Cysteine substitutions reveal dual functions of the amino-terminal tail in cystic fibrosis transmembrane conductance regulator channel gating.
about
CFTR chloride channels are regulated by a SNAP-23/syntaxin 1A complex.ABC transporter architecture and regulatory roles of accessory domains.Insight in eukaryotic ABC transporter function by mutation analysis.Current insights into the role of PKA phosphorylation in CFTR channel activity and the pharmacological rescue of cystic fibrosis disease-causing mutants.Interference with ubiquitination in CFTR modifies stability of core glycosylated and cell surface pools.Cysteine-independent inhibition of the CFTR chloride channel by the cysteine-reactive reagent sodium (2-sulphonatoethyl) methanethiosulphonate.
P2860
Cysteine substitutions reveal dual functions of the amino-terminal tail in cystic fibrosis transmembrane conductance regulator channel gating.
description
2001 nî lūn-bûn
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2001年の論文
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2001年学术文章
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name
Cysteine substitutions reveal ...... ance regulator channel gating.
@en
Cysteine substitutions reveal ...... ance regulator channel gating.
@nl
type
label
Cysteine substitutions reveal ...... ance regulator channel gating.
@en
Cysteine substitutions reveal ...... ance regulator channel gating.
@nl
prefLabel
Cysteine substitutions reveal ...... ance regulator channel gating.
@en
Cysteine substitutions reveal ...... ance regulator channel gating.
@nl
P2860
P356
P1476
Cysteine substitutions reveal ...... ance regulator channel gating.
@en
P2860
P304
35660-35668
P356
10.1074/JBC.M105079200
P407
P577
2001-07-23T00:00:00Z