about
The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesisStructure of a serpin-enzyme complex probed by cysteine substitutions and fluorescence spectroscopy.Proteomic profiling of urine identifies specific fragments of SERPINA1 and albumin as biomarkers of preeclampsia.Collapse of a long axis: single-molecule Förster resonance energy transfer and serpin equilibrium unfolding.Altered native stability is the dominant basis for susceptibility of α1-antitrypsin mutants to polymerization.The high resolution crystal structure of a native thermostable serpin reveals the complex mechanism underpinning the stressed to relaxed transition.The roles of helix I and strand 5A in the folding, function and misfolding of α1-antitrypsin.Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap.Therapeutic targeting of misfolding and conformational change in α1-antitrypsin deficiency.Folding mechanism of the metastable serpin α1-antitrypsin.Deficiency Mutations of Alpha-1 Antitrypsin. Effects on Folding, Function, and Polymerization.Molecular Mechanism of Z α1-Antitrypsin DeficiencySmoothing a rugged protein folding landscape by sequence-based redesign.An antibody that prevents serpin polymerisation acts by inducing a novel allosteric behaviour.Probing serpin conformational change using mass spectrometry and related methods.alpha(1)-antitrypsin can increase insulin-induced mitogenesis in various fibroblast and epithelial cell lines.Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerizationStructural dynamics associated with intermediate formation in an archetypal conformational disease.Two latent and two hyperstable polymeric forms of human neuroserpin.Local and global effects of a cavity filling mutation in a metastable serpin.The high resolution crystal structure of the human tumor suppressor maspin reveals a novel conformational switch in the G-helix.Effects of glycosylation on the stability and flexibility of a metastable protein: the human serpin α(1)-antitrypsin.Alleviation of a defect in protein folding by increasing the rate of subunit assembly.Osmolytes as modulators of conformational changes in serpins.The selective inhibition of serpin aggregation by the molecular chaperone, alpha-crystallin, indicates a nucleation-dependent specificity.Probing the folding pathway of a consensus serpin using single tryptophan mutants.On the folding of a structurally complex protein to its metastable active state.All-Atom Simulations Reveal How Single-Point Mutations Promote Serpin Misfolding
P2860
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P2860
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
Probing the unfolding pathway of alpha1-antitrypsin.
@en
Probing the unfolding pathway of alpha1-antitrypsin.
@nl
type
label
Probing the unfolding pathway of alpha1-antitrypsin.
@en
Probing the unfolding pathway of alpha1-antitrypsin.
@nl
prefLabel
Probing the unfolding pathway of alpha1-antitrypsin.
@en
Probing the unfolding pathway of alpha1-antitrypsin.
@nl
P2093
P2860
P356
P1476
Probing the unfolding pathway of alpha1-antitrypsin.
@en
P2093
P2860
P304
P356
10.1074/JBC.274.14.9482
P407
P577
1999-04-01T00:00:00Z