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

Conformational properties of the disease-causing Z variant of α1-antitrypsin revealed by theory and experiment.

Biophysical journal - 20 Jun 2012

Kass Itamar, Knaupp Anja S, Bottomley Stephen P, Buckle Ashley M

Abstract excerpt

The human serine protease inhibitor (serpin) α-1 antitrypsin (α1-AT) protects tissues from proteases of inflammatory cells. The most common disease-causing mutation in α1-AT is the Z-mutation (E342K) that results in an increased propensity of α1-AT to polymerize in the ER of hepatocytes, leading to a lack of secretion into the circulation. The structural consequences of this mutation, however, remain elusive. We...

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 Disease
Share to Protein Stability

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Protein Structure, Quaternary

Share to Solvents

Share to Spectrometry, Fluorescence

Share to Static Electricity

Share to Stereoisomerism

Source

Open in PubMed Open full text

Identifiers

PMID: 22735536
DOI: 10.1016/j.bpj.2012.05.023
PMCID: PMC3379022

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conformational properties of the disease-causing Z variant of α1-antitrypsin revealed by theory and experiment.PMID 22735536Read ↗

Molecular insights on the mechanism of <i>α</i> <sub>1</sub> -antitrypsin condensate formation and maturationSemantic proximity Read ↗

Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization.Semantic proximity Read ↗

Alpha 1-antitrypsin deficiency. A conformational disease.Semantic proximity Read ↗

The Z mutation alters the global structural dynamics of α1-antitrypsin.Semantic proximity Read ↗

A protein structural approach to the solution of biological problems: alpha 1-antitrypsin as a recent example.Semantic proximity Read ↗

Reactive Center Loop Insertion in α-1-Antitrypsin Captured by Accelerated Molecular Dynamics Simulation.Semantic proximity Read ↗

A novel pathological mutant reveals the role of torsional flexibility in the serpin breach in adoption of an aggregation-prone intermediate.Semantic proximity Read ↗

The effect of the Glu342Lys mutation in alpha1-antitrypsin on its structure, studied by molecular modelling methods.Semantic proximity Read ↗

Reactive centre loop mutants of α-1-antitrypsin reveal position-specific effects on intermediate formation along the polymerization pathway.Semantic proximity Read ↗

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.Semantic proximity Read ↗

Development of a small molecule that corrects misfolding and increases secretion of Z α <sub>1</sub> -antitrypsinSemantic proximity Read ↗

Small molecules block the polymerization of Z alpha1-antitrypsin and increase the clearance of intracellular aggregates.Semantic proximity Read ↗

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