Mutation of conserved residues in Escherichia coli thioredoxin: effects on stability and function
about
Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductaseCrystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanismMycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of MycobacteriaA relationship between protein stability and protein functionHow thioredoxin dissociates its mixed disulfideThe regulation of N-methyl-D-aspartate receptors by Src kinase.The molecular determinants of the increased reduction potential of the rubredoxin domain of rubrerythrin relative to rubredoxin.Protein contributions to redox potentials of homologous rubredoxins: an energy minimization study.Enzyme-like proteins by computational designStructural origins of redox potentials in Fe-S proteins: electrostatic potentials of crystal structuresPrediction of reduction potential changes in rubredoxin: a molecular mechanics approach.Amino acid residues important for folding of thioredoxin are revealed only by study of the physiologically relevant reduced form of the protein.Structure-based identification of catalytic residues.On the non-respect of the thermodynamic cycle by DsbA variants.A bacterial thioredoxin-like protein that is exposed to the periplasm has redox properties comparable with those of cytoplasmic thioredoxins.Identification and functional characterization of thioredoxin from Trypanosoma brucei brucei.Conservative substitutions in the hydrophobic core of Rhodobacter sphaeroides thioredoxin produce distinct functional effects.Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis.Functional and physicochemical characterization of the thioredoxin system in Trypanosoma brucei.Expression, purification and molecular structure modeling of thioredoxin (Trx) and thioredoxin reductase (TrxR) from Acidithiobacillus ferrooxidans.Role of electrostatic interactions on the affinity of thioredoxin for target proteins. Recognition of chloroplast fructose-1, 6-bisphosphatase by mutant Escherichia coli thioredoxins.Trypanosoma brucei tryparedoxin, a thioredoxin-like protein in African trypanosomes.Kinetic-based trapping by intervening sequence variants of the active sites of protein-disulfide isomerase identifies platelet protein substrates.
P2860
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P2860
Mutation of conserved residues in Escherichia coli thioredoxin: effects on stability and function
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
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1992年學術文章
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1992年學術文章
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name
Mutation of conserved residues ...... ects on stability and function
@ast
Mutation of conserved residues ...... ects on stability and function
@en
type
label
Mutation of conserved residues ...... ects on stability and function
@ast
Mutation of conserved residues ...... ects on stability and function
@en
prefLabel
Mutation of conserved residues ...... ects on stability and function
@ast
Mutation of conserved residues ...... ects on stability and function
@en
P2860
P356
P1433
P1476
Mutation of conserved residues ...... ects on stability and function
@en
P2093
Gleason FK
P2860
P304
P356
10.1002/PRO.5560010507
P577
1992-05-01T00:00:00Z