A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units
about
The genomics of disulfide bonding and protein stabilization in thermophilesThe modular respiratory complexes involved in hydrogen and sulfur metabolism by heterotrophic hyperthermophilic archaea and their evolutionary implicationsThe high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-IStructures and Functional Implications of an AMP-Binding Cystathionine β-Synthase Domain Protein from a Hyperthermophilic ArchaeonSulfolobus solfataricus thiol redox puzzle: characterization of an atypical protein disulfide oxidoreductaseCalculating ensemble averaged descriptions of protein rigidity without samplingCatalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule MimicsSurR regulates hydrogen production in Pyrococcus furiosus by a sulfur-dependent redox switch.Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus.Stress genes and proteins in the archaea.Cold shock of a hyperthermophilic archaeon: Pyrococcus furiosus exhibits multiple responses to a suboptimal growth temperature with a key role for membrane-bound glycoproteins.Characterization of a thioredoxin-thioredoxin reductase system from the hyperthermophilic bacterium Thermotoga maritima.Disulfide bond formation in prokaryotes: history, diversity and designPosttranslational protein modification in Archaea.Native disulfide bond formation in proteinsProtein disulfides and protein disulfide oxidoreductases in hyperthermophiles.Redox-dependent dynamics of a dual thioredoxin fold protein: evolution of specialized folds.SurR: a transcriptional activator and repressor controlling hydrogen and elemental sulphur metabolism in Pyrococcus furiosusDisulfide bond formation system in Escherichia coli.Effects of metal ions on stability and activity of hyperthermophilic pyrolysin and further stabilization of this enzyme by modification of a Ca2+-binding siteDisulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals.Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1.Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site.Aeropyrum pernix membrane topology of protein VKOR promotes protein disulfide bond formation in two subcellular compartments.Novel disulfide oxidoreductase in search of a function.New Design of a Disulfurating Reagent: Facile and Straightforward Pathway to Unsymmetrical Disulfanes by Copper-Catalyzed Oxidative Cross-Coupling.
P2860
Q24814780-2BFAFF10-B7E1-4A2F-893A-6DE2639B5791Q26859416-9FB38EDE-F4B0-45EA-AB2E-29B231D410B7Q27619480-86D46E97-C268-4542-B480-D2963F8E487BQ27650725-4C3A401C-8177-404A-98A7-3C8F26FA05B5Q27687820-664699F3-013C-4D73-8C3D-A0485BDC761CQ28481155-06CE94A8-8956-4731-A85C-307EDF114543Q29999427-40E30EA9-8C2E-4ABF-B7CE-1B4AE6602A69Q30497306-A84573B7-09A2-472E-8DFD-32CAB9AB7FC3Q31072248-35F960C6-BADA-4D07-A7B9-0ADB090A663BQ33334155-5E0973AB-7355-4586-9A07-DCE0C75EE67AQ33553697-125106D6-CF05-44FA-9EB4-16E032FE87ECQ33648692-E8F6F3C4-5DED-447B-B05D-7A0CB2B00D8CQ33723782-39C489C9-1975-409C-94FE-2B76EFE7858BQ33940312-D435DB35-298F-4E23-98FE-7F1238BC95D6Q34046362-D2C71A5F-741B-4AF7-B860-03EB58203321Q36575813-C7A90FB1-7F65-45AD-AFC9-34823B51B712Q37348276-F4DAF30B-0A0F-4858-8A81-6362CFEC4EA9Q37349856-1494ABA9-D5BF-4259-A730-D325E761782EQ37536471-29CD8EC3-03BC-4660-90A1-AE073A505B85Q37713083-D9BFDFD3-B6FD-4D2B-AA15-4FD3457DA106Q38001127-6E8DAB06-3189-480E-ABE0-B70D181CA32EQ42411869-2C8ADDE4-2BEF-4E9B-AFFC-FBCC37059896Q43029782-31FE4E29-E978-4DBA-A9FE-C9D00E93192CQ44571670-C118A41E-DC90-4B7E-9592-66781B312D44Q46261151-580B0113-3362-4FE5-BA49-763EB5A4BA92Q47842126-886752EB-083C-4C59-BE2F-86742B9AEF7EQ50216709-0A0EC194-0C54-42D8-BC19-A59FD86DDD7A
P2860
A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units
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
A protein disulfide oxidoreduc ...... ins two thioredoxin fold units
@ast
A protein disulfide oxidoreduc ...... ins two thioredoxin fold units
@en
A protein disulfide oxidoreduc ...... ins two thioredoxin fold units
@nl
type
label
A protein disulfide oxidoreduc ...... ins two thioredoxin fold units
@ast
A protein disulfide oxidoreduc ...... ins two thioredoxin fold units
@en
A protein disulfide oxidoreduc ...... ins two thioredoxin fold units
@nl
prefLabel
A protein disulfide oxidoreduc ...... ins two thioredoxin fold units
@ast
A protein disulfide oxidoreduc ...... ins two thioredoxin fold units
@en
A protein disulfide oxidoreduc ...... ins two thioredoxin fold units
@nl
P2093
P2860
P356
P1476
A protein disulfide oxidoreduc ...... ins two thioredoxin fold units
@en
P2093
D de Pascale
G Tibbelin
R Ladenstein
P2860
P2888
P304
P356
10.1038/862
P577
1998-07-01T00:00:00Z
P6179
1008198509