Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin.
about
Kinetics and mechanisms of thiol-disulfide exchange covering direct substitution and thiol oxidation-mediated pathwaysMass spectrometry in studies of protein thiol chemistry and signaling: opportunities and caveatsChemical approaches to detect and analyze protein sulfenic acidsCrystal Structure and Catalytic Properties of Bacillus anthracis CoADR-RHD: Implications for Flavin-Linked Sulfur TraffickingProtein Engineering of the Quaternary Sulfiredoxin{middle dot}Peroxiredoxin Enzyme{middle dot}Substrate Complex Reveals the Molecular Basis for Cysteine Sulfinic Acid PhosphorylationTime-Resolved Crystallography of the Reaction Intermediate of Nitrile Hydratase: Revealing a Role for the Cysteinesulfenic Acid Ligand as a Catalytic NucleophileThioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signalingThe cysteine proteomeBiological Chemistry and Functionality of Protein Sulfenic Acids and Related Thiol ModificationsSelf-subunit swapping chaperone needed for the maturation of multimeric metalloenzyme nitrile hydratase by a subunit exchange mechanism also carries out the oxidation of the metal ligand cysteine residues and insertion of cobalt.Protein redox modification as a cellular defense mechanism against tissue ischemic injury.Redox-regulated chaperones.Effects of ionizing radiation on biological molecules--mechanisms of damage and emerging methods of detectionCysteine-mediated redox signaling: chemistry, biology, and tools for discoveryReduction of cysteine sulfinic acid in eukaryotic, typical 2-Cys peroxiredoxins by sulfiredoxin.Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins.Protein glutathionylation in the regulation of peroxiredoxins: a family of thiol-specific peroxidases that function as antioxidants, molecular chaperones, and signal modulators.Oxidative stress in fungi: its function in signal transduction, interaction with plant hosts, and lignocellulose degradationSimple synthesis of 1,3-cyclopentanedione derived probes for labeling sulfenic acid proteinsRole of sulfiredoxin as a peroxiredoxin-2 denitrosylase in human iPSC-derived dopaminergic neurons.Protein oxidation: role in signalling and detection by mass spectrometry.Role of sulfiredoxin in systemic diseases influenced by oxidative stress.Cysteine-mediated redox signalling in the mitochondria.Characterization of plant sulfiredoxin and role of sulphinic form of 2-Cys peroxiredoxin.Evidence that glutathione and the glutathione system efficiently recycle 1-cys sulfiredoxin in vivo.Selenite and tellurite form mixed seleno- and tellurotrisulfides with CstR from Staphylococcus aureus.Catalytic mechanism of Sulfiredoxin from Saccharomyces cerevisiae passes through an oxidized disulfide sulfiredoxin intermediate that is reduced by thioredoxinObservation of a chemically labile, noncovalent enzyme intermediate in the reaction of metal-dependent Aquifex pyrophilus KDO8PS by time-resolved mass spectrometry.A eukaryotic-like sulfiredoxin involved in oxidative stress responses and in the reduction of the sulfinic form of 2-Cys peroxiredoxin in the cyanobacterium Anabaena PCC 7120.The rate-limiting step of sulfiredoxin is associated with the transfer of the γ-phosphate of ATP to the sulfinic acid of overoxidized typical 2-Cys peroxiredoxins.Insights into the respiratory chain and oxidative stress
P2860
Q26827753-60D5B84D-2E53-4911-95CE-9AC22A8AB8B1Q26853590-043B8316-10FF-4464-9511-981AD461A6B2Q26996075-83AD67A2-C4C0-4969-9220-80038F3BC765Q27657276-4A09984F-3319-4767-B48D-4895A970B3AFQ27657723-52B2653F-C88C-47D5-8C04-E30221CC2539Q27702089-4BFD3958-42CD-44AC-AEA3-2C2B7BA8DBFDQ28389739-A985B4C9-23F7-4222-8A02-9D757DF3EA4BQ28395817-BC77C954-35C5-4005-8914-C4F6E6F1E3DCQ29248463-1530846F-8013-46ED-BBB1-6A0D7B5C1265Q33426734-FFDAA568-8079-47FF-A6B1-34D837667023Q33634920-07CCBD85-FDB0-4EB7-AD74-FFF6189AE613Q33766707-8859155C-7934-4338-878B-BFD45ADD006AQ33767975-BBEA6403-DCDF-460F-989E-AF0A936CD0B0Q35001796-2A1235BE-B8B6-45C2-8F97-FC6DB44A9AEBQ35031209-C911831D-F438-4692-9756-81D63AC0549BQ35075095-A340D2D9-693C-47DA-AE72-474F975DD625Q35721861-6FC5D9B1-99A2-4DC3-8FFC-73214E88046AQ35833976-A54F89D7-C9A3-498F-A837-16107BC59898Q36653594-6F631585-8686-4DCB-B676-FAAD5BA7AF6BQ37450863-57D45073-FF04-4F9A-A75E-0C20CCD7B5B3Q37733368-7AE1DD3F-0D89-4DF3-B008-80654F2E7889Q38280568-2B845A20-F5F9-419C-8095-82FE9D78F1CCQ38292320-245F01F3-DF9D-4793-8342-5765FDFADF36Q39580876-3E1D362A-6030-4872-8538-4F8821F14E53Q41767815-5BD5324A-D48C-4378-94EC-5E24E6EAAD54Q41821397-5CA3B519-01B5-48DD-803A-FF32C1F0BC04Q42002140-1696CCDE-E7AD-4CEF-8E5A-B013A275DB48Q42094933-389AD088-5522-4EB9-9AF1-481106EEDA5CQ47291762-5BB5D494-F427-41A4-A9C7-6B2F5125C2FFQ51613015-090ED8B8-6DDE-496D-95EE-1BBF2867A205Q57044357-B998BFDD-626C-4398-B8E8-73A0E5E01ACF
P2860
Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Identification of intact prote ...... redoxin by human sulfiredoxin.
@en
Identification of intact prote ...... redoxin by human sulfiredoxin.
@nl
type
label
Identification of intact prote ...... redoxin by human sulfiredoxin.
@en
Identification of intact prote ...... redoxin by human sulfiredoxin.
@nl
prefLabel
Identification of intact prote ...... redoxin by human sulfiredoxin.
@en
Identification of intact prote ...... redoxin by human sulfiredoxin.
@nl
P2093
P2860
P356
P1476
Identification of intact prote ...... redoxin by human sulfiredoxin.
@en
P2093
Allen W Tsang
Cristina M Furdui
Thomas J Jönsson
W Todd Lowther
P2860
P304
22890-22894
P356
10.1074/JBC.C800124200
P407
P577
2008-06-30T00:00:00Z