Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1
about
Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductaseInvolvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductaseComparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriaeUnusual Diheme Conformation of the Heme-Degrading Protein from Mycobacterium tuberculosisA Novel, “Double-Clamp” Binding Mode for Human Heme Oxygenase-1 InhibitionThe 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 reductaseRedox, haem and CO in enzymatic catalysis and regulationA review on hemeoxygenase-2: focus on cellular protection and oxygen response1H NMR investigation of the solution structure of substrate-free human heme oxygenase: comparison to the cyanide-inhibited, substrate-bound complex.Modulation of the axial water hydrogen-bonding properties by chemical modification of the substrate in resting state, substrate-bound heme oxygenase from Neisseria meningitidis; coupling to the distal H-bond network via ordered water molecules.Protein kinase Akt/PKB phosphorylates heme oxygenase-1 in vitro and in vivo.Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase.Isocyanides inhibit human heme oxygenases at the verdoheme stage.Identification of ligand binding sites of proteins using the Gaussian Network Model.Interactions of multiple gas-transducing systems: hallmarks and uncertainties of CO, NO, and H2S gas biology.Spectroscopic insights into axial ligation and active-site H-bonding in substrate-bound human heme oxygenase-2.Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexesThiol/Disulfide redox switches in the regulation of heme binding to proteins.Spectroscopic studies reveal that the heme regulatory motifs of heme oxygenase-2 are dynamically disordered and exhibit redox-dependent interaction with heme.Structure prediction and activity analysis of human heme oxygenase-1 and its mutant.Comparison of the Mechanisms of Heme Hydroxylation by Heme Oxygenases-1 and -2: Kinetic and Cryoreduction StudiesStructural insights into human heme oxygenase-1 inhibition by potent and selective azole-based compoundsStructural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins.The orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: implications for the enzyme mechanism.GEC-targeted HO-1 expression reduces proteinuria in glomerular immune injury.Structures of the substrate-free and product-bound forms of HmuO, a heme oxygenase from corynebacterium diphtheriae: x-ray crystallography and molecular dynamics investigation.C-Terminal membrane spanning region of human heme oxygenase-1 mediates a time-dependent complex formation with cytochrome P450 reductase.Heme on innate immunity and inflammation.Regulatory Fe(II/III) heme: the reconstruction of a molecule's biography.The iron chaperone poly(rC)-binding protein 2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer.Small molecule antivirulents targeting the iron-regulated heme oxygenase (HemO) of P. aeruginosa.Heme Oxygenase 2 Binds Myristate to Regulate Retrovirus Assembly and TLR4 Signaling.Extracting protein dynamics information from overlapped NMR signals using relaxation dispersion difference NMR spectroscopy.In-Cell Enzymology To Probe His-Heme Ligation in Heme Oxygenase Catalysis.Function Coupling Mechanism of PhuS and HemO in Heme Degradation.Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism.Heme cytotoxicity and the pathogenesis of immune-mediated inflammatory diseases.In silico analysis of heme oxygenase structural homologues identifies group-specific conservations.
P2860
Q24296465-C8ABF5A5-F748-47EA-A779-5FFF2068235FQ24310223-751B720B-BA5E-4E22-B217-194D3F098292Q24621015-9932BC12-FC38-4A25-883B-509C1D21F92BQ27642658-3600F8C2-A190-4497-8832-D035053C4B9DQ27658200-55335A73-564A-4FA5-BDCA-6544045F729BQ27676882-40602750-7A35-4704-B772-FBB2999A5983Q28566694-CB99C84E-720F-4A39-AB19-226CD7BBB01CQ28569380-E65CB497-5036-45FD-BDFD-5E3888B6B930Q28709561-560EC22D-DC81-4B43-8563-D5EAC911B4A0Q30365836-466B7443-19A3-44FE-B70D-79B25CB28F93Q30885667-2C294BDE-B7BB-45CE-91E2-B9DC3E19EBAFQ31039839-E16C709E-D9E3-4A83-9B87-752EF3637017Q33288892-C1995FDE-1BB8-48F6-996B-C987CFF3CB54Q33511502-7D2D9974-CA41-4F6A-8D8D-97DB0252265CQ33802460-F70B96A7-F2A7-4314-8804-6832B8F9FE71Q33808628-195FE7E5-364E-49B4-8072-60BBCB564535Q34078151-8944C794-7844-4CD8-BDE5-486524FCD4F8Q34274056-DD6AE78A-0964-47CB-843B-72F94974A076Q34433464-E676699F-3211-406C-B861-60ABA7A36515Q34589250-F478918B-37E5-40DF-BEA2-BEDE54A812C3Q35579385-909690FE-DC74-46B5-87E2-D63D34FD6F2EQ36076532-8DA12C66-A3C3-4C2C-BF1F-4D8FC3891F4AQ36557800-96358CC7-E504-469E-9196-AA27E82E2235Q36591335-C686C853-D6C9-42B5-B3E6-E174D922CA42Q36671880-169540DC-5F56-4A5C-BF22-CF552C5666EAQ37178924-47B226E4-FA93-42C0-92E1-C6936C8CB02BQ37337345-D8B53ED6-2B03-40B7-A23A-5D42127BDAD1Q37348889-9292A28B-EE3C-447B-9806-627B158CEEC8Q37462854-AD1983AE-AD3C-43B0-9C85-C76642B755A8Q38218093-16E5E728-6CDE-4DA6-AD4A-FA4DC31F024EQ38246763-C7D7373E-CD79-48C2-A829-492A6B137017Q38698813-6D8B822C-4A89-43D9-9601-561143F44476Q40348769-89705FB5-AB96-42D1-8E52-28BF55D875D9Q40359979-79AA9B51-499C-4794-A95B-34A2F8501976Q40420040-235B8ECF-4DD4-44BB-B77E-3FDF9E4085B0Q40989137-40A27391-0ABF-414A-9CEE-39A8D8AEC540Q41193258-7ED75147-235B-4FA5-ABC6-2AC8EE99BE57Q41237558-27DE15A0-2A2D-4706-A60B-E5C332503099Q41776151-2922231E-FAD2-4B7B-8104-556D15F36F8CQ42288774-CA26BB2D-E50A-4A4B-9062-8C1013136755
P2860
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1
description
2003 nî lūn-bûn
@nan
2003 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մարտին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1
@ast
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1
@en
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1
@nl
type
label
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1
@ast
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1
@en
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1
@nl
prefLabel
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1
@ast
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1
@en
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1
@nl
P2093
P2860
P356
P1476
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1
@en
P2093
David J Schuller
Hideaki Shimizu
Huiying Li
Jonathan Friedman
Latesh Lad
Paul R Ortiz de Montellano
Thomas L Poulos
P2860
P304
P356
10.1074/JBC.M211450200
P407
P577
2003-03-07T00:00:00Z