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Volumn 6, Issue 3, 2011, Pages

Identification of local conformational similarity in structurally variable regions of homologous proteins using protein blocks

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; COMPUTER ANALYSIS; CONTROLLED STUDY; HOMOLOGOUS PROTEIN STRUCTURE; PROTEIN BLOCKS ANALYSIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; STRUCTURAL DISTANCE MATRIX; STRUCTURALLY CONSERVED REGION; STRUCTURALLY VARIABLE REGION; STRUCTURE ANALYSIS; CHEMICAL STRUCTURE; CHEMISTRY;

EID: 79952784062     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0017826     Document Type: Article
Times cited : (6)

References (82)
  • 1
    • 0033597176 scopus 로고    scopus 로고
    • The relationship between protein structure and function: a comprehensive survey with application to the yeast genome
    • Hegyi H, Gerstein M, (1999) The relationship between protein structure and function: a comprehensive survey with application to the yeast genome. J Mol Biol 288: 147-164.
    • (1999) J Mol Biol , vol.288 , pp. 147-164
    • Hegyi, H.1    Gerstein, M.2
  • 2
    • 0036600834 scopus 로고    scopus 로고
    • Evolution of protein structures and functions
    • Kinch LN, Grishin NV, (2002) Evolution of protein structures and functions. Curr Opin Struct Biol 12: 400-408.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 400-408
    • Kinch, L.N.1    Grishin, N.V.2
  • 3
    • 0035782687 scopus 로고    scopus 로고
    • Review: what can structural classifications reveal about protein evolution?
    • Orengo CA, Sillitoe I, Reeves G, Pearl FM, (2001) Review: what can structural classifications reveal about protein evolution? J Struct Biol 134: 145-165.
    • (2001) J Struct Biol , vol.134 , pp. 145-165
    • Orengo, C.A.1    Sillitoe, I.2    Reeves, G.3    Pearl, F.M.4
  • 4
    • 22244450719 scopus 로고    scopus 로고
    • Protein families and their evolution-a structural perspective
    • Orengo CA, Thornton JM, (2005) Protein families and their evolution-a structural perspective. Annu Rev Biochem 74: 867-900.
    • (2005) Annu Rev Biochem , vol.74 , pp. 867-900
    • Orengo, C.A.1    Thornton, J.M.2
  • 6
    • 0019332167 scopus 로고
    • How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins
    • Lesk AM, Chothia C, (1980) How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins. J Mol Biol 136: 225-270.
    • (1980) J Mol Biol , vol.136 , pp. 225-270
    • Lesk, A.M.1    Chothia, C.2
  • 7
    • 0031020765 scopus 로고    scopus 로고
    • Protein evolution. How far can sequences diverge?
    • Chothia C, Gerstein M, (1997) Protein evolution. How far can sequences diverge? Nature 385: 579, 581.
    • (1997) Nature , vol.385
    • Chothia, C.1    Gerstein, M.2
  • 8
    • 0031666414 scopus 로고    scopus 로고
    • Analogous enzymes: independent inventions in enzyme evolution
    • Galperin MY, Walker DR, Koonin EV, (1998) Analogous enzymes: independent inventions in enzyme evolution. Genome Res 8: 779-790.
    • (1998) Genome Res , vol.8 , pp. 779-790
    • Galperin, M.Y.1    Walker, D.R.2    Koonin, E.V.3
  • 9
    • 33744783371 scopus 로고    scopus 로고
    • Evolution of protein fold in the presence of functional constraints
    • Andreeva A, Murzin AG, (2006) Evolution of protein fold in the presence of functional constraints. Curr Opin Struct Biol 16: 399-408.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 399-408
    • Andreeva, A.1    Murzin, A.G.2
  • 10
    • 70349470948 scopus 로고    scopus 로고
    • Structural and functional constraints in the evolution of protein families
    • Worth CL, Gong S, Blundell TL, (2009) Structural and functional constraints in the evolution of protein families. Nat Rev Mol Cell Biol 10: 709-720.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 709-720
    • Worth, C.L.1    Gong, S.2    Blundell, T.L.3
  • 11
    • 0028961335 scopus 로고
    • SCOP: a structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C, (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247: 536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 13
    • 24344476038 scopus 로고    scopus 로고
    • YAKUSA: a fast structural database scanning method
    • Carpentier M, Brouillet S, Pothier J, (2005) YAKUSA: a fast structural database scanning method. Proteins 61: 137-151.
    • (2005) Proteins , vol.61 , pp. 137-151
    • Carpentier, M.1    Brouillet, S.2    Pothier, J.3
  • 14
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L, Park J, (2000) DaliLite workbench for protein structure comparison. Bioinformatics 16: 566-567.
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 15
    • 75149163046 scopus 로고    scopus 로고
    • A relational extension of the notion of motifs: application to the common 3D substructures searching problem
    • Pisanti N, Soldano H, Carpentier M, Pothier J, (2009) A relational extension of the notion of motifs: application to the common 3D substructures searching problem. Journal of Computational Biology 16: 1635-1660.
    • (2009) Journal of Computational Biology , vol.16 , pp. 1635-1660
    • Pisanti, N.1    Soldano, H.2    Carpentier, M.3    Pothier, J.4
  • 17
    • 33747831751 scopus 로고    scopus 로고
    • Protein Block Expert (PBE): a web-based protein structure analysis server using a structural alphabet
    • Tyagi M, Sharma P, Swamy CS, Cadet F, Srinivasan N, et al. (2006) Protein Block Expert (PBE): a web-based protein structure analysis server using a structural alphabet. Nucleic Acids Res 34: W119-123.
    • (2006) Nucleic Acids Res , vol.34
    • Tyagi, M.1    Sharma, P.2    Swamy, C.S.3    Cadet, F.4    Srinivasan, N.5
  • 18
    • 77955814959 scopus 로고    scopus 로고
    • A structural-alphabet-based strategy for finding structural motifs across protein families
    • Wu C, Chen Y, Lim C, (2010) A structural-alphabet-based strategy for finding structural motifs across protein families. Nucleic Acids Res 38: e150.
    • (2010) Nucleic Acids Res , vol.38
    • Wu, C.1    Chen, Y.2    Lim, C.3
  • 20
    • 77952938726 scopus 로고    scopus 로고
    • Global dynamics of proteins: bridging between structure and function
    • Bahar I, Lezon TR, Yang LW, Eyal E, (2010) Global dynamics of proteins: bridging between structure and function. Annu Rev Biophys 39: 23-42.
    • (2010) Annu Rev Biophys , vol.39 , pp. 23-42
    • Bahar, I.1    Lezon, T.R.2    Yang, L.W.3    Eyal, E.4
  • 21
    • 0037008011 scopus 로고    scopus 로고
    • Multiple conformational changes in enzyme catalysis
    • Hammes GG, (2002) Multiple conformational changes in enzyme catalysis. Biochemistry 41: 8221-8228.
    • (2002) Biochemistry , vol.41 , pp. 8221-8228
    • Hammes, G.G.1
  • 22
    • 0037666888 scopus 로고    scopus 로고
    • Implications of protein flexibility for drug discovery
    • Teague SJ, (2003) Implications of protein flexibility for drug discovery. Nat Rev Drug Discov 2: 527-541.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 527-541
    • Teague, S.J.1
  • 23
    • 0029982530 scopus 로고    scopus 로고
    • The structural alignment between two proteins: is there a unique answer?
    • Godzik A, (1996) The structural alignment between two proteins: is there a unique answer? Protein Sci 5: 1325-1338.
    • (1996) Protein Sci , vol.5 , pp. 1325-1338
    • Godzik, A.1
  • 24
    • 0024349252 scopus 로고
    • Protein structure alignment
    • Taylor WR, Orengo CA, (1989) Protein structure alignment. J Mol Biol 208: 1-22.
    • (1989) J Mol Biol , vol.208 , pp. 1-22
    • Taylor, W.R.1    Orengo, C.A.2
  • 25
    • 25144458667 scopus 로고    scopus 로고
    • A new progressive-iterative algorithm for multiple structure alignment
    • Lupyan D, Leo-Macias A, Ortiz AR, (2005) A new progressive-iterative algorithm for multiple structure alignment. Bioinformatics 21: 3255-3263.
    • (2005) Bioinformatics , vol.21 , pp. 3255-3263
    • Lupyan, D.1    Leo-Macias, A.2    Ortiz, A.R.3
  • 26
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov IN, Bourne PE, (1998) Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng 11: 739-747.
    • (1998) Protein Eng , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 27
    • 0025317502 scopus 로고
    • Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming
    • Sali A, Blundell TL, (1990) Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming. J Mol Biol 212: 403-428.
    • (1990) J Mol Biol , vol.212 , pp. 403-428
    • Sali, A.1    Blundell, T.L.2
  • 28
    • 3042581007 scopus 로고    scopus 로고
    • Flexible structure alignment by chaining aligned fragment pairs allowing twists
    • Ye Y, Godzik A, (2003) Flexible structure alignment by chaining aligned fragment pairs allowing twists. Bioinformatics 19 (Suppl 2): ii246-255.
    • (2003) Bioinformatics , vol.19 , Issue.SUPPL. 2
    • Ye, Y.1    Godzik, A.2
  • 29
    • 38949150854 scopus 로고    scopus 로고
    • Matt: local flexibility aids protein multiple structure alignment
    • Menke M, Berger B, Cowen L, (2008) Matt: local flexibility aids protein multiple structure alignment. PLoS Comput Biol 4: e10.
    • (2008) PLoS Comput Biol , vol.4
    • Menke, M.1    Berger, B.2    Cowen, L.3
  • 30
    • 13444279981 scopus 로고    scopus 로고
    • Comprehensive evaluation of protein structure alignment methods: scoring by geometric measures
    • Kolodny R, Koehl P, Levitt M, (2005) Comprehensive evaluation of protein structure alignment methods: scoring by geometric measures. J Mol Biol 346: 1173-1188.
    • (2005) J Mol Biol , vol.346 , pp. 1173-1188
    • Kolodny, R.1    Koehl, P.2    Levitt, M.3
  • 32
    • 0347719528 scopus 로고    scopus 로고
    • Evaluation of protein fold comparison servers
    • Novotny M, Madsen D, Kleywegt GJ, (2004) Evaluation of protein fold comparison servers. Proteins 54: 260-270.
    • (2004) Proteins , vol.54 , pp. 260-270
    • Novotny, M.1    Madsen, D.2    Kleywegt, G.J.3
  • 33
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels
    • Russell RB, Barton GJ, (1992) Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels. Proteins 14: 309-323.
    • (1992) Proteins , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2
  • 34
    • 1842450688 scopus 로고    scopus 로고
    • FlexProt: alignment of flexible protein structures without a predefinition of hinge regions
    • Shatsky M, Nussinov R, Wolfson HJ, (2004) FlexProt: alignment of flexible protein structures without a predefinition of hinge regions. J Comput Biol 11: 83-106.
    • (2004) J Comput Biol , vol.11 , pp. 83-106
    • Shatsky, M.1    Nussinov, R.2    Wolfson, H.J.3
  • 35
    • 66549119395 scopus 로고    scopus 로고
    • Advances and pitfalls of protein structural alignment
    • Hasegawa H, Holm L, (2009) Advances and pitfalls of protein structural alignment. Curr Opin Struct Biol 19: 341-348.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 341-348
    • Hasegawa, H.1    Holm, L.2
  • 36
    • 0034951219 scopus 로고    scopus 로고
    • Use of a database of structural alignments and phylogenetic trees in investigating the relationship between sequence and structural variability among homologous proteins
    • Balaji S, Srinivasan N, (2001) Use of a database of structural alignments and phylogenetic trees in investigating the relationship between sequence and structural variability among homologous proteins. Protein Eng 14: 219-226.
    • (2001) Protein Eng , vol.14 , pp. 219-226
    • Balaji, S.1    Srinivasan, N.2
  • 37
    • 0026566796 scopus 로고
    • Analysis of insertions/deletions in protein structures
    • Pascarella S, Argos P, (1992) Analysis of insertions/deletions in protein structures. J Mol Biol 224: 461-471.
    • (1992) J Mol Biol , vol.224 , pp. 461-471
    • Pascarella, S.1    Argos, P.2
  • 39
    • 65349190709 scopus 로고    scopus 로고
    • The effect of sequence evolution on protein structural divergence
    • Williams SG, Lovell SC, (2009) The effect of sequence evolution on protein structural divergence. Mol Biol Evol 26: 1055-1065.
    • (2009) Mol Biol Evol , vol.26 , pp. 1055-1065
    • Williams, S.G.1    Lovell, S.C.2
  • 40
    • 64049085201 scopus 로고    scopus 로고
    • Length variations amongst protein domain superfamilies and consequences on structure and function
    • Sandhya S, Rani SS, Pankaj B, Govind MK, Offmann B, et al. (2009) Length variations amongst protein domain superfamilies and consequences on structure and function. PLoS One 4: e4981.
    • (2009) PLoS One , vol.4
    • Sandhya, S.1    Rani, S.S.2    Pankaj, B.3    Govind, M.K.4    Offmann, B.5
  • 42
    • 23144437382 scopus 로고    scopus 로고
    • New assessment of a structural alphabet
    • de Brevern AG, (2005) New assessment of a structural alphabet. In Silico Biol 5: 283-289.
    • (2005) In Silico Biol , vol.5 , pp. 283-289
    • de Brevern, A.G.1
  • 43
    • 0034669774 scopus 로고    scopus 로고
    • Bayesian probabilistic approach for predicting backbone structures in terms of protein blocks
    • de Brevern AG, Etchebest C, Hazout S, (2000) Bayesian probabilistic approach for predicting backbone structures in terms of protein blocks. Proteins 41: 271-287.
    • (2000) Proteins , vol.41 , pp. 271-287
    • de Brevern, A.G.1    Etchebest, C.2    Hazout, S.3
  • 45
    • 33748280492 scopus 로고    scopus 로고
    • A substitution matrix for structural alphabet based on structural alignment of homologous proteins and its applications
    • Tyagi M, Gowri VS, Srinivasan N, de Brevern AG, Offmann B, (2006) A substitution matrix for structural alphabet based on structural alignment of homologous proteins and its applications. Proteins 65: 32-39.
    • (2006) Proteins , vol.65 , pp. 32-39
    • Tyagi, M.1    Gowri, V.S.2    Srinivasan, N.3    de Brevern, A.G.4    Offmann, B.5
  • 47
    • 2942541294 scopus 로고    scopus 로고
    • Use of a structural alphabet for analysis of short loops connecting repetitive structures
    • Fourrier L, Benros C, de Brevern AG, (2004) Use of a structural alphabet for analysis of short loops connecting repetitive structures. BMC Bioinformatics 5: 58.
    • (2004) BMC Bioinformatics , vol.5 , pp. 58
    • Fourrier, L.1    Benros, C.2    de Brevern, A.G.3
  • 49
    • 33947526348 scopus 로고    scopus 로고
    • "Pinning strategy": a novel approach for predicting the backbone structure in terms of protein blocks from sequence
    • De Brevern AG, Etchebest C, Benros C, Hazout S, (2007) "Pinning strategy": a novel approach for predicting the backbone structure in terms of protein blocks from sequence. J Biosci 32: 51-70.
    • (2007) J Biosci , vol.32 , pp. 51-70
    • de Brevern, A.G.1    Etchebest, C.2    Benros, C.3    Hazout, S.4
  • 51
    • 34147202792 scopus 로고    scopus 로고
    • Discovering structural motifs using a structural alphabet: application to magnesium-binding sites
    • Dudev M, Lim C, (2007) Discovering structural motifs using a structural alphabet: application to magnesium-binding sites. BMC Bioinformatics 8: 106.
    • (2007) BMC Bioinformatics , vol.8 , pp. 106
    • Dudev, M.1    Lim, C.2
  • 52
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ, (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 53
    • 0026565850 scopus 로고
    • A variable gap penalty function and feature weights for protein 3-D structure comparisons
    • Zhu ZY, Sali A, Blundell TL, (1992) A variable gap penalty function and feature weights for protein 3-D structure comparisons. Protein Eng 5: 43-51.
    • (1992) Protein Eng , vol.5 , pp. 43-51
    • Zhu, Z.Y.1    Sali, A.2    Blundell, T.L.3
  • 55
    • 0025270037 scopus 로고
    • Phylogenetic relationships from three-dimensional protein structures
    • Johnson MS, Sali A, Blundell TL, (1990) Phylogenetic relationships from three-dimensional protein structures. Methods Enzymol 183: 670-690.
    • (1990) Methods Enzymol , vol.183 , pp. 670-690
    • Johnson, M.S.1    Sali, A.2    Blundell, T.L.3
  • 56
    • 0025070240 scopus 로고
    • Molecular anatomy: phyletic relationships derived from three-dimensional structures of proteins
    • Johnson MS, Sutcliffe MJ, Blundell TL, (1990) Molecular anatomy: phyletic relationships derived from three-dimensional structures of proteins. J Mol Evol 30: 43-59.
    • (1990) J Mol Evol , vol.30 , pp. 43-59
    • Johnson, M.S.1    Sutcliffe, M.J.2    Blundell, T.L.3
  • 57
    • 0027219115 scopus 로고
    • Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains
    • Brady RL, Dodson EJ, Dodson GG, Lange G, Davis SJ, et al. (1993) Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains. Science 260: 979-983.
    • (1993) Science , vol.260 , pp. 979-983
    • Brady, R.L.1    Dodson, E.J.2    Dodson, G.G.3    Lange, G.4    Davis, S.J.5
  • 58
    • 0037145075 scopus 로고    scopus 로고
    • Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: high resolution structure and functional properties
    • Park SY, Yamane K, Adachi S, Shiro Y, Weiss KE, et al. (2002) Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: high resolution structure and functional properties. J Inorg Biochem 91: 491-501.
    • (2002) J Inorg Biochem , vol.91 , pp. 491-501
    • Park, S.Y.1    Yamane, K.2    Adachi, S.3    Shiro, Y.4    Weiss, K.E.5
  • 60
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL, (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 61
    • 0032475938 scopus 로고    scopus 로고
    • Functional analysis of the Escherichia coli genome using the sequence-to-structure-to-function paradigm: identification of proteins exhibiting the glutaredoxin/thioredoxin disulfide oxidoreductase activity
    • Fetrow JS, Godzik A, Skolnick J, (1998) Functional analysis of the Escherichia coli genome using the sequence-to-structure-to-function paradigm: identification of proteins exhibiting the glutaredoxin/thioredoxin disulfide oxidoreductase activity. J Mol Biol 282: 703-711.
    • (1998) J Mol Biol , vol.282 , pp. 703-711
    • Fetrow, J.S.1    Godzik, A.2    Skolnick, J.3
  • 62
    • 0031565725 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites using patch analysis
    • Jones S, Thornton JM, (1997) Prediction of protein-protein interaction sites using patch analysis. J Mol Biol 272: 133-143.
    • (1997) J Mol Biol , vol.272 , pp. 133-143
    • Jones, S.1    Thornton, J.M.2
  • 63
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser A, Do RK, Sali A, (2000) Modeling of loops in protein structures. Protein Sci 9: 1753-1773.
    • (2000) Protein Sci , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.2    Sali, A.3
  • 64
    • 0036283048 scopus 로고    scopus 로고
    • Evolution and physics in comparative protein structure modeling
    • Fiser A, Feig M, Brooks CL 3rd, Sali A, (2002) Evolution and physics in comparative protein structure modeling. Acc Chem Res 35: 413-421.
    • (2002) Acc Chem Res , vol.35 , pp. 413-421
    • Fiser, A.1    Feig, M.2    Brooks III, C.L.3    Sali, A.4
  • 66
    • 0019028066 scopus 로고
    • Model for haptoglobin heavy chain based upon structural homology
    • Greer J, (1980) Model for haptoglobin heavy chain based upon structural homology. Proc Natl Acad Sci U S A 77: 3393-3397.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 3393-3397
    • Greer, J.1
  • 67
    • 0022701772 scopus 로고
    • Using known substructures in protein model building and crystallography
    • Jones TA, Thirup S, (1986) Using known substructures in protein model building and crystallography. Embo J 5: 819-822.
    • (1986) Embo J , vol.5 , pp. 819-822
    • Jones, T.A.1    Thirup, S.2
  • 68
    • 0031564640 scopus 로고    scopus 로고
    • PDB-based protein loop prediction: parameters for selection and methods for optimization
    • van Vlijmen HW, Karplus M, (1997) PDB-based protein loop prediction: parameters for selection and methods for optimization. J Mol Biol 267: 975-1001.
    • (1997) J Mol Biol , vol.267 , pp. 975-1001
    • van Vlijmen, H.W.1    Karplus, M.2
  • 69
    • 0027220648 scopus 로고
    • An evaluation of the performance of an automated procedure for comparative modelling of protein tertiary structure
    • Srinivasan N, Blundell TL, (1993) An evaluation of the performance of an automated procedure for comparative modelling of protein tertiary structure. Protein Eng 6: 501-512.
    • (1993) Protein Eng , vol.6 , pp. 501-512
    • Srinivasan, N.1    Blundell, T.L.2
  • 70
    • 0022788691 scopus 로고
    • An algorithm for determining the conformation of polypeptide segments in proteins by systematic search
    • Moult J, James MN, (1986) An algorithm for determining the conformation of polypeptide segments in proteins by systematic search. Proteins 1: 146-163.
    • (1986) Proteins , vol.1 , pp. 146-163
    • Moult, J.1    James, M.N.2
  • 71
    • 0023173201 scopus 로고
    • Prediction of the folding of short polypeptide segments by uniform conformational sampling
    • Bruccoleri RE, Karplus M, (1987) Prediction of the folding of short polypeptide segments by uniform conformational sampling. Biopolymers 26: 137-168.
    • (1987) Biopolymers , vol.26 , pp. 137-168
    • Bruccoleri, R.E.1    Karplus, M.2
  • 72
    • 0022842039 scopus 로고
    • Predicting antibody hypervariable loop conformations. II: Minimization and molecular dynamics studies of MCPC603 from many randomly generated loop conformations
    • Fine RM, Wang H, Shenkin PS, Yarmush DL, Levinthal C, (1986) Predicting antibody hypervariable loop conformations. II: Minimization and molecular dynamics studies of MCPC603 from many randomly generated loop conformations. Proteins 1: 342-362.
    • (1986) Proteins , vol.1 , pp. 342-362
    • Fine, R.M.1    Wang, H.2    Shenkin, P.S.3    Yarmush, D.L.4    Levinthal, C.5
  • 73
    • 17644434949 scopus 로고    scopus 로고
    • Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase
    • Hovel K, Shallom D, Niefind K, Belakhov V, Shoham G, et al. (2003) Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase. Embo J 22: 4922-4932.
    • (2003) Embo J , vol.22 , pp. 4922-4932
    • Hovel, K.1    Shallom, D.2    Niefind, K.3    Belakhov, V.4    Shoham, G.5
  • 74
    • 79952778883 scopus 로고    scopus 로고
    • Crystal Structure of 1,4-Beta-D-Xylan Xylohydrolase from Geobacillus Stearothermophilus
    • (to be published)
    • Jakoncic J, Shoham G, Stojanoff V, (2010) Crystal Structure of 1,4-Beta-D-Xylan Xylohydrolase from Geobacillus Stearothermophilus. (to be published).
    • (2010)
    • Jakoncic, J.1    Shoham, G.2    Stojanoff, V.3
  • 75
    • 0034708342 scopus 로고    scopus 로고
    • High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP
    • Andersen GR, Thirup S, Spremulli LL, Nyborg J, (2000) High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP. J Mol Biol 297: 421-436.
    • (2000) J Mol Biol , vol.297 , pp. 421-436
    • Andersen, G.R.1    Thirup, S.2    Spremulli, L.L.3    Nyborg, J.4
  • 76
    • 33744951325 scopus 로고    scopus 로고
    • Structural basis of the action of pulvomycin and GE2270 A on elongation factor Tu
    • Parmeggiani A, Krab IM, Okamura S, Nielsen RC, Nyborg J, et al. (2006) Structural basis of the action of pulvomycin and GE2270 A on elongation factor Tu. Biochemistry 45: 6846-6857.
    • (2006) Biochemistry , vol.45 , pp. 6846-6857
    • Parmeggiani, A.1    Krab, I.M.2    Okamura, S.3    Nielsen, R.C.4    Nyborg, J.5
  • 77
    • 0030931534 scopus 로고    scopus 로고
    • Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors
    • Fan QR, Mosyak L, Winter CC, Wagtmann N, Long EO, et al. (1997) Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors. Nature 389: 96-100.
    • (1997) Nature , vol.389 , pp. 96-100
    • Fan, Q.R.1    Mosyak, L.2    Winter, C.C.3    Wagtmann, N.4    Long, E.O.5
  • 78
    • 0034640103 scopus 로고    scopus 로고
    • Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity
    • Plotnikov AN, Hubbard SR, Schlessinger J, Mohammadi M, (2000) Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity. Cell 101: 413-424.
    • (2000) Cell , vol.101 , pp. 413-424
    • Plotnikov, A.N.1    Hubbard, S.R.2    Schlessinger, J.3    Mohammadi, M.4
  • 80
    • 0020068152 scopus 로고
    • Self-organized formation of topologically correct feature maps
    • Kohonen T, (1982) Self-organized formation of topologically correct feature maps. Biological Cybernetics 43: 59-69.
    • (1982) Biological Cybernetics , vol.43 , pp. 59-69
    • Kohonen, T.1
  • 81
    • 0024610919 scopus 로고
    • A tutorial on hidden Markov models and selected application in speech recognition
    • Rabiner L, (1989) A tutorial on hidden Markov models and selected application in speech recognition. Proceedings of the IEEE 77: 257-286.
    • (1989) Proceedings of the IEEE , vol.77 , pp. 257-286
    • Rabiner, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.