Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites.
about
Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli.Molecular dynamics simulation of Escherichia coli dihydrofolate reductase and its protein fragments: relative stabilities in experiment and simulationsTobacco budworm dihydrofolate reductase is a promising target for insecticide discovery.The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli.Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase.Analysis of kinetics using a hybrid maximum-entropy/nonlinear-least-squares method: application to protein folding.An NADH-induced conformational change that mediates the sequential 3 beta-hydroxysteroid dehydrogenase/isomerase activities is supported by affinity labeling and the time-dependent activation of isomerase.Structure of a partially unfolded form of Escherichia coli dihydrofolate reductase provides insight into its folding pathway.Cooperative effects of potassium, magnesium, and magnesium-ADP on the release of Escherichia coli dihydrofolate reductase from the chaperonin GroEL.Functions of the gene products of Escherichia coli.A thermodynamic coupling mechanism for GroEL-mediated unfolding.Thermal unfolding molecular dynamics simulation of Escherichia coli dihydrofolate reductase: thermal stability of protein domains and unfolding pathway.Ligand binding to a high-energy partially unfolded protein.Molecular dynamics simulation of thermal unfolding of Thermatoga maritima DHFR.Highly site-selective stability increases by glycosylation of dihydrofolate reductase.Analysis of a conditional degradation signal in yeast and mammalian cells.Characterization of a highly conserved FAD-binding site in human monoamine oxidase B.Stabilization of hyperactive dihydrofolate reductase by cyanocysteine-mediated backbone cyclization.
P2860
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P2860
Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites.
description
1990 nî lūn-bûn
@nan
1990 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Refolding of Escherichia coli ...... on of substrate binding sites.
@ast
Refolding of Escherichia coli ...... on of substrate binding sites.
@en
type
label
Refolding of Escherichia coli ...... on of substrate binding sites.
@ast
Refolding of Escherichia coli ...... on of substrate binding sites.
@en
prefLabel
Refolding of Escherichia coli ...... on of substrate binding sites.
@ast
Refolding of Escherichia coli ...... on of substrate binding sites.
@en
P2860
P356
P1476
Refolding of Escherichia coli ...... on of substrate binding sites.
@en
P2093
P2860
P304
P356
10.1073/PNAS.87.12.4413
P407
P577
1990-06-01T00:00:00Z