메뉴 건너뛰기




Volumn 419, Issue 1-2, 2012, Pages 41-60

Allosteric modulation balances thermodynamic stability and restores function of Δf508 CFTR

Author keywords

ABC transporters; CFTR; DMD simulations; ion channel; protein thermal stability

Indexed keywords

ALPHA PHOSPHATE; PHOSPHATE; TRANSMEMBRANE CONDUCTANCE REGULATOR; UNCLASSIFIED DRUG;

EID: 84860271643     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.03.001     Document Type: Article
Times cited : (79)

References (62)
  • 1
    • 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., and White G.A. 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
  • 2
    • 15544371839 scopus 로고    scopus 로고
    • Assembly of functional CFTR chloride channels
    • Riordan J.R. 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
  • 3
    • 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. 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
  • 4
    • 0032957204 scopus 로고    scopus 로고
    • Biosynthesis and degradation of CFTR
    • Kopito R.R. Biosynthesis and degradation of CFTR Physiol. Rev. 79 1999 S167 173
    • (1999) Physiol. Rev. , vol.79 , pp. 167-173
    • Kopito, R.R.1
  • 5
    • 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. 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
  • 6
    • 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. 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
  • 7
    • 77957302946 scopus 로고    scopus 로고
    • Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1
    • Protasevich I., Yang Z., Wang C., Atwell S., Zhao X., and Emtage S. Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1 Protein Sci. 19 2010 1917 1931
    • (2010) Protein Sci. , vol.19 , pp. 1917-1931
    • Protasevich, I.1    Yang, Z.2    Wang, C.3    Atwell, S.4    Zhao, X.5    Emtage, S.6
  • 8
    • 77957309337 scopus 로고    scopus 로고
    • Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis
    • Wang C., Protasevich I., Yang Z., Seehausen D., Skalak T., and Zhao X. Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis Protein Sci. 19 2010 1932 1947
    • (2010) Protein Sci. , vol.19 , pp. 1932-1947
    • Wang, C.1    Protasevich, I.2    Yang, Z.3    Seehausen, D.4    Skalak, T.5    Zhao, X.6
  • 9
    • 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., Zhao X., Wang C., Sauder J.M., Rooney I., and Noland B.W. 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
  • 10
    • 84856629737 scopus 로고    scopus 로고
    • Insights into CFTR folding, misfolding and correction of the deltaF508 CFTR conformational defect
    • Lukacs G.L., and Verkman A.S. Insights into CFTR folding, misfolding and correction of the deltaF508 CFTR conformational defect Trends Mol. Med. 18 2011 81 91
    • (2011) Trends Mol. Med. , vol.18 , pp. 81-91
    • Lukacs, G.L.1    Verkman, A.S.2
  • 12
    • 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. Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by high-throughput screening J. Clin. Invest. 115 2005 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
  • 13
    • 0033153764 scopus 로고    scopus 로고
    • Rescue of dysfunctional Delta F508-CFTR chloride channel activity by IBMX
    • Schultz B.D., Frizzell R.A., and Bridges R.J. Rescue of dysfunctional Delta F508-CFTR chloride channel activity by IBMX J. Membr. Biol. 170 1999 51 66
    • (1999) J. Membr. Biol. , vol.170 , pp. 51-66
    • Schultz, B.D.1    Frizzell, R.A.2    Bridges, R.J.3
  • 14
    • 82755162382 scopus 로고    scopus 로고
    • Thermally unstable gating of the most common cystic fibrosis mutant channel ({Delta}F508): 'Rescue' by suppressor mutations in nucleotide binding domain 1 and by constitutive mutations in the cytosolic loops
    • Wang W., Okeyo G.O., Tao B., Hong J.S., and Kirk K.L. Thermally unstable gating of the most common cystic fibrosis mutant channel ({Delta}F508): 'Rescue' by suppressor mutations in nucleotide binding domain 1 and by constitutive mutations in the cytosolic loops J. Biol. Chem. 286 2011 41937 41948
    • (2011) J. Biol. Chem. , vol.286 , pp. 41937-41948
    • Wang, W.1    Okeyo, G.O.2    Tao, B.3    Hong, J.S.4    Kirk, K.L.5
  • 16
    • 84863012811 scopus 로고    scopus 로고
    • Human-mouse cystic fibrosis transmembrane conductance regulator (CFTR) chimeras identify regions that partially rescue CFTR-Delta F508 processing and alter its gating defect
    • Dong Q., Ostedgaard L.S., Rogers C., Vermeer D.W., Zhang Y.P., and Welsh M.J. Human-mouse cystic fibrosis transmembrane conductance regulator (CFTR) chimeras identify regions that partially rescue CFTR-Delta F508 processing and alter its gating defect Proc. Natl Acad. Sci. USA 109 2012 917 922
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 917-922
    • Dong, Q.1    Ostedgaard, L.S.2    Rogers, C.3    Vermeer, D.W.4    Zhang, Y.P.5    Welsh, M.J.6
  • 17
    • 0029816943 scopus 로고    scopus 로고
    • - channels and use of human-Xenopus chimeras to investigate the pore properties of CFTR
    • - channels and use of human-Xenopus chimeras to investigate the pore properties of CFTR J. Biol. Chem. 271 1996 25184 25191
    • (1996) J. Biol. Chem. , vol.271 , pp. 25184-25191
    • Price, M.P.1    Ishihara, H.2    Sheppard, D.N.3    Welsh, M.J.4
  • 18
    • 0002578791 scopus 로고
    • Low-conductance chloride channel activated by cAMP in the rectal gland of the shark Squalus acanthias and in cells heterologously expressing the shark CFTR gene
    • Hanrahan J.W., Duguay F., Sansom S., Alon N., Jensen T.J., Riordan J.R., and Grzelczak Z. Low-conductance chloride channel activated by cAMP in the rectal gland of the shark Squalus acanthias and in cells heterologously expressing the shark CFTR gene MDIBL Bull. 32 1993 48 49
    • (1993) MDIBL Bull. , vol.32 , pp. 48-49
    • Hanrahan, J.W.1    Duguay, F.2    Sansom, S.3    Alon, N.4    Jensen, T.J.5    Riordan, J.R.6    Grzelczak, Z.7
  • 19
    • 77955086020 scopus 로고    scopus 로고
    • Regulatory insertion removal restores maturation, stability and function of DeltaF508 CFTR
    • Aleksandrov A.A., Kota P., Aleksandrov L.A., He L., Jensen T., and Cui L. Regulatory insertion removal restores maturation, stability and function of DeltaF508 CFTR J. Mol. Biol. 401 2010 194 210
    • (2010) J. Mol. Biol. , vol.401 , pp. 194-210
    • Aleksandrov, A.A.1    Kota, P.2    Aleksandrov, L.A.3    He, L.4    Jensen, T.5    Cui, L.6
  • 20
    • 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. F508del CFTR with two altered RXR motifs escapes from ER quality control but its channel activity is thermally sensitive Biochim. Biophys. Acta 1758 2006 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
  • 21
    • 78649775607 scopus 로고    scopus 로고
    • The primary folding defect and rescue of DeltaF508 CFTR emerge during translation of the mutant domain
    • Hoelen H., Kleizen B., Schmidt A., Richardson J., Charitou P., Thomas P.J., and Braakman I. The primary folding defect and rescue of DeltaF508 CFTR emerge during translation of the mutant domain PLoS One 5 2010 e15458
    • (2010) PLoS One , vol.5 , pp. 15458
    • Hoelen, H.1    Kleizen, B.2    Schmidt, A.3    Richardson, J.4    Charitou, P.5    Thomas, P.J.6    Braakman, I.7
  • 22
    • 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. 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
  • 23
    • 77955607650 scopus 로고    scopus 로고
    • Peripheral protein quality control removes unfolded CFTR from the plasma membrane
    • Okiyoneda T., Barriere H., Bagdany M., Rabeh W.M., Du K., and Hohfeld J. Peripheral protein quality control removes unfolded CFTR from the plasma membrane Science 329 2010 805 810
    • (2010) Science , vol.329 , pp. 805-810
    • Okiyoneda, T.1    Barriere, H.2    Bagdany, M.3    Rabeh, W.M.4    Du, K.5    Hohfeld, J.6
  • 24
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins
    • Ward C.L., and Kopito R.R. 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
  • 25
    • 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. 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
  • 26
    • 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. 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
  • 27
    • 78149270037 scopus 로고    scopus 로고
    • The cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis
    • Thibodeau P.H., Richardson J.M. III, Wang W., Millen L., Watson J., and Mendoza J.L. 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 Iii, J.M.2    Wang, W.3    Millen, L.4    Watson, J.5    Mendoza, J.L.6
  • 28
    • 61949448788 scopus 로고    scopus 로고
    • Energy landscape along an enzymatic reaction trajectory: Hinges or cracks?
    • Whitford P.C., Onuchic J.N., and Wolynes P.G. Energy landscape along an enzymatic reaction trajectory: hinges or cracks? HFSP J. 2 2008 61 64
    • (2008) HFSP J. , vol.2 , pp. 61-64
    • Whitford, P.C.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 29
    • 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. 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    Riordan, J.R.7
  • 30
    • 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. 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
  • 31
    • 77955025743 scopus 로고    scopus 로고
    • The V510D suppressor mutation stabilizes DeltaF508-CFTR at the cell surface
    • Loo T.W., Bartlett M.C., and Clarke D.M. The V510D suppressor mutation stabilizes DeltaF508-CFTR at the cell surface Biochemistry 49 2010 6352 6357
    • (2010) Biochemistry , vol.49 , pp. 6352-6357
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 32
    • 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. 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 1996 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
  • 33
    • 55549094466 scopus 로고    scopus 로고
    • Multiple membrane-cytoplasmic domain contacts in the cystic fibrosis transmembrane conductance regulator (CFTR) mediate regulation of channel gating
    • He L., Aleksandrov A.A., Serohijos A.W., Hegedus T., Aleksandrov L.A., and Cui L. Multiple membrane-cytoplasmic domain contacts in the cystic fibrosis transmembrane conductance regulator (CFTR) mediate regulation of channel gating J. Biol. Chem. 283 2008 26383 26390
    • (2008) J. Biol. Chem. , vol.283 , pp. 26383-26390
    • He, L.1    Aleksandrov, A.A.2    Serohijos, A.W.3    Hegedus, T.4    Aleksandrov, L.A.5    Cui, L.6
  • 34
    • 33746537716 scopus 로고    scopus 로고
    • A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer
    • Zaitseva J., Oswald C., Jumpertz T., Jenewein S., Wiedenmann A., Holland I.B., and Schmitt L. A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer EMBO J. 25 2006 3432 3443
    • (2006) EMBO J. , vol.25 , pp. 3432-3443
    • Zaitseva, J.1    Oswald, C.2    Jumpertz, T.3    Jenewein, S.4    Wiedenmann, A.5    Holland, I.B.6    Schmitt, L.7
  • 35
    • 77449160593 scopus 로고    scopus 로고
    • Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry
    • Lewis H.A., Wang C., Zhao X., Hamuro Y., Conners K., and Kearins M.C. 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
  • 36
    • 10744230777 scopus 로고    scopus 로고
    • Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator
    • Lewis H.A., Buchanan S.G., Burley S.K., Conners K., Dickey M., and Dorwart M. Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator EMBO J. 23 2004 282 293
    • (2004) EMBO J. , vol.23 , pp. 282-293
    • Lewis, H.A.1    Buchanan, S.G.2    Burley, S.K.3    Conners, K.4    Dickey, M.5    Dorwart, M.6
  • 37
    • 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.W., and Soares C.M. 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 2006 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.W.5    Soares, C.M.6
  • 38
    • 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., and Cai Z. Solubilizing mutations used to crystallize one CFTR domain attenuate the trafficking and channel defects caused by the major cystic fibrosis mutation Chem. Biol. 15 2008 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
  • 39
    • 77951118320 scopus 로고    scopus 로고
    • Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant
    • Atwell S., Brouillette C.G., Conners K., Emtage S., Gheyi T., and Guggino W.B. Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant Protein Eng. Des. Sel. 23 2010 375 384
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 375-384
    • Atwell, S.1    Brouillette, C.G.2    Conners, K.3    Emtage, S.4    Gheyi, T.5    Guggino, W.B.6
  • 40
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar S., Tsai C.J., and Nussinov R. Factors enhancing protein thermostability Protein Eng. 13 2000 179 191
    • (2000) Protein Eng. , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 42
    • 0026316725 scopus 로고
    • Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006
    • Watanabe K., Chishiro K., Kitamura K., and Suzuki Y. Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006 J. Biol. Chem. 266 1991 24287 24294
    • (1991) J. Biol. Chem. , vol.266 , pp. 24287-24294
    • Watanabe, K.1    Chishiro, K.2    Kitamura, K.3    Suzuki, Y.4
  • 43
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • Matthews B.W., Nicholson H., and Becktel W.J. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding Proc. Natl Acad. Sci. USA 84 1987 6663 6667
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 44
    • 0026955827 scopus 로고
    • Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme
    • Nicholson H., Tronrud D.E., Becktel W.J., and Matthews B.W. Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme Biopolymers 32 1992 1431 1441
    • (1992) Biopolymers , vol.32 , pp. 1431-1441
    • Nicholson, H.1    Tronrud, D.E.2    Becktel, W.J.3    Matthews, B.W.4
  • 45
    • 0031837178 scopus 로고    scopus 로고
    • Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase
    • Bogin O., Peretz M., Hacham Y., Korkhin Y., Frolow F., Kalb A.J., and Burstein Y. Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase Protein Sci. 7 1998 1156 1163
    • (1998) Protein Sci. , vol.7 , pp. 1156-1163
    • Bogin, O.1    Peretz, M.2    Hacham, Y.3    Korkhin, Y.4    Frolow, F.5    Kalb, A.J.6    Burstein, Y.7
  • 46
    • 67349154996 scopus 로고    scopus 로고
    • The contribution of proline residues to protein stability is associated with isomerization equilibrium in both unfolded and folded states
    • Ge M., and Pan X.M. The contribution of proline residues to protein stability is associated with isomerization equilibrium in both unfolded and folded states Extremophiles 13 2009 481 489
    • (2009) Extremophiles , vol.13 , pp. 481-489
    • Ge, M.1    Pan, X.M.2
  • 47
  • 48
    • 72049086684 scopus 로고    scopus 로고
    • Molecular dynamics analysis of the wild type and dF508 mutant structures of the human CFTR-nucleotide binding domain 1
    • Bisignano P., and Moran O. Molecular dynamics analysis of the wild type and dF508 mutant structures of the human CFTR-nucleotide binding domain 1 Biochimie 92 2010 51 57
    • (2010) Biochimie , vol.92 , pp. 51-57
    • Bisignano, P.1    Moran, O.2
  • 49
    • 46749137537 scopus 로고    scopus 로고
    • DeltaF508 mutation increases conformational flexibility of CFTR protein
    • Wieczorek G., and Zielenkiewicz P. DeltaF508 mutation increases conformational flexibility of CFTR protein J. Cyst. Fibros. 7 2008 295 300
    • (2008) J. Cyst. Fibros. , vol.7 , pp. 295-300
    • Wieczorek, G.1    Zielenkiewicz, P.2
  • 50
    • 0026325533 scopus 로고
    • Altered chloride-ion channel kinetics associated with the Delta-F508 cystic-fibrosis mutation
    • Dalemans W., Barbry P., Champigny G., Jallat S., Dott K., and Dreyer D. 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
  • 51
    • 79958135819 scopus 로고    scopus 로고
    • Benzbromarone stabilizes DeltaF508 CFTR at the cell surface
    • Loo T.W., Bartlett M.C., and Clarke D.M. Benzbromarone stabilizes DeltaF508 CFTR at the cell surface Biochemistry 50 2011 4393 4395
    • (2011) Biochemistry , vol.50 , pp. 4393-4395
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 53
    • 33645533055 scopus 로고    scopus 로고
    • The role of cystic fibrosis transmembrane conductance regulator phenylalanine 508 side chain in ion channel gating
    • Cui L., Aleksandrov L., Hou Y.X., Gentzsch M., Chen J.H., Riordan J.R., and Aleksandrov A.A. The role of cystic fibrosis transmembrane conductance regulator phenylalanine 508 side chain in ion channel gating J. Physiol. 572 2006 347 358
    • (2006) J. Physiol. , vol.572 , pp. 347-358
    • Cui, L.1    Aleksandrov, L.2    Hou, Y.X.3    Gentzsch, M.4    Chen, J.H.5    Riordan, J.R.6    Aleksandrov, A.A.7
  • 54
    • 0027311276 scopus 로고
    • Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites
    • Chang X.B., Tabcharani J.A., Hou Y.X., Jensen T.J., Kartner N., and Alon N. Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites J. Biol. Chem. 268 1993 11304 11311
    • (1993) J. Biol. Chem. , vol.268 , pp. 11304-11311
    • Chang, X.B.1    Tabcharani, J.A.2    Hou, Y.X.3    Jensen, T.J.4    Kartner, N.5    Alon, N.6
  • 55
    • 0035918147 scopus 로고    scopus 로고
    • Differential interactions of nucleotides at the two nucleotide binding domains of the cystic fibrosis transmembrane conductance regulator
    • Aleksandrov L., Mengos A., Chang X., Aleksandrov A., and Riordan J.R. Differential interactions of nucleotides at the two nucleotide binding domains of the cystic fibrosis transmembrane conductance regulator J. Biol. Chem. 276 2001 12918 12923
    • (2001) J. Biol. Chem. , vol.276 , pp. 12918-12923
    • Aleksandrov, L.1    Mengos, A.2    Chang, X.3    Aleksandrov, A.4    Riordan, J.R.5
  • 56
    • 0032443390 scopus 로고    scopus 로고
    • Discrete molecular dynamics studies of the folding of a protein-like model
    • Dokholyan N.V., Buldyrev S.V., Stanley H.E., and Shakhnovich E.I. Discrete molecular dynamics studies of the folding of a protein-like model Folding Des. 3 1998 577 587
    • (1998) Folding Des. , vol.3 , pp. 577-587
    • Dokholyan, N.V.1    Buldyrev, S.V.2    Stanley, H.E.3    Shakhnovich, E.I.4
  • 57
    • 46049096322 scopus 로고    scopus 로고
    • Ab initio folding of proteins with all-atom discrete molecular dynamics
    • Ding F., Tsao D., Nie H., and Dokholyan N.V. Ab initio folding of proteins with all-atom discrete molecular dynamics Structure 16 2008 1010 1018
    • (2008) Structure , vol.16 , pp. 1010-1018
    • Ding, F.1    Tsao, D.2    Nie, H.3    Dokholyan, N.V.4
  • 58
    • 33746639718 scopus 로고    scopus 로고
    • Emergence of protein fold families through rational design
    • Ding F., and Dokholyan N.V. Emergence of protein fold families through rational design PLoS Comput. Biol. 2 2006 e85
    • (2006) PLoS Comput. Biol. , vol.2 , pp. 85
    • Ding, F.1    Dokholyan, N.V.2
  • 59
    • 78649763344 scopus 로고    scopus 로고
    • Automated minimization of steric clashes in protein structures
    • Ramachandran S., Kota P., Ding F., and Dokholyan N.V. Automated minimization of steric clashes in protein structures Proteins 79 2011 261 270
    • (2011) Proteins , vol.79 , pp. 261-270
    • Ramachandran, S.1    Kota, P.2    Ding, F.3    Dokholyan, N.V.4
  • 60
    • 33847770470 scopus 로고    scopus 로고
    • Multiscale modeling of nucleosome dynamics
    • Sharma S., Ding F., and Dokholyan N.V. Multiscale modeling of nucleosome dynamics Biophys. J. 92 2007 1457 1470
    • (2007) Biophys. J. , vol.92 , pp. 1457-1470
    • Sharma, S.1    Ding, F.2    Dokholyan, N.V.3
  • 61
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method
    • Kumar S., Bouzida D., Swendsen R.H., Kollman P.A., and Rosenberg J.M. The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method J. Comput. Chem. 13 1992 1011 1021
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Swendsen, R.H.3    Kollman, P.A.4    Rosenberg, J.M.5
  • 62
    • 1942423619 scopus 로고    scopus 로고
    • MMTSB Tool Set: Enhanced sampling and multiscale modeling methods for applications in structural biology
    • Feig M., Karanicolas J., and Brooks C.L. III MMTSB Tool Set: enhanced sampling and multiscale modeling methods for applications in structural biology J. Mol. Graphics Modell. 22 2004 377 395
    • (2004) J. Mol. Graphics Modell. , vol.22 , pp. 377-395
    • Feig, M.1    Karanicolas, J.2    Brooks Iii, C.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.