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Volumn 8, Issue SUPPL. 1, 2007, Pages

The role of the UPS in cystic fibrosis

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFIBROTIC AGENT; CFPOT 532; CORR 3A; CORR 4A; CURCUMIN; OMEPRAZOLE; PROTEASOME; TRANSMEMBRANE CONDUCTANCE REGULATOR; UBIQUITIN; VRT 325; CFTR PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 38449087466     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-8-S1-S11     Document Type: Review
Times cited : (66)

References (88)
  • 1
    • 0024453308 scopus 로고
    • Identification of the cystic fibrosis gene: Chromosome walking and jumping
    • 10.1126/science.2772657. 2772657
    • Identification of the cystic fibrosis gene: chromosome walking and jumping. J.M. Rommens, Science 1989 245 4922 1059 65 10.1126/science.2772657 2772657
    • (1989) Science , vol.245 , Issue.4922 , pp. 1059-65
    • Rommens, J.M.1
  • 2
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA
    • 10.1126/science.2475911. 2475911
    • Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. J.R. Riordan, Science 1989 245 4922 1066 73 10.1126/science.2475911 2475911
    • (1989) Science , vol.245 , Issue.4922 , pp. 1066-73
    • Riordan, J.R.1
  • 3
    • 0028223850 scopus 로고
    • The amino-terminal portion of CFTR forms a regulated Cl- channel
    • 10.1016/0092-8674(94)90385-9. 7511062
    • The amino-terminal portion of CFTR forms a regulated Cl- channel. D.N. Sheppard, Cell 1994 76 6 1091 8 10.1016/0092-8674(94)90385-9 7511062
    • (1994) Cell , vol.76 , Issue.6 , pp. 1091-8
    • Sheppard, D.N.1
  • 4
    • 18244377969 scopus 로고    scopus 로고
    • Characterization of wild-type and deltaF508 cystic fibrosis transmembrane regulator in human respiratory epithelia
    • 15716351. 10.1091/mbc.E04-11-1010
    • Characterization of wild-type and deltaF508 cystic fibrosis transmembrane regulator in human respiratory epithelia. S.M. Kreda, Mol Biol Cell 2005 16 5 2154 67 15716351 10.1091/mbc.E04-11-1010
    • (2005) Mol Biol Cell , vol.16 , Issue.5 , pp. 2154-67
    • Kreda, S.M.1
  • 5
    • 0242363119 scopus 로고    scopus 로고
    • Pharmacological approaches to correcting the ion transport defect in cystic fibrosis
    • 14719993
    • Pharmacological approaches to correcting the ion transport defect in cystic fibrosis. G.M. Roomans, Am J Respir Med 2003 2 5 413 31 14719993
    • (2003) Am J Respir Med , vol.2 , Issue.5 , pp. 413-31
    • Roomans, G.M.1
  • 6
    • 0037043328 scopus 로고    scopus 로고
    • Tiny dancers: The integrin-growth factor nexus in angiogenic signaling
    • 10.1083/jcb.200202100. 12105178
    • Tiny dancers: the integrin-growth factor nexus in angiogenic signaling. S.S. Smyth C. Patterson, J Cell Biol 2002 158 1 17 21 10.1083/jcb.200202100 12105178
    • (2002) J Cell Biol , vol.158 , Issue.1 , pp. 17-21
    • Smyth, S.S.1    Patterson, C.2
  • 7
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • 10075921. 10.1093/emboj/18.6.1492
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. G.C. Meacham, Embo J 1999 18 6 1492 505 10075921 10.1093/emboj/18.6.1492
    • (1999) Embo J , vol.18 , Issue.6 , pp. 1492-505
    • Meacham, G.C.1
  • 8
    • 0031017634 scopus 로고    scopus 로고
    • Association of domains within the cystic fibrosis transmembrane conductance regulator
    • 10.1021/bi962174s. 9063876
    • Association of domains within the cystic fibrosis transmembrane conductance regulator. L.S. Ostedgaard, Biochemistry 1997 36 6 1287 94 10.1021/bi962174s 9063876
    • (1997) Biochemistry , vol.36 , Issue.6 , pp. 1287-94
    • Ostedgaard, L.S.1
  • 9
    • 0030931382 scopus 로고    scopus 로고
    • Structural cues involved in endoplasmic reticulum degradation of G85E and G91R mutant cystic fibrosis transmembrane conductance regulator
    • 9276724
    • Structural cues involved in endoplasmic reticulum degradation of G85E and G91R mutant cystic fibrosis transmembrane conductance regulator. X. Xiong, J Clin Invest 1997 100 5 1079 88 9276724
    • (1997) J Clin Invest , vol.100 , Issue.5 , pp. 1079-88
    • Xiong, X.1
  • 10
    • 0037154448 scopus 로고    scopus 로고
    • A new gun in town: The U box is a ubiquitin ligase domain
    • 11805346
    • A new gun in town: the U box is a ubiquitin ligase domain. C. Patterson, Sci STKE 2002 2002 116 PE4 11805346
    • (2002) Sci STKE , vol.2002 , Issue.116 , pp. 4
    • Patterson, C.1
  • 11
    • 26944503059 scopus 로고    scopus 로고
    • Folding of CFTR is predominantly cotranslational
    • 10.1016/j.molcel.2005.09.007. 16246729
    • Folding of CFTR is predominantly cotranslational. B. Kleizen, Mol Cell 2005 20 2 277 87 10.1016/j.molcel.2005.09.007 16246729
    • (2005) Mol Cell , vol.20 , Issue.2 , pp. 277-87
    • Kleizen, B.1
  • 12
    • 0036896021 scopus 로고    scopus 로고
    • Rescuing protein conformation: Prospects for pharmacological therapy in cystic fibrosis
    • 12464661. 10.1172/JCI200216786
    • Rescuing protein conformation: prospects for pharmacological therapy in cystic fibrosis. M.S. Gelman R.R. Kopito, J Clin Invest 2002 110 11 1591 7 12464661 10.1172/JCI200216786
    • (2002) J Clin Invest , vol.110 , Issue.11 , pp. 1591-7
    • Gelman, M.S.1    Kopito, R.R.2
  • 13
    • 0028559511 scopus 로고
    • Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP
    • 7529176
    • Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP. G.L. Lukacs, Embo J 1994 13 24 6076 86 7529176
    • (1994) Embo J , vol.13 , Issue.24 , pp. 6076-86
    • Lukacs, G.L.1
  • 14
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins
    • 7523390
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins. C.L. Ward R.R. Kopito, J Biol Chem 1994 269 41 25710 8 7523390
    • (1994) J Biol Chem , vol.269 , Issue.41 , pp. 25710-8
    • Ward, C.L.1    Kopito, R.R.2
  • 15
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • 10.1016/0092-8674(95)90241-4. 7553864
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. T.J. Jensen, Cell 1995 83 1 129 35 10.1016/0092-8674(95)90241-4 7553864
    • (1995) Cell , vol.83 , Issue.1 , pp. 129-35
    • Jensen, T.J.1
  • 16
    • 5444220240 scopus 로고    scopus 로고
    • COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code
    • 10.1083/jcb.200401035. 15479737
    • COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code. X. Wang, J Cell Biol 2004 167 1 65 74 10.1083/jcb.200401035 15479737
    • (2004) J Cell Biol , vol.167 , Issue.1 , pp. 65-74
    • Wang, X.1
  • 17
    • 0037192856 scopus 로고    scopus 로고
    • Non-conventional trafficking of the cystic fibrosis transmembrane conductance regulator through the early secretory pathway
    • 10.1074/jbc.M110263200. 11799116
    • Non-conventional trafficking of the cystic fibrosis transmembrane conductance regulator through the early secretory pathway. J.S. Yoo, J Biol Chem 2002 277 13 11401 9 10.1074/jbc.M110263200 11799116
    • (2002) J Biol Chem , vol.277 , Issue.13 , pp. 11401-9
    • Yoo, J.S.1
  • 18
    • 18344387226 scopus 로고    scopus 로고
    • Cystic fibrosis
    • 10.1056/NEJMra043184. 15888700
    • Cystic fibrosis. S.M. Rowe S. Miller E.J. Sorscher, N Engl J Med 2005 352 19 1992 2001 10.1056/NEJMra043184 15888700
    • (2005) N Engl J Med , vol.352 , Issue.19 , pp. 1992-2001
    • Rowe, S.M.1    Miller, S.2    Sorscher, E.J.3
  • 19
    • 20344363920 scopus 로고    scopus 로고
    • Novel, mechanism-based therapies for cystic fibrosis
    • 10.1097/01.mop.0000158846.95469.6f. 15891431
    • Novel, mechanism-based therapies for cystic fibrosis. R.C. Rubenstein, Curr Opin Pediatr 2005 17 3 385 92 10.1097/01.mop.0000158846.95469.6f 15891431
    • (2005) Curr Opin Pediatr , vol.17 , Issue.3 , pp. 385-92
    • Rubenstein, R.C.1
  • 20
    • 0029616734 scopus 로고
    • Cystic fibrosis: Genotypic and phenotypic variations
    • 10.1146/annurev.ge.29.120195.004021. 8825494
    • Cystic fibrosis: genotypic and phenotypic variations. J. Zielenski L.C. Tsui, Annu Rev Genet 1995 29 777 807 10.1146/annurev.ge.29.120195.004021 8825494
    • (1995) Annu Rev Genet , vol.29 , pp. 777-807
    • Zielenski, J.1    Tsui, L.C.2
  • 21
    • 11444267334 scopus 로고    scopus 로고
    • Arrest of CFTRDeltaF508 folding
    • 10.1038/nsmb0105-2. 15689966
    • Arrest of CFTRDeltaF508 folding. D.M. Cyr, Nat Struct Mol Biol 2005 12 1 2 3 10.1038/nsmb0105-2 15689966
    • (2005) Nat Struct Mol Biol , vol.12 , Issue.1 , pp. 2-3
    • Cyr, D.M.1
  • 22
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • 10.1016/0092-8674(95)90240-6. 7553863
    • Degradation of CFTR by the ubiquitin-proteasome pathway. C.L. Ward S. Omura R.R. Kopito, Cell 1995 83 1 121 7 10.1016/0092-8674(95)90240-6 7553863
    • (1995) Cell , vol.83 , Issue.1 , pp. 121-7
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 23
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • 10.1083/jcb.143.7.1883. 9864362
    • Aggresomes: a cellular response to misfolded proteins. J.A. Johnston C.L. Ward R.R. Kopito, J Cell Biol 1998 143 7 1883 98 10.1083/jcb.143.7.1883 9864362
    • (1998) J Cell Biol , vol.143 , Issue.7 , pp. 1883-98
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 24
    • 0033614038 scopus 로고    scopus 로고
    • Evidence that endoplasmic reticulum (ER)-associated degradation of cystic fibrosis transmembrane conductance regulator is linked to retrograde translocation from the ER membrane
    • 10.1074/jbc.274.5.2616. 9915789
    • Evidence that endoplasmic reticulum (ER)-associated degradation of cystic fibrosis transmembrane conductance regulator is linked to retrograde translocation from the ER membrane. X. Xiong E. Chong W.R. Skach, J Biol Chem 1999 274 5 2616 24 10.1074/jbc.274.5.2616 9915789
    • (1999) J Biol Chem , vol.274 , Issue.5 , pp. 2616-24
    • Xiong, X.1    Chong, E.2    Skach, W.R.3
  • 25
    • 0037023764 scopus 로고    scopus 로고
    • A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator
    • 10.1074/jbc.M111958200. 11812794
    • A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator. M.S. Gelman E.S. Kannegaard R.R. Kopito, J Biol Chem 2002 277 14 11709 14 10.1074/jbc.M111958200 11812794
    • (2002) J Biol Chem , vol.277 , Issue.14 , pp. 11709-14
    • Gelman, M.S.1    Kannegaard, E.S.2    Kopito, R.R.3
  • 26
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • 9857172. 10.1093/emboj/17.24.7151
    • The ubiquitin-proteasome pathway: on protein death and cell life. A. Ciechanover, Embo J 1998 17 24 7151 60 9857172 10.1093/emboj/17.24.7151
    • (1998) Embo J , vol.17 , Issue.24 , pp. 7151-60
    • Ciechanover, A.1
  • 27
    • 16244373679 scopus 로고    scopus 로고
    • Multiubiquitylation by E4 enzymes: 'One size' doesn't fit all
    • 10.1016/j.tibs.2005.02.004. 15817394
    • Multiubiquitylation by E4 enzymes: 'one size' doesn't fit all. T. Hoppe, Trends Biochem Sci 2005 30 4 183 7 10.1016/j.tibs.2005.02.004 15817394
    • (2005) Trends Biochem Sci , vol.30 , Issue.4 , pp. 183-7
    • Hoppe, T.1
  • 28
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • 10.1016/S0968-0004(02)02125-4. 12114026
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold. D.M. Cyr J. Hohfeld C. Patterson, Trends Biochem Sci 2002 27 7 368 75 10.1016/S0968-0004(02)02125-4 12114026
    • (2002) Trends Biochem Sci , vol.27 , Issue.7 , pp. 368-75
    • Cyr, D.M.1    Hohfeld, J.2    Patterson, C.3
  • 29
    • 20444399163 scopus 로고    scopus 로고
    • The regulation of proteasome degradation by multi-ubiquitin chain binding proteins
    • 10.1016/j.febslet.2005.03.042. 15943965
    • The regulation of proteasome degradation by multi-ubiquitin chain binding proteins. J. Miller C. Gordon, FEBS Lett 2005 579 15 3224 30 10.1016/j.febslet.2005.03.042 15943965
    • (2005) FEBS Lett , vol.579 , Issue.15 , pp. 3224-30
    • Miller, J.1    Gordon, C.2
  • 30
    • 30344482590 scopus 로고    scopus 로고
    • Lingering mysteries of ubiquitin-chain assembly
    • 10.1016/j.cell.2005.12.025. 16413479
    • Lingering mysteries of ubiquitin-chain assembly. M. Hochstrasser, Cell 2006 124 1 27 34 10.1016/j.cell.2005.12.025 16413479
    • (2006) Cell , vol.124 , Issue.1 , pp. 27-34
    • Hochstrasser, M.1
  • 31
    • 23144449208 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins as multifunctional signals
    • 10.1038/nrm1700. 16064136
    • Ubiquitin and ubiquitin-like proteins as multifunctional signals. R.L. Welchman C. Gordon R.J. Mayer, Nat Rev Mol Cell Biol 2005 6 8 599 609 10.1038/nrm1700 16064136
    • (2005) Nat Rev Mol Cell Biol , vol.6 , Issue.8 , pp. 599-609
    • Welchman, R.L.1    Gordon, C.2    Mayer, R.J.3
  • 32
    • 0034602845 scopus 로고    scopus 로고
    • Recognition of the polyubiquitin proteolytic signal
    • 10619848. 10.1093/emboj/19.1.94
    • Recognition of the polyubiquitin proteolytic signal. J.S. Thrower, Embo J 2000 19 1 94 102 10619848 10.1093/emboj/19.1.94
    • (2000) Embo J , vol.19 , Issue.1 , pp. 94-102
    • Thrower, J.S.1
  • 33
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • 10.1038/35050509. 11146634
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. G.C. Meacham, Nat Cell Biol 2001 3 1 100 5 10.1038/35050509 11146634
    • (2001) Nat Cell Biol , vol.3 , Issue.1 , pp. 100-5
    • Meacham, G.C.1
  • 34
    • 11244349206 scopus 로고    scopus 로고
    • A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase
    • 10.1083/jcb.200410065. 15611333
    • A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase. J.M. Younger, J Cell Biol 2004 167 6 1075 85 10.1083/jcb.200410065 15611333
    • (2004) J Cell Biol , vol.167 , Issue.6 , pp. 1075-85
    • Younger, J.M.1
  • 35
    • 33746675669 scopus 로고    scopus 로고
    • Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator
    • 10.1016/j.cell.2006.06.041. 16901789
    • Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. J.M. Younger, Cell 2006 126 3 571 82 10.1016/j.cell.2006.06.041 16901789
    • (2006) Cell , vol.126 , Issue.3 , pp. 571-82
    • Younger, J.M.1
  • 36
    • 0034756104 scopus 로고    scopus 로고
    • From the cradle to the grave: Molecular chaperones that may choose between folding and degradation
    • 11600451. 10.1093/embo-reports/kve206
    • From the cradle to the grave: molecular chaperones that may choose between folding and degradation. J. Hohfeld D.M. Cyr C. Patterson, EMBO Rep 2001 2 10 885 90 11600451 10.1093/embo-reports/kve206
    • (2001) EMBO Rep , vol.2 , Issue.10 , pp. 885-90
    • Hohfeld, J.1    Cyr, D.M.2    Patterson, C.3
  • 37
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: A link between the chaperone and proteasome systems
    • 15115282. 10.1379/1466-1268(2003)008<0303:CALBTC>2.0.CO;2
    • CHIP: a link between the chaperone and proteasome systems. H. McDonough C. Patterson, Cell Stress Chaperones 2003 8 4 303 8 15115282 10.1379/1466-1268(2003)008<0303:CALBTC>2.0.CO;2
    • (2003) Cell Stress Chaperones , vol.8 , Issue.4 , pp. 303-8
    • McDonough, H.1    Patterson, C.2
  • 38
    • 0037401714 scopus 로고    scopus 로고
    • CHIP: A quality-control E3 ligase collaborating with molecular chaperones
    • 10.1016/S1357-2725(02)00394-1. 12672450
    • CHIP: a quality-control E3 ligase collaborating with molecular chaperones. S. Murata T. Chiba K. Tanaka, Int J Biochem Cell Biol 2003 35 5 572 8 10.1016/S1357-2725(02)00394-1 12672450
    • (2003) Int J Biochem Cell Biol , vol.35 , Issue.5 , pp. 572-8
    • Murata, S.1    Chiba, T.2    Tanaka, K.3
  • 39
    • 4344578534 scopus 로고    scopus 로고
    • The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator
    • 15215316. 10.1091/mbc.E04-04-0293
    • The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. S. Alberti, Mol Biol Cell 2004 15 9 4003 10 15215316 10.1091/mbc.E04-04-0293
    • (2004) Mol Biol Cell , vol.15 , Issue.9 , pp. 4003-10
    • Alberti, S.1
  • 40
    • 28644442088 scopus 로고    scopus 로고
    • BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP
    • 16207813. 10.1091/mbc.E05-07-0660
    • BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. V. Arndt, Mol Biol Cell 2005 16 12 5891 900 16207813 10.1091/mbc.E05-07- 0660
    • (2005) Mol Biol Cell , vol.16 , Issue.12 , pp. 5891-900
    • Arndt, V.1
  • 41
    • 33644690646 scopus 로고    scopus 로고
    • Regulation of the Cytoplasmic Quality Control Protein Degradation Pathway by BAG2
    • 10.1074/jbc.M507986200. 16169850
    • Regulation of the Cytoplasmic Quality Control Protein Degradation Pathway by BAG2. Q. Dai, J Biol Chem 2005 280 46 38673 38681 10.1074/jbc.M507986200 16169850
    • (2005) J Biol Chem , vol.280 , Issue.46 , pp. 38673-38681
    • Dai, Q.1
  • 42
    • 0034532302 scopus 로고    scopus 로고
    • Post-translational disruption of the delta Δf508 cystic fibrosis transmembrane conductance regulator (CFTR)-molecular chaperone complex with geldanamycin stabilizes delta Δf508 CFTR in the rabbit reticulocyte lysate
    • 10.1074/jbc.M006278200. 10982807
    • Post-translational disruption of the delta ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR)-molecular chaperone complex with geldanamycin stabilizes delta ΔF508 CFTR in the rabbit reticulocyte lysate. W. Fuller A.W. Cuthbert, J Biol Chem 2000 275 48 37462 8 10.1074/jbc.M006278200 10982807
    • (2000) J Biol Chem , vol.275 , Issue.48 , pp. 37462-8
    • Fuller, W.1    Cuthbert, A.W.2
  • 43
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • 10.1016/0092-8674(90)90148-8. 1699669
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. S.H. Cheng, Cell 1990 63 4 827 34 10.1016/0092-8674(90)90148-8 1699669
    • (1990) Cell , vol.63 , Issue.4 , pp. 827-34
    • Cheng, S.H.1
  • 44
    • 0034811082 scopus 로고    scopus 로고
    • Induction of HSP70 promotes DeltaF508 CFTR trafficking
    • 11404246
    • Induction of HSP70 promotes DeltaF508 CFTR trafficking. L.R. Choo-Kang P.L. Zeitlin, Am J Physiol Lung Cell Mol Physiol 2001 281 1 L58 68 11404246
    • (2001) Am J Physiol Lung Cell Mol Physiol , vol.281 , Issue.1 , pp. 58-68
    • Choo-Kang, L.R.1    Zeitlin, P.L.2
  • 45
    • 44949106027 scopus 로고    scopus 로고
    • Derlin-1 promotes the efficient degradation of CFTR and CFTR folding mutants
    • Derlin-1 promotes the efficient degradation of CFTR and CFTR folding mutants. F. Sun, J Biol Chem 2006
    • (2006) J Biol Chem
    • Sun, F.1
  • 46
    • 26444621357 scopus 로고    scopus 로고
    • Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane
    • 16186510. 10.1073/pnas.0505006102
    • Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Y. Ye, Proc Natl Acad Sci U S A 2005 102 40 14132 8 16186510 10.1073/pnas.0505006102
    • (2005) Proc Natl Acad Sci U S a , vol.102 , Issue.40 , pp. 14132-8
    • Ye, Y.1
  • 47
    • 26244431960 scopus 로고    scopus 로고
    • Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane
    • 16186509. 10.1073/pnas.0505014102
    • Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane. B.N. Lilley H.L. Ploegh, Proc Natl Acad Sci U S A 2005 102 40 14296 301 16186509 10.1073/pnas.0505014102
    • (2005) Proc Natl Acad Sci U S a , vol.102 , Issue.40 , pp. 14296-301
    • Lilley, B.N.1    Ploegh, H.L.2
  • 48
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • 10.1038/nature02656. 15215856
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Y. Ye, Nature 2004 429 6994 841 7 10.1038/nature02656 15215856
    • (2004) Nature , vol.429 , Issue.6994 , pp. 841-7
    • Ye, Y.1
  • 49
    • 28144436887 scopus 로고    scopus 로고
    • The Ubiquitin-domain Protein HERP forms a Complex with Components of the Endoplasmic Reticulum Associated Degradation Pathway
    • 16289116
    • The Ubiquitin-domain Protein HERP forms a Complex with Components of the Endoplasmic Reticulum Associated Degradation Pathway. A. Schulze, J Mol Biol 2005 16289116
    • (2005) J Mol Biol
    • Schulze, A.1
  • 50
    • 27144539523 scopus 로고    scopus 로고
    • Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation
    • 10.1038/ncb1299. 16179952
    • Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation. C. Schuberth A. Buchberger, Nat Cell Biol 2005 7 10 999 1006 10.1038/ncb1299 16179952
    • (2005) Nat Cell Biol , vol.7 , Issue.10 , pp. 999-1006
    • Schuberth, C.1    Buchberger, A.2
  • 51
    • 26244466567 scopus 로고    scopus 로고
    • The retrotranslocation protein Derlin-1 binds peptide: N-glycanase to the endoplasmic reticulum
    • 16055502. 10.1091/mbc.E05-04-0345
    • The retrotranslocation protein Derlin-1 binds peptide: N-glycanase to the endoplasmic reticulum. S. Katiyar S. Joshi W.J. Lennarz, Mol Biol Cell 2005 16 10 4584 94 16055502 10.1091/mbc.E05-04-0345
    • (2005) Mol Biol Cell , vol.16 , Issue.10 , pp. 4584-94
    • Katiyar, S.1    Joshi, S.2    Lennarz, W.J.3
  • 52
    • 0032076341 scopus 로고    scopus 로고
    • RMA1, an Arabidopsis thaliana gene whose cDNA suppresses the yeast sec15 mutation, encodes a novel protein with a RING finger motif and a membrane anchor
    • 9664717
    • RMA1, an Arabidopsis thaliana gene whose cDNA suppresses the yeast sec15 mutation, encodes a novel protein with a RING finger motif and a membrane anchor. N. Matsuda A. Nakano, Plant Cell Physiol 1998 39 5 545 54 9664717
    • (1998) Plant Cell Physiol , vol.39 , Issue.5 , pp. 545-54
    • Matsuda, N.1    Nakano, A.2
  • 53
    • 0034989296 scopus 로고    scopus 로고
    • Rma1, a novel type of RING finger protein conserved from Arabidopsis to human, is a membrane-bound ubiquitin ligase
    • 11329381
    • Rma1, a novel type of RING finger protein conserved from Arabidopsis to human, is a membrane-bound ubiquitin ligase. N. Matsuda, J Cell Sci 2001 114 Pt 10 1949 57 11329381
    • (2001) J Cell Sci , vol.114 , Issue.PART 10 , pp. 1949-57
    • Matsuda, N.1
  • 54
    • 0037099034 scopus 로고    scopus 로고
    • A role for mammalian Ubc6 homologues in ER-associated protein degradation
    • 12082160
    • A role for mammalian Ubc6 homologues in ER-associated protein degradation. U. Lenk, J Cell Sci 2002 115 Pt 14 3007 14 12082160
    • (2002) J Cell Sci , vol.115 , Issue.PART 14 , pp. 3007-14
    • Lenk, U.1
  • 55
    • 0030041781 scopus 로고    scopus 로고
    • Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast
    • 8631297
    • Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. M. Knop, Embo J 1996 15 4 753 63 8631297
    • (1996) Embo J , vol.15 , Issue.4 , pp. 753-63
    • Knop, M.1
  • 56
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • 10.1038/nature02592. 15215855
    • A membrane protein required for dislocation of misfolded proteins from the ER. B.N. Lilley H.L. Ploegh, Nature 2004 429 6994 834 40 10.1038/nature02592 15215855
    • (2004) Nature , vol.429 , Issue.6994 , pp. 834-40
    • Lilley, B.N.1    Ploegh, H.L.2
  • 57
    • 4344560565 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast
    • 15215312. 10.1091/mbc.E04-01-0024
    • Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast. A. Gnann J.R. Riordan D.H. Wolf, Mol Biol Cell 2004 15 9 4125 35 15215312 10.1091/mbc.E04-01- 0024
    • (2004) Mol Biol Cell , vol.15 , Issue.9 , pp. 4125-35
    • Gnann, A.1    Riordan, J.R.2    Wolf, D.H.3
  • 58
    • 31144470450 scopus 로고    scopus 로고
    • Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation
    • 10.1093/hmg/ddi426. 16321991
    • Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation. C.C. Weihl, Hum Mol Genet 2006 15 2 189 99 10.1093/hmg/ddi426 16321991
    • (2006) Hum Mol Genet , vol.15 , Issue.2 , pp. 189-99
    • Weihl, C.C.1
  • 59
    • 32544437041 scopus 로고    scopus 로고
    • Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways
    • 16437165. 10.1038/sj.emboj.7600946
    • Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways. T. Ravid S.G. Kreft M. Hochstrasser, Embo J 2006 25 3 533 43 16437165 10.1038/sj.emboj.7600946
    • (2006) Embo J , vol.25 , Issue.3 , pp. 533-43
    • Ravid, T.1    Kreft, S.G.2    Hochstrasser, M.3
  • 60
    • 33745190973 scopus 로고    scopus 로고
    • Selective inhibition of endoplasmic reticulum-associated degradation rescues DeltaF508-cystic fibrosis transmembrane regulator and suppresses interleukin-8 levels: Therapeutic implications
    • 10.1074/jbc.M600509200. 16621797
    • Selective inhibition of endoplasmic reticulum-associated degradation rescues DeltaF508-cystic fibrosis transmembrane regulator and suppresses interleukin-8 levels: therapeutic implications. N. Vij S. Fang P.L. Zeitlin, J Biol Chem 2006 281 25 17369 78 10.1074/jbc.M600509200 16621797
    • (2006) J Biol Chem , vol.281 , Issue.25 , pp. 17369-78
    • Vij, N.1    Fang, S.2    Zeitlin, P.L.3
  • 61
    • 0742323006 scopus 로고    scopus 로고
    • Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway
    • 14617820. 10.1091/mbc.E03-02-0097
    • Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway. S. Dalal, Mol Biol Cell 2004 15 2 637 48 14617820 10.1091/mbc.E03-02-0097
    • (2004) Mol Biol Cell , vol.15 , Issue.2 , pp. 637-48
    • Dalal, S.1
  • 62
    • 20344393652 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator as a model substrate to study endoplasmic reticulum protein quality control in mammalian cells
    • 15917641
    • Cystic fibrosis transmembrane conductance regulator as a model substrate to study endoplasmic reticulum protein quality control in mammalian cells. J.M. Younger, Methods Mol Biol 2005 301 293 303 15917641
    • (2005) Methods Mol Biol , vol.301 , pp. 293-303
    • Younger, J.M.1
  • 63
    • 0028155017 scopus 로고
    • Expression of cystic fibrosis transmembrane conductance regulator in a model epithelium
    • 7513963
    • Expression of cystic fibrosis transmembrane conductance regulator in a model epithelium. D.N. Sheppard, Am J Physiol 1994 266 4 Pt 1 L405 13 7513963
    • (1994) Am J Physiol , vol.266 , Issue.4 PART 1 , pp. 405-13
    • Sheppard, D.N.1
  • 64
    • 11044234181 scopus 로고    scopus 로고
    • Murine epithelial cells: Isolation and culture
    • 10.1016/j.jcf.2004.05.013. 15463928
    • Murine epithelial cells: isolation and culture. D.J. Davidson, J Cyst Fibros 2004 3 Suppl 2 59 62 10.1016/j.jcf.2004.05.013 15463928
    • (2004) J Cyst Fibros , vol.3 , Issue.SUPPL. 2 , pp. 59-62
    • Davidson, D.J.1
  • 65
    • 0033864526 scopus 로고    scopus 로고
    • Pharmacological modulation of ion transport across wild-type and DeltaF508 CFTR-expressing human bronchial epithelia
    • 10913013
    • Pharmacological modulation of ion transport across wild-type and DeltaF508 CFTR-expressing human bronchial epithelia. D.C. Devor R.J. Bridges J.M. Pilewski, Am J Physiol Cell Physiol 2000 279 2 C461 79 10913013
    • (2000) Am J Physiol Cell Physiol , vol.279 , Issue.2 , pp. 461-79
    • Devor, D.C.1    Bridges, R.J.2    Pilewski, J.M.3
  • 66
    • 33846117944 scopus 로고    scopus 로고
    • Cystic fibrosis mouse models
    • 10.1165/rcmb.2006-0184TR. 16888286
    • Cystic fibrosis mouse models. C. Guilbault, Am J Respir Cell Mol Biol 2007 36 1 1 7 10.1165/rcmb.2006-0184TR 16888286
    • (2007) Am J Respir Cell Mol Biol , vol.36 , Issue.1 , pp. 1-7
    • Guilbault, C.1
  • 67
    • 29944441207 scopus 로고    scopus 로고
    • Species-specific differences in mouse and human airway epithelial biology of recombinant adeno-associated virus transduction
    • 16195538. 10.1165/rcmb.2005-0189OC
    • Species-specific differences in mouse and human airway epithelial biology of recombinant adeno-associated virus transduction. X. Liu, Am J Respir Cell Mol Biol 2006 34 1 56 64 16195538 10.1165/rcmb.2005-0189OC
    • (2006) Am J Respir Cell Mol Biol , vol.34 , Issue.1 , pp. 56-64
    • Liu, X.1
  • 68
    • 0029086350 scopus 로고
    • A mouse model for the cystic fibrosis delta Δf508 mutation
    • 7556083
    • A mouse model for the cystic fibrosis delta ΔF508 mutation. J.H. van Doorninck, Embo J 1995 14 18 4403 11 7556083
    • (1995) Embo J , vol.14 , Issue.18 , pp. 4403-11
    • Van Doorninck, J.H.1
  • 69
    • 0029153220 scopus 로고
    • Generation and characterization of a delta F508 cystic fibrosis mouse model
    • 10.1038/ng0895-445. 7545494
    • Generation and characterization of a delta F508 cystic fibrosis mouse model. W.H. Colledge, Nat Genet 1995 10 4 445 52 10.1038/ng0895-445 7545494
    • (1995) Nat Genet , vol.10 , Issue.4 , pp. 445-52
    • Colledge, W.H.1
  • 70
    • 0028892299 scopus 로고
    • A mouse model for the delta F508 allele of cystic fibrosis
    • 7560099
    • A mouse model for the delta F508 allele of cystic fibrosis. B.G. Zeiher, J Clin Invest 1995 96 4 2051 64 7560099
    • (1995) J Clin Invest , vol.96 , Issue.4 , pp. 2051-64
    • Zeiher, B.G.1
  • 71
    • 0029813969 scopus 로고    scopus 로고
    • A demonstration using mouse models that successful gene therapy for cystic fibrosis requires only partial gene correction
    • 8875228
    • A demonstration using mouse models that successful gene therapy for cystic fibrosis requires only partial gene correction. J.R. Dorin, Gene Ther 1996 3 9 797 801 8875228
    • (1996) Gene Ther , vol.3 , Issue.9 , pp. 797-801
    • Dorin, J.R.1
  • 72
    • 0032584074 scopus 로고    scopus 로고
    • Analysis of ClC-2 channels as an alternative pathway for chloride conduction in cystic fibrosis airway cells
    • 9520461. 10.1073/pnas.95.7.3879
    • Analysis of ClC-2 channels as an alternative pathway for chloride conduction in cystic fibrosis airway cells. E.M. Schwiebert, Proc Natl Acad Sci U S A 1998 95 7 3879 84 9520461 10.1073/pnas.95.7.3879
    • (1998) Proc Natl Acad Sci U S a , vol.95 , Issue.7 , pp. 3879-84
    • Schwiebert, E.M.1
  • 73
    • 0034810492 scopus 로고    scopus 로고
    • ClC-2 Cl- channels in human lung epithelia: Activation by arachidonic acid, amidation, and acid-activated omeprazole
    • 11401826
    • ClC-2 Cl- channels in human lung epithelia: activation by arachidonic acid, amidation, and acid-activated omeprazole. J. Cuppoletti, Am J Physiol Cell Physiol 2001 281 1 C46 54 11401826
    • (2001) Am J Physiol Cell Physiol , vol.281 , Issue.1 , pp. 46-54
    • Cuppoletti, J.1
  • 74
    • 0030773897 scopus 로고    scopus 로고
    • Genistein potentiates wild-type and delta F508-CFTR channel activity
    • 9316420
    • Genistein potentiates wild-type and delta F508-CFTR channel activity. T.C. Hwang, Am J Physiol 1997 273 3 Pt 1 C988 98 9316420
    • (1997) Am J Physiol , vol.273 , Issue.3 PART 1 , pp. 988-98
    • Hwang, T.C.1
  • 75
    • 0031028588 scopus 로고    scopus 로고
    • Modulation of CFTR chloride channels by calyculin a and genistein
    • 9038820
    • Modulation of CFTR chloride channels by calyculin A and genistein. I.C. Yang, Am J Physiol 1997 272 1 Pt 1 C142 55 9038820
    • (1997) Am J Physiol , vol.272 , Issue.1 PART 1 , pp. 142-55
    • Yang, I.C.1
  • 76
    • 0023664272 scopus 로고
    • Genistein, a specific inhibitor of tyrosine-specific protein kinases
    • 3106339
    • Genistein, a specific inhibitor of tyrosine-specific protein kinases. T. Akiyama, J Biol Chem 1987 262 12 5592 5 3106339
    • (1987) J Biol Chem , vol.262 , Issue.12 , pp. 5592-5
    • Akiyama, T.1
  • 77
    • 0028928015 scopus 로고
    • CAMP-independent activation of CFTR Cl channels by the tyrosine kinase inhibitor genistein
    • 7537452
    • cAMP-independent activation of CFTR Cl channels by the tyrosine kinase inhibitor genistein. B. Illek, Am J Physiol 1995 268 4 Pt 1 C886 93 7537452
    • (1995) Am J Physiol , vol.268 , Issue.4 PART 1 , pp. 886-93
    • Illek, B.1
  • 78
    • 15044353957 scopus 로고    scopus 로고
    • Binding site of activators of the cystic fibrosis transmembrane conductance regulator in the nucleotide binding domains
    • 10.1007/s00018-004-4422-3. 15719171
    • Binding site of activators of the cystic fibrosis transmembrane conductance regulator in the nucleotide binding domains. O. Moran L.J. Galietta O. Zegarra-Moran, Cell Mol Life Sci 2005 62 4 446 60 10.1007/s00018-004-4422-3 15719171
    • (2005) Cell Mol Life Sci , vol.62 , Issue.4 , pp. 446-60
    • Moran, O.1    Galietta, L.J.2    Zegarra-Moran, O.3
  • 79
    • 21844448588 scopus 로고    scopus 로고
    • A quantitative description of the activation and inhibition of CFTR by potentiators: Genistein
    • 10.1016/j.febslet.2005.06.026. 15996659
    • A quantitative description of the activation and inhibition of CFTR by potentiators: Genistein. O. Moran O. Zegarra-Moran, FEBS Lett 2005 579 18 3979 83 10.1016/j.febslet.2005.06.026 15996659
    • (2005) FEBS Lett , vol.579 , Issue.18 , pp. 3979-83
    • Moran, O.1    Zegarra-Moran, O.2
  • 80
    • 33745282127 scopus 로고    scopus 로고
    • Specific rescue of cystic fibrosis transmembrane conductance regulator processing mutants using pharmacological chaperones
    • 16624886
    • Specific rescue of cystic fibrosis transmembrane conductance regulator processing mutants using pharmacological chaperones. Y. Wang, Mol Pharmacol 2006 70 1 297 302 16624886
    • (2006) Mol Pharmacol , vol.70 , Issue.1 , pp. 297-302
    • Wang, Y.1
  • 81
    • 33744831154 scopus 로고    scopus 로고
    • Rescue of DeltaF508-CFTR trafficking and gating in human cystic fibrosis airway primary cultures by small molecules
    • 10.1152/ajplung.00169.2005. 16443646
    • Rescue of DeltaF508-CFTR trafficking and gating in human cystic fibrosis airway primary cultures by small molecules. F. Van Goor, Am J Physiol Lung Cell Mol Physiol 2006 290 6 L1117 30 10.1152/ajplung.00169.2005 16443646
    • (2006) Am J Physiol Lung Cell Mol Physiol , vol.290 , Issue.6 , pp. 1117-30
    • Van Goor, F.1
  • 82
    • 24644464284 scopus 로고    scopus 로고
    • Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by high-throughput screening
    • 16127463. 10.1172/JCI24898
    • Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by high-throughput screening. N. Pedemonte, J Clin Invest 2005 115 9 2564 71 16127463 10.1172/JCI24898
    • (2005) J Clin Invest , vol.115 , Issue.9 , pp. 2564-71
    • Pedemonte, N.1
  • 83
    • 11144355340 scopus 로고    scopus 로고
    • Curcumin, a major constituent of turmeric, corrects cystic fibrosis defects
    • 10.1126/science.1093941. 15105504
    • Curcumin, a major constituent of turmeric, corrects cystic fibrosis defects. M.E. Egan, Science 2004 304 5670 600 2 10.1126/science.1093941 15105504
    • (2004) Science , vol.304 , Issue.5670 , pp. 600-2
    • Egan, M.E.1
  • 84
    • 0141676059 scopus 로고    scopus 로고
    • 2-(dialkylamino)-4H-1-benzopyran-4-one derivatives modify chloride conductance in CFTR expressing cells
    • 10.1016/S0014-827X(03)00155-1. 13679192
    • 2-(dialkylamino)-4H-1-benzopyran-4-one derivatives modify chloride conductance in CFTR expressing cells. M. Mazzei, Farmaco 2003 58 9 961 70 10.1016/S0014-827X(03)00155-1 13679192
    • (2003) Farmaco , vol.58 , Issue.9 , pp. 961-70
    • Mazzei, M.1
  • 85
    • 4644360693 scopus 로고    scopus 로고
    • Evidence against the rescue of defective DeltaF508-CFTR cellular processing by curcumin in cell culture and mouse models
    • 10.1074/jbc.M407308200. 15280357
    • Evidence against the rescue of defective DeltaF508-CFTR cellular processing by curcumin in cell culture and mouse models. Y. Song, J Biol Chem 2004 279 39 40629 33 10.1074/jbc.M407308200 15280357
    • (2004) J Biol Chem , vol.279 , Issue.39 , pp. 40629-33
    • Song, Y.1
  • 86
    • 6044268094 scopus 로고    scopus 로고
    • Curcumin does not stimulate cAMP-mediated chloride transport in cystic fibrosis airway epithelial cells
    • 10.1016/j.bbrc.2004.07.146. 15325250
    • Curcumin does not stimulate cAMP-mediated chloride transport in cystic fibrosis airway epithelial cells. A. Dragomir, Biochem Biophys Res Commun 2004 322 2 447 51 10.1016/j.bbrc.2004.07.146 15325250
    • (2004) Biochem Biophys Res Commun , vol.322 , Issue.2 , pp. 447-51
    • Dragomir, A.1
  • 87
    • 7644238103 scopus 로고    scopus 로고
    • Thapsigargin or curcumin does not promote maturation of processing mutants of the ABC transporters, CFTR, and P-glycoprotein
    • 10.1016/j.bbrc.2004.10.070. 15530432
    • Thapsigargin or curcumin does not promote maturation of processing mutants of the ABC transporters, CFTR, and P-glycoprotein. T.W. Loo M.C. Bartlett D.M. Clarke, Biochem Biophys Res Commun 2004 325 2 580 5 10.1016/j.bbrc.2004.10.070 15530432
    • (2004) Biochem Biophys Res Commun , vol.325 , Issue.2 , pp. 580-5
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 88
    • 33645530653 scopus 로고    scopus 로고
    • The chemical chaperone CFcor-325 repairs folding defects in the transmembrane domains of CFTR-processing mutants
    • 16417523. 10.1042/BJ20060013
    • The chemical chaperone CFcor-325 repairs folding defects in the transmembrane domains of CFTR-processing mutants. T.W. Loo, Biochem J 2006 395 3 537 42 16417523 10.1042/BJ20060013
    • (2006) Biochem J , vol.395 , Issue.3 , pp. 537-42
    • Loo, T.W.1


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