about
The IsdG-family of haem oxygenases degrades haem to a novel chromophoreStructural Basis for Hydration Dynamics in Radical Stabilization of Bilin Reductase MutantsCrystal Structure and Biochemical Features of EfeB/YcdB from Escherichia coli O157Insights into the Biosynthesis and Assembly of Cryptophycean PhycobiliproteinsOverlapping specificities of the mitochondrial cytochrome c and c1 heme lyases.Direct tests of enzymatic heme degradation by the malaria parasite Plasmodium falciparumBacillus subtilis Fur represses one of two paralogous haem-degrading monooxygenases.Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases.Haem oxygenase delays programmed cell death in wheat aleurone layers by modulation of hydrogen peroxide metabolismModulation 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.Characterization of the spontaneous "aging" of the heme oxygenase from the pathological bacterium Neisseria meningitidis via cleavage of the C-terminus in contact with the substrate. Implications for functional studies and the crystal structure.1H NMR study of the magnetic properties and electronic structure of the hydroxide complex of substrate-bound heme oxygenase from Neisseria meningitidis: influence of the axial water deprotonation on the distal H-bond network.Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase.The battle for iron between bacterial pathogens and their vertebrate hosts.SHB1/HY1 Alleviates Excess Boron Stress by Increasing BOR4 Expression Level and Maintaining Boron Homeostasis in Arabidopsis Roots.Biliverdin amides reveal roles for propionate side chains in bilin reductase recognition and in holophytochrome assembly and photoconversion.Analysis of a heme-dependent signal transduction system in Corynebacterium diphtheriae: deletion of the chrAS genes results in heme sensitivity and diminished heme-dependent activation of the hmuO promoter.Human heme oxygenase-1 efficiently catabolizes heme in the absence of biliverdin reductaseNutritional immunity: transition metals at the pathogen-host interface.Bacillus anthracis IsdG, a heme-degrading monooxygenaseSolution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexesMetal limitation and toxicity at the interface between host and pathogenA heme-degradation pathway in a blood-sucking insect.Cobalt alleviates GA-induced programmed cell death in wheat aleurone layers via the regulation of H2O2 production and heme oxygenase-1 expression.A product of heme catabolism modulates bacterial function and survivalAutomated selection of compounds with physicochemical properties to maximize bioavailability and druglikeness.Surface protein IsdC and Sortase B are required for heme-iron scavenging of Bacillus anthracis.Heme Oxygenase-1: A Critical Link between Iron Metabolism, Erythropoiesis, and DevelopmentStreptophyte phytochromes exhibit an N-terminus of cyanobacterial origin and a C-terminus of proteobacterial origin.Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study.Time-resolved Studies of IsdG Protein Identify Molecular Signposts along the Non-canonical Heme Oxygenase PathwayRole of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance studyHeme Oxygenase-1 Delays Gibberellin-Induced Programmed Cell Death of Rice Aleurone Layers Subjected to Drought Stress by Interacting with Nitric OxideStructural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins.The mechanism of heme transfer from the cytoplasmic heme binding protein PhuS to the delta-regioselective heme oxygenase of Pseudomonas aeruginosaThe orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: implications for the enzyme mechanism.Analysis of nitric oxide-stabilized mRNAs in human fibroblasts reveals HuR-dependent heme oxygenase 1 upregulationBacterial heme-transport proteins and their heme-coordination modes.Across intra-mammalian stages of the liver f luke Fasciola hepatica: a proteomic study1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure.
P2860
Q27660036-39722CA1-33B7-4300-A104-477B5FCD5950Q27662407-E6D19667-2575-4090-8207-D15BAAA8ED65Q27666975-7196B991-6291-480C-AD56-1E0A81DE10A0Q27684946-7C493F8D-61A4-4F53-A9B4-533ED4233F50Q27931671-0DE4D5C7-8A72-4550-9BE7-EE36E5880933Q27973434-AD5C41BF-73B5-47F0-A425-B5D273F6669BQ29346701-80D94002-9510-43D8-B530-88719555DA37Q30160416-1FA72CC5-4C2B-4912-9675-07E11F76FB8FQ30987671-3E2C5B9D-4CF4-4FC3-97FB-3EC7D5E27EE3Q31039839-F52F6347-CBCA-4FB2-A788-8DCF2C30D03AQ33237045-A63DFC10-C6D1-4092-823B-F6EEAE37DFA8Q33243618-64D4AE6D-028B-4BD9-BCA7-541397FD6E56Q33511502-F81706B7-0D09-4911-A3A0-7954610F8FC7Q33658687-458C3A81-2FB3-4F88-923A-F17E5F6A1845Q33690113-228C2400-76A3-476A-94E0-41747072CB77Q34078020-6E0DB5C7-9C6A-41BD-907B-21E43C87BB81Q34111872-ACB8C1BB-DECF-4994-8BDA-7866F7AD88B6Q34257481-5DF404B4-ACB2-445A-B7E0-088570733007Q34288184-113D437C-4BC4-452D-B46E-4FA573D0010EQ34303390-4F83CDB2-19C6-461E-B8E5-780EB62DDD08Q34433464-3DCE2133-408A-416D-ACEC-583BBFE71197Q34490463-6D65E000-F105-4AD9-AD54-93D87B3EFAADQ34650036-0C3BD859-CB44-472F-AB2E-8126FD351D8AQ34685667-3531B765-BC7D-408E-93B0-3835D61842F2Q34916684-FC904289-E0CC-4DD3-866A-9AFF6C0C9A84Q35176797-7CC60141-8133-452A-ABA6-D2EF2AD91946Q35220586-5D4BE60C-DCCA-48E2-BE4D-F939BD139C11Q35579428-C04933E3-C0C4-4BB7-8DD9-DA360B2A8472Q35606396-2407BF54-9F5A-4B50-8324-0CD222BB0FD1Q35648424-077A60AF-C937-4BBE-873E-FCC6320ECE52Q36442427-D452FC38-D413-4B70-9614-579BF24CE770Q36445749-61CCEEF3-FD06-42D4-A394-FDDEB95E7D6EQ36475321-AF1E1EDD-C13D-4747-9A21-01A3592A326AQ36671880-A50A9FED-F13C-4AD7-91F7-58A1FB197A55Q37073939-B67BC50A-E07A-4283-8549-C94CCE019940Q37178924-510F75B7-9C7D-4C4C-96B5-D4F032667D95Q37192054-A0B7C124-2C00-48B6-AFF3-B7D647504970Q37195856-BBE4B5EE-9A22-4A57-B6C2-586833206739Q37236789-3B86A835-F01F-41A5-A2EB-A3C41CE91A5AQ37298678-E82D3386-CDC9-4444-BB7A-619623471AA6
P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Heme oxygenase: evolution, structure, and mechanism.
@ast
Heme oxygenase: evolution, structure, and mechanism.
@en
Heme oxygenase: evolution, structure, and mechanism.
@nl
type
label
Heme oxygenase: evolution, structure, and mechanism.
@ast
Heme oxygenase: evolution, structure, and mechanism.
@en
Heme oxygenase: evolution, structure, and mechanism.
@nl
prefLabel
Heme oxygenase: evolution, structure, and mechanism.
@ast
Heme oxygenase: evolution, structure, and mechanism.
@en
Heme oxygenase: evolution, structure, and mechanism.
@nl
P1476
Heme oxygenase: evolution, structure, and mechanism.
@en
P2093
Angela Wilks
P304
P356
10.1089/15230860260220102
P577
2002-08-01T00:00:00Z