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Volumn 3, Issue 6, 2005, Pages 1391-1409

Covariation analysis of local amino acid sequences in recurrent protein local structures

Author keywords

Covariation; Local structure; Local structure based sequence profile database; Protein folding initiation

Indexed keywords

AMINO ACID;

EID: 31044435608     PISSN: 02197200     EISSN: None     Source Type: Journal    
DOI: 10.1142/S0219720005001648     Document Type: Article
Times cited : (7)

References (31)
  • 1
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • Daggett V, Fersht A, The present view of the mechanism of protein folding, Nature Reviews Molecular Cell Biology 4(6):497-502, 2003.
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.6 , pp. 497-502
    • Daggett, V.1    Fersht, A.2
  • 2
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding?
    • Daggett V, Fersht AR, Is there a unifying mechanism for protein folding? Trends in Biochemical Sciences 28(1):18-25, 2003.
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.1 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2
  • 3
  • 4
    • 0032972986 scopus 로고    scopus 로고
    • Is protein folding hierarchic? I. Local structure and peptide folding
    • Baldwin RL, Rose GD, Is protein folding hierarchic? I. Local structure and peptide folding, Trends Biochem Sci 24(1):26-33, 1999.
    • (1999) Trends Biochem Sci , vol.24 , Issue.1 , pp. 26-33
    • Baldwin, R.L.1    Rose, G.D.2
  • 5
    • 0033080081 scopus 로고    scopus 로고
    • Is protein folding hierarchic? II. Folding intermediates and transition states
    • Baldwin RL, Rose GD, Is protein folding hierarchic? II. Folding intermediates and transition states, Trends Biochem Sci 24(2):77-83, 1999.
    • (1999) Trends Biochem Sci , vol.24 , Issue.2 , pp. 77-83
    • Baldwin, R.L.1    Rose, G.D.2
  • 6
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill KA, Chan HS, From Levinthal to pathways to funnels, Nature Structural Biology 4(1):10-9, 1997.
    • (1997) Nature Structural Biology , vol.4 , Issue.1 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 7
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • Hutchinson EG, Thornton JM, A revised set of potentials for beta-turn formation in proteins, Protein Sci 3(12):2207-2216, 1994.
    • (1994) Protein Sci , vol.3 , Issue.12 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 8
    • 0024279235 scopus 로고
    • Analysis and prediction of the different types of beta-turn in proteins
    • Wilmot CM, Thornton JM, Analysis and prediction of the different types of beta-turn in proteins, Journal of Molecular Biology 203(1):221-232, 1988.
    • (1988) Journal of Molecular Biology , vol.203 , Issue.1 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 9
    • 0024743902 scopus 로고
    • Amino acid sequence templates derived from recurrent turn motifs in proteins: Critical evaluation of their predictive power
    • Rooman MJ, Wodak SJ, Thornton JM, Amino acid sequence templates derived from recurrent turn motifs in proteins: Critical evaluation of their predictive power, Protein Engineering 3(1):23-27, 1989.
    • (1989) Protein Engineering , vol.3 , Issue.1 , pp. 23-27
    • Rooman, M.J.1    Wodak, S.J.2    Thornton, J.M.3
  • 10
    • 0024391832 scopus 로고
    • Conformation of beta-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering
    • Sibanda BL, Blundell TL, Thornton JM, Conformation of beta-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering, J Mol Biol 206(4):759-777, 1989.
    • (1989) J Mol Biol , vol.206 , Issue.4 , pp. 759-777
    • Sibanda, B.L.1    Blundell, T.L.2    Thornton, J.M.3
  • 11
    • 0030596522 scopus 로고    scopus 로고
    • Free energy determinants of secondary structure formation: III. beta-turns and their role in protein folding
    • Yang AS, Hitz B, Honig B, Free energy determinants of secondary structure formation: III. beta-turns and their role in protein folding, J Mol Biol 259(4): 873-882, 1996.
    • (1996) J Mol Biol , vol.259 , Issue.4 , pp. 873-882
    • Yang, A.S.1    Hitz, B.2    Honig, B.3
  • 13
    • 0028295169 scopus 로고
    • Correlated mutations and residue contacts in proteins
    • Gobel U et al., Correlated mutations and residue contacts in proteins, Proteins 18(4):309-317, 1994.
    • (1994) Proteins , vol.18 , Issue.4 , pp. 309-317
    • Gobel, U.1
  • 14
    • 0030970646 scopus 로고    scopus 로고
    • An analysis of simultaneous variation in protein structuresm
    • Chelvanayagam G et al., An analysis of simultaneous variation in protein structuresm, Protein Eng 10(4):307-316, 1997.
    • (1997) Protein Eng , vol.10 , Issue.4 , pp. 307-316
    • Chelvanayagam, G.1
  • 15
    • 0035793216 scopus 로고    scopus 로고
    • Contributions of residue pairing to beta-sheet formation: Conservation and covariation of amino acid residue pairs on antiparallel beta-strands
    • Mandel-Gutfreund Y, Zaremba SM, Gregoret LM, Contributions of residue pairing to beta-sheet formation: Conservation and covariation of amino acid residue pairs on antiparallel beta-strands, J Mol Biol 305(5):1145-1159, 2001.
    • (2001) J Mol Biol , vol.305 , Issue.5 , pp. 1145-1159
    • Mandel-Gutfreund, Y.1    Zaremba, S.M.2    Gregoret, L.M.3
  • 16
    • 0034721944 scopus 로고    scopus 로고
    • Analysis of covariation in an SH3 domain sequence alignment: Applications in tertiary contact prediction and the design of compensating hydrophobic core substitutions
    • Larson SM, Di Nardo AA, Davidson AR, Analysis of covariation in an SH3 domain sequence alignment: Applications in tertiary contact prediction and the design of compensating hydrophobic core substitutions, J Mol Biol 303(3):433-446, 2000.
    • (2000) J Mol Biol , vol.303 , Issue.3 , pp. 433-446
    • Larson, S.M.1    Di Nardo, A.A.2    Davidson, A.R.3
  • 17
    • 0042767572 scopus 로고    scopus 로고
    • Using multiple sequence correlation analysis to characterize functionally important protein regions
    • Saraf MC, Moore GL, Maranas CD, Using multiple sequence correlation analysis to characterize functionally important protein regions, Protein Eng 16(6): 397-406, 2003.
    • (2003) Protein Eng , vol.16 , Issue.6 , pp. 397-406
    • Saraf, M.C.1    Moore, G.L.2    Maranas, C.D.3
  • 18
    • 0037449144 scopus 로고    scopus 로고
    • Systematic variation of amino acid substitutions for stringent assessment of pairwise covariation
    • Govindarajan S et al., Systematic variation of amino acid substitutions for stringent assessment of pairwise covariation, Journal of Molecular Biology 328(5):1061-1069, 2003.
    • (2003) Journal of Molecular Biology , vol.328 , Issue.5 , pp. 1061-1069
    • Govindarajan, S.1
  • 19
    • 0024084164 scopus 로고
    • Coordinated amino acid changes in homologous protein families
    • Altschuh D et al., Coordinated amino acid changes in homologous protein families, Protein Eng 2(3): 193-199, 1988.
    • (1988) Protein Eng , vol.2 , Issue.3 , pp. 193-199
    • Altschuh, D.1
  • 20
    • 0027092678 scopus 로고
    • Selection of representative protein data sets
    • Hobohm U et al., Selection of representative protein data sets, Protein Sci 1(3):409-417, 1992.
    • (1992) Protein Sci , vol.1 , Issue.3 , pp. 409-417
    • Hobohm, U.1
  • 21
    • 0031557395 scopus 로고    scopus 로고
    • An automated classification of the structure of protein loops
    • Oliva B et al., An automated classification of the structure of protein loops, J Mol Biol 266(4):814-830, 1997.
    • (1997) J Mol Biol , vol.266 , Issue.4 , pp. 814-830
    • Oliva, B.1
  • 22
    • 0037818341 scopus 로고    scopus 로고
    • Local structure prediction with local structure-based sequence profiles
    • Yang A-S, Wang L-Y, Local structure prediction with local structure-based sequence profiles, Bioinformatics 19(10):1267-1274, 2003.
    • (2003) Bioinformatics , vol.19 , Issue.10 , pp. 1267-1274
    • Yang, A.-S.1    Wang, L.-Y.2
  • 23
    • 84972545970 scopus 로고
    • A survey of exact inference for contingency tables
    • Agresi A, A survey of exact inference for contingency tables, Statistical Sciences 7(1): 131-177, 1992.
    • (1992) Statistical Sciences , vol.7 , Issue.1 , pp. 131-177
    • Agresi, A.1
  • 25
    • 0032568649 scopus 로고    scopus 로고
    • A unified statistical framework for sequence comparison and structure comparison
    • Levitt M, Gerstein M, A unified statistical framework for sequence comparison and structure comparison, Proc Natl Acad Sci USA 95(11):5913-5920, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.11 , pp. 5913-5920
    • Levitt, M.1    Gerstein, M.2
  • 26
    • 0029906607 scopus 로고    scopus 로고
    • Dirichlet mixtures: A method for improved detection of weak but significant protein sequence homology
    • Sjolander K et al., Dirichlet mixtures: A method for improved detection of weak but significant protein sequence homology, Comput Appl Biosci 12(4):327-345, 1996.
    • (1996) Comput Appl Biosci , vol.12 , Issue.4 , pp. 327-345
    • Sjolander, K.1
  • 27
    • 0031604140 scopus 로고    scopus 로고
    • Phylogenetic inference in protein superfamilies: Analysis of SH2 domains
    • Sjolander K, Phylogenetic inference in protein superfamilies: Analysis of SH2 domains, Proc Int Conf Intell Syst Mol Biol 6:165-174, 1998.
    • (1998) Proc Int Conf Intell Syst Mol Biol , vol.6 , pp. 165-174
    • Sjolander, K.1
  • 28
    • 0013673629 scopus 로고    scopus 로고
    • A Bayesian-information theoretic method for evolutionary inference in proteins
    • PhD dissertation, University of California, Santa Cruz
    • Sjolander K, A Bayesian-information theoretic method for evolutionary inference in proteins, PhD dissertation, University of California, Santa Cruz, 1997.
    • (1997)
    • Sjolander, K.1
  • 29
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • Hutchinson EG, Thornton JM, PROMOTIF - A program to identify and analyze structural motifs in proteins, Protein Sci 5(2):212-220, 1996.
    • (1996) Protein Sci , vol.5 , Issue.2 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 30
    • 31044441785 scopus 로고    scopus 로고
    • Stabilization of helical interactions in the heart Na+ channel carboxy terminal domain by a disease-associated mutation: Evidence from theoretical and experimental analysis
    • in preparation
    • Tateyama M et al., Stabilization of helical interactions in the heart Na+ channel carboxy terminal domain by a disease-associated mutation: Evidence from theoretical and experimental analysis, in preparation, 2003.
    • (2003)
    • Tateyama, M.1
  • 31
    • 0036952917 scopus 로고    scopus 로고
    • Local structure-based sequence profile database for local and global protein structure predictions
    • Yang AS, Wang L, Local structure-based sequence profile database for local and global protein structure predictions, Bioinformatics 18(12):1650-1657, 2002.
    • (2002) Bioinformatics , vol.18 , Issue.12 , pp. 1650-1657
    • Yang, A.S.1    Wang, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.