A novel monoclonal antibody to characterize pathogenic polymers in liver disease associated with alpha1-antitrypsin deficiency. - Wikidata - awgldk - TriplyDB

A novel monoclonal antibody to characterize pathogenic polymers in liver disease associated with alpha1-antitrypsin deficiency.

A novel monoclonal antibody to characterize pathogenic polymers in liver disease associated with alpha1-antitrypsin deficiency.

http://www.wikidata.org/entity/Q34123062

about

Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer The structural diversity in α1-antitrypsin misfolding Alpha-1-antitrypsin deficiency Deficient and Null Variants of SERPINA1 Are Proteotoxic in a Caenorhabditis elegans Model of α1-Antitrypsin Deficiency Discovery of an inhibitor of Z-alpha1 antitrypsin polymerization Improved bi-allelic modification of a transcriptionally silent locus in patient-derived iPSC by Cas9 nickase New Concepts in Alpha-1 Antitrypsin Deficiency Disease Mechanisms.Modeling inherited metabolic disorders of the liver using human induced pluripotent stem cells.Altered native stability is the dominant basis for susceptibility of α1-antitrypsin mutants to polymerization.Defining the mechanism of polymerization in the serpinopathies.The tempered polymerization of human neuroserpin.The role of bronchial epithelial cells in the pathogenesis of COPD in Z-alpha-1 antitrypsin deficiency Three new alpha1-antitrypsin deficiency variants help to define a C-terminal region regulating conformational change and polymerization.The shapes of Z-α1-antitrypsin polymers in solution support the C-terminal domain-swap mechanism of polymerization.The roles of helix I and strand 5A in the folding, function and misfolding of α1-antitrypsin.Therapeutic targeting of misfolding and conformational change in α1-antitrypsin deficiency.Why has it been so difficult to prove the efficacy of alpha-1-antitrypsin replacement therapy? Insights from the study of disease pathogenesis Proinsulin misfolding and endoplasmic reticulum stress during the development and progression of diabetes.How Can We Improve the Detection of Alpha1-Antitrypsin Deficiency?Stem cell-based therapy for α₁-antitrypsin deficiency A single-chain variable fragment intrabody prevents intracellular polymerization of Z α1-antitrypsin while allowing its antiproteinase activity The effects of weekly augmentation therapy in patients with PiZZ α1-antitrypsin deficiency.Deficiency Mutations of Alpha-1 Antitrypsin. Effects on Folding, Function, and Polymerization.Molecular Mechanism of Z α1-Antitrypsin Deficiency Sustained knockdown of a disease-causing gene in patient-specific induced pluripotent stem cells using lentiviral vector-based gene therapy.UDP-glucose:glycoprotein glucosyltransferase (UGGT1) promotes substrate solubility in the endoplasmic reticulum.The endoplasmic reticulum remains functionally connected by vesicular transport after its fragmentation in cells expressing Z-α1-antitrypsin.Endoplasmic reticulum polymers impair luminal protein mobility and sensitize to cellular stress in alpha1-antitrypsin deficiency An antibody that prevents serpin polymerisation acts by inducing a novel allosteric behaviour.Proteostasis strategies for restoring alpha1-antitrypsin deficiency.α(1)-antitrypsin deficiency and inflammation.Unravelling the twists and turns of the serpinopathies.Twenty years of polymers: a personal perspective on alpha-1 antitrypsin deficiency.Recent advances in α-1-antitrypsin deficiency-related lung disease.Broad spectrum of hepatocyte inclusions in humans, animals, and experimental models.Aberrant disulphide bonding contributes to the ER retention of alpha1-antitrypsin deficiency variants.Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.Characterising the association of latency with α(1)-antitrypsin polymerisation using a novel monoclonal antibody Increased ERK signalling promotes inflammatory signalling in primary airway epithelial cells expressing Z α1-antitrypsin An antibody raised against a pathogenic serpin variant induces mutant-like behaviour in the wild-type protein.

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P2860

A novel monoclonal antibody to characterize pathogenic polymers in liver disease associated with alpha1-antitrypsin deficiency.

http://www.wikidata.org/entity/Q34123062

description

2010 nî lūn-bûn

@nan

2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

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2010年論文

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2010年论文

@wuu

name

A novel monoclonal antibody to ...... alpha1-antitrypsin deficiency.

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A novel monoclonal antibody to ...... alpha1-antitrypsin deficiency.

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A novel monoclonal antibody to ...... alpha1-antitrypsin deficiency.

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type

label

A novel monoclonal antibody to ...... alpha1-antitrypsin deficiency.

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A novel monoclonal antibody to ...... alpha1-antitrypsin deficiency.

@en

A novel monoclonal antibody to ...... alpha1-antitrypsin deficiency.

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prefLabel

A novel monoclonal antibody to ...... alpha1-antitrypsin deficiency.

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A novel monoclonal antibody to ...... alpha1-antitrypsin deficiency.

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A novel monoclonal antibody to ...... alpha1-antitrypsin deficiency.

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A novel monoclonal antibody to ...... alpha1-antitrypsin deficiency

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P2093

Bernard Portmann

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David A Lomas

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Didier Belorgey

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

Graeme J Alexander

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Juan Pérez

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Marian Hill

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Nedim Hadzic

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Noor Kalsheker

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Susan Chambers

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Ugo I Ekeowa

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

P2860

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

Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins

Serpin polymerization is prevented by a hydrogen bond network that is centered on his-334 and stabilized by glycerol

Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization

Crystallographic and Cellular Characterisation of Two Mechanisms Stabilising the Native Fold of α1-Antitrypsin: Implications for Disease and Drug Design

Inhibitory conformation of the reactive loop of alpha 1-antitrypsin

Association between conformational mutations in neuroserpin and onset and severity of dementia

Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum

Differential detection of PAS-positive inclusions formed by the Z, Siiyama, and Mmalton variants of alpha1-antitrypsin.

Novel serpinopathy in rat kidney and pancreas induced by overexpression of megsin.

P304

1078-1088

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scholarly article

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10.1002/HEP.23760

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3

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52

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Stefan J Marciniak

Jeffrey Teckman

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2010-09-01T00:00:00Z

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44804922

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20583215

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