Potentiation of disease-associated cystic fibrosis transmembrane conductance regulator mutants by hydrolyzable ATP analogs.
about
Myotonia congenita mutation enhances the degradation of human CLC-1 chloride channelsStructure-activity analysis of a CFTR channel potentiator: Distinct molecular parts underlie dual gating effects.A single amino acid substitution in CFTR converts ATP to an inhibitory ligand.Optimization of the degenerated interfacial ATP binding site improves the function of disease-related mutant cystic fibrosis transmembrane conductance regulator (CFTR) channels.Improvement of chloride transport defect by gonadotropin-releasing hormone (GnRH) in cystic fibrosis epithelial cells.Loss of CFTR affects biliary epithelium innate immunity and causes TLR4-NF-κB-mediated inflammatory response in miceInteraction non grata between CFTR's correctors and potentiatorsThermally unstable gating of the most common cystic fibrosis mutant channel (ΔF508): "rescue" by suppressor mutations in nucleotide binding domain 1 and by constitutive mutations in the cytosolic loops.Improved fluorescence assays to measure the defects associated with F508del-CFTR allow identification of new active compounds.Vx-770 potentiates CFTR function by promoting decoupling between the gating cycle and ATP hydrolysis cycle.Effects of curcumin on ion channels and transporters.Catalyst-like modulation of transition states for CFTR channel opening and closing: new stimulation strategy exploits nonequilibrium gating.Combating cystic fibrosis: in search for CF transmembrane conductance regulator (CFTR) modulators.A unified view of cystic fibrosis transmembrane conductance regulator (CFTR) gating: combining the allosterism of a ligand-gated channel with the enzymatic activity of an ATP-binding cassette (ABC) transporterTargeting F508del-CFTR to develop rational new therapies for cystic fibrosis.Two Small Molecules Restore Stability to a Subpopulation of the Cystic Fibrosis Transmembrane Conductance Regulator with the Predominant Disease-causing Mutation.Revertant mutants modify, but do not rescue, the gating defect of the cystic fibrosis mutant G551D-CFTR.Synergistic Potentiation of Cystic Fibrosis Transmembrane Conductance Regulator Gating by Two Chemically Distinct Potentiators, Ivacaftor (VX-770) and 5-Nitro-2-(3-Phenylpropylamino) Benzoate.Thermal unfolding simulations of NBD1 domain variants reveal structural motifs associated with the impaired folding of F508del-CFTR.The most common cystic fibrosis-associated mutation destabilizes the dimeric state of the nucleotide-binding domains of CFTR.On the mechanism of gating defects caused by the R117H mutation in cystic fibrosis transmembrane conductance regulator.Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell.Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions.Buserelin alleviates chloride transport defect in human cystic fibrosis nasal epithelial cells.CFTR potentiators: from bench to bedside.A common mechanism for CFTR potentiators.Structural mechanisms of CFTR function and dysfunction.Molecular dynamics simulation study on the structural instability of the most common cystic fibrosis-associated mutant ΔF508-CFTR.
P2860
Q28486132-CC72C2D5-B76F-443B-81FF-06EC38C50673Q34262476-2B5C6D30-DA57-43ED-917E-C5FD9DFB430AQ34262494-615BB43A-A14E-4435-B93E-217CE711266DQ34333750-87427F0C-D98C-4FC1-AEDC-C257ED4D7896Q35106485-0F58D0EB-5C5A-4F25-BBDA-50A393923F15Q35269164-D79A9E2C-C23F-471D-B7E9-76058B20E3E6Q35561343-74721FF2-3A2F-4813-BA49-FC03A77C7366Q35605109-4D4AC520-357C-479F-9758-5ACEE3D5755DQ36251047-1E9E0DDE-4DE9-478A-8CEE-6FCB910ECF7AQ36692979-674CD5CA-BD73-45A5-A0B2-CC1C2054F6EEQ37629713-65F84197-5D1A-4680-8228-9EBF9BAF719BQ37727045-3C73C4F9-50BC-4296-B4C8-B85C1C814F4FQ37833017-DADA1FEE-4932-4AAB-8AF4-559C90ED86D0Q37836188-C5FD25AE-3E33-40D2-AAF7-D0524288F28DQ37885153-1FD1ECB5-4AC4-40A2-B31E-60A23A31B968Q38721354-788AA85E-C5AE-4664-BB74-12597031FA81Q39018857-41974E96-1B69-499D-BDAC-BE3CEE4A9967Q39603833-0CCEA5BF-9372-47E4-95DE-2B792163C6B5Q39647261-90DC05BC-0228-40C4-A848-28DFC5EAABABQ39761315-BE99961E-BA55-43BD-9186-422C43A8F672Q40023091-61A44729-2F26-4446-B727-408275EDDCEBQ41565850-8DC6BA6F-19AB-4DDD-84F9-3F23B56BD9B8Q42283021-FF32BACC-DB14-4D78-BE2A-7F757B88ED5FQ46911058-B66C90D1-3F3B-4DD3-A0F5-4E731CC12564Q47599899-05D118F6-B763-4821-86FA-17B5AEC7A045Q48111581-7F5372CE-F2C3-4910-AB58-0009FC7934F0Q52629670-B48FA3BE-F9F9-4969-B6BF-A8A5A060E7F0Q55441392-EE54FC65-BCB0-44F1-AF62-CA8B0FCD8EE1
P2860
Potentiation of disease-associated cystic fibrosis transmembrane conductance regulator mutants by hydrolyzable ATP analogs.
description
2010 nî lūn-bûn
@nan
2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Potentiation of disease-associ ...... s by hydrolyzable ATP analogs.
@ast
Potentiation of disease-associ ...... s by hydrolyzable ATP analogs.
@en
type
label
Potentiation of disease-associ ...... s by hydrolyzable ATP analogs.
@ast
Potentiation of disease-associ ...... s by hydrolyzable ATP analogs.
@en
prefLabel
Potentiation of disease-associ ...... s by hydrolyzable ATP analogs.
@ast
Potentiation of disease-associ ...... s by hydrolyzable ATP analogs.
@en
P2093
P2860
P356
P1476
Potentiation of disease-associ ...... s by hydrolyzable ATP analogs.
@en
P2093
Haruna Miki
Silvia G Bompadre
Tzyh-Chang Hwang
P2860
P304
19967-19975
P356
10.1074/JBC.M109.092684
P407
P577
2010-04-20T00:00:00Z