Interactions causing the kinetic trap in serpin protein folding - Wikidata - awgldk - TriplyDB

Interactions causing the kinetic trap in serpin protein folding

Interactions causing the kinetic trap in serpin protein folding

http://www.wikidata.org/entity/Q27639675

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The transcription factor p53: not a repressor, solely an activator Serpin polymerization is prevented by a hydrogen bond network that is centered on his-334 and stabilized by glycerol C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease Crystallographic and Cellular Characterisation of Two Mechanisms Stabilising the Native Fold of α1-Antitrypsin: Implications for Disease and Drug Design Therapeutic target-site variability in α1-antitrypsin characterized at high resolution Latent S49P neuroserpin forms polymers in the dementia familial encephalopathy with neuroserpin inclusion bodies In silico assessment of potential druggable pockets on the surface of α1-antitrypsin conformers Reliable protein folding on complex energy landscapes: the free energy reaction path Scaffold protein FHL2 facilitates MDM2-mediated degradation of IER3 to regulate proliferation of cervical cancer cells.Collapse of a long axis: single-molecule Förster resonance energy transfer and serpin equilibrium unfolding.Serpin latency transition at atomic resolution Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular Dynamics Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization.Alpha1-antitrypsin deficiency. 4: Molecular pathophysiology Folding mechanism of the metastable serpin α1-antitrypsin.Smoothing a rugged protein folding landscape by sequence-based redesign.Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.The length of the reactive center loop modulates the latency transition of plasminogen activator inhibitor-1.Specific interactions of serpins in their native forms attenuate their conformational transitions.Functional unfolding of alpha1-antitrypsin probed by hydrogen-deuterium exchange coupled with mass spectrometry.Probing neuroserpin polymerization and interaction with amyloid-beta peptides using single molecule fluorescence.Serpins show structural basis for oligomer toxicity and amyloid ubiquity.Cleaved serpin refolds into the relaxed state via a stressed conformer.On the folding of a structurally complex protein to its metastable active state.Functional analysis of novel alpha-1 antitrypsin variants G320R and V321F.

P2860

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P2860

Interactions causing the kinetic trap in serpin protein folding

http://www.wikidata.org/entity/Q27639675

description

2002 nî lūn-bûn

@nan

2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年学术文章

@wuu

2002年学术文章

@zh-cn

2002年学术文章

@zh-hans

2002年学术文章

@zh-my

2002年学术文章

@zh-sg

2002年學術文章

@yue

name

Interactions causing the kinetic trap in serpin protein folding

@ast

Interactions causing the kinetic trap in serpin protein folding

@en

Interactions causing the kinetic trap in serpin protein folding

@nl

type

label

Interactions causing the kinetic trap in serpin protein folding

@ast

Interactions causing the kinetic trap in serpin protein folding

@en

Interactions causing the kinetic trap in serpin protein folding

@nl

prefLabel

Interactions causing the kinetic trap in serpin protein folding

@ast

Interactions causing the kinetic trap in serpin protein folding

@en

Interactions causing the kinetic trap in serpin protein folding

@nl

P1433

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P2860

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P356

P1433

Journal of Biological Chemistry

P1476

Interactions causing the kinetic trap in serpin protein folding

@en

P2093

Hana Im

http://www.w3.org/2001/XMLSchema#string

Kwang Yeon Hwang

http://www.w3.org/2001/XMLSchema#string

Mi-Sook Woo

http://www.w3.org/2001/XMLSchema#string

Myeong-Hee Yu

http://www.w3.org/2001/XMLSchema#string

P2860

Structure of a serpin-protease complex shows inhibition by deformation

The serpin PAI-1 inhibits cell migration by blocking integrin alpha V beta 3 binding to vitronectin

Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease

PROCHECK: a program to check the stereochemical quality of protein structures

Processing of X-ray diffraction data collected in oscillation mode

The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation

A 2.1 A resolution structure of an uncleaved alpha(1)-antitrypsin shows variability of the reactive center and other loops

Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1

Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition

Structure of influenza haemagglutinin at the pH of membrane fusion

P304

46347-54

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scholarly article

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3348647

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10.1074/JBC.M207682200

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P433

48

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P478

277

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2002-11-29T00:00:00Z

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P698

12244055

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P921

protein folding