Non-pore lining amino acid side chains influence anion selectivity of the human CFTR Cl- channel expressed in mammalian cell lines.
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Relationship between anion binding and anion permeability revealed by mutagenesis within the cystic fibrosis transmembrane conductance regulator chloride channel poreDual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation.Molecular determinants of anion selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel pore.Interaction between permeation and gating in a putative pore domain mutant in the cystic fibrosis transmembrane conductance regulator.CFTR: a cysteine at position 338 in TM6 senses a positive electrostatic potential in the pore.Localizing a gate in CFTR.Full-open and closed CFTR channels, with lateral tunnels from the cytoplasm and an alternative position of the F508 region, as revealed by molecular dynamics.Cystic fibrosis transmembrane conductance regulator: a molecular model defines the architecture of the anion conduction path and locates a "bottleneck" in the pore.Mechanism of chloride permeation in the cystic fibrosis transmembrane conductance regulator chloride channel.Insight in eukaryotic ABC transporter function by mutation analysis.Voltage-dependent gating of the cystic fibrosis transmembrane conductance regulator Cl- channel.Cystic fibrosis transmembrane conductance regulator. Physical basis for lyotropic anion selectivity patternsCFTR: covalent and noncovalent modification suggests a role for fixed charges in anion conduction.Functional architecture of the CFTR chloride channel.A reciprocating twin-channel model for ABC transporters.Nucleotide-binding domain 1 of cystic fibrosis transmembrane conductance regulator production of a suitable protein for structural studies.Architecture and functional properties of the CFTR channel pore.Regulation of conductance by the number of fixed positive charges in the intracellular vestibule of the CFTR chloride channel pore.Mutation-induced blocker permeability and multiion block of the CFTR chloride channel pore.Alternating access to the transmembrane domain of the ATP-binding cassette protein cystic fibrosis transmembrane conductance regulator (ABCC7).On the origin of asymmetric interactions between permeant anions and the cystic fibrosis transmembrane conductance regulator chloride channel pore.Direct comparison of the functional roles played by different transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore.Introduction to section IV: biophysical methods to approach CFTR structure.Stable dimeric assembly of the second membrane-spanning domain of CFTR (cystic fibrosis transmembrane conductance regulator) reconstitutes a chloride-selective pore.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.Relative contribution of different transmembrane segments to the CFTR chloride channel pore.Mechanism of lonidamine inhibition of the CFTR chloride channel.Identification of a region of strong discrimination in the pore of CFTR.Molecular determinants and role of an anion binding site in the external mouth of the CFTR chloride channel pore.Extent of the selectivity filter conferred by the sixth transmembrane region in the CFTR chloride channel pore.A combined analysis of the cystic fibrosis transmembrane conductance regulator: implications for structure and disease models.Functional differences in pore properties between wild-type and cysteine-less forms of the CFTR chloride channel.Functional arrangement of the 12th transmembrane region in the CFTR chloride channel pore based on functional investigation of a cysteine-less CFTR variant.Structural mechanisms of CFTR function and dysfunction.ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.
P2860
Q28349189-195C8E50-B6D3-4FDE-A687-44D87EE63CBDQ34096449-8B990FD0-A259-40CA-970B-C27144E12598Q34173245-900364C4-2E3E-4CD5-9524-E7DCE93F872CQ34173438-31AB504A-451F-4E2F-AA26-F6DB9BA86D05Q34188063-5B5A3759-2F53-4135-8983-D7AA6CB0D403Q35134541-4EC446C3-A825-4BFD-8708-F9021E86804BQ35306053-2923B2C7-BF18-4E81-A1DD-62F947DB7513Q35862414-382E68C5-F627-4111-87F4-4F16F21151F8Q36255649-2B9E67F5-F484-47E1-B0FD-167CD2A782F6Q36379776-1CBF67E1-E429-45E1-9E8B-F96A2C8E47E8Q36436627-7089356C-634A-4C22-ACC8-627DB33F0AFAQ36439003-C652F984-ECF3-4773-920B-CB9B41F73A17Q36444784-5C0B1EA3-4115-45FF-9410-F82801D8D7B2Q38171539-A70EA146-09FC-4E39-9AC1-5D99425711CFQ38208521-B680403D-DE09-46FB-8967-AF3ED52DDA45Q38309187-5419F3EB-1314-4323-BD44-5449C5B245B3Q38971502-522D54BF-D23C-409D-A819-F9ABB158B95CQ39289067-AC4DC339-1D34-428B-BFB0-987B45C9C715Q39388172-D743F587-BC1C-4A49-AA79-EF0689A92109Q39401986-A0BB3B4A-3268-4239-9CE5-52028CC5DABFQ40201664-6B7BE7FB-7D5B-42CA-97AA-61BCBF078BFBQ40500058-A67531AE-4543-4BD7-85E6-D0BCF4EBF660Q41136041-3B581780-FE7B-44A1-B322-FC03A27E67A2Q42024754-9AF0EB7F-9AD5-41DA-A9B2-9753CFAFA1B2Q42588798-7DC676B0-15E1-41E6-99C7-8E030FE6CB14Q42614303-62792651-EC80-4805-B2EF-A834307722EEQ43263628-1058FF49-7DB1-45ED-B8A2-2D9A144CBB83Q43737971-E4131ECC-480B-4774-843F-EA7F6921F512Q44392759-ACD88F57-7393-4381-A1F9-6317F0C45551Q44440273-B8C4EAAB-2A6D-4544-A9C9-C56AEBD6A100Q48347827-7A70D760-A7C2-4820-BB19-B095D466A0DDQ51766345-1617FFEF-9F9E-4191-90AD-87B49D4D92E8Q51766349-8786AB67-935A-4DE2-AF7F-43B78A497F91Q52629670-B135A78D-8F51-4E3E-82A0-47F0668FB8CAQ54211454-FFFAA049-48E1-4F03-8391-FA05CAD2A7ED
P2860
Non-pore lining amino acid side chains influence anion selectivity of the human CFTR Cl- channel expressed in mammalian cell lines.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Non-pore lining amino acid sid ...... essed in mammalian cell lines.
@en
type
label
Non-pore lining amino acid sid ...... essed in mammalian cell lines.
@en
prefLabel
Non-pore lining amino acid sid ...... essed in mammalian cell lines.
@en
P2093
P2860
P1476
Non-pore lining amino acid sid ...... essed in mammalian cell lines.
@en
P2093
P2860
P356
10.1111/J.1469-7793.1998.001BF.X
P407
P478
512 ( Pt 1)
P577
1998-10-01T00:00:00Z