Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide‐binding domain 1 (Q41148574)
scientific article published on October 1, 2010
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(P304) 1917-1931
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(P953) https://europepmc.org/articles/pmc2998726?pdf=render
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20687133/pdf/?tool=EBI
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20687133/?tool=EBI
http://www.proteinscience.org/cgi/content/abstract/19/10/1917
https://europepmc.org/articles/PMC2998726
https://europepmc.org/articles/PMC2998726?pdf=render
https://doi.org/10.1002/pro.479
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fpro.479
https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.479
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(P1476) "Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide‐binding domain 1" (language: en)
"Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1" (language: en)
(P2093) Irina Protasevich
Zhengrong Yang
Chi Wang
Xun Zhao
Spencer Emtage
Diana Wetmore
John F. Hunt
Christie G. Brouillette
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description scientific article published on October 1, 2010

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