"peptide synthesis"

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Ubiquitin-Conjugating Enzyme E2 Variant 2 (UBE2V2) is an enzyme that belongs to the ubiquitin-conjugating enzyme family. UBE2V2 can be detected in the placenta, colon, liver, and skin. It forms a heterodimer with UBE2N. The UBE2V2/UBE2N heterodimer catalyses the synthesis of non-canonical poly-ubiquitin chains and which leads to protein degradation by the proteasome. UBE2V2 mediates transcriptional activation of target genes. It plays a role in the control of progress through the cell cycle and differentiation. It also plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage.

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Heat-Responsive Protein 12 (HRSP12) is an endoribonuclease that belongs to the Rut family. HRSP12 is found mainly in the human adult kidney and liver and is responsible for inhibiting protein translation by cleaving mRNA. HRSP12 only cleaves phosphodiester bonds in single-stranded RNA and inhibits cell-free protein synthesis. The levels of both mRNA and protein are markedly reduced in heptatocellular tumors and in human hepatoma cell lines compared with normal liver tissues. Moreover the levels of HRSP12 are different depending on the grade of the tumor. This had led to the suggestion that HRSP12 may be an important biomarker for heptatic carcinoma.

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Chemokine (C-X-C motif) Ligand 1 Protein (CXCL1) is a growth factor for melanoma cells and a chemotaxin for neutrophils and a member of the CXC chemokine family that is a potent neutrophil attractant and activator and is also active toward basophils. CXCL1 is expressed by macrophages, neutrophils and epithelial cells; it has neutrophil chemoattractant activity. CXCL1 plays a critical nonredundant role in the development of experimental Lyme arthritis and carditis via CXCR2-mediated recruitment of neutrophils into the site of infection and may also have important pro-nociceptive effects via its direct actions on sensory neurons, and may induce long-term changes that involve protein synthesis.

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Peroxisomes are essential organelles that participate in multiple important metabolic processes, including the beta -oxidation of fatty acids, plasmalogen synthesis, and the metabolism of reactive oxygen species (ROS). Peroxiredoxins is overexpressed in breast cancer tissues to a great extent suggesting that they has a proliferative effect and may be related to cancer development or progression. Peroxiredoxin 5 (PRDX5) is a thioredoxin peroxidase that belongs to the atypical 2-Cys class of the TSA/ahpC family of peroxiredoxins. PRDX5 is a widely expressed mitochondrial antioxidant enzyme that reduces hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite. In human cells, this enzyme is present in the cytosol, mitochondria, peroxisomes, and nucleus.

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Mouse Il10 is the prototypic member of the IL-10 cytokine family, including IL-10, IL-19, IL-20, IL-22 (IL-TIF), IL-24 and IL-26. Many viruses encode viral members of the IL-10 family, such as Epstein-Barr virus (EBV) and human cytomegalovirus (HCMV).Its main function is inhibiting the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells. Although human and mouse IL-10 are 81% identical at the nucleotide and amino acid level, mouse IL-10 is species-specific and does not act on human cells. Interestingly, Human IL-10 is active on mouse cells.

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Glucose-6-Phosphate 1-Dehydrogenase (G6PD) is a cytosolic enzyme that belongs to the glucose-6-phosphate dehydrogenase family. G6PD participates in the pentose phosphate pathway that supplies reducing energy to cells by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). G6PD produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power. NADPH in turn maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage. It is notable in humans that G6PD is remarkable for its genetic diversity. G6PD deficiency may cause neonatal jaundice, acute hemolysis, or severe chronic non-spherocytic hemolytic anemia.

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Tryptophan 2,3-dioxygenase (TDO) is a heme-containing dioxygenase catalyzing the addition of molecular oxygen across the 2,3-double bond of the indole ring of tryptophan to form N-formylkynurenine (NFK). In Anopheles gambiae, TDO is the only enzyme able to catalyze the first and rate-limiting step in L-Trp catabolism through the kynurenine pathway. Tryptophan is an essential amino acid for protein synthesis and also the precursor for production of a number of neurotransmitters, such as serotonin and melatonin; in mosquitoes, the kynurenine pathway is essential for eye pigmentation. Conceivably, the tryptophan-using pathways should be regulated in a coordinated manner in mosquitoes as well as in other species and TDO activation/inactivation processes could play an essential role in these phenomena.

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Fatty Acid-Binding Protein 2 (FABP2) is a cytoplasm protein that belongs to the Fatty-acid binding protein (FABP) family of calycin superfamily. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids. FABP2 is expressed in the small intestine and at much lower levels in the large intestine, the highest expression levels in the jejunum. FABP2 binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis and may also help maintain energy homeostasis by functioning as a lipid sensor.

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Granulocyte-colony stimulating factor (G-CSF) is a cytokine that functions as a potent inducer of neutrophilic granulocyte proliferation, terminal differentiation, and activation. G-CSF synthesis occurs in monocyte, macrophage, epithelial, endothelial, and fibroblast cells after activation by bacterial endotoxins, tumor necrosis factor alpha (TNF-α), interleukin 1 (IL-1), or interleukin 17 (IL-17). The functional activity of G-CSF is mediated through the granulocyte colony-stimulating factor receptor (G-CSF-R) to activate JAK/STAT and MAPK signal transduction pathways. G-CSF also promotes neurogenesis and inhibits neuronal apoptosis. Human and mouse G-CSF proteins are cross-reactive. 

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Apoptosis-Inducing Factor 1, Mitochondrial (AIFM1) is a flavoprotein essential for nuclear disassembly in apoptotic cells that is found in the mitochondrial intermembrane space in healthy cells. During apoptosis, it is translocated from the mitochondria to the nucleus to function as a proapoptotic factor in a caspase-independent pathway, while in normal mitochondria, it functions as an antiapoptotic factor via its oxidoreductase activity. The soluble form (AIFsol) found in the nucleus induces parthanatos i.e., caspase-independent fragmentation of chromosomal DNA. AIFM1 interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates casapse-7 to amplify apoptosis. It binds to DNA in a sequence-independent manner and plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells.

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Ubiquitin-Conjugating Enzyme Variant 1a (UBE2V1) is a member of the Ubiquitin-conjugating (E2) enzyme family. The E2 catalytic core domain of UBE2V1 lacks an active site cysteine residue, rendering it catalytically inactive on its own. However, in the cytoplasm UBE2V1 is able to form a catalytically active complex with UBE2N/Ubc13, which mediates the synthesis Lys63-linked Ubiquitin chains and is required for NF-kappa B activation. UBE2V1 is required for UBE2N (Ubc13)/UBE2V1 Complex-dependent Lys63-linked Ubiquitin chain formation. More specifically, UBE2V1 orients the Ubiquitin molecule to favor linkage at Lys63 via a non-covalent interaction with the Ubiquitin molecule. The UBE2V1-UBE2N heterodimer catalyses the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys63. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. UBE2V1 plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6, and TRAF2. It mediates transcriptional activation of target genes. UBE2V1 also controls the progress through the cell cycle and differentiation, the error-free DNA repair pathway and contributes to the survival of cells after DNA damage.

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Natural Cytotoxicity Triggering Receptor 3 (NCR3) along with NKp44 and NKp46 constitute a group of receptors termed “Natural Cytotoxicity Receptors”. They play a major role in triggering NK-mediated killing of most tumour cells lines. NKp30 is a type I transmembrane protein having a single extracellular V-like immunoglobulin domain. NKp30 is selectively expressed both in resting and activated human NK cells. In addition, NKp30 is also involved in NK-mediated induction of dendritic cell (DC) maturation. It has been demonstrated that NK cell activation signalling specifically induces lytic activity against several tumour cell types and synthesis of new NF-κB dependent proteins during the initiation of cytotoxicity.

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CD27 (TNFRSF7) is a member of the TNF-receptor superfamily limited to cells of the lymphoid lineage and exists as both a dimeric glycoprotein on the cell surface and as a soluble protein in serum. As a T and B cell co-stimulatory molecule, the activity of CD27 is governed by its TNF-like ligand CD70 on lymphocytes and dendritic cells. The CD27-CD70 interaction is required for Th1 generation responses to differentiation signals and long-term maintenance of T cell immunity, and meanwhile, plays a key role in regulating B cell differentiation, activation and immunoglobulin synthesis. The CD27 receptor transduces signals and subsequently leads to the activation of NF-kappaB and MAPK8/JNK, mediated by the adaptor proteins TRAF2 and TRAF5. In addition, the proapoptotic protein SIVA is capable of binding the cytoplasmic tail of CD27 and exerts action in the process of apoptosis.

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Fatty acid-binding protein 2 (FABP2), is also known as Fatty acid-binding protein, intestinal (FABPI), Intestinal-type fatty acid-binding protein (I-FABP). FABP2 belongs to the calycin superfamily and Fatty-acid binding protein (FABP) family. FABP2 / FABPI is expressed in the small intestine and at much lower levels in the large intestine and is highest expressed in the jejunum. FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. FABP2 binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor.

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Interleukin-1 Receptor Antagonist (IL-1RN) is a member of the IL-1 family. Endogenous IL-1RN is produced in numerous animal disease models as well as in human autoimmune and chronic inflammatory diseases. It binds to IL-1 receptors in competition with IL-1, but does not elicit intracellular response from this binding. Its role in counteracting the proinflammatory effects of IL-1 is being studied by numerous research groups. IL-4 and IL-13 have been shown to amplify the stimulatory effect of IL1-beta on the production of soluble and intracellular forms of IL-1RN. The regulated expression of IL-1RN in various cell types has been shown to be influenced by cytokines. In synovial fibroblasts, IL-1, TNF-alpha, or PDGF markedly enhances the synthesis of IL-1RN.

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CD27 (TNFRSF7) is a member of the TNF-receptor superfamily limited to cells of the lymphoid lineage and exists as both a dimeric glycoprotein on the cell surface and as a soluble protein in serum. As a T and B cell co-stimulatory molecule, the activity of CD27 is governed by its TNF-like ligand CD70 on lymphocytes and dendritic cells. The CD27-CD70 interaction is required for Th1 generation responses to differentiation signals and long-term maintenance of T cell immunity, and meanwhile, plays a key role in regulating B cell differentiation, activation and immunoglobulin synthesis. The CD27 receptor transduces signals and subsequently leads to the activation of NF-kappaB and MAPK8/JNK, mediated by the adaptor proteins TRAF2 and TRAF5. In addition, the proapoptotic protein SIVA is capable of binding the cytoplasmic tail of CD27 and exerts action in the process of apoptosis.