionless 3-like (REV3L) also known as DNA polymerase zeta catalytic subunit (POLZ) is an enzyme that in humans is encoded by the ''REV3L'' gene. The Rev3 subunit interacts with Rev7 to form Pol ζ, a B family polymerase. Pol ζ lacks .... References Further reading

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SH3GL2
Endophilin-A1 is a protein that in humans is encoded by the ''SH3GL2'' gene. Interactions SH3GL2 has been shown to interact with DNM1, Amphiphysin, ADAM9, SH3KBP1 and ADAM15 Disintegrin and metalloproteinase domain-containing protein 15 is an enzyme that in humans is encoded by the ''ADAM15'' gene. Function The protein encoded by this gene is a member of the A disintegrin and metalloproteinase, ADAM (a disintegrin .... References Further reading

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SNX9
Sorting nexin-9 is a protein that in humans is encoded by the ''SNX9'' gene. This gene encodes a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. This protein does not contain a coiled coil region, like some family members, but does contain an SH3 domain near its N-terminus. This protein interacts with the cytoplasmic domains of the precursor but not the processed forms of a disintegrin and metalloprotease domain 9 and 15. This protein binds the beta-appendage domain of adaptor protein 2 and may function to assist adaptor protein 2 in its role at the plasma membrane. This protein interacts with activated Cdc42-associated kinase-2 to regulate the degradation of epidermal growth factor receptor protein. Interactions SNX9 has been shown to interact with ADAM9, DNM2 and ADAM15 Disintegrin and metalloproteinase domain-containing protein 15 is an enzyme that ...
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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 ...
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Gene
In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a basic unit of heredity and the molecular gene is a sequence of nucleotides in DNA that is transcribed to produce a functional RNA. There are two types of molecular genes: protein-coding genes and noncoding genes. During gene expression, the DNA is first copied into RNA. The RNA can be directly functional or be the intermediate template for a protein that performs a function. The transmission of genes to an organism's offspring is the basis of the inheritance of phenotypic traits. These genes make up different DNA sequences called genotypes. Genotypes along with environmental and developmental factors determine what the phenotypes will be. Most biological traits are under the influence of polygenes (many different genes) as well as gen ...
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Disintegrin
Disintegrins are a family of small proteins (45–84 amino acids in length) from viper venoms that function as potent inhibitors of both platelet aggregation and integrin-dependent cell adhesion. Operation Disintegrins work by countering the blood clotting steps, inhibiting the clumping of platelets. They interact with the beta-1 and -3 families of integrins receptors. Integrins are cell receptors involved in cell–cell and cell–extracellular matrix interactions, serving as the final common pathway leading to aggregation via formation of platelet–platelet bridges, which are essential in thrombosis and haemostasis. Disintegrins contain an RGD (Arg-Gly-Asp) or KGD (Lys-Gly-Asp) sequence motif that binds specifically to integrin IIb-IIIa receptors on the platelet surface, thereby blocking the binding of fibrinogen to the receptor–glycoprotein complex of activated platelets. Disintegrins act as receptor antagonists, inhibiting aggregation induced by ADP, thrombin, platelet-a ...
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SH3 Domain
The SRC Homology 3 Domain (or SH3 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 ...
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Ectodomain
An ectodomain is the domain of a membrane protein that extends into the extracellular space (the space outside a cell). Ectodomains are usually the parts of proteins that initiate contact with surfaces, which leads to signal transduction.A notable example of an ectodomain is the S protein, commonly known as the spike protein, of the viral particle responsible for the COVID-19 pandemic. The ectodomain region of the spike protein (S) is essential for attachment and eventual entry of the viral protein into the host cell. Ectodomains play a crucial part in the signaling pathways of viruses. Recent findings have indicated that certain antibodies including the anti-receptor binding domain (anti-RBD) or anti-spike ectodomain (anti-ECD) IgG titers can act as virus neutralization titers (VN titers) which can be identified in individuals with diseases, dyspnea and hospitalizations. In perspective of severe acute respiratory syndrome corona virus 2 (SARS-Cov-2) these specific ectodomains ma ...
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Atlas Of Genetics And Cytogenetics In Oncology And Haematology
The Atlas of Genetics and Cytogenetics in Oncology and Haematology, created in 1997 by Jean-Loup Huret (with bioinformatics by Philippe Dessen) is a collection of resources on genes, chromosomes anomalies, leukemias, solid tumours, and cancer-prone diseases. The project is accessible through Internet and is made of encyclopedic-style files, as well as traditional overviews, links towards websites and databases devoted to cancer and/or genetics, case reports in haematology. It also encompasses teaching items in various languages. Starting first from cytogenetics in the nineteens, the Atlas now combines different types of knowledge in a single web site: genes and their function, cell biology (ex: Apoptosis), pathological data, diseases and their clinical implications, cytogenetics, but also medical genetics, with hereditary disorders associated with an increased risk of cancer. This gives a wider and more global view of cancer genetics, while these data are usually dispersed. It inc ...
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Proteases
A protease (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalyzes (increases reaction rate or "speeds up") 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 bonds. Proteases are involved in many biological functions, including 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 evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Hierarchy of proteases Based on catalytic residue Proteases can be classified into seven broad groups: * Serine proteases - ...
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