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Volumn 427, Issue 6, 2015, Pages 1464-1479

Synonymous codon usage affects the expression of wild type and f508del CFTR

Author keywords

CFTR; CFTR F508del; nonsense mediated decay; protein folding; synonymous codon usage

Indexed keywords

CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; DNA; MESSENGER RNA; CFTR PROTEIN, HUMAN; CHLORIDE; CODON;

EID: 84924063047     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2015.02.003     Document Type: Article
Times cited : (25)

References (108)
  • 1
    • 42149120706 scopus 로고    scopus 로고
    • Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
    • A.W. Serohijos, T. Hegedus, A.A. Aleksandrov, L. He, L. Cui, and N.V. Dokholyan Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function Proc Natl Acad Sci USA 105 2008 3256 3261
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3256-3261
    • Serohijos, A.W.1    Hegedus, T.2    Aleksandrov, A.A.3    He, L.4    Cui, L.5    Dokholyan, N.V.6
  • 2
    • 33745772850 scopus 로고    scopus 로고
    • New insights into cystic fibrosis: Molecular switches that regulate CFTR
    • W.B. Guggino, and B.A. Stanton New insights into cystic fibrosis: molecular switches that regulate CFTR Nat Rev Mol Cell Biol 7 2006 426 436
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 426-436
    • Guggino, W.B.1    Stanton, B.A.2
  • 3
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA
    • J.R. Riordan, J.M. Rommens, B. Kerem, N. Alon, R. Rozmahel, and Z. Grzelczak Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA Science 245 1989 1066 1073
    • (1989) Science , vol.245 , pp. 1066-1073
    • Riordan, J.R.1    Rommens, J.M.2    Kerem, B.3    Alon, N.4    Rozmahel, R.5    Grzelczak, Z.6
  • 4
    • 84874710058 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator (ABCC7) structure
    • J.F. Hunt, C. Wang, and R.C. Ford Cystic fibrosis transmembrane conductance regulator (ABCC7) structure Cold Spring Harbor Perspect Med 3 2013 a009514
    • (2013) Cold Spring Harbor Perspect Med , vol.3 , pp. a009514
    • Hunt, J.F.1    Wang, C.2    Ford, R.C.3
  • 5
    • 0025807911 scopus 로고
    • CAMP-inducible chloride conductance in mouse fibroblast lines stably expressing the human cystic fibrosis transmembrane conductance regulator
    • J.M. Rommens, S. Dho, C.E. Bear, N. Kartner, D. Kennedy, and J.R. Riordan cAMP-inducible chloride conductance in mouse fibroblast lines stably expressing the human cystic fibrosis transmembrane conductance regulator Proc Natl Acad Sci USA 88 1991 7500 7504
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7500-7504
    • Rommens, J.M.1    Dho, S.2    Bear, C.E.3    Kartner, N.4    Kennedy, D.5    Riordan, J.R.6
  • 6
    • 0025760318 scopus 로고
    • Genomic DNA sequence of the cystic fibrosis transmembrane conductance regulator (CFTR) gene
    • J. Zielenski, R. Rozmahel, D. Bozon, B. Kerem, Z. Grzelczak, and J.R. Riordan Genomic DNA sequence of the cystic fibrosis transmembrane conductance regulator (CFTR) gene Genomics 10 1991 214 228
    • (1991) Genomics , vol.10 , pp. 214-228
    • Zielenski, J.1    Rozmahel, R.2    Bozon, D.3    Kerem, B.4    Grzelczak, Z.5    Riordan, J.R.6
  • 7
    • 77956537712 scopus 로고    scopus 로고
    • A synonymous single nucleotide polymorphism in DeltaF508 CFTR alters the secondary structure of the mRNA and the expression of the mutant protein
    • R.A. Bartoszewski, M. Jablonsky, S. Bartoszewska, L. Stevenson, Q. Dai, and J. Kappes A synonymous single nucleotide polymorphism in DeltaF508 CFTR alters the secondary structure of the mRNA and the expression of the mutant protein J Biol Chem 285 2010 28741 28748
    • (2010) J Biol Chem , vol.285 , pp. 28741-28748
    • Bartoszewski, R.A.1    Jablonsky, M.2    Bartoszewska, S.3    Stevenson, L.4    Dai, Q.5    Kappes, J.6
  • 8
    • 84887108066 scopus 로고    scopus 로고
    • The silent codon change I507-ATC → ATT contributes to the severity of the DeltaF508 CFTR channel dysfunction
    • A. Lazrak, L. Fu, V. Bali, R. Bartoszewski, A. Rab, and V. Havasi The silent codon change I507-ATC → ATT contributes to the severity of the DeltaF508 CFTR channel dysfunction FASEB J 27 2013 4630 4645
    • (2013) FASEB J , vol.27 , pp. 4630-4645
    • Lazrak, A.1    Fu, L.2    Bali, V.3    Bartoszewski, R.4    Rab, A.5    Havasi, V.6
  • 9
    • 84866180204 scopus 로고    scopus 로고
    • Molecular chaperones as targets to circumvent the CFTR defect in cystic fibrosis
    • R.A. Chanoux, and R.C. Rubenstein Molecular chaperones as targets to circumvent the CFTR defect in cystic fibrosis Front Pharmacol 3 2012 137
    • (2012) Front Pharmacol , vol.3 , pp. 137
    • Chanoux, R.A.1    Rubenstein, R.C.2
  • 10
    • 84901603981 scopus 로고    scopus 로고
    • Biosynthesis of cystic fibrosis transmembrane conductance regulator
    • I.M. Pranke, and I. Sermet-Gaudelus Biosynthesis of cystic fibrosis transmembrane conductance regulator Int J Biochem Cell Biol 52 2014 26 38
    • (2014) Int J Biochem Cell Biol , vol.52 , pp. 26-38
    • Pranke, I.M.1    Sermet-Gaudelus, I.2
  • 11
    • 19944432524 scopus 로고    scopus 로고
    • Impact of the deltaF508 mutation in first nucleotide-binding domain of human cystic fibrosis transmembrane conductance regulator on domain folding and structure
    • H.A. Lewis, X. Zhao, C. Wang, J.M. Sauder, I. Rooney, and B.W. Noland Impact of the deltaF508 mutation in first nucleotide-binding domain of human cystic fibrosis transmembrane conductance regulator on domain folding and structure J Biol Chem 280 2005 1346 1353
    • (2005) J Biol Chem , vol.280 , pp. 1346-1353
    • Lewis, H.A.1    Zhao, X.2    Wang, C.3    Sauder, J.M.4    Rooney, I.5    Noland, B.W.6
  • 12
    • 77449160593 scopus 로고    scopus 로고
    • Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry
    • H.A. Lewis, C. Wang, X. Zhao, Y. Hamuro, K. Conners, and M.C. Kearins Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry J Mol Biol 396 2010 406 430
    • (2010) J Mol Biol , vol.396 , pp. 406-430
    • Lewis, H.A.1    Wang, C.2    Zhao, X.3    Hamuro, Y.4    Conners, K.5    Kearins, M.C.6
  • 13
    • 0031006695 scopus 로고    scopus 로고
    • Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding
    • B.H. Qu, E.H. Strickland, and P.J. Thomas Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding J Biol Chem 272 1997 15739 15744
    • (1997) J Biol Chem , vol.272 , pp. 15739-15744
    • Qu, B.H.1    Strickland, E.H.2    Thomas, P.J.3
  • 14
    • 77954983869 scopus 로고    scopus 로고
    • Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTR
    • L. He, L.A. Aleksandrov, L. Cui, T.J. Jensen, K.L. Nesbitt, and J.R. Riordan Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTR FASEB J 24 2010 3103 3112
    • (2010) FASEB J , vol.24 , pp. 3103-3112
    • He, L.1    Aleksandrov, L.A.2    Cui, L.3    Jensen, T.J.4    Nesbitt, K.L.5    Riordan, J.R.6
  • 15
    • 0037184104 scopus 로고    scopus 로고
    • Mutations in the nucleotide binding domain 1 signature motif region rescue processing and functional defects of cystic fibrosis transmembrane conductance regulator delta f508
    • A.C. DeCarvalho, L.J. Gansheroff, and J.L. Teem Mutations in the nucleotide binding domain 1 signature motif region rescue processing and functional defects of cystic fibrosis transmembrane conductance regulator delta f508 J Biol Chem 277 2002 35896 35905
    • (2002) J Biol Chem , vol.277 , pp. 35896-35905
    • Decarvalho, A.C.1    Gansheroff, L.J.2    Teem, J.L.3
  • 16
    • 0029864612 scopus 로고    scopus 로고
    • Mutation of R555 in CFTR-delta F508 enhances function and partially corrects defective processing
    • J.L. Teem, M.R. Carson, and M.J. Welsh Mutation of R555 in CFTR-delta F508 enhances function and partially corrects defective processing Receptors Channels 4 1996 63 72
    • (1996) Receptors Channels , vol.4 , pp. 63-72
    • Teem, J.L.1    Carson, M.R.2    Welsh, M.J.3
  • 17
    • 0027153083 scopus 로고
    • Identification of revertants for the cystic fibrosis delta F508 mutation using STE6-CFTR chimeras in yeast
    • J.L. Teem, H.A. Berger, L.S. Ostedgaard, D.P. Rich, L.C. Tsui, and M.J. Welsh Identification of revertants for the cystic fibrosis delta F508 mutation using STE6-CFTR chimeras in yeast Cell 73 1993 335 346
    • (1993) Cell , vol.73 , pp. 335-346
    • Teem, J.L.1    Berger, H.A.2    Ostedgaard, L.S.3    Rich, D.P.4    Tsui, L.C.5    Welsh, M.J.6
  • 19
    • 17744395499 scopus 로고    scopus 로고
    • Biogenesis of CFTR and other polytopic membrane proteins: New roles for the ribosome-translocon complex
    • H. Sadlish, and W.R. Skach Biogenesis of CFTR and other polytopic membrane proteins: new roles for the ribosome-translocon complex J Membr Biol 202 2004 115 126
    • (2004) J Membr Biol , vol.202 , pp. 115-126
    • Sadlish, H.1    Skach, W.R.2
  • 21
    • 65249147217 scopus 로고    scopus 로고
    • Cooperative assembly and misfolding of CFTR domains in vivo
    • K. Du, and G.L. Lukacs Cooperative assembly and misfolding of CFTR domains in vivo Mol Biol Cell 20 2009 1903 1915
    • (2009) Mol Biol Cell , vol.20 , pp. 1903-1915
    • Du, K.1    Lukacs, G.L.2
  • 22
    • 33750842131 scopus 로고    scopus 로고
    • Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
    • X. Wang, J. Venable, P. LaPointe, D.M. Hutt, A.V. Koulov, and J. Coppinger Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis Cell 127 2006 803 815
    • (2006) Cell , vol.127 , pp. 803-815
    • Wang, X.1    Venable, J.2    Lapointe, P.3    Hutt, D.M.4    Koulov, A.V.5    Coppinger, J.6
  • 24
    • 0028094779 scopus 로고
    • Folding of firefly luciferase during translation in a cell-free system
    • V.A. Kolb, E.V. Makeyev, and A.S. Spirin Folding of firefly luciferase during translation in a cell-free system EMBO J 13 1994 3631 3637
    • (1994) EMBO J , vol.13 , pp. 3631-3637
    • Kolb, V.A.1    Makeyev, E.V.2    Spirin, A.S.3
  • 25
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding during glycoprotein synthesis
    • W. Chen, J. Helenius, I. Braakman, and A. Helenius Cotranslational folding and calnexin binding during glycoprotein synthesis Proc Natl Acad Sci USA 92 1995 6229 6233
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6229-6233
    • Chen, W.1    Helenius, J.2    Braakman, I.3    Helenius, A.4
  • 26
    • 0018590219 scopus 로고
    • Co-translational modification of nascent immunoglobulin heavy and light chains
    • L.W. Bergman, and W.M. Kuehl Co-translational modification of nascent immunoglobulin heavy and light chains J Supramol Struct 11 1979 9 24
    • (1979) J Supramol Struct , vol.11 , pp. 9-24
    • Bergman, L.W.1    Kuehl, W.M.2
  • 27
    • 0032983520 scopus 로고    scopus 로고
    • Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
    • J. Frydman, H. Erdjument-Bromage, P. Tempst, and F.U. Hartl Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase Nat Struct Biol 6 1999 697 705
    • (1999) Nat Struct Biol , vol.6 , pp. 697-705
    • Frydman, J.1    Erdjument-Bromage, H.2    Tempst, P.3    Hartl, F.U.4
  • 28
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • W.J. Netzer, and F.U. Hartl Recombination of protein domains facilitated by co-translational folding in eukaryotes Nature 388 1997 343 349
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 30
  • 31
    • 79957798888 scopus 로고    scopus 로고
    • Codon usage: Nature's roadmap to expression and folding of proteins
    • E. Angov Codon usage: nature's roadmap to expression and folding of proteins Biotechnol J 6 2011 650 659
    • (2011) Biotechnol J , vol.6 , pp. 650-659
    • Angov, E.1
  • 32
    • 84874683740 scopus 로고    scopus 로고
    • Non-optimal codon usage affects expression, structure and function of clock protein FRQ
    • M. Zhou, J. Guo, J. Cha, M. Chae, S. Chen, and J.M. Barral Non-optimal codon usage affects expression, structure and function of clock protein FRQ Nature 495 2013 111 115
    • (2013) Nature , vol.495 , pp. 111-115
    • Zhou, M.1    Guo, J.2    Cha, J.3    Chae, M.4    Chen, S.5    Barral, J.M.6
  • 33
    • 79952289327 scopus 로고    scopus 로고
    • Multiparameter RNA and codon optimization: A standardized tool to assess and enhance autologous mammalian gene expression
    • S. Fath, A.P. Bauer, M. Liss, A. Spriestersbach, B. Maertens, and P. Hahn Multiparameter RNA and codon optimization: a standardized tool to assess and enhance autologous mammalian gene expression PLoS One 6 2011 e17596
    • (2011) PLoS One , vol.6 , pp. e17596
    • Fath, S.1    Bauer, A.P.2    Liss, M.3    Spriestersbach, A.4    Maertens, B.5    Hahn, P.6
  • 34
    • 84888617099 scopus 로고    scopus 로고
    • Organizing principles of mammalian nonsense-mediated mRNA decay
    • M.W. Popp, and L.E. Maquat Organizing principles of mammalian nonsense-mediated mRNA decay Annu Rev Genet 47 2013 139 165
    • (2013) Annu Rev Genet , vol.47 , pp. 139-165
    • Popp, M.W.1    Maquat, L.E.2
  • 35
    • 84877818178 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay - Mechanisms of substrate mRNA recognition and degradation in mammalian cells
    • C. Schweingruber, S.C. Rufener, D. Zund, A. Yamashita, and O. Muhlemann Nonsense-mediated mRNA decay - mechanisms of substrate mRNA recognition and degradation in mammalian cells Biochim Biophys Acta 1829 2013 612 623
    • (2013) Biochim Biophys Acta , vol.1829 , pp. 612-623
    • Schweingruber, C.1    Rufener, S.C.2    Zund, D.3    Yamashita, A.4    Muhlemann, O.5
  • 36
    • 84874706482 scopus 로고    scopus 로고
    • When a ribosome encounters a premature termination codon
    • J. Hwang, and Y.K. Kim When a ribosome encounters a premature termination codon BMB Rep 46 2013 9 16
    • (2013) BMB Rep , vol.46 , pp. 9-16
    • Hwang, J.1    Kim, Y.K.2
  • 37
    • 84867850145 scopus 로고    scopus 로고
    • NMD: A multifaceted response to premature translational termination
    • S. Kervestin, and A. Jacobson NMD: a multifaceted response to premature translational termination Nat Rev Mol Cell Biol 13 2012 700 712
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 700-712
    • Kervestin, S.1    Jacobson, A.2
  • 38
    • 23144444226 scopus 로고    scopus 로고
    • JCat: A novel tool to adapt codon usage of a target gene to its potential expression host
    • A. Grote, K. Hiller, M. Scheer, R. Munch, B. Nortemann, and D.C. Hempel JCat: a novel tool to adapt codon usage of a target gene to its potential expression host Nucleic Acids Res 33 2005 W526 W531
    • (2005) Nucleic Acids Res , vol.33 , pp. W526-W531
    • Grote, A.1    Hiller, K.2    Scheer, M.3    Munch, R.4    Nortemann, B.5    Hempel, D.C.6
  • 39
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • N. Ban, P. Nissen, J. Hansen, P.B. Moore, and T.A. Steitz The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution Science 289 2000 905 920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 41
    • 6944256813 scopus 로고    scopus 로고
    • Nonsense surveillance regulates expression of diverse classes of mammalian transcripts and mutes genomic noise
    • J.T. Mendell, N.A. Sharifi, J.L. Meyers, F. Martinez-Murillo, and H.C. Dietz Nonsense surveillance regulates expression of diverse classes of mammalian transcripts and mutes genomic noise Nat Genet 36 2004 1073 1078
    • (2004) Nat Genet , vol.36 , pp. 1073-1078
    • Mendell, J.T.1    Sharifi, N.A.2    Meyers, J.L.3    Martinez-Murillo, F.4    Dietz, H.C.5
  • 42
    • 84884692094 scopus 로고    scopus 로고
    • Comparison of EJC-enhanced and EJC-independent NMD in human cells reveals two partially redundant degradation pathways
    • S. Metze, V.A. Herzog, M.D. Ruepp, and O. Muhlemann Comparison of EJC-enhanced and EJC-independent NMD in human cells reveals two partially redundant degradation pathways RNA 19 2013 1432 1448
    • (2013) RNA , vol.19 , pp. 1432-1448
    • Metze, S.1    Herzog, V.A.2    Ruepp, M.D.3    Muhlemann, O.4
  • 44
    • 33744994837 scopus 로고    scopus 로고
    • EJC-independent degradation of nonsense immunoglobulin-mu mRNA depends on 3′ UTR length
    • M. Buhler, S. Steiner, F. Mohn, A. Paillusson, and O. Muhlemann EJC-independent degradation of nonsense immunoglobulin-mu mRNA depends on 3′ UTR length Nat Struct Mol Biol 13 2006 462 464
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 462-464
    • Buhler, M.1    Steiner, S.2    Mohn, F.3    Paillusson, A.4    Muhlemann, O.5
  • 45
    • 2442442114 scopus 로고    scopus 로고
    • RNA surveillance down-regulates expression of nonfunctional kappa alleles and detects premature termination within the last kappa exon
    • L. Delpy, C. Sirac, E. Magnoux, S. Duchez, and M. Cogne RNA surveillance down-regulates expression of nonfunctional kappa alleles and detects premature termination within the last kappa exon Proc Natl Acad Sci USA 101 2004 7375 7380
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7375-7380
    • Delpy, L.1    Sirac, C.2    Magnoux, E.3    Duchez, S.4    Cogne, M.5
  • 46
    • 43249093760 scopus 로고    scopus 로고
    • Posttranscriptional gene regulation by spatial rearrangement of the 3′ untranslated region
    • A.B. Eberle, L. Stalder, H. Mathys, R.Z. Orozco, and O. Muhlemann Posttranscriptional gene regulation by spatial rearrangement of the 3′ untranslated region PLoS Biol 6 2008 e92
    • (2008) PLoS Biol , vol.6 , pp. e92
    • Eberle, A.B.1    Stalder, L.2    Mathys, H.3    Orozco, R.Z.4    Muhlemann, O.5
  • 47
    • 2342644903 scopus 로고    scopus 로고
    • Unspliced Rous sarcoma virus genomic RNAs are translated and subjected to nonsense-mediated mRNA decay before packaging
    • J.J. LeBlanc, and K.L. Beemon Unspliced Rous sarcoma virus genomic RNAs are translated and subjected to nonsense-mediated mRNA decay before packaging J Virol 78 2004 5139 5146
    • (2004) J Virol , vol.78 , pp. 5139-5146
    • Leblanc, J.J.1    Beemon, K.L.2
  • 48
    • 34948854852 scopus 로고    scopus 로고
    • Failsafe nonsense-mediated mRNA decay does not detectably target eIF4E-bound mRNA
    • D. Matsuda, N. Hosoda, Y.K. Kim, and L.E. Maquat Failsafe nonsense-mediated mRNA decay does not detectably target eIF4E-bound mRNA Nat Struct Mol Biol 14 2007 974 979
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 974-979
    • Matsuda, D.1    Hosoda, N.2    Kim, Y.K.3    Maquat, L.E.4
  • 49
    • 0034928832 scopus 로고    scopus 로고
    • Nonsense-mediated decay of human HEXA mRNA
    • K.S. Rajavel, and E.F. Neufeld Nonsense-mediated decay of human HEXA mRNA Mol Cell Biol 21 2001 5512 5519
    • (2001) Mol Cell Biol , vol.21 , pp. 5512-5519
    • Rajavel, K.S.1    Neufeld, E.F.2
  • 50
    • 43249084802 scopus 로고    scopus 로고
    • A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay
    • G. Singh, I. Rebbapragada, and J. Lykke-Andersen A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay PLoS Biol 6 2008 e111
    • (2008) PLoS Biol , vol.6 , pp. e111
    • Singh, G.1    Rebbapragada, I.2    Lykke-Andersen, J.3
  • 51
    • 0031870169 scopus 로고    scopus 로고
    • Intron function in the nonsense-mediated decay of beta-globin mRNA: Indications that pre-mRNA splicing in the nucleus can influence mRNA translation in the cytoplasm
    • J. Zhang, X. Sun, Y. Qian, and L.E. Maquat Intron function in the nonsense-mediated decay of beta-globin mRNA: indications that pre-mRNA splicing in the nucleus can influence mRNA translation in the cytoplasm RNA 4 1998 801 815
    • (1998) RNA , vol.4 , pp. 801-815
    • Zhang, J.1    Sun, X.2    Qian, Y.3    Maquat, L.E.4
  • 52
    • 44349167189 scopus 로고    scopus 로고
    • Hypoxic inhibition of nonsense-mediated RNA decay regulates gene expression and the integrated stress response
    • L.B. Gardner Hypoxic inhibition of nonsense-mediated RNA decay regulates gene expression and the integrated stress response Mol Cell Biol 28 2008 3729 3741
    • (2008) Mol Cell Biol , vol.28 , pp. 3729-3741
    • Gardner, L.B.1
  • 53
    • 67649307109 scopus 로고    scopus 로고
    • Processing bodies are not required for mammalian nonsense-mediated mRNA decay
    • L. Stalder, and O. Muhlemann Processing bodies are not required for mammalian nonsense-mediated mRNA decay RNA 15 2009 1265 1273
    • (2009) RNA , vol.15 , pp. 1265-1273
    • Stalder, L.1    Muhlemann, O.2
  • 54
    • 8544253956 scopus 로고    scopus 로고
    • A faux 3′-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay
    • N. Amrani, R. Ganesan, S. Kervestin, D.A. Mangus, S. Ghosh, and A. Jacobson A faux 3′-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay Nature 432 2004 112 118
    • (2004) Nature , vol.432 , pp. 112-118
    • Amrani, N.1    Ganesan, R.2    Kervestin, S.3    Mangus, D.A.4    Ghosh, S.5    Jacobson, A.6
  • 55
    • 33947609704 scopus 로고    scopus 로고
    • A conserved role for cytoplasmic poly(A)-binding protein 1 (PABPC1) in nonsense-mediated mRNA decay
    • I. Behm-Ansmant, D. Gatfield, J. Rehwinkel, V. Hilgers, and E. Izaurralde A conserved role for cytoplasmic poly(A)-binding protein 1 (PABPC1) in nonsense-mediated mRNA decay EMBO J 26 2007 1591 1601
    • (2007) EMBO J , vol.26 , pp. 1591-1601
    • Behm-Ansmant, I.1    Gatfield, D.2    Rehwinkel, J.3    Hilgers, V.4    Izaurralde, E.5
  • 56
    • 40949148553 scopus 로고    scopus 로고
    • Interactions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways
    • P.V. Ivanov, N.H. Gehring, J.B. Kunz, M.W. Hentze, and A.E. Kulozik Interactions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways EMBO J 27 2008 736 747
    • (2008) EMBO J , vol.27 , pp. 736-747
    • Ivanov, P.V.1    Gehring, N.H.2    Kunz, J.B.3    Hentze, M.W.4    Kulozik, A.E.5
  • 57
    • 40449131535 scopus 로고    scopus 로고
    • Proximity of the poly(A)-binding protein to a premature termination codon inhibits mammalian nonsense-mediated mRNA decay
    • A.L. Silva, P. Ribeiro, A. Inacio, S.A. Liebhaber, and L. Romao Proximity of the poly(A)-binding protein to a premature termination codon inhibits mammalian nonsense-mediated mRNA decay RNA 14 2008 563 576
    • (2008) RNA , vol.14 , pp. 563-576
    • Silva, A.L.1    Ribeiro, P.2    Inacio, A.3    Liebhaber, S.A.4    Romao, L.5
  • 58
    • 78149270037 scopus 로고    scopus 로고
    • The cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis
    • P.H. Thibodeau, J.M. Richardson, W. Wang, L. Millen, J. Watson, and J.L. Mendoza The cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis J Biol Chem 285 2010 35825 35835
    • (2010) J Biol Chem , vol.285 , pp. 35825-35835
    • Thibodeau, P.H.1    Richardson, J.M.2    Wang, W.3    Millen, L.4    Watson, J.5    Mendoza, J.L.6
  • 59
    • 84862908028 scopus 로고    scopus 로고
    • Correction of both NBD1 energetics and domain interface is required to restore DeltaF508 CFTR folding and function
    • W.M. Rabeh, F. Bossard, H. Xu, T. Okiyoneda, M. Bagdany, and C.M. Mulvihill Correction of both NBD1 energetics and domain interface is required to restore DeltaF508 CFTR folding and function Cell 148 2012 150 163
    • (2012) Cell , vol.148 , pp. 150-163
    • Rabeh, W.M.1    Bossard, F.2    Xu, H.3    Okiyoneda, T.4    Bagdany, M.5    Mulvihill, C.M.6
  • 60
    • 40149102264 scopus 로고    scopus 로고
    • Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding
    • A.W. Serohijos, T. Hegedus, J.R. Riordan, and N.V. Dokholyan Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding PLoS Comput Biol 4 2008 e1000008
    • (2008) PLoS Comput Biol , vol.4 , pp. e1000008
    • Serohijos, A.W.1    Hegedus, T.2    Riordan, J.R.3    Dokholyan, N.V.4
  • 61
    • 0029997424 scopus 로고    scopus 로고
    • Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway
    • B.H. Qu, and P.J. Thomas Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway J Biol Chem 271 1996 7261 7264
    • (1996) J Biol Chem , vol.271 , pp. 7261-7264
    • Qu, B.H.1    Thomas, P.J.2
  • 62
    • 11444266284 scopus 로고    scopus 로고
    • The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR
    • K. Du, M. Sharma, and G.L. Lukacs The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR Nat Struct Mol Biol 12 2005 17 25
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 17-25
    • Du, K.1    Sharma, M.2    Lukacs, G.L.3
  • 63
    • 4544232744 scopus 로고    scopus 로고
    • The DeltaF508 mutation disrupts packing of the transmembrane segments of the cystic fibrosis transmembrane conductance regulator
    • E.Y. Chen, M.C. Bartlett, T.W. Loo, and D.M. Clarke The DeltaF508 mutation disrupts packing of the transmembrane segments of the cystic fibrosis transmembrane conductance regulator J Biol Chem 279 2004 39620 39627
    • (2004) J Biol Chem , vol.279 , pp. 39620-39627
    • Chen, E.Y.1    Bartlett, M.C.2    Loo, T.W.3    Clarke, D.M.4
  • 64
    • 58149279835 scopus 로고    scopus 로고
    • Assembly and misassembly of cystic fibrosis transmembrane conductance regulator: Folding defects caused by deletion of F508 occur before and after the calnexin-dependent association of membrane spanning domain (MSD) 1 and MSD2
    • M.F. Rosser, D.E. Grove, L. Chen, and D.M. Cyr Assembly and misassembly of cystic fibrosis transmembrane conductance regulator: folding defects caused by deletion of F508 occur before and after the calnexin-dependent association of membrane spanning domain (MSD) 1 and MSD2 Mol Biol Cell 19 2008 4570 4579
    • (2008) Mol Biol Cell , vol.19 , pp. 4570-4579
    • Rosser, M.F.1    Grove, D.E.2    Chen, L.3    Cyr, D.M.4
  • 66
    • 27144481548 scopus 로고    scopus 로고
    • Rescue of DeltaF508 and other misprocessed CFTR mutants by a novel quinazoline compound
    • T.W. Loo, M.C. Bartlett, and D.M. Clarke Rescue of DeltaF508 and other misprocessed CFTR mutants by a novel quinazoline compound Mol Pharm 2 2005 407 413
    • (2005) Mol Pharm , vol.2 , pp. 407-413
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 67
    • 33744831154 scopus 로고    scopus 로고
    • Rescue of DeltaF508-CFTR trafficking and gating in human cystic fibrosis airway primary cultures by small molecules
    • F. Van Goor, K.S. Straley, D. Cao, J. Gonzalez, S. Hadida, and A. Hazlewood Rescue of DeltaF508-CFTR trafficking and gating in human cystic fibrosis airway primary cultures by small molecules Am J Physiol Lung Cell Mol Physiol 290 2006 L1117 L1130
    • (2006) Am J Physiol Lung Cell Mol Physiol , vol.290 , pp. L1117-L1130
    • Van Goor, F.1    Straley, K.S.2    Cao, D.3    Gonzalez, J.4    Hadida, S.5    Hazlewood, A.6
  • 68
    • 34548154971 scopus 로고    scopus 로고
    • Additive effect of multiple pharmacological chaperones on maturation of CFTR processing mutants
    • Y. Wang, T.W. Loo, M.C. Bartlett, and D.M. Clarke Additive effect of multiple pharmacological chaperones on maturation of CFTR processing mutants Biochem J 406 2007 257 263
    • (2007) Biochem J , vol.406 , pp. 257-263
    • Wang, Y.1    Loo, T.W.2    Bartlett, M.C.3    Clarke, D.M.4
  • 69
    • 36348989763 scopus 로고    scopus 로고
    • Correctors promote maturation of cystic fibrosis transmembrane conductance regulator (CFTR)-processing mutants by binding to the protein
    • Y. Wang, T.W. Loo, M.C. Bartlett, and D.M. Clarke Correctors promote maturation of cystic fibrosis transmembrane conductance regulator (CFTR)-processing mutants by binding to the protein J Biol Chem 282 2007 33247 33251
    • (2007) J Biol Chem , vol.282 , pp. 33247-33251
    • Wang, Y.1    Loo, T.W.2    Bartlett, M.C.3    Clarke, D.M.4
  • 70
    • 53849149321 scopus 로고    scopus 로고
    • Chemical and biological folding contribute to temperature-sensitive DeltaF508 CFTR trafficking
    • X. Wang, A.V. Koulov, W.A. Kellner, J.R. Riordan, and W.E. Balch Chemical and biological folding contribute to temperature-sensitive DeltaF508 CFTR trafficking Traffic 9 2008 1878 1893
    • (2008) Traffic , vol.9 , pp. 1878-1893
    • Wang, X.1    Koulov, A.V.2    Kellner, W.A.3    Riordan, J.R.4    Balch, W.E.5
  • 72
    • 0027488993 scopus 로고
    • The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment
    • Y. Yang, S. Janich, J.A. Cohn, and J.M. Wilson The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment Proc Natl Acad Sci USA 90 1993 9480 9484
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9480-9484
    • Yang, Y.1    Janich, S.2    Cohn, J.A.3    Wilson, J.M.4
  • 73
    • 0028232167 scopus 로고
    • Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator
    • S. Pind, J.R. Riordan, and D.B. Williams Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator J Biol Chem 269 1994 12784 12788
    • (1994) J Biol Chem , vol.269 , pp. 12784-12788
    • Pind, S.1    Riordan, J.R.2    Williams, D.B.3
  • 74
    • 0032401771 scopus 로고    scopus 로고
    • Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
    • M.A. Loo, T.J. Jensen, L. Cui, Y. Hou, X.B. Chang, and J.R. Riordan Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome EMBO J 17 1998 6879 6887
    • (1998) EMBO J , vol.17 , pp. 6879-6887
    • Loo, M.A.1    Jensen, T.J.2    Cui, L.3    Hou, Y.4    Chang, X.B.5    Riordan, J.R.6
  • 75
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • G.C. Meacham, Z. Lu, S. King, E. Sorscher, A. Tousson, and D.M. Cyr The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis EMBO J 18 1999 1492 1505
    • (1999) EMBO J , vol.18 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 76
    • 0742270642 scopus 로고    scopus 로고
    • Delta F508 CFTR pool in the endoplasmic reticulum is increased by calnexin overexpression
    • T. Okiyoneda, K. Harada, M. Takeya, K. Yamahira, I. Wada, and T. Shuto Delta F508 CFTR pool in the endoplasmic reticulum is increased by calnexin overexpression Mol Biol Cell 15 2004 563 574
    • (2004) Mol Biol Cell , vol.15 , pp. 563-574
    • Okiyoneda, T.1    Harada, K.2    Takeya, M.3    Yamahira, K.4    Wada, I.5    Shuto, T.6
  • 77
    • 0028559511 scopus 로고
    • Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP
    • G.L. Lukacs, A. Mohamed, N. Kartner, X.B. Chang, J.R. Riordan, and S. Grinstein Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP EMBO J 13 1994 6076 6086
    • (1994) EMBO J , vol.13 , pp. 6076-6086
    • Lukacs, G.L.1    Mohamed, A.2    Kartner, N.3    Chang, X.B.4    Riordan, J.R.5    Grinstein, S.6
  • 78
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins
    • C.L. Ward, and R.R. Kopito Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins J Biol Chem 269 1994 25710 25718
    • (1994) J Biol Chem , vol.269 , pp. 25710-25718
    • Ward, C.L.1    Kopito, R.R.2
  • 79
    • 0031915434 scopus 로고    scopus 로고
    • Limited proteolysis as a probe for arrested conformational maturation of delta F508 CFTR
    • F. Zhang, N. Kartner, and G.L. Lukacs Limited proteolysis as a probe for arrested conformational maturation of delta F508 CFTR Nat Struct Biol 5 1998 180 183
    • (1998) Nat Struct Biol , vol.5 , pp. 180-183
    • Zhang, F.1    Kartner, N.2    Lukacs, G.L.3
  • 80
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • S.H. Cheng, R.J. Gregory, J. Marshall, S. Paul, D.W. Souza, and G.A. White Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis Cell 63 1990 827 834
    • (1990) Cell , vol.63 , pp. 827-834
    • Cheng, S.H.1    Gregory, R.J.2    Marshall, J.3    Paul, S.4    Souza, D.W.5    White, G.A.6
  • 81
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • C.L. Ward, S. Omura, and R.R. Kopito Degradation of CFTR by the ubiquitin-proteasome pathway Cell 83 1995 121 127
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 82
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • T.J. Jensen, M.A. Loo, S. Pind, D.B. Williams, A.L. Goldberg, and J.R. Riordan Multiple proteolytic systems, including the proteasome, contribute to CFTR processing Cell 83 1995 129 135
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 83
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
    • G.M. Denning, M.P. Anderson, J.F. Amara, J. Marshall, A.E. Smith, and M.J. Welsh Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive Nature 358 1992 761 764
    • (1992) Nature , vol.358 , pp. 761-764
    • Denning, G.M.1    Anderson, M.P.2    Amara, J.F.3    Marshall, J.4    Smith, A.E.5    Welsh, M.J.6
  • 84
    • 0026325533 scopus 로고
    • Altered chloride ion channel kinetics associated with the delta F508 cystic fibrosis mutation
    • W. Dalemans, P. Barbry, G. Champigny, S. Jallat, K. Dott, and D. Dreyer Altered chloride ion channel kinetics associated with the delta F508 cystic fibrosis mutation Nature 354 1991 526 528
    • (1991) Nature , vol.354 , pp. 526-528
    • Dalemans, W.1    Barbry, P.2    Champigny, G.3    Jallat, S.4    Dott, K.5    Dreyer, D.6
  • 85
    • 79960114415 scopus 로고    scopus 로고
    • Probing conformational rescue induced by a chemical corrector of F508del-cystic fibrosis transmembrane conductance regulator (CFTR) mutant
    • W. Yu, P. Kim Chiaw, and C.E. Bear Probing conformational rescue induced by a chemical corrector of F508del-cystic fibrosis transmembrane conductance regulator (CFTR) mutant J Biol Chem 286 2011 24714 24725
    • (2011) J Biol Chem , vol.286 , pp. 24714-24725
    • Yu, W.1    Kim Chiaw, P.2    Bear, C.E.3
  • 87
    • 66849129301 scopus 로고    scopus 로고
    • A small-molecule modulator interacts directly with deltaPhe508-CFTR to modify its ATPase activity and conformational stability
    • L. Wellhauser, P. Kim Chiaw, S. Pasyk, C. Li, M. Ramjeesingh, and C.E. Bear A small-molecule modulator interacts directly with deltaPhe508-CFTR to modify its ATPase activity and conformational stability Mol Pharmacol 75 2009 1430 1438
    • (2009) Mol Pharmacol , vol.75 , pp. 1430-1438
    • Wellhauser, L.1    Kim Chiaw, P.2    Pasyk, S.3    Li, C.4    Ramjeesingh, M.5    Bear, C.E.6
  • 88
    • 0030042386 scopus 로고    scopus 로고
    • Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation
    • S. Sato, C.L. Ward, M.E. Krouse, J.J. Wine, and R.R. Kopito Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation J Biol Chem 271 1996 635 638
    • (1996) J Biol Chem , vol.271 , pp. 635-638
    • Sato, S.1    Ward, C.L.2    Krouse, M.E.3    Wine, J.J.4    Kopito, R.R.5
  • 89
    • 0030154323 scopus 로고    scopus 로고
    • Influence of molecular and chemical chaperones on protein folding
    • W.J. Welch, and C.R. Brown Influence of molecular and chemical chaperones on protein folding Cell Stress Chaperones 1 1996 109 115
    • (1996) Cell Stress Chaperones , vol.1 , pp. 109-115
    • Welch, W.J.1    Brown, C.R.2
  • 90
    • 0030154620 scopus 로고    scopus 로고
    • Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein
    • C.R. Brown, L.Q. Hong-Brown, J. Biwersi, A.S. Verkman, and W.J. Welch Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein Cell Stress Chaperones 1 1996 117 125
    • (1996) Cell Stress Chaperones , vol.1 , pp. 117-125
    • Brown, C.R.1    Hong-Brown, L.Q.2    Biwersi, J.3    Verkman, A.S.4    Welch, W.J.5
  • 91
    • 33745282127 scopus 로고    scopus 로고
    • Specific rescue of cystic fibrosis transmembrane conductance regulator processing mutants using pharmacological chaperones
    • Y. Wang, M.C. Bartlett, T.W. Loo, and D.M. Clarke Specific rescue of cystic fibrosis transmembrane conductance regulator processing mutants using pharmacological chaperones Mol Pharmacol 70 2006 297 302
    • (2006) Mol Pharmacol , vol.70 , pp. 297-302
    • Wang, Y.1    Bartlett, M.C.2    Loo, T.W.3    Clarke, D.M.4
  • 92
    • 77950428804 scopus 로고    scopus 로고
    • Reduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosis
    • D.M. Hutt, D. Herman, A.P. Rodrigues, S. Noel, J.M. Pilewski, and J. Matteson Reduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosis Nat Chem Biol 6 2010 25 33
    • (2010) Nat Chem Biol , vol.6 , pp. 25-33
    • Hutt, D.M.1    Herman, D.2    Rodrigues, A.P.3    Noel, S.4    Pilewski, J.M.5    Matteson, J.6
  • 93
    • 79551678082 scopus 로고    scopus 로고
    • The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508
    • D.E. Grove, C.Y. Fan, H.Y. Ren, and D.M. Cyr The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508 Mol Biol Cell 22 2011 301 314
    • (2011) Mol Biol Cell , vol.22 , pp. 301-314
    • Grove, D.E.1    Fan, C.Y.2    Ren, H.Y.3    Cyr, D.M.4
  • 94
    • 0030798979 scopus 로고    scopus 로고
    • The molecular chaperone Hsc70 assists the in vitro folding of the N-terminal nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator
    • E. Strickland, B.H. Qu, L. Millen, and P.J. Thomas The molecular chaperone Hsc70 assists the in vitro folding of the N-terminal nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator J Biol Chem 272 1997 25421 25424
    • (1997) J Biol Chem , vol.272 , pp. 25421-25424
    • Strickland, E.1    Qu, B.H.2    Millen, L.3    Thomas, P.J.4
  • 95
    • 51349113842 scopus 로고    scopus 로고
    • Chaperone displacement from mutant cystic fibrosis transmembrane conductance regulator restores its function in human airway epithelia
    • F. Sun, Z. Mi, S.B. Condliffe, C.A. Bertrand, X. Gong, and X. Lu Chaperone displacement from mutant cystic fibrosis transmembrane conductance regulator restores its function in human airway epithelia FASEB J 22 2008 3255 3263
    • (2008) FASEB J , vol.22 , pp. 3255-3263
    • Sun, F.1    Mi, Z.2    Condliffe, S.B.3    Bertrand, C.A.4    Gong, X.5    Lu, X.6
  • 96
    • 84455173094 scopus 로고    scopus 로고
    • 4-Phenylbutyrate stimulates Hsp70 expression through the Elp2 component of elongator and STAT-3 in cystic fibrosis epithelial cells
    • L. Suaud, K. Miller, A.E. Panichelli, R.L. Randell, C.M. Marando, and R.C. Rubenstein 4-Phenylbutyrate stimulates Hsp70 expression through the Elp2 component of elongator and STAT-3 in cystic fibrosis epithelial cells J Biol Chem 286 2011 45083 45092
    • (2011) J Biol Chem , vol.286 , pp. 45083-45092
    • Suaud, L.1    Miller, K.2    Panichelli, A.E.3    Randell, R.L.4    Marando, C.M.5    Rubenstein, R.C.6
  • 97
    • 15544371839 scopus 로고    scopus 로고
    • Assembly of functional CFTR chloride channels
    • J.R. Riordan Assembly of functional CFTR chloride channels Annu Rev Physiol 67 2005 701 718
    • (2005) Annu Rev Physiol , vol.67 , pp. 701-718
    • Riordan, J.R.1
  • 98
    • 80051689133 scopus 로고    scopus 로고
    • Role of Hsc70 binding cycle in CFTR folding and endoplasmic reticulum-associated degradation
    • Y. Matsumura, L.L. David, and W.R. Skach Role of Hsc70 binding cycle in CFTR folding and endoplasmic reticulum-associated degradation Mol Biol Cell 22 2011 2797 2809
    • (2011) Mol Biol Cell , vol.22 , pp. 2797-2809
    • Matsumura, Y.1    David, L.L.2    Skach, W.R.3
  • 99
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • W.E. Balch, R.I. Morimoto, A. Dillin, and J.W. Kelly Adapting proteostasis for disease intervention Science 319 2008 916 919
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 100
    • 68649100255 scopus 로고    scopus 로고
    • The proteostasis boundary in misfolding diseases of membrane traffic
    • D.M. Hutt, E.T. Powers, and W.E. Balch The proteostasis boundary in misfolding diseases of membrane traffic FEBS Lett 583 2009 2639 2646
    • (2009) FEBS Lett , vol.583 , pp. 2639-2646
    • Hutt, D.M.1    Powers, E.T.2    Balch, W.E.3
  • 101
  • 103
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • H. Towbin, T. Staehelin, and J. Gordon Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications Proc Natl Acad Sci USA 76 1979 4350 4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 104
    • 0019061278 scopus 로고
    • Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose
    • P.S. Thomas Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose Proc Natl Acad Sci USA 77 1980 5201 5205
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 5201-5205
    • Thomas, P.S.1
  • 105
    • 24944534978 scopus 로고    scopus 로고
    • Real-time PCR for mRNA quantitation
    • M.L. Wong, and J.F. Medrano Real-time PCR for mRNA quantitation Biotechniques 39 2005 75 85
    • (2005) Biotechniques , vol.39 , pp. 75-85
    • Wong, M.L.1    Medrano, J.F.2
  • 106
    • 0034668118 scopus 로고    scopus 로고
    • Quantitative reverse transcription-polymerase chain reaction to study mRNA decay: Comparison of endpoint and real-time methods
    • T.D. Schmittgen, B.A. Zakrajsek, A.G. Mills, V. Gorn, M.J. Singer, and M.W. Reed Quantitative reverse transcription-polymerase chain reaction to study mRNA decay: comparison of endpoint and real-time methods Anal Biochem 285 2000 194 204
    • (2000) Anal Biochem , vol.285 , pp. 194-204
    • Schmittgen, T.D.1    Zakrajsek, B.A.2    Mills, A.G.3    Gorn, V.4    Singer, M.J.5    Reed, M.W.6
  • 107
    • 34447306625 scopus 로고    scopus 로고
    • A novel synthetic compound that interrupts androgen receptor signaling in human prostate cancer cells
    • S. Lu, A. Wang, and Z. Dong A novel synthetic compound that interrupts androgen receptor signaling in human prostate cancer cells Mol Cancer Ther 6 2007 2057 2064
    • (2007) Mol Cancer Ther , vol.6 , pp. 2057-2064
    • Lu, S.1    Wang, A.2    Dong, Z.3


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