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Article

CFTR trafficking mutations disrupt cotranslational protein folding by targeting biosynthetic intermediates.

Nature communications - 26 Aug 2020

Shishido Hideki, Yoon Jae Seok, Yang Zhongying, Skach William R

Abstract excerpt

Protein misfolding causes a wide spectrum of human disease, and therapies that target misfolding are transforming the clinical care of cystic fibrosis. Despite this success, however, very little is known about how disease-causing mutations affect the de novo folding landscape. Here we show that inherited, disease-causing mutations located within the first nucleotide-binding domain (NBD1) of the cystic fibrosis...

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Share to Cystic Fibrosis
Share to Cystic Fibrosis Transmembrane Conductance Regulator

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 32848127
DOI: 10.1038/s41467-020-18101-8
PMCID: PMC7450043

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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CFTR trafficking mutations disrupt cotranslational protein folding by targeting biosynthetic intermediates.PMID 32848127Read ↗

Cystic fibrosis: a disease of altered protein folding.Semantic proximity Read ↗

The primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domain.Semantic proximity Read ↗

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Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding.Semantic proximity Read ↗

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Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function.Semantic proximity Read ↗

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