Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator - Wikidata - thesis-toulmin - TriplyDB

Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator

Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator

http://www.wikidata.org/entity/Q27642825

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Correcting the cystic fibrosis disease mutant, A455E CFTR Mechanisms of CFTR Folding at the Endoplasmic Reticulum H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP.The ABC protein turned chloride channel whose failure causes cystic fibrosis CFTR gating II: Effects of nucleotide binding on the stability of open states Cystic fibrosis transmembrane conductance regulator dysfunction and its treatment Integrated analysis of residue coevolution and protein structure in ABC transporters Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant ABC ATPase signature helices in Rad50 link nucleotide state to Mre11 interface for DNA repair.Crystal structure of the maltose transporter in a pretranslocation intermediate state Requirements for Efficient Correction of ΔF508 CFTR Revealed by Analyses of Evolved Sequences Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.Cystic fibrosis transmembrane conductance regulator modulators in cystic fibrosis: current perspectives Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding The primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domain Rescue of NBD2 mutants N1303K and S1235R of CFTR by small-molecule correctors and transcomplementation New insights into interactions between the nucleotide-binding domain of CFTR and keratin 8.Stabilization of Nucleotide Binding Domain Dimers Rescues ABCC6 Mutants Associated with Pseudoxanthoma Elasticum.Development of CFTR Structure ATP and AMP mutually influence their interaction with the ATP-binding cassette (ABC) adenylate kinase cystic fibrosis transmembrane conductance regulator (CFTR) at separate binding sites.Charge environments around phosphorylation sites in proteins.Folding and rescue of a cystic fibrosis transmembrane conductance regulator trafficking mutant identified using human-murine chimeric proteins Normal gating of CFTR requires ATP binding to both nucleotide-binding domains and hydrolysis at the second nucleotide-binding domain.The cystic fibrosis transmembrane conductance regulator (CFTR) is expressed in maturation stage ameloblasts, odontoblasts and bone cells The H-loop in the second nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator is required for efficient chloride channel closing Complement yourself: Transcomplementation rescues partially folded mutant proteins.Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channel Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin ADP inhibits function of the ABC transporter cystic fibrosis transmembrane conductance regulator via its adenylate kinase activity.Fast and automated functional classification with MED-SuMo: an application on purine-binding proteins.Decoding F508del misfolding in cystic fibrosis.The A-loop, a novel conserved aromatic acid subdomain upstream of the Walker A motif in ABC transporters, is critical for ATP binding.Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTR Divergent signature motifs of nucleotide binding domains of ABC multidrug transporter, CaCdr1p of pathogenic Candida albicans, are functionally asymmetric and noninterchangeable The hydroxyl group of S685 in Walker A motif and the carboxyl group of D792 in Walker B motif of NBD1 play a crucial role for multidrug resistance protein folding and function.ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation A single amino acid substitution in CFTR converts ATP to an inhibitory ligand.The cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis.

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P2860

Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator

http://www.wikidata.org/entity/Q27642825

description

2004 nî lūn-bûn

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2004 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2004 թվականի հունվարին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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Structure of nucleotide-bindin ...... membrane conductance regulator

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Structure of nucleotide-bindin ...... membrane conductance regulator

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Structure of nucleotide-bindin ...... membrane conductance regulator

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Structure of nucleotide-bindin ...... membrane conductance regulator

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Structure of nucleotide-bindin ...... membrane conductance regulator

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Structure of nucleotide-bindin ...... membrane conductance regulator

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Structure of nucleotide-bindin ...... membrane conductance regulator

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Structure of nucleotide-bindin ...... membrane conductance regulator

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Structure of nucleotide-bindin ...... membrane conductance regulator

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SJ.EMBOJ.7600040

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The EMBO Journal

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Structure of nucleotide-bindin ...... membrane conductance regulator

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Don Lorimer

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Hal A Lewis

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J Michael Sauder

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John F Hunt

http://www.w3.org/2001/XMLSchema#string

Kai W Post

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Kanagalaghatta R Rajashankar

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Kris Conners

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Marc E Rutter

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Margaret C Kearins

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Marie Zhang

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P2860

ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer

Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast

Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily

The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter

Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter

The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism

Crystal structure of the nucleotide-binding domain of the ABC-transporter haemolysin B: identification of a variable region within ABC helical domains

Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations

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10.1038/SJ.EMBOJ.7600040

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2

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23

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2004-01-28T00:00:00Z

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14685259

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cystic fibrosis

transmembrane protein

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1271750

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