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Article

Structural basis for misfolding at a disease phenotypic position in CFTR: comparison of TM3/4 helix-loop-helix constructs with TM4 peptides.

Biochimica et biophysica acta - 1 Jan 2012

Mulvihill Cory M, Deber Charles M

Abstract excerpt

Understanding the residue-dependent effects of disease-phenotypic mutations in multi-spanning membrane proteins is an essential step toward the development of corrective therapies. As a systematic approach to further elucidate mutant-dependent mis-folding consequences, we prepared two libraries: one consisting of 20 helix-loop-helix ("hairpin") constructs derived from helices 3 and 4 of the human cystic fibrosis...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 21996038
DOI: 10.1016/j.bbamem.2011.09.027

Genes

CFTR
SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

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Structural basis for misfolding at a disease phenotypic position in CFTR: comparison of TM3/4 helix-loop-helix constructs with TM4 peptides.PMID 21996038Read ↗

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