In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer.
about
Biochemical Basis of the Interaction between Cystic Fibrosis Transmembrane Conductance Regulator and Immunoglobulin-like Repeats of FilaminAllosteric coupling between the intracellular coupling helix 4 and regulatory sites of the first nucleotide-binding domain of CFTRCurcumin and genistein: the combined effects on disease-associated CFTR mutants and their clinical implicationsDevelopment of CFTR StructureATP and AMP mutually influence their interaction with the ATP-binding cassette (ABC) adenylate kinase cystic fibrosis transmembrane conductance regulator (CFTR) at separate binding sites.Small molecule correctors of F508del-CFTR discovered by structure-based virtual screeningATP-independent CFTR channel gating and allosteric modulation by phosphorylation.Directed evolution of P-glycoprotein cysteines reveals site-specific, non-conservative substitutions that preserve multidrug resistance.Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channelPotentiation of disease-associated cystic fibrosis transmembrane conductance regulator mutants by hydrolyzable ATP analogs.Contribution of casein kinase 2 and spleen tyrosine kinase to CFTR trafficking and protein kinase A-induced activity.Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation.Intragenic suppressing mutations correct the folding and intracellular traffic of misfolded mutants of Yor1p, a eukaryotic drug transporter.State-dependent regulation of cystic fibrosis transmembrane conductance regulator (CFTR) gating by a high affinity Fe3+ bridge between the regulatory domain and cytoplasmic loop 3.An electrostatic interaction at the tetrahelix bundle promotes phosphorylation-dependent cystic fibrosis transmembrane conductance regulator (CFTR) channel opening.The inhibition mechanism of non-phosphorylated Ser768 in the regulatory domain of cystic fibrosis transmembrane conductance regulatorMutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gatingCysteine accessibility probes timing and extent of NBD separation along the dimer interface in gating CFTR channels.Regulatory domain phosphorylation to distinguish the mechanistic basis underlying acute CFTR modulators.Structural basis for the channel function of a degraded ABC transporter, CFTR (ABCC7).Cystic fibrosis transmembrane conductance regulator: a molecular model defines the architecture of the anion conduction path and locates a "bottleneck" in the pore.Identification of a novel post-hydrolytic state in CFTR gating.Regulation of the cystic fibrosis transmembrane conductance regulator anion channel by tyrosine phosphorylation.Benzopyrimido-pyrrolo-oxazine-dione (R)-BPO-27 Inhibits CFTR Chloride Channel Gating by Competition with ATPMurine and human CFTR exhibit different sensitivities to CFTR potentiators.Molecular modelling and molecular dynamics of CFTR.Nonintegral stoichiometry in CFTR gating revealed by a pore-lining mutation.Deletion of Phenylalanine 508 in the First Nucleotide-binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator Increases Conformational Exchange and Inhibits Dimerization.Transmembrane helical interactions in the CFTR channel pore.Locating a plausible binding site for an open-channel blocker, GlyH-101, in the pore of the cystic fibrosis transmembrane conductance regulator.The CFTR ion channel: gating, regulation, and anion permeationLong-range coupling between the extracellular gates and the intracellular ATP binding domains of multidrug resistance protein pumps and cystic fibrosis transmembrane conductance regulator channelsPositioning of extracellular loop 1 affects pore gating of the cystic fibrosis transmembrane conductance regulatorStructure and function of ABC transporters.Spatial positioning of CFTR's pore-lining residues affirms an asymmetrical contribution of transmembrane segments to the anion permeation pathwayTwo salt bridges differentially contribute to the maintenance of cystic fibrosis transmembrane conductance regulator (CFTR) channel function.RACK1 interacts with filamin-A to regulate plasma membrane levels of the cystic fibrosis transmembrane conductance regulator.Nonequilibrium gating of CFTR on an equilibrium theme.CLC-0 and CFTR: chloride channels evolved from transporters.State-dependent modulation of CFTR gating by pyrophosphate.
P2860
Q27660360-082399DC-C609-473B-B34C-F7217ECFC95CQ28533617-5249595A-4AA0-4D3D-9E46-B594298530AFQ28830793-1E1F636F-18BF-465C-86DA-D4DD1EF453FBQ30421217-FF276CD8-CF43-4DA1-8769-DA335AC41B18Q30545926-1CB64AC1-3D77-4644-90E9-3D01DB0935B4Q30577535-0A5DDDE6-9092-4B64-BBA5-71FFCDF704A2Q33734745-AB3619C6-84E2-4529-AB72-23D2C56D3512Q33802134-534FCFF1-1916-4E43-B1B6-01BD7002C62AQ33814258-93D3289A-D85E-4896-9E2B-03A0B94000BCQ33924312-B9C2605C-BFFD-4127-8665-AE3133D64CE1Q34022687-666DF051-0185-42B0-B10B-0322CD4AE9AAQ34096449-DB32D239-6CBA-4833-AF6E-823D3BE23686Q34298963-74E0F6F8-4109-4660-A549-B2A09023BCE7Q34412519-13005D0D-E80C-454C-9BED-0D6AAF038A69Q34430936-95021B93-C114-4BA7-8C80-5A850865FBC6Q34503233-80D06116-1199-4CE4-81DA-A19007C41093Q35018175-F56B928F-D45E-4E01-9B11-AAD54CF520A5Q35234571-AA5CD4E4-E121-422B-A8A4-327D2E9506F5Q35325226-F4F2E942-3552-4EDF-AEE5-56F9207A590FQ35503245-7B23F7CE-D10A-4B79-863D-0E2B26BC47D5Q35862414-427C7444-8E1D-4446-B7DC-1E75690C7D98Q35931859-893DBD24-FB41-4D4E-AF6E-EE91D94B5342Q35997983-0AD873D1-36B0-4C2B-8735-FDDE829284AAQ36077753-7A61BAEE-1DD9-41E1-BC54-779E37BF2629Q36122891-395AEADA-DE0D-44E1-A321-43868777B26BQ36158194-91A54485-0718-4CB2-AD5C-42BE6504CF80Q36277880-45D40DD6-CF07-4FFA-9D6D-F094D65DF3E9Q36281743-B29CC979-82AB-4A93-8E67-8944BE73C43AQ36412336-61B9B6DD-DA52-441B-955D-BC0402AF14ADQ36412828-B5BB354B-E0B4-491A-B331-C68480D8692BQ36488258-7B4EDA22-B29B-43A9-9B77-BD256BEF2BCCQ36570921-55CAB52F-10E8-497A-BA6D-3E96F9F2A7CBQ36638473-7FCEF09A-2474-4637-B88E-270B00249CDCQ36786255-2599925B-95AF-436E-A45A-A59D2B27297EQ36837526-6169276C-C4A4-4D59-B34A-9C4341818D78Q37012562-2CA95772-BD91-42AC-9398-7E8B96909F3DQ37050934-0F00321B-A1E0-47FC-8123-F142466173B5Q37061709-934F0A6D-B75F-4510-A9AE-CC3C6421CD6BQ37129332-AD878837-11C6-42CC-8FFC-8A15E75F2721Q37234233-A5884DB3-6360-43AE-9E52-6A0D01F9A504
P2860
In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
In vivo phosphorylation of CFT ...... de-binding domain heterodimer.
@en
type
label
In vivo phosphorylation of CFT ...... de-binding domain heterodimer.
@en
prefLabel
In vivo phosphorylation of CFT ...... de-binding domain heterodimer.
@en
P2093
P2860
P356
P1433
P1476
In vivo phosphorylation of CFT ...... de-binding domain heterodimer.
@en
P2093
David C Gadsby
Dennis M White
Gal Altberg
Martin Mense
P2860
P304
P356
10.1038/SJ.EMBOJ.7601373
P407
P577
2006-10-12T00:00:00Z