about
NAD(+)-dependent formate dehydrogenaseStructure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase3D domain swapping: as domains continue to swapThe widespread role of non-enzymatic reactions in cellular metabolismUnusual folded conformation of nicotinamide adenine dinucleotide bound to flavin reductase PInteraction of nitric oxide with catalase: structural and kinetic analysis.Structure of the monofunctional heme catalase DR1998 from Deinococcus radioduransInterdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, crystallographic and modeling studies of histidine 162 and arginine 269 variantsCatalases are NAD(P)H-dependent tellurite reductasesLoop anchor modification causes the population of an alternative native state in an SH3-like domain.Metabolism and genetics of Helicobacter pylori: the genome era.Enzyme-nanoporous gold biocomposite: excellent biocatalyst with improved biocatalytic performance and stabilityTheoretical study of model compound I complexes of horseradish peroxidase and catalase.Intramolecular C(sp(3))H amination of arylsulfonyl azides with engineered and artificial myoglobin-based catalysts.Topological distribution of four-alpha-helix bundlesRNAi-mediated knockdown of catalase causes cell cycle arrest in SL-1 cells and results in low survival rate of Spodoptera litura (Fabricius).Heme-protein fission under nondenaturing conditionsStructural analysis of NADPH depleted bovine liver catalase and its inhibitor complexesCloning and characterization of the katA gene of Rhizobium meliloti encoding a hydrogen peroxide-inducible catalase.A peroxide/ascorbate-inducible catalase from Haemophilus influenzae is homologous to the Escherichia coli katE gene product.Molecular evolution and domain structure of plasminogen-related growth factors (HGF/SF and HGF1/MSP)Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilisMechanisms of oxidant generation by catalase.Human catalase: looking for complete identity.Role of the lateral channel in catalase HPII of Escherichia coli.Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII.The antiproliferative activity of di-2-pyridylketone dithiocarbamate is partly attributed to catalase inhibition: detailing the interaction by spectroscopic methods.Structure of catalase determined by MicroEDIdentification and characterization of a fatty acyl reductase from a Spodoptera littoralis female gland involved in pheromone biosynthesis.Multiple subunit fitting into a low-resolution density map of a macromolecular complex using a gaussian mixture model.Interaction of phlorizin, a potent inhibitor of the Na+/D-glucose cotransporter, with the NADPH-binding site of mammalian catalases.NADPH binding and control of catalase compound II formation: comparison of bovine, yeast, and Escherichia coli enzymes.Aldehyde and Ketone Synthesis by P450-Catalyzed Oxidative Deamination of Alkyl Azides.A novel NADPH:(bound) NADP+ reductase and NADH:(bound) NADP+ transhydrogenase function in bovine liver catalase.Unusual conformation of nicotinamide adenine dinucleotide (NAD) bound to diphtheria toxin: a comparison with NAD bound to the oxidoreductase enzymes.Biodegradable microspheres as carriers for native superoxide dismutase and catalase delivery.The molecular characterization of a catalase from Chinese mitten crab Eriocheir sinensis.A mechanism for NADPH inhibition of catalase compound II formation.Production, characterization, cloning and sequence analysis of a monofunctional catalase from Serratia marcescens SYBC08.cDNA and deduced amino acid sequences of dog catalase.
P2860
Q24528257-7AC647DB-EEC6-49FE-8608-1CE9B024A8D1Q24603764-51E3C869-1F03-423B-BE75-A0DA1E14F37BQ24644990-B39FC1E2-1219-48F3-8FA0-AD63A85C7EF0Q26996495-751CFE16-EE00-4AB2-A67E-7E975474F9A1Q27619660-93249311-DB98-4DEC-8852-6D13C1DA85F8Q27667584-30D7B6B4-AA95-4B7B-A924-DE464D382861Q27690818-0501E5BE-4788-40F1-A089-9B4551C7A215Q27764924-5619FBA4-5A63-45EB-AC35-782C410DE222Q28469096-BC7DD7A0-4B52-484E-ABE3-C2EE54AEAA2DQ30157992-F0838E91-257C-4C57-AD79-2CF5F85CF1ADQ33637624-EABAFE13-1C71-497B-B43A-618B167DAE9FQ34017876-29AB0E43-8858-4EFC-B5F5-6B6662134560Q34128301-88FF5F14-7FA7-4C19-AFB0-8F16CEC8CCCDQ34276305-3171BFC7-DA28-483F-B41F-CF9EAAB563DEQ34300549-DC34664B-3631-4A59-9944-78DBF4E9ECCFQ34651423-B34D86ED-FB8C-44BA-B53B-0330CE9CD705Q34777789-0C1EBAA9-9E29-493C-AF4A-A084D15F99F2Q35232233-1195C20A-30E5-45C8-B1B9-FE63B4749A96Q35617417-14B5DA9A-7627-4566-A3C7-0277693A4461Q36107576-A2B7859B-D62E-45F4-A8E4-C000FED86BD8Q36704207-44082CD2-F8B1-47B4-9ADA-7BA92D4D1CE5Q36706059-68623AB1-F754-4116-821F-6DBFB168595EQ37780594-A1A279EE-46E3-465E-B2EE-CD0D84E8EFE2Q37825842-9D2CB5BE-13F0-4E22-BDDB-69830F162F61Q38326772-AA06EFD9-59A5-43D1-97D7-691EFA14BB19Q38337281-1E7CFCC3-511C-4EF2-843A-5B0A124321F2Q38676094-CB196FAB-56F5-4FE0-9909-18F78D55850CQ41607227-E9BB9CD3-AB17-417C-A01F-6ED8D6283A88Q41625735-541B0DF1-2F47-4CF7-98B8-67F7F0476491Q41774671-8154076A-B12D-4D45-986F-51A39B4E58E9Q41775325-CFFD3248-539D-46B3-8BD3-1DF5E66901EFQ41825681-FAA07B00-9486-49C2-8D66-10FED4715161Q41913322-159EC8A5-8F7D-45FA-B3A6-3D277BDD92BEQ42098038-81A700E5-B1A1-4782-8CB5-3C545472D31FQ42167298-47029279-BF02-402E-8FA5-59D685CBD688Q42184855-AE71AEC4-258D-4F6A-BED5-CC4709FE7A15Q42677639-4FA26C80-417A-4AC1-8534-1DD01A148B89Q43586640-C7C4446C-E128-4D88-921F-7615160B79E8Q44559426-FF5FE970-0D2D-463E-BE7C-2E0ADE728805Q47919291-D8F42869-F4CA-4CD3-8706-36E141E8CC8A
P2860
description
1985 nî lūn-bûn
@nan
1985 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1985 թվականի մարտին հրատարակված գիտական հոդված
@hy
1985年の論文
@ja
1985年学术文章
@wuu
1985年学术文章
@zh-cn
1985年学术文章
@zh-hans
1985年学术文章
@zh-my
1985年学术文章
@zh-sg
1985年學術文章
@yue
name
The NADPH binding site on beef liver catalase
@ast
The NADPH binding site on beef liver catalase
@en
The NADPH binding site on beef liver catalase
@nl
type
label
The NADPH binding site on beef liver catalase
@ast
The NADPH binding site on beef liver catalase
@en
The NADPH binding site on beef liver catalase
@nl
prefLabel
The NADPH binding site on beef liver catalase
@ast
The NADPH binding site on beef liver catalase
@en
The NADPH binding site on beef liver catalase
@nl
P2860
P356
P1476
The NADPH binding site on beef liver catalase
@en
P2093
P2860
P304
P356
10.1073/PNAS.82.6.1604
P407
P577
1985-03-01T00:00:00Z