reference/7964547

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endingPage	1931
issn	1469-896X 0961-8368
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publicationName	Protein science : a publication of the Protein Society
startingPage	1917
bibliographicCitation	Protasevich I, Yang Z, Wang C, Atwell S, Zhao X, Emtage S, Wetmore D, Hunt JF, Brouillette CG. Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. Protein Sci. 2010 Oct;19(10):1917–31. PMID: 20687133; PMCID: PMC2998726.
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date	2010-08-04-04:00^^<http://www.w3.org/2001/XMLSchema#date>
identifier	https://doi.org/10.1002/pro.479 https://pubmed.ncbi.nlm.nih.gov/20687133 https://pubmed.ncbi.nlm.nih.gov/PMC2998726
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language	English
source	https://pubmed.ncbi.nlm.nih.gov/ https://www.crossref.org/
title	Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide‐binding domain 1
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