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Article

High-resolution ex vivo NMR spectroscopy of human Z α1-antitrypsin.

Nature communications - 11 Dec 2020

Jagger Alistair M, Waudby Christopher A, Irving James A, Christodoulou John, Lomas David A

Abstract excerpt

Genetic mutations predispose the serine protease inhibitor α1-antitrypsin to misfolding and polymerisation within hepatocytes, causing liver disease and chronic obstructive pulmonary disease. This misfolding occurs via a transiently populated intermediate state, but our structural understanding of this process is limited by the instability of recombinant α1-antitrypsin variants in solution. Here we apply NMR...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 33311470
DOI: 10.1038/s41467-020-20147-7
PMCID: PMC7732992

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.

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