Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage - Wikidata - awgldk - TriplyDB

Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage

Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage

http://www.wikidata.org/entity/Q57980256

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α-1 Antitrypsin regulates human neutrophil chemotaxis induced by soluble immune complexes and IL-8 The structural diversity in α1-antitrypsin misfolding Small molecules block the polymerization of Z alpha1-antitrypsin and increase the clearance of intracellular aggregates The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology Serpin polymerization is prevented by a hydrogen bond network that is centered on his-334 and stabilized by glycerol Crystallographic and Cellular Characterisation of Two Mechanisms Stabilising the Native Fold of α1-Antitrypsin: Implications for Disease and Drug Design The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesis Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum Latent S49P neuroserpin forms polymers in the dementia familial encephalopathy with neuroserpin inclusion bodies Protein fiber linear dichroism for structure determination and kinetics in a low-volume, low-wavelength couette flow cell Polymerization of plasminogen activator inhibitor-1.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.A novel monoclonal antibody to characterize pathogenic polymers in liver disease associated with alpha1-antitrypsin deficiency.Familial conformational diseases and dementias.The tempered polymerization of human neuroserpin.Alpha-1 antitrypsin deficiency Mechanisms of liver injury relevant to pediatric hepatology.Blocking formation of large protein aggregates by small peptides.Protein misfolding and the serpinopathies.Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular Dynamics Mixture-based combinatorial libraries from small individual peptide libraries: a case study on α1-antitrypsin deficiency.Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization.Polymers of Z alpha1-antitrypsin co-localize with neutrophils in emphysematous alveoli and are chemotactic in vivo Alpha1-antitrypsin deficiency. 4: Molecular pathophysiology Folding mechanism of the metastable serpin α1-antitrypsin.Fluorescence correlation spectroscopic study of serpin depolymerization by computationally designed peptides.SVIP regulates Z variant alpha-1 antitrypsin retro-translocation by inhibiting ubiquitin ligase gp78.Encapsulation of alpha-1 antitrypsin in PLGA nanoparticles: in vitro characterization as an effective aerosol formulation in pulmonary diseases.The selective advantage of alpha1-antitrypsin deficiency.The human serpin proteinase inhibitor-9 self-associates at physiological temperatures.The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB.So how do you know you have a macromolecular complex?The design of a new truncated and engineered alpha1-antitrypsin based on theoretical studies: an antiprotease therapeutics for pulmonary diseases.Neuroserpin polymers activate NF-kappaB by a calcium signaling pathway that is independent of the unfolded protein response.Smoothing a rugged protein folding landscape by sequence-based redesign.alpha1-Antitrypsin deficiency, chronic obstructive pulmonary disease and the serpinopathies.An antibody that prevents serpin polymerisation acts by inducing a novel allosteric behaviour.Unravelling the twists and turns of the serpinopathies.Probing serpin conformational change using mass spectrometry and related methods.

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Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage

http://www.wikidata.org/entity/Q57980256

description

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

im August 2000 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published in Journal of Biological Chemistry

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в серпні 2000

@uk

name

Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage

@en

Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage

@nl

type

label

Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage

@en

Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage

@nl

prefLabel

Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage

@en

Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage

@nl

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Journal of Biological Chemistry

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Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage

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David A Lomas

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

Pasupathy Sivasothy

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

Peter G. W. Gettins

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

Timothy R. Dafforn

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

P2860

Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn-->Asp)

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

Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins

The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion

Topography of a 2.0 Å structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational disease

The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions

Biological implications of a 3 A structure of dimeric antithrombin

Inhibitory conformation of the reactive loop of alpha 1-antitrypsin

Implications for function and therapy of a 2.9 A structure of binary-complexed antithrombin

Plasminogen-activator inhibitor type 2 (PAI-2) is a spontaneously polymerising SERPIN. Biochemical characterisation of the recombinant intracellular and extracellular forms

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33663-33668

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scholarly article

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10.1074/JBC.M004054200

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P433

43

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275

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2000-08-02T00:00:00Z

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10924508

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