The NMR solution structure of human glutaredoxin in the fully reduced form
about
The high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-IStructure-Function Relationship of the Chloroplastic Glutaredoxin S12 with an Atypical WCSYS Active SiteStructure of the thioredoxin-fold domain of human phosducin-like protein 2Structure ofArabidopsischloroplastic monothiol glutaredoxin AtGRXcpComparative analysis of glutaredoxin domains from bacterial opportunistic pathogensElectrostatics of cysteine residues in proteins: parameterization and validation of a simple model.Molecular mapping of functionalities in the solution structure of reduced Grx4, a monothiol glutaredoxin from Escherichia coli.Selective inactivation of glutaredoxin by sporidesmin and other epidithiopiperazinedionesMechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulationPrediction of protein deamidation rates from primary and three-dimensional structure.Purification, crystallization and preliminary diffraction studies of an ectromelia virus glutaredoxin.An NMR-Guided Screening Method for Selective Fragment Docking and Synthesis of a Warhead Inhibitor.The biological roles of glutaredoxins.Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions.Structural and biochemical characterization of peroxiredoxin Qbeta from Xylella fastidiosa: catalytic mechanism and high reactivity.Structure-function analysis of yeast Grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein.The concerted action of a positive charge and hydrogen bonds dynamically regulates the pKa of the nucleophilic cysteine in the NrdH-redoxin family.Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: implications for intracellular roles.Oxidation and S-nitrosylation of cysteines in human cytosolic and mitochondrial glutaredoxins: effects on structure and activity.The busulfan metabolite EdAG irreversibly glutathionylates glutaredoxins.Crystallization and preliminary X-ray crystallographic studies of glutaredoxin 2 from Saccharomyces cerevisiae in different oxidation states.Redox sulfur chemistry of the copper chaperone Atox1 is regulated by the enzyme glutaredoxin 1, the reduction potential of the glutathione couple GSSG/2GSH and the availability of Cu(I).Identification of the first human glutaredoxin pseudogene localized to human chromosome 20q11.2.Cu(I)-dependent biogenesis of the galactose oxidase redox cofactor.Novel chloroacetamido compound CWR-J02 is an anti-inflammatory glutaredoxin-1 inhibitor.ROXY1 and ROXY2, two Arabidopsis glutaredoxin genes, are required for anther development.RNR (M1M2) reduces nucleotide diphosphates to deoxynucleotide diphosphates (glutaredoxin)RNR (M1M2) reduces nucleotide diphosphates to deoxynucleotide diphosphates (thioredoxin)RNR (M1M2B) reduces nucleotide diphosphates to deoxynucleotide diphosphates (glutaredoxin)RNR (M1M2B) reduces nucleotide diphosphates to deoxynucleotide diphosphates (thioredoxin)Structure analysis of yeast glutaredoxin Grx6 protein produced in
P2860
Q27619480-DB8FA86E-A53C-442C-939E-D4ED94EF95CEQ27653480-F2BED9AD-B1D4-4E7E-AB57-11CD63A2C252Q27653651-B1D5EB8D-327A-4A06-B6B7-8AFFCB98C127Q27662094-B7CBA123-3B2B-4CD4-BBF8-F86DB27F4624Q27673632-3759236F-68E7-49A4-AA15-265A58CB02CFQ30418989-4628CE85-729E-4C1F-84B0-F371CBA1D2FDQ33214225-ADF79339-B095-4C5C-BFD2-29F4C04FB872Q33250405-0702F495-53C1-4FEE-AE4D-CDC9411FB0BEQ33741131-0248A04F-B719-427B-AB44-0FDDF5238365Q35248578-FCF30EC1-6AC8-48B8-A1AA-04BA34A3C6BAQ35950731-139E482A-5E9B-4E8F-A348-73F13FE484D5Q36083038-58600195-F655-4A8F-BBE1-DC431FDD8B53Q38038631-E94477DD-0919-4D24-A1FD-F8168A1B68ECQ38634845-3CBDE960-A822-4272-9B7E-BC45B515EEE8Q40602718-42675289-AA54-4461-9D2A-288F39131140Q40715849-033EA5FB-074D-418E-B223-08D26676179AQ41960433-CB88C82F-4CD8-4077-876A-26464EB89B18Q42025221-F4E4F015-17D5-4AC8-8D24-B5D3E9CF6796Q42170005-5D03FBC4-C052-4715-961D-49CB8DFE1928Q42233328-A17C72E8-D303-4165-A80A-B92F3C8DFC7FQ42411730-61F2DA85-0B73-4842-96FA-4988F8E12BFEQ42706883-ABA08CC7-58E5-4CE0-B3D2-856129E1889EQ43790984-A5A271B7-55AC-4C4E-9230-0EB3E788B2A7Q44388726-65971CB6-D1E6-486B-B44C-07C57E93F065Q46238307-C2B9930F-3E2D-4EB6-BC73-835699B412FAQ46884105-5965980B-D6E2-4950-87C0-1347A44CE97FQ50294592-83DF07F0-D275-488D-9F78-5A27065C36DEQ50294593-578AFD8A-BD77-4466-B0D5-783B893725C9Q50294594-B52FFAB2-D7DC-4D64-BA01-897DD9090766Q50294595-16CCFA09-8EB2-46CC-9076-1E5B572E9D33Q58798877-73DEC125-5D64-4DE2-B3D8-E49D37240B2D
P2860
The NMR solution structure of human glutaredoxin in the fully reduced form
description
1998 nî lūn-bûn
@nan
1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
The NMR solution structure of human glutaredoxin in the fully reduced form
@ast
The NMR solution structure of human glutaredoxin in the fully reduced form
@en
The NMR solution structure of human glutaredoxin in the fully reduced form
@nl
type
label
The NMR solution structure of human glutaredoxin in the fully reduced form
@ast
The NMR solution structure of human glutaredoxin in the fully reduced form
@en
The NMR solution structure of human glutaredoxin in the fully reduced form
@nl
prefLabel
The NMR solution structure of human glutaredoxin in the fully reduced form
@ast
The NMR solution structure of human glutaredoxin in the fully reduced form
@en
The NMR solution structure of human glutaredoxin in the fully reduced form
@nl
P356
P1476
The NMR solution structure of human glutaredoxin in the fully reduced form
@en
P2093
P304
P356
10.1006/JMBI.1998.1913
P407
P577
1998-07-01T00:00:00Z