Identification of cystic fibrosis transmembrane conductance regulator channel-lining residues in and flanking the M6 membrane-spanning segment.
about
Anion transport in heartThe mitochondrial citrate transport protein: probing the secondary structure of transmembrane domain III, identification of residues that likely comprise a portion of the citrate transport pathway, and development of a model for the putative TMDIII-Cystic fibrosis transmembrane conductance regulator. Structure and function of an epithelial chloride channel.Cystic fibrosis transmembrane conductance regulator and the outwardly rectifying chloride channel: a relationship between two chloride channels expressed in epithelial cells.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.Molecular modelling and molecular dynamics of CFTR.Insight in eukaryotic ABC transporter function by mutation analysis.Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel.Transmembrane helical interactions in the CFTR channel pore.Probing the structure of the diphtheria toxin channel. Reactivity in planar lipid bilayer membranes of cysteine-substituted mutant channels with methanethiosulfonate derivativesHalide permeation in wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channelsPermeability of wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels to polyatomic anions.Multi-Ion mechanism for ion permeation and block in the cystic fibrosis transmembrane conductance regulator chloride channelVoltage-dependent gating of the cystic fibrosis transmembrane conductance regulator Cl- channel.CFTR: covalent and noncovalent modification suggests a role for fixed charges in anion conduction.Transmembrane topology of a CLC chloride channel.Identification of an Extracellular Gate for the Proton-coupled Folate Transporter (PCFT-SLC46A1) by Cysteine Cross-linking.Functional architecture of the CFTR chloride channel.The second half of the cystic fibrosis transmembrane conductance regulator forms a functional chloride channel.Relative movements of transmembrane regions at the outer mouth of the cystic fibrosis transmembrane conductance regulator channel pore during channel gatingCystic fibrosis transmembrane conductance regulator: temperature-dependent cysteine reactivity suggests different stable conformers of the conduction pathwayChanges in accessibility of cytoplasmic substances to the pore associated with activation of the cystic fibrosis transmembrane conductance regulator chloride channel.Cysteine-independent inhibition of the CFTR chloride channel by the cysteine-reactive reagent sodium (2-sulphonatoethyl) methanethiosulphonate.NBCe1-A Transmembrane Segment 1 Lines the Ion Translocation Pathway.State-dependent access of anions to the cystic fibrosis transmembrane conductance regulator chloride channel pore.On the origin of asymmetric interactions between permeant anions and the cystic fibrosis transmembrane conductance regulator chloride channel pore.Two mechanisms of genistein inhibition of cystic fibrosis transmembrane conductance regulator Cl- channels expressed in murine cell line.The two halves of CFTR form a dual-pore ion channel.Identification of residues lining the translocation pore of human AE1, plasma membrane anion exchange protein.Non-pore lining amino acid side chains influence anion selectivity of the human CFTR Cl- channel expressed in mammalian cell lines.Direct activation of cystic fibrosis transmembrane conductance regulator channels by 8-cyclopentyl-1,3-dipropylxanthine (CPX) and 1,3-diallyl-8-cyclohexylxanthine (DAX).CFTR Cl- channel and CFTR-associated ATP channel: distinct pores regulated by common gates.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.Alignment of transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore.Structural and ionic determinants of 5-nitro-2-(3-phenylprophyl-amino)-benzoic acid block of the CFTR chloride channel.Cysteine substitutions reveal dual functions of the amino-terminal tail in cystic fibrosis transmembrane conductance regulator channel gating.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.
P2860
Q28141703-ECB21E48-A489-43B5-ADAB-405AAF257C02Q30882330-90A53E21-E450-4CAE-AE25-76E55D2DBEBDQ33830343-6E8C3EA7-B4F5-4E0A-B42A-8B411F104398Q34079148-80FC999E-1BB2-4B32-A636-69DB3A014251Q34173245-D8B0C427-B336-4917-A179-813480333438Q34173438-6C8D35CF-721C-43A6-87F3-2FBD6226B72DQ34188063-745786AB-CDCD-421E-B3B2-27E3E23CDAE0Q36158194-2446857F-25B4-4D31-BFAA-957928CBACC6Q36379776-14311770-7BE4-4AFE-ABFA-9B65F5D5B116Q36411911-54DCA28C-EF6D-4B24-8283-76AA4DA22916Q36412336-7B207032-B6AC-4A09-9E47-E2E08FEE4FFFQ36435877-C8A0C5DD-931A-42FA-A414-DB34ECD4C7C9Q36435908-EEE4841B-DE2E-4E4D-B6C4-986D5A9115B9Q36435912-EF0F3176-0527-4F85-B795-71572EAE5B42Q36435917-53D1190F-7772-45F8-A5AA-FD9A7B386EF4Q36436627-B69DE65C-895A-434D-A9DE-E4E025F4784DQ36444784-6D1C988F-CC2C-4E29-8682-31DE46ED01C5Q36663768-7601D9B8-A1C0-44F3-AD70-55C8347361B3Q36778842-7A161637-47A6-4F8E-A9BC-55C8433023F8Q38171539-E35CEF6D-C823-4661-A663-BFB80D1F78C9Q38331988-72AA8DC9-26CA-446F-98DF-8E130A2EE46EQ39306475-F0DEA9ED-8C47-4C00-AE6E-E483FFF3CF6CQ39554405-C0DBDF44-ACF4-4B41-877F-A894C66F5951Q39673058-D73A30C9-5110-4798-9E22-E4EEB3F181D6Q39847523-F6250378-A8AE-42AB-9A7B-1F977539B162Q39892796-288D29AB-3F9D-4789-A7DB-F5A83FDD533DQ40029008-77CE0BFC-3977-4983-9F11-16AAE843F189Q40201664-062244EF-17ED-4ED2-89B8-589D978975E1Q40886609-A9E0B002-072B-42AC-85D3-0E71E8592098Q40890137-6E4922A1-9CE6-498B-9F18-C28412B55EB2Q40977569-8B328774-F857-455E-9099-3A3FE76187E5Q41010624-B2DC8568-F11D-4612-BC46-D34751CCC622Q41052360-871C8EA0-3CD0-43EC-AC65-84B2899F69BBQ41056312-215B78AC-2456-4C26-972E-968AE33DE7CCQ42588798-45C900BD-6CFC-4E79-BFDA-CFB8FEF57B7DQ42854492-43248D52-6FFD-42A1-B755-BF3EF2F84BE0Q43192446-ABB10BED-0EA9-46DA-9C59-B0A4AF89AF00Q43684821-1E1C0094-E956-44BB-97FE-44E9D317D782Q43737971-F811377A-6263-4035-B90E-65CB0E0686DDQ44392759-E8F95B7C-BD3C-450B-B413-CAE63A13E573
P2860
Identification of cystic fibrosis transmembrane conductance regulator channel-lining residues in and flanking the M6 membrane-spanning segment.
description
1996 nî lūn-bûn
@nan
1996 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Identification of cystic fibro ...... M6 membrane-spanning segment.
@ast
Identification of cystic fibro ...... M6 membrane-spanning segment.
@en
Identification of cystic fibro ...... M6 membrane-spanning segment.
@nl
type
label
Identification of cystic fibro ...... M6 membrane-spanning segment.
@ast
Identification of cystic fibro ...... M6 membrane-spanning segment.
@en
Identification of cystic fibro ...... M6 membrane-spanning segment.
@nl
prefLabel
Identification of cystic fibro ...... M6 membrane-spanning segment.
@ast
Identification of cystic fibro ...... M6 membrane-spanning segment.
@en
Identification of cystic fibro ...... M6 membrane-spanning segment.
@nl
P2860
P1433
P1476
Identification of cystic fibro ...... e M6 membrane-spanning segment
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(96)79838-7
P407
P577
1996-06-01T00:00:00Z