about
Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase (GILT)ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulumModelling and bioinformatics studies of the human Kappa-class glutathione transferase predict a novel third glutathione transferase family with similarity to prokaryotic 2-hydroxychromene-2-carboxylate isomerasesStructure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamilyTwo pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulumThe CXXCXXC motif determines the folding, structure and stability of human Ero1-LalphaThe role of glutathione S-transferase P in signaling pathways and S-glutathionylation in cancerReactivity of thioredoxin as a protein thiol-disulfide oxidoreductaseThioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology and structure similarity to the theta class enzymeImpact of domain interchange on conformational stability and equilibrium folding of chimeric class micro glutathione transferasesCellular and molecular basis of deiodinase-regulated thyroid hormone signalingCrystal structure of the YffB protein from Pseudomonas aeruginosa suggests a glutathione-dependent thiol reductase functionOn the role of the cis-proline residue in the active site of DsbAThe high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-ISolution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschiiStructural basis for the thioredoxin-like activity profile of the glutaredoxin-like NrdH-redoxin from Escherichia coliShedding light on disulfide bond formation: engineering a redox switch in green fluorescent proteinThe disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.Structural and functional characterization of the Pseudomonas hydroperoxide resistance protein Ohr.Atomic-resolution crystal structure of thioredoxin from the acidophilic bacterium Acetobacter acetiGram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis3‘-Phosphoadenosine-5‘-phosphosulfate Reductase in Complex with Thioredoxin: A Structural Snapshot in the Catalytic Cycle † , ‡Structures of three members of Pfam PF02663 (FmdE) implicated in microbial methanogenesis reveal a conserved α+β core domain and an auxiliary C-terminal treble-clef zinc fingerCrystal structure of the in vivo-assembled Bacillus subtilis Spx/RNA polymerase α subunit C-terminal domain complexA strategic protein in cytochrome c maturation: three-dimensional structure of CcmH and binding to apocytochrome cCrystallographic trapping in the rebeccamycin biosynthetic enzyme RebCSolution structure of selenoprotein W and NMR analysis of its interaction with 14-3-3 proteinsStructural and mechanistic insights into type II trypanosomatid tryparedoxin-dependent peroxidasesStructural and biochemical characterization of the oxidoreductase NmDsbA3 from Neisseria meningitidisStructure-Function Relationship of the Chloroplastic Glutaredoxin S12 with an Atypical WCSYS Active SiteProperties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid ResidueThe Structure of the Bacterial Oxidoreductase Enzyme DsbA in Complex with a Peptide Reveals a Basis for Substrate Specificity in the Catalytic Cycle of DsbA EnzymesCrystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITEAn Extracellular Disulfide Bond Forming Protein (DsbF) from Mycobacterium tuberculosis: Structural, Biochemical, and Gene Expression AnalysisArabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into GlutaredoxinsNMR Structure of Carcinoscorpius rotundicauda Thioredoxin-related Protein 16 and Its Role in Regulating Transcription Factor NF- B ActivitySolution structure of an arsenate reductase-related protein, YffB, from Brucella melitensis , the etiological agent responsible for brucellosisStructural and functional characterization of Helicobacter pylori DsbGSolution structures of Mycobacterium tuberculosis thioredoxin C and models of intact thioredoxin system suggest new approaches to inhibitor and drug designStructural and Mechanistic Insights into Unusual Thiol Disulfide Oxidoreductase
P2860
Q22011094-8BC05A95-9F78-4A9E-A365-D92799979B9CQ22253168-36CA5043-FA3A-4CFD-81A7-C1A51B16FF41Q24530734-454FC573-CCB5-4538-A145-5BA82507CA84Q24533519-AC223CC2-BB47-4598-B9C8-938AEBF700C5Q24550637-92FB0AAA-4655-4447-A3B0-9761CBA63208Q24599012-9F1F1669-31D0-4A5C-9795-A0F9D5433FD3Q24603861-264E12A4-E2B0-4C59-93A3-54F50DCCBB50Q24630110-C36F9FEC-9B95-43CA-859C-B843F822740CQ24644230-93E0B1CD-2B6F-485D-9D4F-76055D21C299Q24645073-71128D65-BD3E-42B7-9DAF-23CCD5E89733Q24648381-857C2625-D341-47E9-A8BF-EC8C784900F3Q24805132-D82C69DC-B217-48B6-81D6-7AD6BD4E2AA4Q27617979-B126171D-9BBE-4649-A6FF-E504AE41E0BEQ27619480-EBC56CEC-2B98-43C6-93B5-F85A27FD2D46Q27630806-1C8EE4EE-E88C-4EF2-919F-78BBC1781F6FQ27633082-BAAAEA51-9A56-4AD8-B908-696D5E2DCF88Q27635911-D170E52E-824B-40B4-8891-6C839C8175D7Q27639655-40A1E87A-7FDA-417A-BEA5-0D6A2341FA8DQ27640170-D22FF081-90F6-43C0-B5B0-5B59A682D7DFQ27640985-0304E95B-2F1D-46F3-AA40-0D28FB949E4BQ27642487-B14042E7-86F5-4E69-AE2B-4A318092B8CEQ27644033-854E8011-0175-42F5-91C4-D8399B16F3EAQ27644457-D46DF561-E2A5-4E61-B795-E2D144360CE8Q27646482-42F21FA5-19D8-4839-8929-450E697CDCAEQ27646618-73D3420B-4DCA-4A72-B99E-F56E0A8E0C11Q27648208-B99F8A15-C8FA-45B4-B695-D5E2A196D691Q27648748-92F9782D-79DD-460F-8FE1-FE989B6B6CEBQ27650739-3698D980-1DAD-471D-84C6-BC210A6A9840Q27651712-EEE9BD9F-2302-4C05-A5A6-7EDC6B8A331BQ27653480-57502268-A398-421B-909E-F64BFA813C61Q27653607-2EF0E987-113D-405B-B5BD-6E706086F718Q27655136-F79B9989-402F-4888-8368-431B6F3D705BQ27656012-580F3D02-36EC-4343-8365-424AAAB61707Q27658897-3DC157C8-4E2E-44BF-BF9B-E69E9FAE7D2BQ27668124-964004FE-D0D1-4A6A-AD0F-B57BD925B9F9Q27670644-B48A71B5-1114-4CEB-B0A6-4BBFECA5C2C1Q27673621-8C78944F-50D4-4042-920A-F6DEA801E064Q27675432-CCBA7415-BD84-4C01-A083-CB5A128CA02BQ27675444-39CE42AD-A931-4910-B862-540969DB7444Q27675878-D493E5E7-2B04-4C92-A1C9-942A3556D3B5
P2860
description
1995 nî lūn-bûn
@nan
1995 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մարտին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Thioredoxin--a fold for all reasons
@ast
Thioredoxin--a fold for all reasons
@en
type
label
Thioredoxin--a fold for all reasons
@ast
Thioredoxin--a fold for all reasons
@en
prefLabel
Thioredoxin--a fold for all reasons
@ast
Thioredoxin--a fold for all reasons
@en
P3181
P1433
P1476
Thioredoxin--a fold for all reasons
@en
P2093
P304
P3181
P356
10.1016/S0969-2126(01)00154-X
P407
P577
1995-03-15T00:00:00Z