How small peptides block and reverse serpin polymerisation.
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Preventing serpin aggregation: The molecular mechanism of citrate action upon antitrypsin unfoldingCrystallographic and Cellular Characterisation of Two Mechanisms Stabilising the Native Fold of α1-Antitrypsin: Implications for Disease and Drug DesignDefining the mechanism of polymerization in the serpinopathies.Small Molecule Probes That Perturb A Protein-protein Interface In AntithrombinBlocking formation of large protein aggregates by small peptides.Use of a small peptide fragment as an inhibitor of insulin fibrillation process: a study by high and low resolution spectroscopyMixture-based combinatorial libraries from small individual peptide libraries: a case study on α1-antitrypsin deficiency.A single-chain variable fragment intrabody prevents intracellular polymerization of Z α1-antitrypsin while allowing its antiproteinase activityFluorescence correlation spectroscopic study of serpin depolymerization by computationally designed peptides.Molecular Mechanism of Z α1-Antitrypsin Deficiencyalpha1-Antitrypsin deficiency, chronic obstructive pulmonary disease and the serpinopathies.An antibody that prevents serpin polymerisation acts by inducing a novel allosteric behaviour.Twenty years of polymers: a personal perspective on alpha-1 antitrypsin deficiency.Recent advances in α-1-antitrypsin deficiency-related lung disease.Structural differences between active forms of plasminogen activator inhibitor type 1 revealed by conformationally sensitive ligands.Small-molecule peptides inhibit Z alpha1-antitrypsin polymerization.An antibody raised against a pathogenic serpin variant induces mutant-like behaviour in the wild-type protein.An integrative approach combining ion mobility mass spectrometry, X-ray crystallography, and nuclear magnetic resonance spectroscopy to study the conformational dynamics of α1 -antitrypsin upon ligand binding.A peptide mimicking the C-terminal part of the reactive center loop induces the transition to the latent form of plasminogen activator inhibitor type-1.The structural basis of serpin polymerization studied by hydrogen/deuterium exchange and mass spectrometry.Loop-sheet mechanism of serpin polymerization tested by reactive center loop mutations.The mechanism of fibril formation of a non-inhibitory serpin ovalbumin revealed by the identification of amyloidogenic core regions.Serpins show structural basis for oligomer toxicity and amyloid ubiquity.Molecular contortionism - on the physical limits of serpin 'loop-sheet' polymers.Reactive centre loop mutants of α-1-antitrypsin reveal position-specific effects on intermediate formation along the polymerization pathway.Identification of a 4-mer Peptide Inhibitor that Effectively Blocks the Polymerization of Pathogenic Z α1-Antitrypsin
P2860
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P2860
How small peptides block and reverse serpin polymerisation.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年學術文章
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name
How small peptides block and reverse serpin polymerisation.
@en
How small peptides block and reverse serpin polymerisation.
@nl
type
label
How small peptides block and reverse serpin polymerisation.
@en
How small peptides block and reverse serpin polymerisation.
@nl
prefLabel
How small peptides block and reverse serpin polymerisation.
@en
How small peptides block and reverse serpin polymerisation.
@nl
P2093
P1476
How small peptides block and reverse serpin polymerisation
@en
P2093
David A Lomas
James A Huntington
Pasupathy Sivasothy
Penelope E Stein
Robin W Carrell
P304
P356
10.1016/J.JMB.2004.07.078
P407
P50
P577
2004-09-01T00:00:00Z