Crystal structure of rat heme oxygenase-1 in complex with heme
about
Involvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductaseOligomerization is crucial for the stability and function of heme oxygenase-1 in the endoplasmic reticulumComparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide. Implication for regiospecific hydroxylation of heme at the alpha-meso carbonComparison of the heme-free and -bound crystal structures of human heme oxygenase-1Crystal structure of rat heme oxygenase-1 in complex with biliverdin-iron chelate. Conformational change of the distal helix during the heme cleavage reactionCrystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activationThe crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriaeCrystallographic and Spectroscopic Insights into Heme Degradation by Mycobacterium tuberculosis MhuDAlternative cyanide-binding modes to the haem iron in haem oxygenaseUnusual Diheme Conformation of the Heme-Degrading Protein from Mycobacterium tuberculosisThe IsdG-family of haem oxygenases degrades haem to a novel chromophoreStructural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenaseThe reactions of heme- and verdoheme-heme oxygenase-1 complexes with FMN-depleted NADPH-cytochrome P450 reductase. Electrons required for verdoheme oxidation can be transferred through a pathway not involving FMNMass spectrometric identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductaseFlexible mapping of homology onto structure with homolmapper.Structure-based reassessment of the caveolin signaling model: do caveolae regulate signaling through caveolin-protein interactions?Solution 1H NMR of the active site of substrate-bound, cyanide-inhibited human heme oxygenase. comparison to the crystal structure of the water-ligated form.Solution 1H NMR investigation of the active site molecular and electronic structures of substrate-bound, cyanide-inhibited HmuO, a bacterial heme oxygenase from Corynebacterium diphtheriae.1H NMR investigation of the solution structure of substrate-free human heme oxygenase: comparison to the cyanide-inhibited, substrate-bound complex.Two epitopes responsible for the catalytic activity of heme oxygenase-1 identified by phage displayHeme degradation and vascular injury.Electronic properties of the highly ruffled heme bound to the heme degrading enzyme IsdI.Bacillus anthracis IsdG, a heme-degrading monooxygenaseHeme enzyme structure and function.Regulation of heme oxygenase-1 protein expression by miR-377 in combination with miR-217.Design of metal cofactors activated by a protein-protein electron transfer system.Analysis of heme oxygenase isomers in ratAlteration of the regiospecificity of human heme oxygenase-1 by unseating of the heme but not disruption of the distal hydrogen bonding networkC-Terminal membrane spanning region of human heme oxygenase-1 mediates a time-dependent complex formation with cytochrome P450 reductase.Signaling function of heme oxygenase proteins.Haem oxygenase (HO): an overlooked enzyme of plant metabolism and defence.Artificial metalloenzymes constructed from hierarchically-assembled proteins.Chlamydomonas reinhardtii LFO1 Is an IsdG Family Heme Oxygenase.Homologues of neisserial heme oxygenase in gram-negative bacteria: degradation of heme by the product of the pigA gene of Pseudomonas aeruginosaExpression of heme oxygenase-1 protects endothelial cells from irradiation-induced apoptosis.Replacement of the distal glycine 139 transforms human heme oxygenase-1 into a peroxidase.Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme.Interaction between heme oxygenase-1 and -2 proteins.The reactivity of alpha-hydroxyhaem and verdohaem bound to haem oxygenase-1 to dioxygen and sodium dithionite.
P2860
Q24310223-085A5DF2-8C21-40CD-A283-4CC54744F034Q24339396-F5E12B08-0BC5-4B80-8B0E-09F5291134E5Q24621015-2438B18F-D606-4905-B834-81F93A9E744BQ27639657-ABA734D6-87B1-4EC6-98B0-89A47F15FA69Q27640232-18DC4D41-6DD1-42B9-80F2-136F1C7C047CQ27641404-CFD810A4-939A-4407-A53B-EDC227ABD11DQ27641460-37263682-92C6-4532-979C-9302DD91ED0EQ27642658-08FCECA5-FF83-45B0-BA51-3190A4D13027Q27644563-C8D9D60B-9C31-412A-9E6E-DB5D4C32C9B9Q27645338-E6006DEA-65C5-42F4-AE97-4C3A6E4F0052Q27658200-AF99D07F-7DAA-4970-8F7E-681352881991Q27660036-33AEFAB0-978C-4676-8845-F33CDF7C5BD2Q27681796-A3E64596-16E2-4FC7-AB42-B0854031238EQ28566694-4831DB28-A90E-401C-8A95-D0B69B7511DBQ28569380-7EBDFC2E-5699-4305-86E8-8069EF1F0820Q30361035-D3A979B8-CC00-43F1-B83C-C2EA2CEF2F4DQ30524349-7AB021E6-24C1-458E-B343-83DFA1D90EC3Q30647375-FB1EE4C8-770C-440C-BB09-17ED42845B5CQ30754996-43F86036-9B28-44F5-807E-739E0BB492BEQ30885667-171515C3-E2A2-432C-A5B8-437DD68CC343Q33611222-15F42650-D826-41F4-B648-187CFC7606E7Q33649898-B373F1E1-EA85-4C27-A547-0B639125D409Q33970868-86A17BDE-69E5-4896-B8F7-202A7218C7A8Q34303390-5F7C0132-DBB0-400A-8A93-5FA99C20C1D5Q34396417-597660D7-E932-4E97-AC69-3DCC1F628B80Q34536750-9CFA9D03-26FC-4C74-97DF-26EA6FBA71A1Q34686935-8C0191CA-4A58-4D6D-B823-BE9B307F423AQ36308432-549DD86A-E4BC-4450-BBA8-481F70ED4546Q36828818-55F83B50-5D2A-454F-BDEB-8F551C357EEAQ37462854-E3EB2F30-FC35-4E73-B5AF-F67166D1BA09Q37653688-83DFBDD8-E4DE-4E04-BEED-FD7C024E91FFQ37727714-10F75CDE-8E3F-41F3-8830-1585ACF1FF08Q38109125-F775F1AC-9F91-4BE5-8A0E-0BCADAE5D04AQ38621091-0FEF20D9-FF8C-4D6D-AA5C-50984221E599Q39529862-6CAC43D3-DF62-42DB-ACA0-F4007F0817A1Q40350638-58DD46C5-7DEB-4B5C-B711-FC709DBC2CC1Q41755561-BAEDACE3-4143-42B2-A98A-590C73178BEEQ42641232-DF98D33A-DFC1-4DF1-A654-894401BEB2A2Q43622921-2D691D15-09B7-4ACA-BC6B-AE39A454F5C7Q44188688-74164EFE-C919-4A38-8B4C-4F812C362F68
P2860
Crystal structure of rat heme oxygenase-1 in complex with heme
description
2000 nî lūn-bûn
@nan
2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Crystal structure of rat heme oxygenase-1 in complex with heme
@ast
Crystal structure of rat heme oxygenase-1 in complex with heme
@en
Crystal structure of rat heme oxygenase-1 in complex with heme
@nl
type
label
Crystal structure of rat heme oxygenase-1 in complex with heme
@ast
Crystal structure of rat heme oxygenase-1 in complex with heme
@en
Crystal structure of rat heme oxygenase-1 in complex with heme
@nl
prefLabel
Crystal structure of rat heme oxygenase-1 in complex with heme
@ast
Crystal structure of rat heme oxygenase-1 in complex with heme
@en
Crystal structure of rat heme oxygenase-1 in complex with heme
@nl
P2093
P2860
P1433
P1476
Crystal structure of rat heme oxygenase-1 in complex with heme
@en
P2093
P2860
P356
10.1016/S0014-5793(00)01353-3
P407
P577
2000-04-01T00:00:00Z