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Article

Aberrant disulphide bonding contributes to the ER retention of alpha1-antitrypsin deficiency variants.

Human molecular genetics - 15 Feb 2016

Ronzoni Riccardo, Berardelli Romina, Medicina Daniela, Sitia Roberto, Gooptu Bibek, Fra Anna Maria

Abstract excerpt

Mutations in alpha1-antitrypsin (AAT) can cause the protein to polymerise and be retained in the endoplasmic reticulum (ER) of hepatocytes. The ensuing systemic AAT deficiency leads to pulmonary emphysema, while intracellular polymers are toxic and cause chronic liver disease. The severity of this process varies considerably between individuals, suggesting the involvement of mechanistic co-factors and potential...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 26647313
DOI: 10.1093/hmg/ddv501

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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.

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