Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Alpha1-antitrypsin deficiency. 4: Molecular pathophysiology.

Thorax - 1 Jun 2004

Lomas D A, Parfrey H

Abstract excerpt

The molecular basis of alpha(1)-antitrypsin deficiency is reviewed and is shown to be due to the accumulation of mutant protein as ordered polymers within the endoplasmic reticulum of hepatocytes. The current goals are to determine the cellular response to polymeric alpha(1)-antitrypsin and to develop therapeutic strategies to block polymerisation in vivo.

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to alpha 1-Antitrypsin
Share to alpha 1-Antitrypsin Deficiency
Share to Liver Diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lung Diseases

Share to Mutation

Share to Peptidase Inhibition and Analysis

Share to Polymers

Share to Protease and Inhibitor Mechanisms

Source

Open in PubMed Open full text

Identifiers

PMID: 15170041
DOI: 10.1136/thx.2003.006528
PMCID: PMC1747018

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Alpha1-antitrypsin deficiency. 4: Molecular pathophysiology.PMID 15170041Read ↗

Endoplasmic reticulum polymers impair luminal protein mobility and sensitize to cellular stress in alpha1-antitrypsin deficiency.Semantic proximity Read ↗

New Concepts in Alpha-1 Antitrypsin Deficiency Disease Mechanisms.Semantic proximity Read ↗

Accumulation of mutant alpha1-antitrypsin Z in the endoplasmic reticulum activates caspases-4 and -12, NFkappaB, and BAP31 but not the unfolded protein response.Semantic proximity Read ↗

Both terminal misfolding and polymerisation contribute to disease-relevant responses in cell models of α <sub>1</sub> -antitrypsin deficiency-associated liver diseaseSemantic proximity Read ↗

Alpha-1-antitrypsin deficiency: Genetic variations, clinical manifestations and therapeutic interventions.Semantic proximity Read ↗

Liver disease in alpha-1 antitrypsin deficiency: current understanding and future therapy.Semantic proximity Read ↗

Alpha(1)-antitrypsin deficiency, liver disease and emphysema.Semantic proximity Read ↗

Alpha-1-antitrypsin deficiency: a new paradigm for hepatocellular carcinoma in genetic liver disease.Semantic proximity Read ↗

Three new alpha1-antitrypsin deficiency variants help to define a C-terminal region regulating conformational change and polymerization.Semantic proximity Read ↗

The Alpha-1 Antitrypsin Polymer Load Correlates With Hepatocyte Senescence, Fibrosis Stage and Liver-Related MortalitySemantic proximity Read ↗

Circulating polymers in α1-antitrypsin deficiency.Semantic proximity Read ↗

alpha 1-Antitrypsin Mmalton (Phe52-deleted) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.