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Volumn 7, Issue 4, 2008, Pages 295-300

ΔF508 mutation increases conformational flexibility of CFTR protein

Author keywords

CFTR; Cystic fibrosis; Molecular dynamics; Principal component analysis

Indexed keywords

PHENYLALANINE; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 46749137537     PISSN: 15691993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jcf.2007.11.008     Document Type: Article
Times cited : (35)

References (34)
  • 1
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA
    • Riordan J.R., Rommens J.M., Kerem B., et al. Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science 245 (1989) 1066-1073
    • (1989) Science , vol.245 , pp. 1066-1073
    • Riordan, J.R.1    Rommens, J.M.2    Kerem, B.3
  • 2
    • 0024453308 scopus 로고
    • Identification of the cystic fibrosis gene: chromosome walking and jumping
    • Rommens J.M., Iannuzzi M.C., Kerem B., et al. Identification of the cystic fibrosis gene: chromosome walking and jumping. Science 245 (1989) 1059-1065
    • (1989) Science , vol.245 , pp. 1059-1065
    • Rommens, J.M.1    Iannuzzi, M.C.2    Kerem, B.3
  • 3
    • 28944450468 scopus 로고    scopus 로고
    • Association of the cystic fibrosis transmembrane regulator with cal: structural features and molecular dynamics
    • Piserchio A., Fellows A., Madden D.R., and Mierke D.F. Association of the cystic fibrosis transmembrane regulator with cal: structural features and molecular dynamics. Biochemistry 44 (2005) 16158-16166
    • (2005) Biochemistry , vol.44 , pp. 16158-16166
    • Piserchio, A.1    Fellows, A.2    Madden, D.R.3    Mierke, D.F.4
  • 4
    • 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. 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
  • 5
    • 0032957204 scopus 로고    scopus 로고
    • Biosynthesis and degradation of CFTR
    • Kopito R.R. Biosynthesis and degradation of CFTR. Physiol Rev 79 (1999) 167-173
    • (1999) Physiol Rev , vol.79 , pp. 167-173
    • Kopito, R.R.1
  • 6
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward C.L., Omura S., and Kopito R.R. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83 (1995) 121-127
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 7
    • 0347717877 scopus 로고    scopus 로고
    • Modulation of mature cystic fibrosis transmembrane regulator protein by the pdz domain protein cal
    • Cheng J., Wang H., and Guggino W.B. Modulation of mature cystic fibrosis transmembrane regulator protein by the pdz domain protein cal. J Biol Chem 279 (2004) 1892-1898
    • (2004) J Biol Chem , vol.279 , pp. 1892-1898
    • Cheng, J.1    Wang, H.2    Guggino, W.B.3
  • 9
    • 0035838974 scopus 로고    scopus 로고
    • Extending the accuracy limits of prediction for side-chain conformations
    • Xiang Z., and Honig B. Extending the accuracy limits of prediction for side-chain conformations. J Mol Biol 311 (2001) 421-430
    • (2001) J Mol Biol , vol.311 , pp. 421-430
    • Xiang, Z.1    Honig, B.2
  • 10
    • 0037188507 scopus 로고    scopus 로고
    • Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction
    • Xiang Z., Cinque C.S., and Honig B. Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction. PNAS 99 (2002) 7432-7437
    • (2002) PNAS , vol.99 , pp. 7432-7437
    • Xiang, Z.1    Cinque, C.S.2    Honig, B.3
  • 11
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26 (1993) 283-291
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 12
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski G.A., Friesner R.A., Tirado-Rives J., and Jorgensen W.L. Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J Phys Chem B 105 (2001) 6474-6487
    • (2001) J Phys Chem B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 13
    • 0029633168 scopus 로고
    • Gromacs: a message-passing parallel molecular dynamics implementation
    • Berendsen H.J.C., van der Spoel D., and van Drunen R. Gromacs: a message-passing parallel molecular dynamics implementation. Comp Phys Comm 91 (1995) 43-56
    • (1995) Comp Phys Comm , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    van der Spoel, D.2    van Drunen, R.3
  • 14
    • 0030158429 scopus 로고    scopus 로고
    • Prodrg, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules
    • van Aalten D.M., Bywater R., Findlay J.B., Hendlich M., Hooft R.W., and Vriend G. Prodrg, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules. J Comput Aided Mol Des 10 (1996) 255-262
    • (1996) J Comput Aided Mol Des , vol.10 , pp. 255-262
    • van Aalten, D.M.1    Bywater, R.2    Findlay, J.B.3    Hendlich, M.4    Hooft, R.W.5    Vriend, G.6
  • 15
    • 7544226311 scopus 로고    scopus 로고
    • Prodrg: a tool for high-throughput crystallography of protein-ligand complexes
    • Schüttelkopf A.W., and van Aalten D.M. Prodrg: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr D Biol Crystallogr 60 (2004) 1355-1363
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1355-1363
    • Schüttelkopf, A.W.1    van Aalten, D.M.2
  • 17
    • 23444454552 scopus 로고    scopus 로고
    • The amber biomolecular simulation programs
    • Case D.A., Cheatham T.E., Darden T., et al. The amber biomolecular simulation programs. J Comput Chem 26 (2005) 1668-1688
    • (2005) J Comput Chem , vol.26 , pp. 1668-1688
    • Case, D.A.1    Cheatham, T.E.2    Darden, T.3
  • 18
    • 0242443693 scopus 로고    scopus 로고
    • Force fields for protein simulations
    • Ponder J.W., and Case D.A. Force fields for protein simulations. Adv Protein Chem 66 (2003) 27-85
    • (2003) Adv Protein Chem , vol.66 , pp. 27-85
    • Ponder, J.W.1    Case, D.A.2
  • 20
    • 0347784245 scopus 로고
    • Quiet high-resolution computer models of a plasma
    • Hockney R.W., Goel S.P., and Eastwood J.W. Quiet high-resolution computer models of a plasma. J Comp Phys 14 (1974) 148-158
    • (1974) J Comp Phys , vol.14 , pp. 148-158
    • Hockney, R.W.1    Goel, S.P.2    Eastwood, J.W.3
  • 22
    • 33846823909 scopus 로고
    • Particle mesh Ewald: an N*log(N) method for Ewald sums in large systems
    • Darden T., York D., and Pedersen L. Particle mesh Ewald: an N*log(N) method for Ewald sums in large systems. J Chem Phys 98 (1993) 10089-10092
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 26
    • 0025398721 scopus 로고
    • WHAT IF: a molecular modeling and drug design program
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J Mol Graph 8 (1990) 52-56
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 27
    • 41349089279 scopus 로고    scopus 로고
    • Convergence of sampling in protein simulations
    • Hess B. Convergence of sampling in protein simulations. Phys Rev E 65 (2002) 031910
    • (2002) Phys Rev E , vol.65 , pp. 031910
    • Hess, B.1
  • 28
    • 0345745619 scopus 로고
    • Note on a method for calculating corrected sums of squares and products
    • Welford B.P. Note on a method for calculating corrected sums of squares and products. Technometrics 4 (1962) 419-420
    • (1962) Technometrics , vol.4 , pp. 419-420
    • Welford, B.P.1
  • 29
    • 0003294665 scopus 로고    scopus 로고
    • The art of computer programming
    • Addison-Wesley Longman Publishing Co., Inc.
    • Knuth D.E. The art of computer programming. seminumerical algorithms. 3rd ed. 2 (1997), Addison-Wesley Longman Publishing Co., Inc.
    • (1997) seminumerical algorithms. 3rd ed. , vol.2
    • Knuth, D.E.1
  • 30
    • 0034500645 scopus 로고    scopus 로고
    • Similarities between principal components of protein dynamics and random diffusion
    • Hess B. Similarities between principal components of protein dynamics and random diffusion. Phys Rev E 62 (2000) 8438-8448
    • (2000) Phys Rev E , vol.62 , pp. 8438-8448
    • Hess, B.1
  • 31
    • 46749089950 scopus 로고    scopus 로고
    • Persistence of Vision Raytracer (POV-Ray), http://www.povray.org.
    • Persistence of Vision Raytracer (POV-Ray), http://www.povray.org.
  • 32
    • 0019883893 scopus 로고
    • Effect of macromolecular crowding upon the structure and function of an enzyme: glyceraldehyde-3-phosphate dehydrogenase
    • Minton A.P., and Wilf J. Effect of macromolecular crowding upon the structure and function of an enzyme: glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 20 (1981) 4821-4826
    • (1981) Biochemistry , vol.20 , pp. 4821-4826
    • Minton, A.P.1    Wilf, J.2
  • 33
    • 0347994108 scopus 로고    scopus 로고
    • Protein folding by the effects of macromolecular crowding
    • Tokuriki N., Kinjo M., Negi S., et al. Protein folding by the effects of macromolecular crowding. Protein Sci 13 (2004) 125-133
    • (2004) Protein Sci , vol.13 , pp. 125-133
    • Tokuriki, N.1    Kinjo, M.2    Negi, S.3
  • 34
    • 34249081116 scopus 로고    scopus 로고
    • Discovery of the HCV NS3/4A protease inhibitor (1R,5S)-N-[3-amino-1-(cyclobutylmethyl)-2,3-dioxopropyl]-3-[2(S)-[[[(1,1-dimethylethyl)amino]carbonyl]amino]-3,3-dimethyl-1-oxobutyl]-6,6-dimethyl-3-azabicyclo[3.1.0]hexan-2(S)-carboxamide (Sch 503034) II. Key steps in structure-based optimization
    • Prongay A.J., et al. Discovery of the HCV NS3/4A protease inhibitor (1R,5S)-N-[3-amino-1-(cyclobutylmethyl)-2,3-dioxopropyl]-3-[2(S)-[[[(1,1-dimethylethyl)amino]carbonyl]amino]-3,3-dimethyl-1-oxobutyl]-6,6-dimethyl-3-azabicyclo[3.1.0]hexan-2(S)-carboxamide (Sch 503034) II. Key steps in structure-based optimization. J Med Chem 50 (2007) 2310-2318
    • (2007) J Med Chem , vol.50 , pp. 2310-2318
    • Prongay, A.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.