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

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

The FEBS journal - 1 Jul 2024

Kamuda Kamila, Ronzoni Riccardo, Majumdar Avik, Guan Fiona H X, Irving James A, Lomas David A

Abstract excerpt

Mutants of alpha-1-antitrypsin cause the protein to self-associate and form ordered aggregates ('polymers') that are retained within hepatocytes, resulting in a predisposition to the development of liver disease. The associated reduction in secretion, and for some mutants, impairment of function, leads to a failure to protect lung tissue against proteases released during the inflammatory response and an increased...

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 Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endoplasmic Reticulum

Share to Models, Molecular

Share to Mutation

Share to Protein Aggregates

Share to Protein Aggregation, Pathological

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 38523412
DOI: 10.1111/febs.17121
PMCID: PMC11753496

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

A novel pathological mutant reveals the role of torsional flexibility in the serpin breach in adoption of an aggregation-prone intermediate.PMID 38523412Read ↗

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

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

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

Protein misfolding and the serpinopathies.Semantic proximity Read ↗

A protein family under 'stress' - serpin stability, folding and misfolding.Semantic proximity Read ↗

Aberrant disulphide bonding contributes to the ER retention of alpha1-antitrypsin deficiency variants.Semantic proximity Read ↗

Molecular characterization of the new defective P(brescia) alpha1-antitrypsin allele.Semantic proximity Read ↗

Alpha 1-antitrypsin deficiency. A conformational disease.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 ↗

The conformational landscape of a serpin N-terminal subdomain facilitates folding and in-cell quality controlSemantic proximity Read ↗

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

Polymers and inflammation: disease mechanisms of the serpinopathies.Semantic proximity Read ↗

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