NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR.
about
New and emerging targeted therapies for cystic fibrosisThe primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domainAllosteric coupling between the intracellular coupling helix 4 and regulatory sites of the first nucleotide-binding domain of CFTRDevelopment of CFTR StructureSolution NMR studies of periplasmic binding proteins and their interaction partnersDecoding F508del misfolding in cystic fibrosis.Contribution of casein kinase 2 and spleen tyrosine kinase to CFTR trafficking and protein kinase A-induced activity.Expanding the proteome: disordered and alternatively folded proteins.Physiology of epithelial chloride and fluid secretionOptimization of the degenerated interfacial ATP binding site improves the function of disease-related mutant cystic fibrosis transmembrane conductance regulator (CFTR) channels.Phenotype-optimized sequence ensembles substantially improve prediction of disease-causing mutation in cystic fibrosis.Alteration of CFTR transmembrane span integration by disease-causing mutations.Purification of CFTR for mass spectrometry analysis: identification of palmitoylation and other post-translational modifications.Development and characterization of synthetic antibodies binding to the cystic fibrosis conductance regulator.Transient sampling of aggregation-prone conformations causes pathogenic instability of a parkinsonian mutant of DJ-1 at physiological temperature.Molecular modelling and molecular dynamics of CFTR.Deletion of Phenylalanine 508 in the First Nucleotide-binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator Increases Conformational Exchange and Inhibits Dimerization.The CFTR ion channel: gating, regulation, and anion permeationChannel Gating Regulation by the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) First Cytosolic Loop.Dynamics intrinsic to cystic fibrosis transmembrane conductance regulator function and stabilityBinding screen for cystic fibrosis transmembrane conductance regulator correctors finds new chemical matter and yields insights into cystic fibrosis therapeutic strategyTherapeutic Approaches to Acquired Cystic Fibrosis Transmembrane Conductance Regulator Dysfunction in Chronic Bronchitis.Regulation of ABC transporter function via phosphorylation by protein kinases.Combating cystic fibrosis: in search for CF transmembrane conductance regulator (CFTR) modulators.Functional Rescue of F508del-CFTR Using Small Molecule CorrectorsCystic fibrosis transmembrane conductance regulator (ABCC7) structureStructural changes of CFTR R region upon phosphorylation: a plastic platform for intramolecular and intermolecular interactions.Trafficking and function of the cystic fibrosis transmembrane conductance regulator: a complex network of posttranslational modifications.The gating of the CFTR channel.Current insights into the role of PKA phosphorylation in CFTR channel activity and the pharmacological rescue of cystic fibrosis disease-causing mutants.Regulatory insertion removal restores maturation, stability and function of DeltaF508 CFTRBiochemical and biophysical approaches to probe CFTR structure.Phosphorylation-dependent changes in nucleotide binding, conformation, and dynamics of the first nucleotide binding domain (NBD1) of the sulfonylurea receptor 2B (SUR2B).Introduction to section IV: biophysical methods to approach CFTR structure.Conformational changes relevant to channel activity and folding within the first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator.Attenuation of Phosphorylation-dependent Activation of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) by Disease-causing Mutations at the Transmission Interface.Positive regulation of the Candida albicans multidrug efflux pump Cdr1p function by phosphorylation of its N-terminal extension.Membrane protein stability can be compromised by detergent interactions with the extramembranous soluble domainsFunctional and pharmacological induced structural changes of the cystic fibrosis transmembrane conductance regulator in the membrane solved using SAXS.A SAXS-based ensemble model of the native and phosphorylated regulatory domain of the CFTR.
P2860
Q26749278-11D4ABDA-2313-4B87-9875-A2B789B6B6EDQ28476393-732590AB-82CE-4553-8D11-ABEDEAC34429Q28533617-0C696579-258E-4A8A-B49B-DFF76404453BQ30421217-699A7097-A82C-4972-BD60-32830A4A9D6BQ33896675-AE253357-B5D3-4AF2-A991-B54C698D314BQ33912624-4DCBAD3F-FDFA-4F4A-ADDF-F9ACD484D925Q34022687-B2EF1DEC-507A-4317-ADEF-89A47E2945A1Q34197530-84C04155-A256-492A-BC27-118C6BEC2B6AQ34279597-629077B9-8D31-4C8B-B629-2BD142F719EEQ34333750-6E61711D-B710-43B4-90D7-0D32F47DB41BQ35190186-CB85598A-094D-41C3-9804-96452818C206Q35579788-222E22AE-1399-4177-99C2-17E72485019AQ35747225-54050CEA-9390-44A3-AAF7-597EEC50A3B5Q36019421-B61AACB3-F384-41B3-A55B-0297F4FB9C64Q36125348-63911E82-9861-4ADC-AAD3-52B5884B6D58Q36158194-A4483D9E-4BF3-4D33-A463-564B21FDFB38Q36281743-E450F474-AE87-4AD5-A505-52C91851C18BQ36488258-CC662EAE-2954-4808-B256-22E7DE61B6FCQ36489303-B43EBA8D-7023-4DB9-81C0-302475612583Q36629079-A23B6B88-3A09-4813-910C-643F92C66D23Q36749541-52274ACE-961C-4735-8CB2-24CFD45124B3Q37241561-BD603FDA-B9EE-4110-BF2E-31261C98A6D2Q37813724-D779AF2F-FD16-4556-9768-A18DE467CB9BQ37833017-0BD9D7D6-7B3B-4FBF-A7F9-12709E7A565EQ38051325-844E1FF5-0DFD-4FEE-8487-4EEBA8009776Q38078917-E70CE3AE-48D8-48D4-A6B1-AB977AD74FA5Q38119262-DBE1A122-CAA1-4FD3-80C9-F86127E67543Q38913048-536FB68E-9F2D-4FD8-A5B2-EFF09AEA5C87Q38970505-B7C517C7-A8F6-409E-9231-EBE311CBD346Q38976933-8C373D17-C23C-4A34-A9FF-4986D2E0B173Q39691014-804822AF-CAB9-4311-8035-8D485FC0C38DQ40675816-8D11D129-F548-4F9F-8D58-D9F3C4B3E972Q40710861-5C5A8F97-4B3F-4B33-AD85-ABA7E3D737D5Q41136041-29D64D03-6099-4788-98C3-D0D7EDDB9FACQ41988564-3DD032FC-7A1C-4898-9348-3AEC77808E76Q42324203-84BD5AE0-973A-4198-9B5F-7E8D0BEC00EBQ42676608-7ADBB95C-4113-4C1F-8D74-9A9552F39EDEQ42732315-E264D339-ACB5-4270-9FB0-44EFF3DD9DAEQ42834943-B9E1190D-18BE-4B01-8ABD-6A06E5022E77Q46491265-F2885D14-BD02-4CF4-9477-F6D37C71379E
P2860
NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
NMR evidence for differential ...... ions in WT and DeltaF508 CFTR.
@en
type
label
NMR evidence for differential ...... ions in WT and DeltaF508 CFTR.
@en
prefLabel
NMR evidence for differential ...... ions in WT and DeltaF508 CFTR.
@en
P2093
P2860
P356
P1433
P1476
NMR evidence for differential ...... ions in WT and DeltaF508 CFTR.
@en
P2093
Philip J Thomas
Rhea P Hudson
Voula Kanelis
P2860
P304
P356
10.1038/EMBOJ.2009.329
P407
P577
2009-11-19T00:00:00Z