THOC1 (THO Complex 1) is a Protein Coding gene. Among its related pathways are Cleavage of Growing Transcript in the Termination Region and Transport of Mature Transcript to Cytoplasm. Gene Ontology (GO) annotations related to this gene include RNA binding.
Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated.
THBS1(thrombospondin 1) Homo sapiens The protein encoded by this gene is a subunit of a disulfide-linked homotrimeric protein. This protein is an adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. This protein can bind to fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-V/beta-1. This protein has been shown to play roles in platelet aggregation, angiogenesis, and tumorigenesis.
The protein encoded by this gene is a subunit of a disulfide-linked homotrimeric protein. This protein is an adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. This protein can bind to fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-V/beta-1. This protein has been shown to play roles in platelet aggregation, angiogenesis, and tumorigenesis.
TH (Tyrosine 3-hydroxylase), also known as Tyrosine 3-monooxygenase, is a 60-62 kDa member of the biopterin-dependent aromatic amino acid hydroxylase family of molecules. It is expressed by neurons of the dopamine and autonomic nervous system, plus the neuroendocrine cells of the adrenal medulla. TH is considered the rate limiting enzyme for catecholamine synthesis, and serves to catalyze the hydroxylation of L-tyrosine.
Thymidylate synthase (TS) is a key enzyme in the synthesis of 2'-deoxythymidine-5'-monophosphate, an essential precursor for DNA biosynthesis. Thymine nucleotide synthase is a key enzyme in the de novo synthesis pathway of mitochondrial thymine. For this reason, it is a key target for cancer chemotherapy, and considered to be the main target of 5-fluorouric acid, 5-fluoro-2'-deoxyribonucleic acid and some folate compounds.
Thymidylate synthase is a homodimer composed of two 30 kDa subunits, which catalyze the methylation of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP), an essential step in the formation of thymine nucleotides. Thymidylate synthase is an intracellular enzyme that provides the sole de novo source of thymidylate, making it a required enzyme in DNA biosynthesis with activity highest in proliferating cells. Being the exclusive source of dTMP, investigators have concluded that TS is also an important target for anticancer agents such as 5-fluorouracil (5-FU). 5-FU acts as a TS inhibitor and is active against solid tumors such as colon, breast, head, and neck.
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