Interactions causing the kinetic trap in serpin protein folding
about
The transcription factor p53: not a repressor, solely an activatorSerpin polymerization is prevented by a hydrogen bond network that is centered on his-334 and stabilized by glycerolC1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational diseaseCrystallographic and Cellular Characterisation of Two Mechanisms Stabilising the Native Fold of α1-Antitrypsin: Implications for Disease and Drug DesignTherapeutic target-site variability in α1-antitrypsin characterized at high resolutionLatent S49P neuroserpin forms polymers in the dementia familial encephalopathy with neuroserpin inclusion bodiesIn silico assessment of potential druggable pockets on the surface of α1-antitrypsin conformersReliable protein folding on complex energy landscapes: the free energy reaction pathScaffold 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 resolutionFunctional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular DynamicsSerpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization.Alpha1-antitrypsin deficiency. 4: Molecular pathophysiologyFolding 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
description
2002 nî lūn-bûn
@nan
2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի նոյեմբերին հրատարակված գիտական հոդված
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2002年の論文
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2002年学术文章
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2002年学术文章
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2002年学术文章
@zh-hans
2002年学术文章
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2002年学术文章
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2002年學術文章
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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
P2093
P2860
P3181
P356
P1476
Interactions causing the kinetic trap in serpin protein folding
@en
P2093
Kwang Yeon Hwang
Mi-Sook Woo
Myeong-Hee Yu
P2860
P304
P3181
P356
10.1074/JBC.M207682200
P407
P577
2002-11-29T00:00:00Z