about
Role of Nrf2/HO-1 system in development, oxidative stress response and diseases: an evolutionarily conserved mechanismUnusual Diheme Conformation of the Heme-Degrading Protein from Mycobacterium tuberculosisCrystal Structure and Biochemical Features of EfeB/YcdB from Escherichia coli O157Insights into the Biosynthesis and Assembly of Cryptophycean PhycobiliproteinsIron homeostasis in the Rhodobacter genusBacillus subtilis Fur represses one of two paralogous haem-degrading monooxygenases.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.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.Functional identification of HugZ, a heme oxygenase from Helicobacter pylori.Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase.Global transcriptomic response of Leptospira interrogans serovar Copenhageni upon exposure to serum.Heme uptake in bacterial pathogensIron-sparing response of Mycobacterium avium subsp. paratuberculosis is strain dependent.Genomic analysis reveals key aspects of prokaryotic symbiosis in the phototrophic consortium "Chlorochromatium aggregatum".Genome organization of epidemic Acinetobacter baumannii strainsIdentification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeatsComplex formation between heme oxygenase and phytochrome during biosynthesis in Pseudomonas syringae pv. tomato.Bacillus anthracis IsdG, a heme-degrading monooxygenaseOvercoming the heme paradox: heme toxicity and tolerance in bacterial pathogens.Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexesCrystal structure of HugZ, a novel heme oxygenase from Helicobacter pyloriCrystallization and preliminary crystallographic studies of Campylobacter jejuni ChuZ, a member of a novel haem oxygenase familyInfluence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study.Escherichia coli heme oxygenase modulates host innate immune responses.Role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance studyStructural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins.Intracellular metalloporphyrin metabolism in Staphylococcus aureus.Crystallization and preliminary crystallographic studies of Helicobacter pylori HugZ, a novel haem oxygenase.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.Bacteria capture iron from heme by keeping tetrapyrrol skeleton intact1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure.Radical new paradigm for heme degradation in Escherichia coli O157:H7.Haem oxygenase (HO): an overlooked enzyme of plant metabolism and defence.Heme in the marine environment: from cells to the iron cycle.New biosynthetic pathway for pink pigments from uncultured oceanic viruses.TAT-mediated transduction of bacterial redox proteins generates a cytoprotective effect on neuronal cellsExpression, purification and preliminary X-ray crystallographic analysis of cyanobacterial biliverdin reductase.Heme utilization by pathogenic bacteria: not all pathways lead to biliverdin.Protoporphyrin (PPIX) efflux by the MacAB-TolC pump in Escherichia coli.
P2860
Q26751266-2FCA73AD-04C3-436D-B39B-8F742DB5F371Q27658200-86143966-5A18-434B-AFCC-5C31D1A5395BQ27666975-62425940-BB2A-47BB-8F64-F8C553D712E8Q27684946-397B31DD-3131-463F-9194-D67B5A183E52Q28660942-D036AAC0-511E-47A0-B412-208B90783CACQ29346701-AA5F14A8-BDA9-4BCC-BE87-651A4EF4B77CQ31039839-CE0DB951-8B78-4F5F-B0E3-F5771C5F8637Q33237045-CF0A79FD-FCF5-4659-9B23-1E5632915A3BQ33243618-084B609F-BFD0-4A25-8337-4C3105AABC3BQ33394049-A0D34C4C-9993-4E5F-ACDF-0DB4A8B76E32Q33511502-3D17E3CE-CFFE-40FB-81BB-543FF85A151CQ33527570-F83A7A5B-5C8C-4A76-84E8-EE2CC5FEDAEBQ33555758-3CFF2A22-E55F-4B9B-955A-8012C02C0F41Q33726137-FD013363-35C7-46A0-959F-AB2A72A8F612Q33742621-E7DCFA07-015B-426F-9019-8EA8D6F1EFACQ34045074-C30CFD22-1E8C-4B01-9F36-9C1098FDA2FBQ34144548-657CC9C0-D4F4-4790-A2E8-ABA39BF915ECQ34194881-4735F8A3-E068-4E42-8FB4-036CEE52C808Q34303390-C2315A32-9360-4B77-BA41-940EB297D138Q34309767-A65390E7-16AD-4598-966D-9259DB8401E6Q34433464-A867FDBB-5F20-461A-9758-4651655B7FF7Q34489087-0646F570-66B0-4C2D-B556-282CFCA06D73Q35539088-E3A72112-4054-42B3-863E-B49299898A0BQ35648424-C85AFAD6-7DBE-4F5F-955B-D6E5F11278C7Q36091995-7A45D9DA-B6D7-4462-B605-8E7354498BE5Q36445749-47F80968-A210-4073-A3E0-C55F0EF8E6CFQ36671880-D4670FFF-A747-4D0C-8C47-B1084E860FB7Q36771468-8F5D0035-D0E5-4A75-903E-003E1F72AA70Q37148825-DCA999A0-0841-4F3F-AD68-D652CE27F18CQ37178924-87DB9F10-B635-4ED1-AC35-20E8B5E0D7ADQ37261769-5A55967C-3F60-455C-9832-4A6A5B875280Q37298678-E3797791-35DE-4625-B221-42A49E5552A0Q37379819-29034F89-2204-4AEE-8E74-9D2A315949C1Q37727714-01CF4876-1977-4FC8-89EC-7DFB95CA89E3Q38210422-E1EB1DB1-BAEA-46C7-81CD-26D671B4A079Q39942272-E687EADA-5A08-48A6-8E7E-EC12DC92515EQ41487705-0A03ECE2-967E-47F0-ACB4-B76A8937A1DBQ41839827-A0FEC1C4-098A-41BF-949E-FBD4437A9885Q41991304-CF4EAFD4-B152-4C27-9ACF-C8E3BA82A3C0Q42576991-DB62FADC-77AC-46A0-8EBF-575A39E7C06F
P2860
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Bacterial heme oxygenases.
@ast
Bacterial heme oxygenases.
@en
type
label
Bacterial heme oxygenases.
@ast
Bacterial heme oxygenases.
@en
prefLabel
Bacterial heme oxygenases.
@ast
Bacterial heme oxygenases.
@en
P356
P1476
Bacterial heme oxygenases.
@en
P304
P356
10.1089/ARS.2004.6.825
P577
2004-10-01T00:00:00Z