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  • Proteins
  • Within the nucleus, Nrf2 is believed to exert its transcriptional function by forming heterodimers with small Maf (v-maf musculoaponeurotic fibrosarcoma oncogene family) proteins, binding to ARE-containing promoters, and recruiting transcription coactivators to help remodel chromatin structures and facilitate the formation of basal transcription machinery ( 22 , 29 , 30 , 41 , 50 , 74 ). (pubmedcentralcanada.ca)
  • 2) reactive oxygen species (ROS) processing, and (3) binding of reactive metabolites to proteins/DNA, resulting in inflammation, cell damage, neo-antigen formation, and immune response. (biomedcentral.com)
  • Upon oxidative stress, NRF2 and/or NRF1 dimerize with small MAF or other bZIP proteins in the nucleoplasm, and then the heterodimer binds to the AREs in the promoter regions of various detoxifying and antioxidative stress response genes, such as NADPH: quinone oxidoreductase 1 ( NQO1 ), glutamate cysteine ligase catalytic ( GCLC ) and regulatory ( GCLM ) subunits, and heme oxygenase-1 ( HMOX-1 ). (hindawi.com)
  • The transcription factor BTB and CNC homology 1 (Bach1) is widely expressed in most mammalian tissues and functions primarily as a transcriptional suppressor by heterodimerizing with small Maf proteins and binding to Maf recognition elements in the promoters of targeted genes. (hindawi.com)
  • Dynamic changes of the actin networks are mediated by actin-binding proteins, such as disassembly factors (e.g., cofilin) and stabilizers (e.g. (jneurosci.org)
  • Once released from their inhibitory Regulatory subunit, the catalytic subunits can go on to phosphorylate a huge number of other proteins in the minimal substrate context Arg-Arg-X-Ser/Thr. (wikipedia.org)
  • cofactor
  • The nicotinamide ring of the NAD+ cofactor binds deep in this cleft, which is thought to close during the hydride transfer step of the catalytic cycle. (ebi.ac.uk)
  • Biochemical and structural data for E1s revealed a mechanism of activation of TPP cofactor by forming the conserved hydrogen bond with glutamate residue (Glu59 in human E1) and by imposing a V-conformation that brings the N4' atom of the aminopyrimidine to the distance required for the intramolecular hydrogen bonding with the thiazolium C2 atom. (wikidoc.org)
  • residue
  • They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each case a reversible oxidative deamination reaction. (ebi.ac.uk)
  • This pathway allows protons in the intermembrane space to access an essential ionized carboxylate of a glutamate residue, midmembrane on the C-terminal α-helix of subunit c. (pnas.org)
  • A transfer of the phosphoric residue from the first active site is seen to be coordinate with a transfer of a phosphoric residue to the second active site suggesting again a cooperative binding catalysis. (proteopedia.org)
  • Two glutamate residues, Glu 208 alpha and Glu 197 beta, are crucial for phosphorylation and dephosphorylation of the active-site histidine residue in succinyl-CoA synthetase. (proteopedia.org)
  • assay
  • Fluorescent 9-anthroylouabain binding assay detected that veratridine exposure results in 60% increase in the membrane density of phosphorylated (active) pump molecules which are composed from a complex of alpha and beta subunits (Fig. 4). (mcmaster.ca)
  • REGULATION
  • RT "A common structural basis for pH- and calmodulin-mediated regulation RT in plant glutamate decarboxylase. (genome.jp)
  • ACTIVITY REGULATION: Up-regulated by calmodulin binding at CC physiological pH. (genome.jp)
  • isoforms
  • RT "Two isoforms of glutamate decarboxylase in Arabidopsis are regulated RT by calcium/calmodulin and differ in organ distribution. (genome.jp)
  • catalyzes
  • Catalyzes successive MgATP-dependent additions of glutamate to a pteroylmonoglutamate substrate, with a high preference for 5,10-methylenetetrahydrofolate (mTHF). (uniprot.org)
  • Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). (uniprot.org)
  • catalysis
  • Both bind nucleotides, but catalysis occurs at the β DP site. (pnas.org)
  • is responsible for the dephosphorylation of ATP and it is suspected that there is another active site on the beta subunit that is responsible for the continued catalysis of the reaction. (proteopedia.org)
  • There is a suspected nucleotide binding site on the N-terminal of the beta subunit which would imply that there are two active sites roughly 35 A apart from each other and that the HIS 246 alpha loop moves between them during catalysis. (proteopedia.org)
  • nucleotide
  • Nucleotide sequence of yeast GDH1 encoding nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase. (ebi.ac.uk)
  • membrane
  • The catalytic domain of the F-ATPase in mitochondria protrudes into the matrix of the organelle, and is attached to the membrane domain by central and peripheral stalks. (pnas.org)
  • The proton-motive force is coupled mechanically to ATP synthesis by the rotation at about 100 times per second of the central stalk and an attached ring of c-subunits in the membrane domain. (pnas.org)
  • Each c-subunit carries a glutamate exposed around the midpoint of the membrane on the external surface of the ring. (pnas.org)
  • In the F-ATPase in the inner membranes of mitochondria, the energy of the transmembrane proton-motive-force, generated by respiration, is coupled mechanically to the synthesis of ATP from ADP and phosphate in its membrane extrinsic catalytic domain by rotating the asymmetrical central stalk in a clockwise direction (as viewed from the membrane) at about 100 times per second ( 1 - 4 ). (pnas.org)
  • Subcellular confocal immunofluorescent quantification of alpha-3 catalytic pump subunit has detected that veratridine-induced rise in internal calcium was followed by significant increase in the pump density both on membrane and within the cytoplasm: 39 and 54%, respectively (Fig. 3). (mcmaster.ca)
  • Molecular
  • Some bacterial E1s, including E1 from Escherichia coli , are composed of two similar subunits, each being as large as the sum of molecular masses of α- and β- subunits. (wikidoc.org)
  • calmodulin
  • The calmodulin-binding CC is calcium-dependent and it is proposed that this may, directly or CC indirectly, form a calcium regulated control of GABA biosynthesis. (genome.jp)
  • domain
  • The spherical catalytic domain, which protrudes into the matrix of the organelle, has three catalytic sites in β-subunits at interfaces with α-subunits ( 5 ). (pnas.org)
  • In a ground state structure of the catalytic domain, two of them, the β DP and the β TP sites, have similar but significantly different closed conformations. (pnas.org)
  • The bipartite catalytic (Cat) domain is split between the C1 and C2 regions. (physiology.org)
  • The catalytic domain of adenylyl cyclases is hypothesized to be bipartite and split between C1 and C2 regions. (physiology.org)
  • intracellular
  • Persistent elevation in intracellular sodium, such as induced by excitatory glutamate cytotoxicity or epileptic discharge may lead to irreversible cell injury and death. (mcmaster.ca)
  • Thus
  • Thus, metabolizes mTHF to the tetraglutamate derivative, but longer glutamate chain length products are not observed. (uniprot.org)