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Neurotrophins function to regulate naturally occurring cell death of neurons during development. The prototype neurotrophin is nerve growth factor (NGF), originally discovered in the 1950s as a soluble peptide promoting the survival of, and neurite outgrowth from, sympathetic ganglia. More recently, three additional structurally homologous neurotrophic factors have been identified. These include brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3) and neurotrophin-4 (NT-4), also de

Neurotrophins function to regulate naturally occurring cell death of neurons during development. The prototype neurotrophin is nerve growth factor (NGF), originally discovered in the 1950s as a soluble peptide promoting the survival of, and neurite outgrowth from, sympathetic ganglia. More recently, three additional structurally homologous neurotrophic factors have been identified. These include brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3) and neurotrophin-4 (NT-4), also de

The protein encoded by this gene is a cell-surface glycoprotein involved in cell-cell interactions, cell adhesion and migration. It is a receptor for hyaluronic acid (HA) and can also interact with other ligands, such as osteopontin, collagens, and matrix metalloproteinases (MMPs). This protein participates in a wide variety of cellular functions including lymphocyte activation, recirculation and homing, hematopoiesis, and tumor metastasis. Transcripts for this gene undergo complex alterna

Arginase I which is expressed almost exclusively in the liver, catalyzes the conversion of arginine to ornithine and urea . The human arginase I gene, which maps to chromosome 6q23, encodes a 322 amino acid protein. Arginase I exists as a homotrimeric protein and contains a binuclear manganese cluster. Arginase II catalyzes the same reaction as arginase I, but differs in its tissue specificity and subcellular location. Specifically, arginase II localizes to the mitochondria. Arginase II is e

Arginase I which is expressed almost exclusively in the liver, catalyzes the conversion of arginine to ornithine and urea . The human arginase I gene, which maps to chromosome 6q23, encodes a 322 amino acid protein. Arginase I exists as a homotrimeric protein and contains a binuclear manganese cluster. Arginase II catalyzes the same reaction as arginase I, but differs in its tissue specificity and subcellular location. Specifically, arginase II localizes to the mitochondria. Arginase II is e

Arginase I which is expressed almost exclusively in the liver, catalyzes the conversion of arginine to ornithine and urea . The human arginase I gene, which maps to chromosome 6q23, encodes a 322 amino acid protein. Arginase I exists as a homotrimeric protein and contains a binuclear manganese cluster. Arginase II catalyzes the same reaction as arginase I, but differs in its tissue specificity and subcellular location. Specifically, arginase II localizes to the mitochondria. Arginase II is e