메뉴 건너뛰기




Volumn 6, Issue 9, 2011, Pages

Determinants, discriminants, conserved residues - a heuristic approach to detection of functional divergence in protein families

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; FALSE POSITIVE RESULT; GENETIC CONSERVATION; LIGAND BINDING; MATHEMATICAL COMPUTING; MATHEMATICAL MODEL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; RESIDUE ANALYSIS; BIOLOGICAL MODEL; METABOLISM; MOLECULAR LIBRARY; MULTIGENE FAMILY; NUCLEOTIDE SEQUENCE; RECEIVER OPERATING CHARACTERISTIC; SEQUENCE HOMOLOGY;

EID: 80052626839     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0024382     Document Type: Article
Times cited : (12)

References (59)
  • 1
    • 0036681416 scopus 로고    scopus 로고
    • Scoring residue conservation
    • Valdar W, (2002) Scoring residue conservation. PROTEINS-NEW YORK- 48: 227-241.
    • (2002) PROTEINS-NEW YORK- , vol.48 , pp. 227-241
    • Valdar, W.1
  • 2
    • 0014828908 scopus 로고
    • An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity
    • Wu T, Kabat E, (1970) An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity. The Journal of Experimental Medicine 132: 211.
    • (1970) The Journal of Experimental Medicine , vol.132 , pp. 211
    • Wu, T.1    Kabat, E.2
  • 6
    • 1242339659 scopus 로고    scopus 로고
    • A family of evolution-entropy hybrid methods for ranking protein residues by importance
    • Mihalek I, Reš I, Lichtarge O, (2004) A family of evolution-entropy hybrid methods for ranking protein residues by importance. Journal of Molecular Biology 336: 1265-1282.
    • (2004) Journal of Molecular Biology , vol.336 , pp. 1265-1282
    • Mihalek, I.1    Reš, I.2    Lichtarge, O.3
  • 7
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues
    • Pupko T, Bell R, Mayrose I, Glaser F, Ben-Tal N, (2002) Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues. Bioinformatics 18: 71-77.
    • (2002) Bioinformatics , vol.18 , pp. 71-77
    • Pupko, T.1    Bell, R.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 8
    • 8544225780 scopus 로고    scopus 로고
    • Accuracy and power of statistical methods for detecting adaptive evolution in protein coding sequences and for identifying positively selected sites
    • Wong W, Yang Z, Goldman N, Nielsen R, (2004) Accuracy and power of statistical methods for detecting adaptive evolution in protein coding sequences and for identifying positively selected sites. Genetics 168: 1041.
    • (2004) Genetics , vol.168 , pp. 1041
    • Wong, W.1    Yang, Z.2    Goldman, N.3    Nielsen, R.4
  • 9
    • 0035957514 scopus 로고    scopus 로고
    • Evolutionary conservation of the folding nucleus1
    • Mirny L, Shakhnovich E, (2001) Evolutionary conservation of the folding nucleus1. Journal of Molecular Biology 308: 123-129.
    • (2001) Journal of Molecular Biology , vol.308 , pp. 123-129
    • Mirny, L.1    Shakhnovich, E.2
  • 10
    • 0035853028 scopus 로고    scopus 로고
    • Identification of protein ologomerization states by analysis of interface conservation
    • Elcock A, McCammon J, (2201) Identification of protein ologomerization states by analysis of interface conservation. PNAS 98: 2990-2994.
    • (2201) PNAS , vol.98 , pp. 2990-2994
    • Elcock, A.1    McCammon, J.2
  • 11
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • Nooren I, Thornton JM, (2003) Structural characterisation and functional significance of transient protein-protein interactions. Journal of Molecular Biology 325: 991-1018.
    • (2003) Journal of Molecular Biology , vol.325 , pp. 991-1018
    • Nooren, I.1    Thornton, J.M.2
  • 12
    • 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: Structure, Function, and Bioinformatics 63: 87-99.
    • (2006) Proteins: Structure, Function, and Bioinformatics , vol.63 , pp. 87-99
    • Mihalek, I.1    Reš, I.2    Lichtarge, O.3
  • 13
    • 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.
    • (1993) Bioinformatics , vol.9 , pp. 745
    • Livingstone, C.1    Barton, G.2
  • 14
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge O, Bourne H, Cohen F, (1996) An evolutionary trace method defines binding surfaces common to protein families. Journal of Molecular Biology 257: 342-358.
    • (1996) Journal of Molecular Biology , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.2    Cohen, F.3
  • 15
    • 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. Molecular Biology and Evolution 16: 1664.
    • (1999) Molecular Biology and Evolution , vol.16 , pp. 1664
    • Gu, X.1
  • 16
    • 0345062357 scopus 로고    scopus 로고
    • Universally conserved residues in protein folds. Reading evolution- ary signals about protein function, stability and folding kinetics
    • Mirny L, Shakhnovich E, (1999) Universally conserved residues in protein folds. Reading evolution- ary signals about protein function, stability and folding kinetics. Journal of Molecular Biology 291: 177-196.
    • (1999) Journal of Molecular Biology , vol.291 , pp. 177-196
    • Mirny, L.1    Shakhnovich, E.2
  • 17
    • 0036352010 scopus 로고    scopus 로고
    • Using orthologous and paralogous proteins to identify specificity-determining residues in bacterial transcription factors
    • Mirny L, Gelfand M, (2002) Using orthologous and paralogous proteins to identify specificity-determining residues in bacterial transcription factors. Journal of Molecular Biology 321: 7-20.
    • (2002) Journal of Molecular Biology , vol.321 , pp. 7-20
    • Mirny, L.1    Gelfand, M.2
  • 18
    • 32144442848 scopus 로고    scopus 로고
    • Prediction of functional specificity determinants from protein sequences using log-likelihood ratios
    • Pei J, Cai W, Kinch L, Grishin N, (2006) Prediction of functional specificity determinants from protein sequences using log-likelihood ratios. Bioinformatics 22: 164.
    • (2006) Bioinformatics , vol.22 , pp. 164
    • Pei, J.1    Cai, W.2    Kinch, L.3    Grishin, N.4
  • 19
    • 0034459679 scopus 로고    scopus 로고
    • Evolutionary trace analysis of TGF-fbetag and related growth factors: implications for site-directed mutagenesis
    • Innis C, Shi J, Blundell T, (2000) Evolutionary trace analysis of TGF-fbetag and related growth factors: implications for site-directed mutagenesis. Protein Engineering Design and Selection 13: 839.
    • (2000) Protein Engineering Design and Selection , vol.13 , pp. 839
    • Innis, C.1    Shi, J.2    Blundell, T.3
  • 20
    • 59149089414 scopus 로고    scopus 로고
    • Joint evolutionary trees: a large-scale method to predict protein interfaces based on sequence sampling
    • Engelen S, Trojan L, Sacquin-Mora S, Lavery R, Carbone A, (2009) Joint evolutionary trees: a large-scale method to predict protein interfaces based on sequence sampling. PLoS Comput Biol 5: e1000267.
    • (2009) PLoS Comput Biol , vol.5
    • Engelen, S.1    Trojan, L.2    Sacquin-Mora, S.3    Lavery, R.4    Carbone, A.5
  • 21
    • 0242666374 scopus 로고    scopus 로고
    • Functional divergence prediction from evolutionary analysis: a case study of vertebrate hemoglobin
    • Gribaldo S, Casane D, Lopez P, Philippe H, (2003) Functional divergence prediction from evolutionary analysis: a case study of vertebrate hemoglobin. Molecular Biology and Evolution 20: 1754.
    • (2003) Molecular Biology and Evolution , vol.20 , pp. 1754
    • Gribaldo, S.1    Casane, D.2    Lopez, P.3    Philippe, H.4
  • 22
    • 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. Molecular Biology and Evolution 18: 453.
    • (2001) Molecular Biology and Evolution , vol.18 , pp. 453
    • Gu, X.1
  • 23
    • 36849090751 scopus 로고    scopus 로고
    • Identification of functional paralog shift mutations: Conversion of Escherichia coli malate dehydrogenase to a lactate dehydrogenase
    • Yin Y, Kirsch J, (2007) Identification of functional paralog shift mutations: Conversion of Escherichia coli malate dehydrogenase to a lactate dehydrogenase. Proceedings of the National Academy of Sciences 104: 17353.
    • (2007) Proceedings of the National Academy of Sciences , vol.104 , pp. 17353
    • Yin, Y.1    Kirsch, J.2
  • 24
    • 1642452921 scopus 로고    scopus 로고
    • Automated selection of positions determining functional specificity of proteins by comparative analysis of orthologous groups in protein families
    • 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 Science: A Publication of the Protein Society 13: 443.
    • (2004) Protein Science: A Publication of the Protein Society , vol.13 , pp. 443
    • Kalinina, O.1    Mironov, A.2    Gelfand, M.3    Rakhmaninova, A.4
  • 26
    • 0036205440 scopus 로고    scopus 로고
    • DIVERGE: phylogeny-based analysis for functional-structural divergence of a protein family
    • Gu X, Vander Velden K, (2002) DIVERGE: phylogeny-based analysis for functional-structural divergence of a protein family. Bioinformatics 18: 500.
    • (2002) Bioinformatics , vol.18 , pp. 500
    • Gu, X.1    vander Velden, K.2
  • 27
    • 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.
    • (2008) Bioinformatics , vol.24 , pp. 2445
    • Sankararaman, S.1    Sjolander, K.2
  • 28
    • 77952356281 scopus 로고    scopus 로고
    • Evolution-guided discovery and recoding of allosteric pathway specificity determinants in psychoactive bioamine receptors
    • Rodriguez G, Yao R, Lichtarge O, Wensel T, (2010) Evolution-guided discovery and recoding of allosteric pathway specificity determinants in psychoactive bioamine receptors. Proceedings of the National Academy of Sciences 107: 7787.
    • (2010) Proceedings of the National Academy of Sciences , vol.107 , pp. 7787
    • Rodriguez, G.1    Yao, R.2    Lichtarge, O.3    Wensel, T.4
  • 29
    • 73849085331 scopus 로고    scopus 로고
    • Comparing the Functional Roles of Nonconserved Sequence Positions in Homologous Transcription Repressors: Implications for Sequence/Function Analyses
    • Tungtur S, Meinhardt S, Swint-Kruse L, (2010) Comparing the Functional Roles of Nonconserved Sequence Positions in Homologous Transcription Repressors: Implications for Sequence/Function Analyses. Journal of Molecular Biology 5: 785.
    • (2010) Journal of Molecular Biology , vol.5 , pp. 785
    • Tungtur, S.1    Meinhardt, S.2    Swint-Kruse, L.3
  • 30
    • 46249099576 scopus 로고    scopus 로고
    • Characterization and prediction of residues determining protein functional specificity
    • Capra J, Singh M, (2008) Characterization and prediction of residues determining protein functional specificity. Bioinformatics 24: 1473.
    • (2008) Bioinformatics , vol.24 , pp. 1473
    • Capra, J.1    Singh, M.2
  • 31
    • 0034644783 scopus 로고    scopus 로고
    • Analysis and prediction of functional sub-types from protein sequence alignments
    • Hannenhalli S, Russell R, (2000) Analysis and prediction of functional sub-types from protein sequence alignments. Journal of Molecular Biology 303: 61-76.
    • (2000) Journal of Molecular Biology , vol.303 , pp. 61-76
    • Hannenhalli, S.1    Russell, R.2
  • 32
    • 33749819303 scopus 로고    scopus 로고
    • Bayesian search of functionally divergent protein subgroups and their function specific residues
    • Marttinen P, Corander J, Toronen P, Holm L, (2006) Bayesian search of functionally divergent protein subgroups and their function specific residues. Bioinformatics 22: 2466.
    • (2006) Bioinformatics , vol.22 , pp. 2466
    • Marttinen, P.1    Corander, J.2    Toronen, P.3    Holm, L.4
  • 33
    • 44949137643 scopus 로고    scopus 로고
    • Determinants of protein function revealed by combinatorial entropy optimization
    • Reva B, Antipin Y, Sander C, (2007) Determinants of protein function revealed by combinatorial entropy optimization. Genome Biology 8: R232.
    • (2007) Genome Biology , vol.8
    • Reva, B.1    Antipin, Y.2    Sander, C.3
  • 34
    • 34249794262 scopus 로고    scopus 로고
    • Supervised multivariate analysis of sequence groups to identify specificity determining residues
    • Wallace I, Higgins D, (2007) Supervised multivariate analysis of sequence groups to identify specificity determining residues. BMC Bioinformatics 8: 135.
    • (2007) BMC Bioinformatics , vol.8 , pp. 135
    • Wallace, I.1    Higgins, D.2
  • 35
    • 0036300444 scopus 로고    scopus 로고
    • Structural clusters of evolutionary trace residues are statistically significant and common in proteins
    • Madabushi S, Yao H, Marsh M, Kristensen D, Philippi A, et al. (2002) Structural clusters of evolutionary trace residues are statistically significant and common in proteins. Journal of Molecular Biology 316: 139-154.
    • (2002) Journal of Molecular Biology , vol.316 , pp. 139-154
    • Madabushi, S.1    Yao, H.2    Marsh, M.3    Kristensen, D.4    Philippi, A.5
  • 36
    • 0037485769 scopus 로고    scopus 로고
    • Combining inference from evolution and geometric probability in protein structure evaluation
    • Mihalek I, Res I, Yao H, Lichtarge O, (2003) Combining inference from evolution and geometric probability in protein structure evaluation. Journal of Molecular Biology 331: 263-279.
    • (2003) Journal of Molecular Biology , vol.331 , pp. 263-279
    • Mihalek, I.1    Res, I.2    Yao, H.3    Lichtarge, O.4
  • 37
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures
    • 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 Research 33: W299.
    • (2005) Nucleic Acids Research , vol.33
    • Landau, M.1    Mayrose, I.2    Rosenberg, Y.3    Glaser, F.4    Martz, E.5
  • 38
    • 68049104351 scopus 로고    scopus 로고
    • Ensemble approach to predict specificity determinants: bench-marking and validation
    • Chakrabarty S, Panchenko A, (2010) Ensemble approach to predict specificity determinants: bench-marking and validation. BMC Bioinformatics 10: 207.
    • (2010) BMC Bioinformatics , vol.10 , pp. 207
    • Chakrabarty, S.1    Panchenko, A.2
  • 39
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless S, Ranganathan R, (1999) Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286: 295.
    • (1999) Science , vol.286 , pp. 295
    • Lockless, S.1    Ranganathan, R.2
  • 41
    • 0003991673 scopus 로고    scopus 로고
    • Sunderland, MA, Sinauer Associates
    • Felsenstein J, (2004) Inferring Phylogenies. Sunderland, MA Sinauer Associates.p. pp 205.
    • (2004) Inferring Phylogenies , pp. 205
    • Felsenstein, J.1
  • 42
    • 0742286995 scopus 로고    scopus 로고
    • A transition probability model for amino acid substitutions from blocks
    • Veerassamy S, Smith A, Tillier E, (2003) A transition probability model for amino acid substitutions from blocks. Journal of Computational Biology 10: 997-1010.
    • (2003) Journal of Computational Biology , vol.10 , pp. 997-1010
    • Veerassamy, S.1    Smith, A.2    Tillier, E.3
  • 44
    • 45849154166 scopus 로고    scopus 로고
    • An improved general amino acid replacement matrix
    • Le S, Gascuel O, (2008) An improved general amino acid replacement matrix. Molecular Biology and Evolution 25: 1307.
    • (2008) Molecular Biology and Evolution , vol.25 , pp. 1307
    • Le, S.1    Gascuel, O.2
  • 45
    • 34548133728 scopus 로고    scopus 로고
    • Predicting functionally important residues from sequence conservation
    • Capra J, Singh M, (2007) Predicting functionally important residues from sequence conservation. Bioinformatics 23: 1875.
    • (2007) Bioinformatics , vol.23 , pp. 1875
    • Capra, J.1    Singh, M.2
  • 46
    • 33646044395 scopus 로고    scopus 로고
    • WHISCY: What information does surface conservation yield? Application to data-driven docking
    • de Vries S, van Dijk A, Bonvin A, (2006) WHISCY: What information does surface conservation yield? Application to data-driven docking. Proteins: Structure, Function, and Bioinformatics 63: 479-489.
    • (2006) Proteins: Structure, Function, and Bioinformatics , vol.63 , pp. 479-489
    • de Vries, S.1    van Dijk, A.2    Bonvin, A.3
  • 47
    • 41049089044 scopus 로고    scopus 로고
    • Background frequencies for residue variability estimates: BLOSUM revisited
    • Mihalek I, Reš I, Lichtarge O, (2007) Background frequencies for residue variability estimates: BLOSUM revisited. BMC Bioinformatics 8: 488.
    • (2007) BMC Bioinformatics , vol.8 , pp. 488
    • Mihalek, I.1    Reš, I.2    Lichtarge, O.3
  • 48
    • 33845882991 scopus 로고    scopus 로고
    • Sequence comparison by sequence harmony identifies subtype-specific functional sites
    • Pirovano W, Feenstra K, Heringa J, (2006) Sequence comparison by sequence harmony identifies subtype-specific functional sites. Nucleic Acids Research pp. 6540-8.
    • (2006) Nucleic Acids Research , pp. 6540-6548
    • Pirovano, W.1    Feenstra, K.2    Heringa, J.3
  • 49
    • 33646813254 scopus 로고    scopus 로고
    • A two-entropies analysis to identify functional positions in the transmembrane region of class AG protein-coupled receptors
    • Ye K, Lameijer E, Beukers M, Ijzerman A, (2006) A two-entropies analysis to identify functional positions in the transmembrane region of class AG protein-coupled receptors. Proteins: Structure, Function and Bioinformatics 63: 1018-1030.
    • (2006) Proteins: Structure, Function and Bioinformatics , vol.63 , pp. 1018-1030
    • Ye, K.1    Lameijer, E.2    Beukers, M.3    Ijzerman, A.4
  • 50
    • 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
    • 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. Journal of Molecular Biology 261: 509-523.
    • (1996) Journal of Molecular Biology , vol.261 , pp. 509-523
    • Suckow, J.1    Markiewicz, P.2    Kleina, L.3    Miller, J.4    Kisters-Woike, B.5
  • 51
    • 0028076771 scopus 로고
    • Genetic studies of the lac repressor. XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues, as well as" spacers" which do not require a specific sequence
    • Markiewicz P, Kleina L, Cruz C, Ehret S, Miller J, (1994) Genetic studies of the lac repressor. XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues, as well as" spacers" which do not require a specific sequence. Journal of Molecular Biology 240: 421.
    • (1994) Journal of Molecular Biology , vol.240 , pp. 421
    • Markiewicz, P.1    Kleina, L.2    Cruz, C.3    Ehret, S.4    Miller, J.5
  • 52
    • 0029879199 scopus 로고    scopus 로고
    • Mutagenesis of transmembrane domain 11 of p-glycoprotein by alanine scanning
    • Hanna M, Brault M, Kwan T, Kast C, Gros P, (1996) Mutagenesis of transmembrane domain 11 of p-glycoprotein by alanine scanning. Biochemistry 35: 3625-3635.
    • (1996) Biochemistry , vol.35 , pp. 3625-3635
    • Hanna, M.1    Brault, M.2    Kwan, T.3    Kast, C.4    Gros, P.5
  • 53
    • 34547829268 scopus 로고    scopus 로고
    • Functional specialization of domains tandemly duplicated within 16s rrna methyltransferase rsmc
    • Sunita S, Purta E, Durawa M, Tkaczuk K, Swaathi J, et al. (2007) Functional specialization of domains tandemly duplicated within 16s rrna methyltransferase rsmc. Nucleic Acids Research 35: 4264.
    • (2007) Nucleic Acids Research , vol.35 , pp. 4264
    • Sunita, S.1    Purta, E.2    Durawa, M.3    Tkaczuk, K.4    Swaathi, J.5
  • 54
    • 68049104351 scopus 로고    scopus 로고
    • Ensemble approach to predict specificity determinants: bench- marking and validation
    • Chakrabarti S, Panchenko A, (2009) Ensemble approach to predict specificity determinants: bench- marking and validation. BMC Bioinformatics 10: 207.
    • (2009) BMC Bioinformatics , vol.10 , pp. 207
    • Chakrabarti, S.1    Panchenko, A.2
  • 55
    • 3242891674 scopus 로고    scopus 로고
    • SDPpred: a tool for prediction of amino acid residues that determine differences in functional specificity of homologous proteins
    • Kalinina O, Novichkov P, Mironov A, Gelfand M, Rakhmaninova A, (2004) SDPpred: a tool for prediction of amino acid residues that determine differences in functional specificity of homologous proteins. Nucleic Acids Research 32: W424.
    • (2004) Nucleic Acids Research , vol.32
    • Kalinina, O.1    Novichkov, P.2    Mironov, A.3    Gelfand, M.4    Rakhmaninova, A.5
  • 56
    • 33645063702 scopus 로고    scopus 로고
    • Structural Snapshots of [beta]-1, 4-Galactosyltransferase-I Along the Kinetic Pathway
    • Ramakrishnan B, Ramasamy V, Qasba P, (2006) Structural Snapshots of [beta]-1, 4-Galactosyltransferase-I Along the Kinetic Pathway. Journal of Molecular Biology 357: 1619-1633.
    • (2006) Journal of Molecular Biology , vol.357 , pp. 1619-1633
    • Ramakrishnan, B.1    Ramasamy, V.2    Qasba, P.3
  • 57
    • 0035719951 scopus 로고    scopus 로고
    • Use of mutagenesis to probe igf-binding protein structure/function relation- ships
    • Clemmons D, (2001) Use of mutagenesis to probe igf-binding protein structure/function relation- ships. Endocrine Reviews 22: 800.
    • (2001) Endocrine Reviews , vol.22 , pp. 800
    • Clemmons, D.1
  • 58
    • 14844331743 scopus 로고    scopus 로고
    • Thrombomodulin changes the molecular surface of interaction and the rate of complex formation between thrombin and protein c
    • Xu H, Bush L, Pineda A, Caccia S, Di Cera E, (2005) Thrombomodulin changes the molecular surface of interaction and the rate of complex formation between thrombin and protein c. Journal of Biological Chemistry 280: 7956.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 7956
    • Xu, H.1    Bush, L.2    Pineda, A.3    Caccia, S.4    Di Cera, E.5
  • 59
    • 33747606306 scopus 로고    scopus 로고
    • Structure of the keap1: Nrf2 interface provides mechanistic insight into nrf2 signaling
    • Lo S, Li X, Henzl M, Beamer L, Hannink M, (2006) Structure of the keap1: Nrf2 interface provides mechanistic insight into nrf2 signaling. The EMBO Journal 25: 3605-3617.
    • (2006) The EMBO Journal , vol.25 , pp. 3605-3617
    • Lo, S.1    Li, X.2    Henzl, M.3    Beamer, L.4    Hannink, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.