The ΔF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR
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Kai Du | K. Du | G. Lukács | Gergely L Lukacs | Manu Sharma | Manu Sharma
[1] Douglas C. Rees,et al. The E. coli BtuCD Structure: A Framework for ABC Transporter Architecture and Mechanism , 2002, Science.
[2] F. Hartl,et al. Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase , 1999, Nature Structural Biology.
[3] Andreas Engel. Faculty Opinions recommendation of The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. , 2002 .
[4] M. Welsh,et al. Structure and function of the CFTR chloride channel. , 1999, Physiological reviews.
[5] G. Lukács,et al. Conformational and Temperature-sensitive Stability Defects of the ΔF508 Cystic Fibrosis Transmembrane Conductance Regulator in Post-endoplasmic Reticulum Compartments* , 2001, The Journal of Biological Chemistry.
[6] G. Lukács,et al. C-terminal Truncations Destabilize the Cystic Fibrosis Transmembrane Conductance Regulator without Impairing Its Biogenesis , 1999, The Journal of Biological Chemistry.
[7] I. Braakman,et al. Coordinated Nonvectorial Folding in a Newly Synthesized Multidomain Protein , 2002, Science.
[8] J. Riordan,et al. Differential Interactions of Nucleotides at the Two Nucleotide Binding Domains of the Cystic Fibrosis Transmembrane Conductance Regulator* , 2001, The Journal of Biological Chemistry.
[9] R. Frizzell,et al. The role of regulated CFTR trafficking in epithelial secretion. , 2003, American journal of physiology. Cell physiology.
[10] J. Wine,et al. Glycerol Reverses the Misfolding Phenotype of the Most Common Cystic Fibrosis Mutation (*) , 1996, The Journal of Biological Chemistry.
[11] J. M. Sauder,et al. Impact of the ΔF508 Mutation in First Nucleotide-binding Domain of Human Cystic Fibrosis Transmembrane Conductance Regulator on Domain Folding and Structure* , 2005, Journal of Biological Chemistry.
[12] E. Schneider,et al. Nucleotide-induced conformational changes of MalK, a bacterial ATP binding cassette transporter protein. , 1994, The Journal of biological chemistry.
[13] Charles R Sanders,et al. Disease-related misassembly of membrane proteins. , 2004, Annual review of biophysics and biomolecular structure.
[14] J. Riordan,et al. The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover* , 2002, The Journal of Biological Chemistry.
[15] G. Lukács,et al. Limited proteolysis as a probe for arrested conformational maturation of ΔF508 CFTR , 1998, Nature Structural Biology.
[16] F. Hartl,et al. Recombination of protein domains facilitated by co-translational folding in eukaryotes , 1997, Nature.
[17] L. Limbird,et al. The role of a conserved inter-transmembrane domain interface in regulating alpha(2a)-adrenergic receptor conformational stability and cell-surface turnover. , 2001, Molecular pharmacology.
[18] Chad A Brautigam,et al. Side chain and backbone contributions of Phe508 to CFTR folding , 2005, Nature Structural &Molecular Biology.
[19] K D Wittrup,et al. Protein Folding Stability Can Determine the Efficiency of Escape from Endoplasmic Reticulum Quality Control* , 1998, The Journal of Biological Chemistry.
[20] P. Pedersen,et al. The cystic fibrosis transmembrane conductance regulator. Effects of the most common cystic fibrosis-causing mutation on the secondary structure and stability of a synthetic peptide. , 1992, The Journal of biological chemistry.
[21] A. Nairn,et al. Severed Molecules Functionally Define the Boundaries of the Cystic Fibrosis Transmembrane Conductance Regulator's Nh2-Terminal Nucleotide Binding Domain , 2000, The Journal of general physiology.
[22] B. Papsin,et al. Misfolding diverts CFTR from recycling to degradation , 2004, The Journal of cell biology.
[23] G. Heda,et al. The ΔF508 mutation shortens the biochemical half-life of plasma membrane CFTR in polarized epithelial cells , 2001 .
[24] J. M. Sauder,et al. Structure of nucleotide‐binding domain 1 of the cystic fibrosis transmembrane conductance regulator , 2004, The EMBO journal.
[25] R. Doolittle. The multiplicity of domains in proteins. , 1995, Annual review of biochemistry.
[26] C. Sanders,et al. Destabilizing mutations promote membrane protein misfolding. , 2004, Biochemistry.
[27] S. Dhani,et al. Stable dimeric assembly of the second membrane-spanning domain of CFTR (cystic fibrosis transmembrane conductance regulator) reconstitutes a chloride-selective pore. , 2003, The Biochemical journal.
[28] P. Pedersen,et al. Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation. , 1999, Biochemistry.
[29] D. Clarke,et al. The ΔF508 Mutation Disrupts Packing of the Transmembrane Segments of the Cystic Fibrosis Transmembrane Conductance Regulator* , 2004, Journal of Biological Chemistry.
[30] J. Brodsky. Chaperoning the maturation of the cystic fibrosis transmembrane conductance regulator. , 2001, American journal of physiology. Lung cellular and molecular physiology.
[31] M. Welsh,et al. The amino-terminal portion of CFTR forms a regulated CI− channel , 1994, Cell.
[32] Wei Chen,et al. Co-translational folding of an alphavirus capsid protein in the cytosol of living cells , 1999, Nature Cell Biology.
[33] L. Tsui,et al. Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. , 1989, Science.
[34] F. Hartl,et al. Principles of Chaperone-Assisted Protein Folding: Differences Between in Vitro and in Vivo Mechanisms , 1996, Science.
[35] S Grinstein,et al. Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP. , 1994, The EMBO journal.
[36] Satoshi Omura,et al. Degradation of CFTR by the ubiquitin-proteasome pathway , 1995, Cell.
[37] G. Tusnády,et al. Membrane Topology and Glycosylation of the Human Multidrug Resistance-associated Protein (*) , 1996, The Journal of Biological Chemistry.
[38] Matthew P. Anderson,et al. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive , 1992, Nature.
[39] P. Thomas,et al. Alteration of the Cystic Fibrosis Transmembrane Conductance Regulator Folding Pathway , 1996, The Journal of Biological Chemistry.
[40] R. Kopito,et al. Rescuing protein conformation: prospects for pharmacological therapy in cystic fibrosis. , 2002, The Journal of clinical investigation.
[41] J. Marshall,et al. Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis , 1990, Cell.
[42] J. Riordan,et al. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing , 1995, Cell.
[43] J. Riordan,et al. Characterization of polyclonal and monoclonal antibodies to cystic fibrosis transmembrane conductance regulator. , 1998, Methods in enzymology.
[44] G. Lukács,et al. Cooh-Terminal Truncations Promote Proteasome-Dependent Degradation of Mature Cystic Fibrosis Transmembrane Conductance Regulator from Post-Golgi Compartments , 2001, The Journal of cell biology.
[45] M. Evans,et al. Aminoglycoside suppression of a premature stop mutation in a Cftr–/– mouse carrying a human CFTR-G542X transgene , 2002, Journal of Molecular Medicine.
[46] Geoffrey Chang,et al. Structure of MsbA from Vibrio cholera: a multidrug resistance ABC transporter homolog in a closed conformation. , 2003, Journal of molecular biology.
[47] R. Kopito,et al. Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins. , 1994, The Journal of biological chemistry.
[48] M. Welsh,et al. Association of domains within the cystic fibrosis transmembrane conductance regulator. , 1997, Biochemistry.
[49] P. Pedersen,et al. Defective protein folding as a basis of human disease. , 1995, Trends in biochemical sciences.
[50] A. D. Robertson,et al. A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution. , 2000, Proceedings of the National Academy of Sciences of the United States of America.