메뉴 건너뛰기




Volumn 21, Issue 4, 2010, Pages 597-609

Interplay between er exit code and domain conformation in cftr misprocessing and rescue

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 70; TRANSMEMBRANE CONDUCTANCE REGULATOR; TRYPSIN;

EID: 76649127413     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E09-05-0427     Document Type: Article
Times cited : (27)

References (59)
  • 1
    • 0032489878 scopus 로고    scopus 로고
    • Cargo selection by the COPII budding machinery during export from the ER
    • Aridor, M., Weissman, J., Bannykh, S., Nuoffer, C., and Balch, W. E. (1998). Cargo selection by the COPII budding machinery during export from the ER. J. Cell Biol. 141, 61-70.
    • (1998) J. Cell Biol , vol.141 , pp. 61-70
    • Aridor, M.1    Weissman, J.2    Bannykh, S.3    Nuoffer, C.4    Balch, W.E.5
  • 3
    • 34547557698 scopus 로고    scopus 로고
    • Correctors of protein trafficking defects identified by a novel high-throughput screening assay
    • Carlile, G. W., Robert, R., Zhang, D., Teske, K. A., Luo, Y., Hanrahan, J. W., and Thomas, D. Y. (2007). Correctors of protein trafficking defects identified by a novel high-throughput screening assay. Chembiochemistry 8, 1012-1020.
    • (2007) Chembiochemistry , vol.8 , pp. 1012-1020
    • Carlile, G.W.1    Robert, R.2    Zhang, D.3    Teske, K.A.4    Luo, Y.5    Hanrahan, J.W.6    Thomas, D.Y.7
  • 4
    • 0033166350 scopus 로고    scopus 로고
    • Removal of multiple arginine-framed trafficking signals overcomes misprocessing of delta F508 CFTR present in most patients with cystic fibrosis
    • Chang, X. B., Cui, L., Hou, Y. X., Jensen, T. J., Aleksandrov, A. A., Mengos, A., and Riordan, J. R. (1999). Removal of multiple arginine-framed trafficking signals overcomes misprocessing of delta F508 CFTR present in most patients with cystic fibrosis. Mol. Cell 4, 137-142.
    • (1999) Mol. Cell , vol.4 , pp. 137-142
    • Chang, X.B.1    Cui, L.2    Hou, Y.X.3    Jensen, T.J.4    Aleksandrov, A.A.5    Mengos, A.6    Riordan, J.R.7
  • 5
    • 4544232744 scopus 로고    scopus 로고
    • The DeltaF508 mutation disrupts packing of the transmembrane segments of the cystic fibrosis transmembrane conductance regulator
    • Chen, E. Y., Bartlett, M. C., Loo, T. W., and Clarke, D. M. (2004). The DeltaF508 mutation disrupts packing of the transmembrane segments of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 279, 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
  • 6
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • Cheng, S. H., Gregory, R. J., Marshall, J., Paul, S., Souza, D. W., White, G. A., O'Riordan, C. R., and Smith, A. E. (1990). Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell 63, 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    O'Riordan, C.R.7    Smith, A.E.8
  • 7
    • 20244390168 scopus 로고    scopus 로고
    • Misprocessing of the CFTR protein leads to mild cystic fibrosis phenotype
    • Clain, J., et al. (2005). Misprocessing of the CFTR protein leads to mild cystic fibrosis phenotype. Hum. Mutat. 25, 360-371.
    • (2005) Hum. Mutat , vol.25 , pp. 360-371
    • Clain, J.1
  • 8
    • 2542532276 scopus 로고    scopus 로고
    • Rescuing cystic fibrosis transmembrane conductance regulator (CFTR)-processing mutants by transcomplementation
    • Cormet-Boyaka, E., Jablonsky, M., Naren, A. P., Jackson, P. L., Muccio, D. D., and Kirk, K. L. (2004). Rescuing cystic fibrosis transmembrane conductance regulator (CFTR)-processing mutants by transcomplementation. Proc. Natl. Acad. Sci. USA 101, 8221-8226.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8221-8226
    • Cormet-Boyaka, E.1    Jablonsky, M.2    Naren, A.P.3    Jackson, P.L.4    Muccio, D.D.5    Kirk, K.L.6
  • 9
    • 33845739839 scopus 로고    scopus 로고
    • Domain interdependence in the biosynthetic assembly of CFTR
    • Cui, L., et al. (2007). Domain interdependence in the biosynthetic assembly of CFTR. J. Mol. Biol. 365, 981-994.
    • (2007) J. Mol. Biol , vol.365 , pp. 981-994
    • Cui, L.1
  • 11
    • 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
    • DeCarvalho, A. C., Gansheroff, L. J., and Teem, J. L. (2002). 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, 35896-35905.
    • (2002) J. Biol. Chem , vol.277 , pp. 35896-35905
    • DeCarvalho, A.C.1    Gansheroff, L.J.2    Teem, J.L.3
  • 12
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
    • Denning, G. M., Anderson, M. P., Amara, J. F., Marshall, J., Smith, A. E., and Welsh, M. J. (1992). Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature 358, 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
  • 13
    • 65249147217 scopus 로고    scopus 로고
    • Cooperative assembly and misfolding of CFTR domains in vivo
    • Du, K., and Lukacs, G. L. (2009). Cooperative assembly and misfolding of CFTR domains in vivo. Mol. Biol. Cell 20, 1903-1915.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1903-1915
    • Du, K.1    Lukacs, G.L.2
  • 14
    • 11444266284 scopus 로고    scopus 로고
    • The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR
    • Du, K., Sharma, M., and Lukacs, G. L. (2005). The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR. Nat. Struct. Mol. Biol. 12, 17-25.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 17-25
    • Du, K.1    Sharma, M.2    Lukacs, G.L.3
  • 15
    • 33745240417 scopus 로고    scopus 로고
    • F508del CFTR with two altered RXR motifs escapes from ER quality control but its channel activity is thermally sensitive
    • Hegedus, T., Aleksandrov, A., Cui, L., Gentzsch, M., Chang, X. B., and Riordan, J. R. (2006). F508del CFTR with two altered RXR motifs escapes from ER quality control but its channel activity is thermally sensitive. Biochim. Biophys. Acta 1758, 565-572.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 565-572
    • Hegedus, T.1    Aleksandrov, A.2    Cui, L.3    Gentzsch, M.4    Chang, X.B.5    Riordan, J.R.6
  • 16
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T. J., Loo, M. A., Pind, S., Williams, D. B., Goldberg, A. L., and Riordan, J. R. (1995). Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83, 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
  • 18
    • 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
    • Lewis, H. A., et al. (2005). 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, 1346-1353.
    • (2005) J. Biol. Chem , vol.280 , pp. 1346-1353
    • Lewis, H.A.1
  • 19
    • 0027380236 scopus 로고
    • The delta F508 mutation decreases the stability of cystic fibrosis transmembrane conductance regulator in the plasma membrane. Determination of functional half-lives on transfected cells
    • Lukacs, G. L., Chang, X. B., Bear, C., Kartner, N., Mohamed, A., Riordan, J. R., and Grinstein, S. (1993). The delta F508 mutation decreases the stability of cystic fibrosis transmembrane conductance regulator in the plasma membrane. Determination of functional half-lives on transfected cells. J. Biol. Chem. 268, 21592-21598.
    • (1993) J. Biol. Chem , vol.268 , pp. 21592-21598
    • Lukacs, G.L.1    Chang, X.B.2    Bear, C.3    Kartner, N.4    Mohamed, A.5    Riordan, J.R.6    Grinstein, S.7
  • 20
    • 0028559511 scopus 로고
    • Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP
    • Lukacs, G. L., Mohamed, A., Kartner, N., Chang, X. B., Riordan, J. R., and Grinstein, S. (1994). Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP. EMBO J. 13, 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
  • 21
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • Meacham, G. C., Lu, Z., King, S., Sorscher, E., Tousson, A., and Cyr, D. M. (1999). The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J. 18, 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
  • 22
    • 0037112755 scopus 로고    scopus 로고
    • Cargo selection into COPII vesicles is driven by the Sec24p subunit
    • Miller, E., Antonny, B., Hamamoto, S., and Schekman, R. (2002). Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J. 21, 6105-6113.
    • (2002) EMBO J , vol.21 , pp. 6105-6113
    • Miller, E.1    Antonny, B.2    Hamamoto, S.3    Schekman, R.4
  • 23
    • 0043029286 scopus 로고    scopus 로고
    • SNARE selectivity of the COPII coat
    • Mossessova, E., Bickford, L. C., and Goldberg, J. (2003). SNARE selectivity of the COPII coat. Cell 114, 483-495.
    • (2003) Cell , vol.114 , pp. 483-495
    • Mossessova, E.1    Bickford, L.C.2    Goldberg, J.3
  • 24
    • 0030812940 scopus 로고    scopus 로고
    • A di-acidic signal required for selective export from the endoplasmic reticulum
    • Nishimura, N., and Balch, W. E. (1997). A di-acidic signal required for selective export from the endoplasmic reticulum. Science 277, 556-558.
    • (1997) Science , vol.277 , pp. 556-558
    • Nishimura, N.1    Balch, W.E.2
  • 25
    • 0032867811 scopus 로고    scopus 로고
    • Processing of CFTR bearing the P574H mutation differs from wild-type and deltaF508-CFTR
    • Ostedgaard, L. S., Zeiher, B., and Welsh, M. J. (1999). Processing of CFTR bearing the P574H mutation differs from wild-type and deltaF508-CFTR. J. Cell Sci. 112(Pt 13), 2091-2098.
    • (1999) J. Cell Sci , vol.112 , Issue.PART 13 , pp. 2091-2098
    • Ostedgaard, L.S.1    Zeiher, B.2    Welsh, M.J.3
  • 26
    • 34548496285 scopus 로고    scopus 로고
    • Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal
    • Pagant, S., Kung, L., Dorrington, M., Lee, M. C., and Miller, E. A. (2007). Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal. Mol. Biol. Cell 18, 3398-3413.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3398-3413
    • Pagant, S.1    Kung, L.2    Dorrington, M.3    Lee, M.C.4    Miller, E.A.5
  • 27
    • 24644464284 scopus 로고    scopus 로고
    • Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by high-throughput screening
    • Pedemonte, N., Lukacs, G. L., Du, K., Caci, E., Zegarra-Moran, O., Galietta, L. J., and Verkman, A. S. (2005). Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by high-throughput screening. J. Clin. Invest. 115, 2564-2571.
    • (2005) J. Clin. Invest , vol.115 , pp. 2564-2571
    • Pedemonte, N.1    Lukacs, G.L.2    Du, K.3    Caci, E.4    Zegarra-Moran, O.5    Galietta, L.J.6    Verkman, A.S.7
  • 28
    • 38349050413 scopus 로고    scopus 로고
    • Solubilizing mutations used to crystallize one CFTR domain attenuate the trafficking and channel defects caused by the major cystic fibrosis mutation
    • Pissarra, L. S., Farinha, C. M., Xu, Z., Schmidt, A., Thibodeau, P. H., Cai, Z., Thomas, P. J., Sheppard, D. N., and Amaral, M. D. (2008). Solubilizing mutations used to crystallize one CFTR domain attenuate the trafficking and channel defects caused by the major cystic fibrosis mutation. Chem. Biol. 15, 62-69.
    • (2008) Chem. Biol , vol.15 , pp. 62-69
    • Pissarra, L.S.1    Farinha, C.M.2    Xu, Z.3    Schmidt, A.4    Thibodeau, P.H.5    Cai, Z.6    Thomas, P.J.7    Sheppard, D.N.8    Amaral, M.D.9
  • 29
    • 84884888474 scopus 로고    scopus 로고
    • Microsome-based assay of endoplasmic reticulum to Golgi transport in mammalian cells
    • ed. J. Celis, San Diego: Elsevier
    • Plutner, H., Gurkan, C., Wang, X., Lapointe, P., and Balch, W. E. (2005). Microsome-based assay of endoplasmic reticulum to Golgi transport in mammalian cells. In: Cell Biology: A Laboratory Handbook, Vol. 2, ed. J. Celis, San Diego: Elsevier, 209-214.
    • (2005) Cell Biology: A Laboratory Handbook , vol.2 , pp. 209-214
    • Plutner, H.1    Gurkan, C.2    Wang, X.3    Lapointe, P.4    Balch, W.E.5
  • 30
    • 0031006695 scopus 로고    scopus 로고
    • Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding
    • Qu, B. H., Strickland, E. H., and Thomas, P. J. (1997). Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding. J. Biol. Chem. 272, 15739-15744.
    • (1997) J. Biol. Chem , vol.272 , pp. 15739-15744
    • Qu, B.H.1    Strickland, E.H.2    Thomas, P.J.3
  • 31
    • 0029997424 scopus 로고    scopus 로고
    • Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway
    • Qu, B. H., and Thomas, P. J. (1996). Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway. J. Biol. Chem. 271, 7261-7264.
    • (1996) J. Biol. Chem , vol.271 , pp. 7261-7264
    • Qu, B.H.1    Thomas, P.J.2
  • 32
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA
    • Riordan, J. R., et al. (1989). Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science 245, 1066-1073.
    • (1989) Science , vol.245 , pp. 1066-1073
    • Riordan, J.R.1
  • 33
    • 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
    • Rosser, M. F., Grove, D. E., Chen, L., and Cyr, D. M. (2008). 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, 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
  • 34
    • 33845197320 scopus 로고    scopus 로고
    • Revertant mutants G550E and 4RK rescue cystic fibrosis mutants in the first nucleotide-binding domain of CFTR by different mechanisms
    • Roxo-Rosa, M., Xu, Z., Schmidt, A., Neto, M., Cai, Z., Soares, C. M., Sheppard, D. N., and Amaral, M. D. (2006). Revertant mutants G550E and 4RK rescue cystic fibrosis mutants in the first nucleotide-binding domain of CFTR by different mechanisms. Proc. Natl. Acad. Sci. USA 103, 17891-17896.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 17891-17896
    • Roxo-Rosa, M.1    Xu, Z.2    Schmidt, A.3    Neto, M.4    Cai, Z.5    Soares, C.M.6    Sheppard, D.N.7    Amaral, M.D.8
  • 35
    • 0030775639 scopus 로고    scopus 로고
    • Disease-associated mutations in cytoplasmic loops 1 and 2 of cystic fibrosis transmembrane conductance regulator impede processing or opening of the channel
    • Seibert, F. S., Jia, Y., Mathews, C. J., Hanrahan, J. W., Riordan, J. R., Loo, T. W., and Clarke, D. M. (1997). Disease-associated mutations in cytoplasmic loops 1 and 2 of cystic fibrosis transmembrane conductance regulator impede processing or opening of the channel. Biochemistry 36, 11966-11974.
    • (1997) Biochemistry , vol.36 , pp. 11966-11974
    • Seibert, F.S.1    Jia, Y.2    Mathews, C.J.3    Hanrahan, J.W.4    Riordan, J.R.5    Loo, T.W.6    Clarke, D.M.7
  • 36
    • 17544374096 scopus 로고    scopus 로고
    • Disease-associated mutations in the fourth cytoplasmic loop of cystic fibrosis transmembrane conductance regulator compromise biosynthetic processing and chloride channel activity
    • Seibert, F. S., Linsdell, P., Loo, T. W., Hanrahan, J. W., Clarke, D. M., and Riordan, J. R. (1996). Disease-associated mutations in the fourth cytoplasmic loop of cystic fibrosis transmembrane conductance regulator compromise biosynthetic processing and chloride channel activity. J. Biol. Chem. 271, 15139-15145.
    • (1996) J. Biol. Chem , vol.271 , pp. 15139-15145
    • Seibert, F.S.1    Linsdell, P.2    Loo, T.W.3    Hanrahan, J.W.4    Clarke, D.M.5    Riordan, J.R.6
  • 37
    • 0028906638 scopus 로고
    • cAMP-dependent protein kinase-mediated phosphorylation of cystic fibrosis transmembrane conductance regulator residue Ser-753 and its role in channel activation
    • Seibert, F. S., Tabcharani, J. A., Chang, X. B., Dulhanty, A. M., Mathews, C., Hanrahan, J. W., and Riordan, J. R. (1995). cAMP-dependent protein kinase-mediated phosphorylation of cystic fibrosis transmembrane conductance regulator residue Ser-753 and its role in channel activation. J. Biol. Chem. 270, 2158-2162.
    • (1995) J. Biol. Chem , vol.270 , pp. 2158-2162
    • Seibert, F.S.1    Tabcharani, J.A.2    Chang, X.B.3    Dulhanty, A.M.4    Mathews, C.5    Hanrahan, J.W.6    Riordan, J.R.7
  • 38
    • 42149120706 scopus 로고    scopus 로고
    • Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
    • Serohijos, A. W., Hegedus, T., Aleksandrov, A. A., He, L., Cui, L., Dokholyan, N. V., and Riordan, J. R. (2008a). 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, 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    Riordan, J.R.7
  • 39
    • 40149102264 scopus 로고    scopus 로고
    • Serohijos, A. W., Hegedus, T., Riordan, J. R., and Dokholyan, N. V. (2008b). Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding. PLoS Comput. Biol. 4, e1000008.
    • Serohijos, A. W., Hegedus, T., Riordan, J. R., and Dokholyan, N. V. (2008b). Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding. PLoS Comput. Biol. 4, e1000008.
  • 40
    • 0035937847 scopus 로고    scopus 로고
    • Conformational and temperature-sensitive stability defects of the delta F508 cystic fibrosis transmembrane conductance regulator in post-endoplasmic reticulum compartments
    • Sharma, M., Benharouga, M., Hu, W., and Lukacs, G. L. (2001). Conformational and temperature-sensitive stability defects of the delta F508 cystic fibrosis transmembrane conductance regulator in post-endoplasmic reticulum compartments. J. Biol. Chem. 276, 8942-8950.
    • (2001) J. Biol. Chem , vol.276 , pp. 8942-8950
    • Sharma, M.1    Benharouga, M.2    Hu, W.3    Lukacs, G.L.4
  • 41
    • 0038363377 scopus 로고    scopus 로고
    • A mutation in the cystic fibrosis transmembrane conductance regulator generates a novel internalization sequence and enhances endocytic rates
    • Silvis, M. R., Picciano, J. A., Bertrand, C., Weixel, K., Bridges, R. J., and Bradbury, N. A. (2003). A mutation in the cystic fibrosis transmembrane conductance regulator generates a novel internalization sequence and enhances endocytic rates. J. Biol. Chem. 278, 11554-11560.
    • (2003) J. Biol. Chem , vol.278 , pp. 11554-11560
    • Silvis, M.R.1    Picciano, J.A.2    Bertrand, C.3    Weixel, K.4    Bridges, R.J.5    Bradbury, N.A.6
  • 42
    • 0028920027 scopus 로고
    • Missense mutation (G480C) in the CFTR gene associated with protein mislocalization but normal chloride channel activity
    • Smit, L. S., et al. (1995). Missense mutation (G480C) in the CFTR gene associated with protein mislocalization but normal chloride channel activity. Hum. Mol. Genet. 4, 269-273.
    • (1995) Hum. Mol. Genet , vol.4 , pp. 269-273
    • Smit, L.S.1
  • 43
    • 0027153083 scopus 로고
    • Identification of revertants for the cystic fibrosis delta F508 mutation using STE6-CFTR chimeras in yeast
    • Teem, J. L., Berger, H. A., Ostedgaard, L. S., Rich, D. P., Tsui, L. C., and Welsh, M. J. (1993). Identification of revertants for the cystic fibrosis delta F508 mutation using STE6-CFTR chimeras in yeast. Cell 73, 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
  • 44
    • 0029864612 scopus 로고    scopus 로고
    • Mutation of R555 in CFTR-delta F508 enhances function and partially corrects defective processing
    • Teem, J. L., Carson, M. R., and Welsh, M. J. (1996). Mutation of R555 in CFTR-delta F508 enhances function and partially corrects defective processing. Receptors Channels 4, 63-72.
    • (1996) Receptors Channels , vol.4 , pp. 63-72
    • Teem, J.L.1    Carson, M.R.2    Welsh, M.J.3
  • 46
    • 33744831154 scopus 로고    scopus 로고
    • Rescue of {Delta}F508-CFTR trafficking and gating in human cystic fibrosis airway primary cultures by small molecules
    • Van Goor, F., et al. (2006). Rescue of {Delta}F508-CFTR trafficking and gating in human cystic fibrosis airway primary cultures by small molecules. Am. J. Physiol. Lung Cell Mol. Physiol. 290, L1117-L1130.
    • (2006) Am. J. Physiol. Lung Cell Mol. Physiol , vol.290
    • Van Goor, F.1
  • 47
    • 0031689866 scopus 로고    scopus 로고
    • Characterization of 19 disease-associated missense mutations in the regulatory domain of the cystic fibrosis transmembrane conductance regulator
    • Vankeerberghen, A., Wei, L., Jaspers, M., Cassiman, J. J., Nilius, B., and Cuppens, H. (1998). Characterization of 19 disease-associated missense mutations in the regulatory domain of the cystic fibrosis transmembrane conductance regulator. Hum. Mol. Genet. 7, 1761-1769.
    • (1998) Hum. Mol. Genet , vol.7 , pp. 1761-1769
    • Vankeerberghen, A.1    Wei, L.2    Jaspers, M.3    Cassiman, J.J.4    Nilius, B.5    Cuppens, H.6
  • 48
    • 41149113942 scopus 로고    scopus 로고
    • Enhanced cell-surface stability of rescued DeltaF508 cystic fibrosis transmembrane conductance regulator (CFTR) by pharmacological chaperones
    • Varga, K., Goldstein, R. F., Jurkuvenaite, A., Chen, L., Matalon, S., Sorscher, E. J., Bebok, Z., and Collawn, J. F. (2008). Enhanced cell-surface stability of rescued DeltaF508 cystic fibrosis transmembrane conductance regulator (CFTR) by pharmacological chaperones. Biochem. J. 410, 555-564.
    • (2008) Biochem. J , vol.410 , pp. 555-564
    • Varga, K.1    Goldstein, R.F.2    Jurkuvenaite, A.3    Chen, L.4    Matalon, S.5    Sorscher, E.J.6    Bebok, Z.7    Collawn, J.F.8
  • 49
    • 53849149321 scopus 로고    scopus 로고
    • Chemical and biological folding contribute to temperature-sensitive DeltaF508 CFTR trafficking
    • Wang, X., Koulov, A. V., Kellner, W. A., Riordan, J. R., and Balch, W. E. (2008). Chemical and biological folding contribute to temperature-sensitive DeltaF508 CFTR trafficking. Traffic 9, 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
  • 50
    • 5444220240 scopus 로고    scopus 로고
    • COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code
    • Wang, X., Matteson, J., An, Y., Moyer, B., Yoo, J. S., Bannykh, S., Wilson, I. A., Riordan, J. R., and Balch, W. E. (2004). COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code. J. Cell Biol. 167, 65-74.
    • (2004) J. Cell Biol , vol.167 , pp. 65-74
    • Wang, X.1    Matteson, J.2    An, Y.3    Moyer, B.4    Yoo, J.S.5    Bannykh, S.6    Wilson, I.A.7    Riordan, J.R.8    Balch, W.E.9
  • 51
    • 33750842131 scopus 로고    scopus 로고
    • Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
    • Wang, X., et al. (2006a). Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 127, 803-815.
    • (2006) Cell , vol.127 , pp. 803-815
    • Wang, X.1
  • 52
    • 33745282127 scopus 로고    scopus 로고
    • Specific rescue of cystic fibrosis transmembrane conductance regulator processing mutants using pharmacological chaperones
    • Wang, Y., Bartlett, M. C., Loo, T. W., and Clarke, D. M. (2006b). Specific rescue of cystic fibrosis transmembrane conductance regulator processing mutants using pharmacological chaperones. Mol. Pharmacol. 70, 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
  • 53
    • 34548154971 scopus 로고    scopus 로고
    • Additive effect of multiple pharmacological chaperones on maturation of CFTR processing mutants
    • Wang, Y., Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2007a). Additive effect of multiple pharmacological chaperones on maturation of CFTR processing mutants. Biochem. J. 406, 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
  • 54
    • 36348989763 scopus 로고    scopus 로고
    • Correctors promote maturation of cystic fibrosis transmembrane conductance regulator (CFTR)-processing mutants by binding to the protein
    • Wang, Y., Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2007b). Correctors promote maturation of cystic fibrosis transmembrane conductance regulator (CFTR)-processing mutants by binding to the protein. J. Biol. Chem. 282, 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
  • 55
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C. L., Omura, S., and Kopito, R. R. (1995). Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 56
    • 1442331948 scopus 로고    scopus 로고
    • Gene expression profile analysis of 4-phenylbutyrate treatment of IB3-1 bronchial epithelial cell line demonstrates a major influence on heatshock proteins
    • Wright, J. M., Zeitlin, P. L., Cebotaru, L., Guggino, S. E., and Guggino, W. B. (2004). Gene expression profile analysis of 4-phenylbutyrate treatment of IB3-1 bronchial epithelial cell line demonstrates a major influence on heatshock proteins. Physiol. Genom. 16, 204-211.
    • (2004) Physiol. Genom , vol.16 , pp. 204-211
    • Wright, J.M.1    Zeitlin, P.L.2    Cebotaru, L.3    Guggino, S.E.4    Guggino, W.B.5
  • 57
    • 0027488993 scopus 로고
    • The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment
    • Yang, Y., Janich, S., Cohn, J. A., and Wilson, J. M. (1993). 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, 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
  • 58
    • 0033103174 scopus 로고    scopus 로고
    • A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels
    • Zerangue, N., Schwappach, B., Jan, Y. N., and Jan, L. Y. (1999). A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels. Neuron 22, 537-548.
    • (1999) Neuron , vol.22 , pp. 537-548
    • Zerangue, N.1    Schwappach, B.2    Jan, Y.N.3    Jan, L.Y.4
  • 59
    • 0031915434 scopus 로고    scopus 로고
    • Limited proteolysis as a probe for arrested conformational maturation of delta F508 CFTR
    • Zhang, F., Kartner, N., and Lukacs, G. L. (1998). Limited proteolysis as a probe for arrested conformational maturation of delta F508 CFTR. Nat. Struct. Biol. 5, 180-183.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 180-183
    • Zhang, F.1    Kartner, N.2    Lukacs, G.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.