CFTR: the nucleotide binding folds regulate the accessibility and stability of the activated state
about
Anion transport in heartA cluster of negative charges at the amino terminal tail of CFTR regulates ATP-dependent channel gatingCystic fibrosis transmembrane conductance regulator. Structure and function of an epithelial chloride channel.Cystic fibrosis transmembrane conductance regulator (CFTR) anion binding as a probe of the poreRegulation of recombinant cardiac cystic fibrosis transmembrane conductance regulator chloride channels by protein kinase C.CFTR: a cysteine at position 338 in TM6 senses a positive electrostatic potential in the pore.The hydroxyl group of S685 in Walker A motif and the carboxyl group of D792 in Walker B motif of NBD1 play a crucial role for multidrug resistance protein folding and function.CFTR: Ligand exchange between a permeant anion ([Au(CN)2]-) and an engineered cysteine (T338C) blocks the pore.Cystic fibrosis transmembrane conductance regulator: a molecular model defines the architecture of the anion conduction path and locates a "bottleneck" in the pore.G551D and G1349D, two CF-associated mutations in the signature sequences of CFTR, exhibit distinct gating defectsInsight in eukaryotic ABC transporter function by mutation analysis.Gating of cystic fibrosis transmembrane conductance regulator chloride channels by adenosine triphosphate hydrolysis. Quantitative analysis of a cyclic gating schemeSevered molecules functionally define the boundaries of the cystic fibrosis transmembrane conductance regulator's NH(2)-terminal nucleotide binding domain.CFTR: covalent modification of cysteine-substituted channels expressed in Xenopus oocytes shows that activation is due to the opening of channels resident in the plasma membraneCFTR: covalent and noncovalent modification suggests a role for fixed charges in anion conduction.Positioning of extracellular loop 1 affects pore gating of the cystic fibrosis transmembrane conductance regulatorA mutation in CFTR modifies the effects of the adenylate kinase inhibitor Ap5A on channel gating.CLC-0 and CFTR: chloride channels evolved from transporters.Regulation of CFTR Cl- channel gating by ATP binding and hydrolysis.Mutation of the aromatic amino acid interacting with adenine moiety of ATP to a polar residue alters the properties of multidrug resistance protein 1.Cytoplasmic loop three of cystic fibrosis transmembrane conductance regulator contributes to regulation of chloride channel activity.Cystic fibrosis transmembrane conductance regulator: using differential reactivity toward channel-permeant and channel-impermeant thiol-reactive probes to test a molecular model for the pore.Conformational changes in a pore-lining helix coupled to cystic fibrosis transmembrane conductance regulator channel gating.Pharmacology of CFTR chloride channel activity.Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis.
P2860
Q28141703-800F4CDA-9FB3-46C0-92DD-0F0BC0A6B257Q28361675-D6528014-ABD2-4721-988C-5A24A212F622Q33830343-1437EA36-7AAF-42FD-8639-4F7F7CBE46EFQ34167378-1422E532-868F-4CDC-B1DC-7072719D3219Q34170201-90FCCA9F-BEAE-4750-B78A-12044290E4A5Q34188063-5E1C834B-E582-4B2B-9FE6-DD96BBDC1F7CQ34201794-1A83FAC2-AB85-4746-A841-04E22E28CB66Q34984671-D2412AAC-543C-4949-8EF9-98ECB179D13CQ35862414-310FD7D1-5ACF-4636-A78D-4325FB369636Q36296010-8F47299A-67BD-443B-B6DC-9975BA08F23BQ36379776-EDC542F1-FF6E-48B2-9D30-9B88448CFCBDQ36412100-A0BBFAC7-BF39-4C0B-AF8C-5709B9BED72EQ36436335-77BE98F7-F304-442B-BA3F-460866E423C3Q36444758-FB1DCF01-E44B-4303-A2A3-D6497DCFBE9DQ36444784-272B84CC-71A6-45ED-9451-DA72FEEFEE35Q36638473-5C1A6434-BAF8-419D-BC0D-BCE4A7A5AD7CQ36981695-A5A5CF8B-0C75-4A2D-9864-5BDA849256E9Q37129332-69F64CDF-31FD-4B4F-BCCA-77D1892C7108Q37238263-7464793A-4479-4473-9C50-FF1643D12F88Q40517912-A9BB5906-FC9F-497F-BC6B-EF4F276CA942Q41155403-DC3D4323-2B6C-40F3-9390-D4E4F69152DEQ42588798-194F3884-0384-40C6-B439-325E08E20ACFQ46868628-745EFCDE-03F1-4A1B-835D-543B16403E9DQ53938452-78B9CD45-A8A5-4C1C-93A7-12FE7AE041CCQ53938455-5A97E765-8FA4-495F-8956-F111FF1B873F
P2860
CFTR: the nucleotide binding folds regulate the accessibility and stability of the activated state
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
CFTR: the nucleotide binding f ...... ability of the activated state
@ast
CFTR: the nucleotide binding f ...... ability of the activated state
@en
type
label
CFTR: the nucleotide binding f ...... ability of the activated state
@ast
CFTR: the nucleotide binding f ...... ability of the activated state
@en
prefLabel
CFTR: the nucleotide binding f ...... ability of the activated state
@ast
CFTR: the nucleotide binding f ...... ability of the activated state
@en
P2093
P2860
P356
P1476
CFTR: the nucleotide binding f ...... ability of the activated state
@en
P2093
D C Dawson
D J Wilkinson
F S Collins
M K Mansoura
P Y Watson
P2860
P304
P356
10.1085/JGP.107.1.103
P577
1996-01-01T00:00:00Z