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Volumn 8, Issue 11, 2013, Pages

Cube - An online tool for comparison and contrasting of protein sequences

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; COMPUTATIONAL BIOLOGY; INTERNET; PROTEINS; SEQUENCE ALIGNMENT; SOFTWARE;

EID: 84894266025     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0079480     Document Type: Article
Times cited : (1)

References (46)
  • 1
    • 0017579545 scopus 로고
    • Genetic studies of the lac repressor: I. Correlation of mutational sites with specific amino acid residues: Construction of a colinear gene-protein map
    • Miller JH, Ganem D, Lu P, Schmitz A (1977) Genetic studies of the lac repressor: I. correlation of mutational sites with specific amino acid residues: Construction of a colinear gene-protein map. J Mol Biol 109: 275-298.
    • (1977) J Mol Biol , vol.109 , pp. 275-298
    • Miller, J.H.1    Ganem, D.2    Lu, P.3    Schmitz, A.4
  • 2
    • 2342519701 scopus 로고    scopus 로고
    • Genetic studies of the Lac repressor XV: 4000 single amino acid substitutions and analysis of the resulting phenotypes on the basis of the protein structure
    • DOI 10.1006/jmbi.1996.0479
    • Suckow J, Markiewicz P, Kleina L, Miller J, Kisters-Woike B, et al. (1996) Genetic studies of the lac repressor XV: 4000 single amino acid substitutions and analysis of the resulting phenotypes on the basis of the protein structure. J Mol Biol 261: 509-523. (Pubitemid 26335943)
    • (1996) Journal of Molecular Biology , vol.261 , Issue.4 , pp. 509-523
    • Suckow, J.1    Markiewicz, P.2    Kleina, L.G.3    Miller, J.4    Kisters-Woike, B.5    Muller-Hill, B.6
  • 3
    • 84874482336 scopus 로고    scopus 로고
    • Coupling mutagenesis and parallel deep sequencing to probe essential residues in a genome or gene
    • Robins WP, Faruque SM, Mekalanos JJ (2013) Coupling mutagenesis and parallel deep sequencing to probe essential residues in a genome or gene. Proc Natl Acad Sci USA 110: E848-E857.
    • (2013) Proc Natl Acad Sci USA , vol.110
    • Robins, W.P.1    Faruque, S.M.2    Mekalanos, J.J.3
  • 4
    • 80053453491 scopus 로고    scopus 로고
    • Separation of recombination and sos response in escherichia coli reca suggests lexa interaction sites
    • Adikesavan AK, Katsonis P, Marciano DC, Lua R, Herman C, et al. (2011) Separation of recombination and sos response in escherichia coli reca suggests lexa interaction sites. PLoS genetics 7: e1002244.
    • (2011) PLoS Genetics , vol.7
    • Adikesavan, A.K.1    Katsonis, P.2    Marciano, D.C.3    Lua, R.4    Herman, C.5
  • 5
    • 10944230777 scopus 로고    scopus 로고
    • Duplication and divergence: The evolution of new genes and old ideas
    • DOI 10.1146/annurev.genet.38.072902.092831
    • Taylor JS, Raes J (2004) Duplication and divergence: the evolution of new genes and old ideas. Annu Rev Genet 38: 615-643. (Pubitemid 40017189)
    • (2004) Annual Review of Genetics , vol.38 , pp. 615-643
    • Taylor, J.S.1    Raes, J.2
  • 6
    • 0032728408 scopus 로고    scopus 로고
    • Statistical methods for testing functional divergence after gene duplication
    • Gu X (1999) Statistical methods for testing functional divergence after gene duplication. Mol Biol Evol 16: 1664-1674.
    • (1999) Mol Biol Evol , vol.16 , pp. 1664-1674
    • Gu, X.1
  • 8
    • 0242666374 scopus 로고    scopus 로고
    • Functional Divergence Prediction from Evolutionary Analysis: A Case Study of Vertebrate Hemoglobin
    • DOI 10.1093/molbev/msg171
    • Gribaldo S, Casane D, Lopez P, Philippe H (2003) Functional divergence prediction from evolutionary analysis: a case study of vertebrate hemoglobin. Mol Biol Evol 20: 1754-1759. (Pubitemid 37420928)
    • (2003) Molecular Biology and Evolution , vol.20 , Issue.11 , pp. 1754-1759
    • Gribaldo, S.1    Casane, D.2    Lopez, P.3    Philippe, H.4
  • 9
    • 80052626839 scopus 로고    scopus 로고
    • Determinants, discriminants, conserved residues - A heuristic approach to detection of functional divergence in protein families
    • Bharatham K, Zhang ZH, Mihalek I (2011) Determinants, discriminants, conserved residues - a heuristic approach to detection of functional divergence in protein families. PLoS ONE 6: e24382.
    • (2011) PLoS ONE , vol.6
    • Bharatham, K.1    Zhang, Z.H.2    Mihalek, I.3
  • 10
    • 70349463121 scopus 로고    scopus 로고
    • Computational design of candida boidinii xylose reductase for altered cofactor specificity
    • Khoury GA, Fazelinia H, Chin JW, Pantazes RJ, Cirino PC, et al. (2009) Computational design of candida boidinii xylose reductase for altered cofactor specificity. Protein Science 18: 2125-2138.
    • (2009) Protein Science , vol.18 , pp. 2125-2138
    • Khoury, G.A.1    Fazelinia, H.2    Chin, J.W.3    Pantazes, R.J.4    Cirino, P.C.5
  • 11
    • 0035914476 scopus 로고    scopus 로고
    • Conservation Helps to Identify Biologically Relevant Crystal Contacts
    • DOI 10.1006/jmbi.2001.5034, PII S002228360195034X
    • Valdar WS, Thornton JM (2001) Conservation helps to identify biologically relevant crystal contacts. J Mol Biol 313: 399-416. (Pubitemid 33587196)
    • (2001) Journal of Molecular Biology , vol.313 , Issue.2 , pp. 399-416
    • Valdar, W.S.J.1    Thornton, J.M.2
  • 12
    • 0036681416 scopus 로고    scopus 로고
    • Scoring residue conservation
    • Valdar W (2002) Scoring residue conservation. Proteins 48: 227-241.
    • (2002) Proteins , vol.48 , pp. 227-241
    • Valdar, W.1
  • 13
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: An algorithmic tool for the identification of functional regions in proteins
    • Pupko T, Bell R, Mayrose I, Glaser F, Ben-Tal N (2002) Rate4Site: an algorithmic tool for the identification of functional regions in proteins. Bioinformatics 18: S71-77.
    • (2002) Bioinformatics , vol.18
    • Pupko, T.1    Bell, R.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 14
    • 57049150788 scopus 로고    scopus 로고
    • The consurf-db: Pre-calculated evolutionary conservation profiles of protein structures
    • Goldenberg O, Erez E, Nimrod G, Ben-Tal N (2009) The consurf-db: pre-calculated evolutionary conservation profiles of protein structures. Nucleic Acids Res 37: D323-D327.
    • (2009) Nucleic Acids Res , vol.37
    • Goldenberg, O.1    Erez, E.2    Nimrod, G.3    Ben-Tal, N.4
  • 15
    • 0035896024 scopus 로고    scopus 로고
    • ConSurf: An algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information
    • DOI 10.1006/jmbi.2000.4474
    • Armon A, Graur D, Ben-Tal N (2001) Consurf: an algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information. J Mol Biol 307: 447-463. (Pubitemid 33029992)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.1 , pp. 447-463
    • Armon, A.1    Graur, D.2    Ben-Tal, N.3
  • 16
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: The projection of evolutionary conservation scores of residues on protein structures
    • DOI 10.1093/nar/gki370
    • Landau M, Mayrose I, Rosenberg Y, Glaser F, Martz E, et al. (2005) ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res 33: W299-302. (Pubitemid 44529930)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS.
    • Landau, M.1    Mayrose, I.2    Rosenberg, Y.3    Glaser, F.4    Martz, E.5    Pupko, T.6    Ben-Tal, N.7
  • 17
    • 0027764344 scopus 로고
    • Protein sequence alignments: A strategy for the hierarchical analysis of residue conservation
    • Livingstone C, Barton G (1993) Protein sequence alignments: a strategy for the hierarchical analysis of residue conservation. Bioinformatics 9: 745-756. (Pubitemid 24016574)
    • (1993) Computer Applications in the Biosciences , vol.9 , Issue.6 , pp. 745-756
    • Livingstone, C.D.1    Barton, G.J.2
  • 18
    • 0031555477 scopus 로고    scopus 로고
    • Identification of functional surfaces of the zinc binding domains of intracellular receptors
    • DOI 10.1006/jmbi.1997.1395
    • Lichtarge O, Yamamoto K, Cohen F (1997) Identification of functional surfaces of the zinc binding domains of intracellular receptors1. J Mol Biol 274: 325-337. (Pubitemid 27520622)
    • (1997) Journal of Molecular Biology , vol.274 , Issue.3 , pp. 325-337
    • Lichtarge, O.1    Yamamoto, K.R.2    Cohen, F.E.3
  • 19
    • 1242339659 scopus 로고    scopus 로고
    • A Family of Evolution-Entropy Hybrid Methods for Ranking Protein Residues by Importance
    • DOI 10.1016/j.jmb.2003.12.078
    • Mihalek I, Reš I, Lichtarge O (2004) A family of evolution-entropy hybrid methods for ranking protein residues by importance. J Mol Biol 336: 1265-1282. (Pubitemid 38229712)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.5 , pp. 1265-1282
    • Mihalek, I.1    Res, I.2    Lichtarge, O.3
  • 20
    • 33645024859 scopus 로고    scopus 로고
    • Evolutionary and structural feedback on selection of sequences for comparative analysis of proteins
    • Mihalek I, Reš I, Lichtarge O (2006) Evolutionary and structural feedback on selection of sequences for comparative analysis of proteins. Proteins 63: 87-99.
    • (2006) Proteins , vol.63 , pp. 87-99
    • Mihalek, I.1    Reš, I.2    Lichtarge, O.3
  • 21
    • 0034459679 scopus 로고    scopus 로고
    • Evolutionary trace analysis of TGF-{beta} and related growth factors: Implications for site-directed mutagenesis
    • Innis C, Shi J, Blundell T (2000) Evolutionary trace analysis of TGF-{beta} and related growth factors: implications for site-directed mutagenesis. Protein Eng 13: 839847.
    • (2000) Protein Eng , vol.13 , pp. 839847
    • Innis, C.1    Shi, J.2    Blundell, T.3
  • 22
    • 33747840720 scopus 로고    scopus 로고
    • ET viewer: An application for predicting and visualizing functional sites in protein structures
    • DOI 10.1093/bioinformatics/btl285
    • Morgan DH, Kristensen DM, Mittelman D, Lichtarge O (2006) Et viewer: an application for predicting and visualizing functional sites in protein structures. Bioinformatics 22: 2049-2050. (Pubitemid 44283020)
    • (2006) Bioinformatics , vol.22 , Issue.16 , pp. 2049-2050
    • Morgan, D.H.1    Kristensen, D.M.2    Mittelman, D.3    Lichtarge, O.4
  • 23
    • 54949145058 scopus 로고    scopus 로고
    • INTREPID-INformation-theoretic TREe traversal for Protein functional site IDentification
    • Sankararaman S, Sjolander K (2008) INTREPID-INformation-theoretic TREe traversal for Protein functional site IDentification. Bioinformatics 24: 2445-2452.
    • (2008) Bioinformatics , vol.24 , pp. 2445-2452
    • Sankararaman, S.1    Sjolander, K.2
  • 24
    • 67849101184 scopus 로고    scopus 로고
    • Intrepid: A web server for prediction of functionally important residues by evolutionary analysis
    • Sankararaman S, Kolaczkowski B, Sjölander K (2009) Intrepid: a web server for prediction of functionally important residues by evolutionary analysis. Nucleic Acids Res 37: W390-W395.
    • (2009) Nucleic Acids Res , vol.37
    • Sankararaman, S.1    Kolaczkowski, B.2    Sjölander, K.3
  • 26
    • 13444302764 scopus 로고    scopus 로고
    • FunShift: A database of function shift analysis on protein subfamilies
    • DOI 10.1093/nar/gki067
    • Abhiman S, Sonnhammer E (2005) Funshift: a database of function shift analysis on protein subfamilies. Nucleic Acids Res 33: D197-200. (Pubitemid 40207859)
    • (2005) Nucleic Acids Research , vol.33 , Issue.DATABASE ISS.
    • Abhiman, S.1    Sonnhammer, E.L.L.2
  • 27
    • 0035061686 scopus 로고    scopus 로고
    • Maximum-likelihood approach for gene family evolution under functional divergence
    • Gu X (2001) Maximum-likelihood approach for gene family evolution under functional divergence. Mol Biol Evol 18: 453-464.
    • (2001) Mol Biol Evol , vol.18 , pp. 453-464
    • Gu, X.1
  • 28
    • 84878925597 scopus 로고    scopus 로고
    • An update of diverge software for functional divergence analysis of protein family
    • Gu X, Zou Y, Su Z, Huang W, Zhou Z, et al. (2013) An update of diverge software for functional divergence analysis of protein family. Mol Biol Evol 30: 1713-1719.
    • (2013) Mol Biol Evol , vol.30 , pp. 1713-1719
    • Gu, X.1    Zou, Y.2    Su, Z.3    Huang, W.4    Zhou, Z.5
  • 29
    • 1642452921 scopus 로고    scopus 로고
    • Automated selection of positions determining functional specificity of proteins by comparative analysis of orthologous groups in protein families
    • DOI 10.1110/ps.03191704
    • Kalinina O, Mironov A, Gelfand M, Rakhmaninova A (2004) Automated selection of positions determining functional specificity of proteins by comparative analysis of orthologous groups in protein families. Protein Sci 13: 443-456. (Pubitemid 38124965)
    • (2004) Protein Science , vol.13 , Issue.2 , pp. 443-456
    • Kalinina, O.V.1    Mironov, A.A.2    Gelfand, M.S.3    Rakhmaninova, A.B.4
  • 30
    • 3242891674 scopus 로고    scopus 로고
    • SDPpred: A tool for prediction of amino acid residues that determine differences in functional specificity of homologous proteins
    • DOI 10.1093/nar/gkh391
    • Kalinina OV, Novichkov PS, Mironov AA, Gelfand MS, Rakhmaninova AB (2004) Sdppred: a tool for prediction of amino acid residues that determine differences in functional specificity of homologous proteins. Nucleic Acids Res 32: W424-W428. (Pubitemid 38997370)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Kalinina, O.V.1    Novichkov, P.S.2    Mironov, A.A.3    Gelfand, M.S.4    Rakhmaninova, A.B.5
  • 31
    • 0037470597 scopus 로고    scopus 로고
    • Automatic methods for predicting functionally important residues
    • del Sol Mesa A, Pazos F, Valencia A (2003) Automatic methods for predicting functionally important residues. J Mol Biol 326: 1289-1302.
    • (2003) J Mol Biol , vol.326 , pp. 1289-1302
    • Del Sol Mesa, A.1    Pazos, F.2    Valencia, A.3
  • 33
    • 34748840163 scopus 로고    scopus 로고
    • Functional Specificity Lies within the Properties and Evolutionary Changes of Amino Acids
    • DOI 10.1016/j.jmb.2007.08.036, PII S0022283607011084
    • Chakrabarti S, Bryant S, Panchenko A (2007) Functional specificity lies within the properties and evolutionary changes of amino acids. J Mol Biol 373: 801-810. (Pubitemid 47488404)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.3 , pp. 801-810
    • Chakrabarti, S.1    Bryant, S.H.2    Panchenko, A.R.3
  • 35
    • 37549049756 scopus 로고    scopus 로고
    • Multi-RELIEF: A method to recognize specificity determining residues from multiple sequence alignments using a Machine-Learning approach for feature weighting
    • Ye K, Anton Feenstra K, Heringa J, Ijzerman A, Marchiori E (2008) Multi-RELIEF: a method to recognize specificity determining residues from multiple sequence alignments using a Machine-Learning approach for feature weighting. Bioinformatics 24: 18-25.
    • (2008) Bioinformatics , vol.24 , pp. 18-25
    • Ye, K.1    Anton Feenstra, K.2    Heringa, J.3    Ijzerman, A.4    Marchiori, E.5
  • 36
    • 46249099576 scopus 로고    scopus 로고
    • Characterization and prediction of residues determining protein functional specificity
    • DOI 10.1093/bioinformatics/btn214
    • Capra J, Singh M (2008) Characterization and prediction of residues determining protein functional specificity. Bioinformatics 24: 1473-1480. (Pubitemid 351911698)
    • (2008) Bioinformatics , vol.24 , Issue.13 , pp. 1473-1480
    • Capra, J.A.1    Singh, M.2
  • 37
    • 84862209014 scopus 로고    scopus 로고
    • Cube-db: Detection of functional divergence in human protein families
    • Zhang ZH, Bharatham K, Chee SM, Mihalek I (2012) Cube-db: detection of functional divergence in human protein families. Nucleic Acids Res 40: D490-D494.
    • (2012) Nucleic Acids Res , vol.40
    • Zhang, Z.H.1    Bharatham, K.2    Chee, S.M.3    Mihalek, I.4
  • 39
    • 0031555477 scopus 로고    scopus 로고
    • Identification of functional surfaces of the zinc binding domains of intracellular receptors
    • DOI 10.1006/jmbi.1997.1395
    • Lichtarge O, Yamamoto K, Cohen F (1997) Identification of functional surfaces of the zinc binding domains of intracellular receptors1. J Mol Biol 274: 325-337. (Pubitemid 27520622)
    • (1997) Journal of Molecular Biology , vol.274 , Issue.3 , pp. 325-337
    • Lichtarge, O.1    Yamamoto, K.R.2    Cohen, F.E.3
  • 40
    • 0014828908 scopus 로고
    • An analysis of the sequences of the variable regions of Bence Jones proteins
    • Te Wu T, Kabat EA (1970) An analysis of the sequences of the variable regions of Bence Jones proteins. J Exp Med 132: 211-250.
    • (1970) J Exp Med , vol.132 , pp. 211-250
    • Te Wu, T.1    Kabat, E.A.2
  • 41
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff S, Henikoff J (1992) Amino acid substitution matrices from protein blocks. Proc Natl Acad Sci USA 89: 10915-10919.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.2
  • 42
    • 0742286995 scopus 로고    scopus 로고
    • A Transition Probability Model for Amino Acid Substitutions from Blocks
    • DOI 10.1089/106652703322756195
    • Veerassamy S, Smith A, Tillier E (2003) A transition probability model for amino acid substitutions from blocks. J Comput Biol 10: 997-1010. (Pubitemid 38156410)
    • (2003) Journal of Computational Biology , vol.10 , Issue.6 , pp. 997-1010
    • Veerassamy, S.1    Smith, A.2    Tillier, E.R.M.3
  • 43
    • 3042666256 scopus 로고    scopus 로고
    • Muscle: Multiple sequence alignment with high accuracy and high throughput
    • Edgar R (2004) Muscle: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32: 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.1
  • 44
    • 84875619226 scopus 로고    scopus 로고
    • Mafft multiple sequence alignment software version 7: Improvements in performance and usability
    • Katoh K, Standley DM (2013) Mafft multiple sequence alignment software version 7: improvements in performance and usability. Mol Biol Evol 30: 772-780.
    • (2013) Mol Biol Evol , vol.30 , pp. 772-780
    • Katoh, K.1    Standley, D.M.2
  • 45
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


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