Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry
about
Mechanisms of CFTR Folding at the Endoplasmic ReticulumMolecular Chaperones as Targets to Circumvent the CFTR Defect in Cystic FibrosisRequirements for Efficient Correction of ΔF508 CFTR Revealed by Analyses of Evolved SequencesEttA regulates translation by binding the ribosomal E site and restricting ribosome-tRNA dynamicsThe primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domainChanges in the Factor VIII C2 domain upon membrane binding determined by hydrogen-deuterium exchange MS.New insights into interactions between the nucleotide-binding domain of CFTR and keratin 8.An ambiguity principle for assigning protein structural domainsDevelopment of CFTR StructureEnhancing the Potency of F508del Correction: A Multi-Layer Combinational Approach to Drug Discovery for Cystic Fibrosis.Complement yourself: Transcomplementation rescues partially folded mutant proteins.Decoding F508del misfolding in cystic fibrosis.Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTRApplications of proteomic technologies for understanding the premature proteolysis of CFTR.Expanding the proteome: disordered and alternatively folded proteins.The cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis.A chaperone trap contributes to the onset of cystic fibrosis.VX-809 corrects folding defects in cystic fibrosis transmembrane conductance regulator protein through action on membrane-spanning domain 1.Modeling the conformational changes underlying channel opening in CFTRRational Coupled Dynamics Network Manipulation Rescues Disease-Relevant Mutant Cystic Fibrosis Transmembrane Conductance Regulator.Probing conformational rescue induced by a chemical corrector of F508del-cystic fibrosis transmembrane conductance regulator (CFTR) mutant.Phenotype-optimized sequence ensembles substantially improve prediction of disease-causing mutation in cystic fibrosis.Types and effects of protein variations.Dynamics of a bacterial multidrug ABC transporter in the inward- and outward-facing conformationsThermal instability of ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) channel function: protection by single suppressor mutations and inhibiting channel activityTransient 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.Combination of Correctors Rescue ΔF508-CFTR by Reducing Its Association with Hsp40 and Hsp27.A synonymous codon change alters the drug sensitivity of ΔF508 cystic fibrosis transmembrane conductance regulator.Non-native Conformers of Cystic Fibrosis Transmembrane Conductance Regulator NBD1 Are Recognized by Hsp27 and Conjugated to SUMO-2 for Degradation.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 strategyCFTR: folding, misfolding and correcting the ΔF508 conformational defect.Mechanism-based corrector combination restores ΔF508-CFTR folding and function.Combating cystic fibrosis: in search for CF transmembrane conductance regulator (CFTR) modulators.Recent advances and new perspectives in targeting CFTR for therapy of cystic fibrosis and enterotoxin-induced secretory diarrheas.Functional Rescue of F508del-CFTR Using Small Molecule CorrectorsCystic fibrosis transmembrane conductance regulator (ABCC7) structureRepairing mutated proteins--development of small molecules targeting defects in the cystic fibrosis transmembrane conductance regulator.
P2860
Q21129277-CFBE1245-DEC5-4D84-8211-53AF185289E7Q21129282-AD11C804-C0A9-45CB-A659-5C67CF84FFD2Q27676826-FC1CEC81-5CE7-4E79-AA7A-0B72A4F8F850Q27681174-73C835C2-B064-491C-9DFE-94C3229CCDD8Q28476393-D98078ED-76C6-4990-BD51-BABF30BCBE6BQ30153398-4A0C1E7F-FA8A-43FA-A258-4982E40388C2Q30395451-8B0DA7E1-8508-493A-B8A6-EDC227082B82Q30397624-A054100A-A387-419D-A02E-0F687AB29F11Q30421217-D744D3EB-1181-4849-B64D-DB3B691B72C4Q33632575-CD5F78D8-5D26-4325-8EC0-FCAAAA737623Q33763709-CA653391-83D4-472A-B19C-512839A87945Q33912624-17FE2A98-64B2-42B1-A4E3-58026F0E284CQ34017049-EC0B1D67-370E-4352-A36B-A190893DBDC3Q34076025-8D8058E6-1786-48FF-AF57-37E991B7648DQ34197530-963D806E-7C26-40FC-A831-E5B73FAB428DQ34285307-E06E5A5D-B5EF-4455-8069-D41CE79B3912Q34305005-43A83535-41B3-4CC3-8197-179CA097C044Q34362524-38E3A379-59D8-4170-BAD2-06335A23447BQ35005061-7C276EB1-FE39-4345-B5CB-6481D4C70977Q35073390-E504C133-94BC-4186-B1D0-D893CD22C1CBQ35107406-A7A67222-588E-4178-9061-BC795E640F71Q35190186-9625CEE8-2A8E-47DE-B544-D382B2872D81Q35548241-8AC0EBD3-1126-4B6A-AD7E-2087066FF844Q36079458-55BA14FD-D89B-49B0-8173-D3C79E628529Q36108986-A943BD27-C40B-435B-8A42-7B1CA77090B4Q36125348-B1B0658E-B3FA-45A3-AB2D-DD9DC2C6CA83Q36158194-39A6D613-ADAD-48CB-8084-08E319435406Q36281743-5D6BDC43-889F-4D34-AC79-C18C79CE0CB4Q36283378-4092A585-3BAE-4E1B-9A7D-4E409815E285Q36385376-BAC06694-5469-4621-8204-29CEF3582B7FQ36489351-570BAD66-7676-433E-B911-6B484FC203B6Q36629079-33DC9FEE-D362-41A3-87B5-63C5E04DA21BQ36749541-FFE8F31D-7686-4AA8-9C14-E416A5AC88D9Q36814102-E98B6AC8-25D1-48B7-B44F-8EFD6718046BQ37341854-DACA6324-7F08-4379-BA84-4D70EC94393BQ37833017-8B0AD69D-66E9-4BE3-99A8-7C92A8B05045Q37990948-2401C5F1-0822-4CF3-B9B9-A55A6E14CB15Q38051325-915F8796-3C6B-45F8-8B0E-60BD0D768565Q38078917-6EB80B24-F2D9-4EA8-B6A0-467C4D5A7868Q38097952-A4E4B304-B86D-4A84-9E8F-60787B407D1B
P2860
Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին 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
Structure and dynamics of NBD1 ...... ium exchange mass spectrometry
@ast
Structure and dynamics of NBD1 ...... ium exchange mass spectrometry
@en
Structure and dynamics of NBD1 ...... ium exchange mass spectrometry
@nl
type
label
Structure and dynamics of NBD1 ...... ium exchange mass spectrometry
@ast
Structure and dynamics of NBD1 ...... ium exchange mass spectrometry
@en
Structure and dynamics of NBD1 ...... ium exchange mass spectrometry
@nl
prefLabel
Structure and dynamics of NBD1 ...... ium exchange mass spectrometry
@ast
Structure and dynamics of NBD1 ...... ium exchange mass spectrometry
@en
Structure and dynamics of NBD1 ...... ium exchange mass spectrometry
@nl
P2093
P1476
Structure and dynamics of NBD1 ...... ium exchange mass spectrometry
@en
P2093
D R Wetmore
J M Sauder
K S Molnar
M C Kearins
P C Maloney
P304
P356
10.1016/J.JMB.2009.11.051
P407
P577
2010-02-19T00:00:00Z