Preferential phosphorylation of R-domain Serine 768 dampens activation of CFTR channels by PKA.
about
The ABC protein turned chloride channel whose failure causes cystic fibrosisCFTR gating I: Characterization of the ATP-dependent gating of a phosphorylation-independent CFTR channel (DeltaR-CFTR).Cystic fibrosis transmembrane conductance regulator modulators in cystic fibrosis: current perspectivesState-dependent regulation of cystic fibrosis transmembrane conductance regulator (CFTR) gating by a high affinity Fe3+ bridge between the regulatory domain and cytoplasmic loop 3.The inhibition mechanism of non-phosphorylated Ser768 in the regulatory domain of cystic fibrosis transmembrane conductance regulatorDetection of phospho-sites generated by protein kinase CK2 in CFTR: mechanistic aspects of Thr1471 phosphorylationPhosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesisIdentification of a novel post-hydrolytic state in CFTR gating.Regulation of the cystic fibrosis transmembrane conductance regulator anion channel by tyrosine phosphorylation.Nonintegral stoichiometry in CFTR gating revealed by a pore-lining mutation.Thermodynamics of CFTR channel gating: a spreading conformational change initiates an irreversible gating cycle.Insight in eukaryotic ABC transporter function by mutation analysis.Regulation of activation and processing of the cystic fibrosis transmembrane conductance regulator (CFTR) by a complex electrostatic interaction between the regulatory domain and cytoplasmic loop 3.The CFTR ion channel: gating, regulation, and anion permeationHow Phosphorylation and ATPase Activity Regulate Anion Flux though the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR).CLC-0 and CFTR: chloride channels evolved from transporters.AMP-activated protein kinase phosphorylation of the R domain inhibits PKA stimulation of CFTR.CFTR regulatory region interacts with NBD1 predominantly via multiple transient helicesSynergy of cAMP and calcium signaling pathways in CFTR regulation.Regulation of ABC transporter function via phosphorylation by protein kinases.Cystic fibrosis transmembrane conductance regulator (ABCC7) structureStructural changes of CFTR R region upon phosphorylation: a plastic platform for intramolecular and intermolecular interactions.In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer.Potential sites of CFTR activation by tyrosine kinases.Trafficking and function of the cystic fibrosis transmembrane conductance regulator: a complex network of posttranslational modifications.The major cystic fibrosis causing mutation exhibits defective propensity for phosphorylation.Current insights into the role of PKA phosphorylation in CFTR channel activity and the pharmacological rescue of cystic fibrosis disease-causing mutants.Mechanistic insight into control of CFTR by AMPK.The Walker B motif of the second nucleotide-binding domain (NBD2) of CFTR plays a key role in ATPase activity by the NBD1-NBD2 heterodimer.Negative regulation of the yeast ABC transporter Ycf1p by phosphorylation within its N-terminal extension.Computational studies reveal phosphorylation-dependent changes in the unstructured R domain of CFTR.Protein kinase A regulates C-terminally truncated CaV 1.2 in Xenopus oocytes: roles of N- and C-termini of the α1C subunit.Structural mechanisms of CFTR function and dysfunction.
P2860
Q24657572-8ADEC59D-A38E-4A99-B50F-3003A6E28C01Q25256649-1FC90DEB-69A7-441F-ABCF-7723632CD14BQ28073063-C65E0340-B9E0-41FA-B586-9820294E2C79Q34412519-765300F3-5844-48CE-8F99-B57400B17654Q34503233-FB6990A4-5D05-4CB6-B108-E0CF37E8F866Q34994567-94FF50AD-ED81-419B-829A-A46457E5D5BCQ35827545-AE7330A2-C1B6-42F7-8D15-7E3B4E09E146Q35931859-E6AAC0EF-CBE2-41D5-8104-3A5B11ADCD35Q35997983-4E3440DC-D2AA-4C46-82C5-07E3D83958DCQ36277880-DBD7A457-7445-4406-BE31-08484DD3D41EQ36295891-0EE091E2-96DA-4019-B822-0AC028B06B8EQ36379776-52CA3A28-AD67-4942-B923-8949EDD01F80Q36418861-C735219A-8EA3-46D6-92EB-A7E18D3C5709Q36488258-2067F298-0222-4113-B631-26603630EB8AQ37078641-10C12777-39CF-41D8-B3E5-2A320BEA40C6Q37129332-5C2DF9B4-F3EA-41F6-BA48-7400A658B81EQ37264143-2C59283B-0B65-4B0A-883B-CFB551DD8B44Q37618800-0BE3E411-B76F-412F-8ED6-5481CB84F856Q37711579-7F33A541-E3C9-401F-AEBE-3388894C82BEQ37813724-F40CBC0C-D613-486C-B498-49FF6F5F46DEQ38078917-3F1C10B2-67AB-45DF-A192-24FF12FCE2D1Q38119262-290DEAF7-96CF-478E-B30C-6B00B14CE3CCQ38774272-FFBAB4BB-06C5-4BD5-8044-2C503193DD1BQ38813705-681C9E8B-A8C5-4A76-A918-F48665AB74E2Q38913048-6B030CFE-9259-413D-BB82-A78112B703FAQ38946518-6DBF19D3-FF97-4E09-960B-E07B2D894524Q38976933-7135537C-61AD-4E63-AE59-37F4A8D1D381Q41856265-83BA50A5-D9F0-496F-AA87-18E2E339AA6AQ42072546-1B2CE17F-2C6E-4476-966A-DB05FE89B90FQ43007858-9B0F0D5E-CB90-41D9-B408-17D8EA8684B7Q43023020-B2F0532F-265A-418D-9E85-7413A053930DQ48241794-9B9DE14F-C7F7-4B19-8705-67323656B462Q52629670-C17A839D-5454-4F91-8F4F-BED19BC3403B
P2860
Preferential phosphorylation of R-domain Serine 768 dampens activation of CFTR channels by PKA.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Preferential phosphorylation o ...... ation of CFTR channels by PKA.
@ast
Preferential phosphorylation o ...... ation of CFTR channels by PKA.
@en
type
label
Preferential phosphorylation o ...... ation of CFTR channels by PKA.
@ast
Preferential phosphorylation o ...... ation of CFTR channels by PKA.
@en
prefLabel
Preferential phosphorylation o ...... ation of CFTR channels by PKA.
@ast
Preferential phosphorylation o ...... ation of CFTR channels by PKA.
@en
P2093
P2860
P356
P1476
Preferential phosphorylation o ...... ation of CFTR channels by PKA.
@en
P2093
Andrew N Krutchinsky
Benjamin B Angel
Brian T Chait
Cristina Cenciarelli
David C Gadsby
Derek T McLachlin
Donna Seto-Young
Kim W Chan
P2860
P304
P356
10.1085/JGP.200409076
P577
2005-01-18T00:00:00Z