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Volumn 19, Issue 4, 2011, Pages 461-470

Remote thioredoxin recognition using evolutionary conservation and structural dynamics

Author keywords

[No Author keywords available]

Indexed keywords

THIOREDOXIN;

EID: 79953892742     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2011.02.007     Document Type: Article
Times cited : (14)

References (77)
  • 3
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • E.S. Arner, and A. Holmgren Physiological functions of thioredoxin and thioredoxin reductase Eur. J. Biochem. 267 2000 6102 6109
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6102-6109
    • Arner, E.S.1    Holmgren, A.2
  • 4
    • 72749084211 scopus 로고    scopus 로고
    • An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations
    • H.J. Atkinson, and P.C. Babbitt An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations PLoS Comput. Biol. 5 2009 e1000541
    • (2009) PLoS Comput. Biol. , vol.5 , pp. 1000541
    • Atkinson, H.J.1    Babbitt, P.C.2
  • 7
    • 0345059376 scopus 로고    scopus 로고
    • Announcing the worldwide Protein Data Bank
    • DOI 10.1038/nsb1203-980
    • H. Berman, K. Henrick, and H. Nakamura Announcing the worldwide Protein Data Bank Nat. Struct. Biol. 10 2003 980 (Pubitemid 37500485)
    • (2003) Nature Structural Biology , vol.10 , Issue.12 , pp. 980
    • Berman, H.1    Henrick, K.2    Nakamura, H.3
  • 8
    • 60549083680 scopus 로고    scopus 로고
    • Thioredoxin-1 is a novel and attractive therapeutic approach for various diseases including cardiovascular disorders
    • L. Billiet, and M. Rouis Thioredoxin-1 is a novel and attractive therapeutic approach for various diseases including cardiovascular disorders Cardiovasc. Hematol. Disord. Drug Targets 8 2008 293 296
    • (2008) Cardiovasc. Hematol. Disord. Drug Targets , vol.8 , pp. 293-296
    • Billiet, L.1    Rouis, M.2
  • 11
    • 38749149916 scopus 로고    scopus 로고
    • Protein crystallization: From purified protein to diffraction-quality crystal
    • DOI 10.1038/nmeth.f.203, PII NMETH.F.203
    • N.E. Chayen, and E. Saridakis Protein crystallization: from purified protein to diffraction-quality crystal Nat. Methods 5 2008 147 153 (Pubitemid 351181740)
    • (2008) Nature Methods , vol.5 , Issue.2 , pp. 147-153
    • Chayen, N.E.1    Saridakis, E.2
  • 12
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • C. Chothia, and A.M. Lesk The relation between the divergence of sequence and structure in proteins EMBO J. 5 1986 823 826
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 15
    • 0029876415 scopus 로고    scopus 로고
    • Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2
    • DOI 10.1038/380548a0
    • P. Colas, B. Cohen, T. Jessen, I. Grishina, J. McCoy, and R. Brent Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2 Nature 380 1996 548 550 (Pubitemid 26110646)
    • (1996) Nature , vol.380 , Issue.6574 , pp. 548-550
    • Colas, P.1    Cohen, B.2    Jessen, T.3    Grishina, I.4    McCoy, J.5    Brent, R.6
  • 17
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • S.R. Eddy Profile hidden Markov models Bioinformatics 14 1998 755 763 (Pubitemid 28552108)
    • (1998) Bioinformatics , vol.14 , Issue.9 , pp. 755-763
    • Eddy, S.R.1
  • 19
    • 0025883245 scopus 로고
    • Structural and functional relations among thioredoxins of different species
    • H. Eklund, F.K. Gleason, and A. Holmgren Structural and functional relations among thioredoxins of different species Proteins 11 1991 13 28
    • (1991) Proteins , vol.11 , pp. 13-28
    • Eklund, H.1    Gleason, F.K.2    Holmgren, A.3
  • 20
    • 0032483312 scopus 로고    scopus 로고
    • 1 ribonucleases
    • DOI 10.1006/jmbi.1998.1993
    • J.S. Fetrow, and J. Skolnick Method for prediction of protein function from sequence using the sequence-to-structure-to-function paradigm with application to glutaredoxins/thioredoxins and T1 ribonucleases J. Mol. Biol. 281 1998 949 968 (Pubitemid 28408440)
    • (1998) Journal of Molecular Biology , vol.281 , Issue.5 , pp. 949-968
    • Fetrow, J.S.1    Skolnick, J.2
  • 21
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • A. Fiser, R.K. Do, and A. Sali Modeling of loops in protein structures Protein Sci. 9 2000 1753 1773
    • (2000) Protein Sci. , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.2    Sali, A.3
  • 22
    • 0346882663 scopus 로고    scopus 로고
    • ModLoop: Automated modeling of loops in protein structures
    • DOI 10.1093/bioinformatics/btg362
    • A. Fiser, and A. Sali ModLoop: automated modeling of loops in protein structures Bioinformatics 19 2003 2500 2501 (Pubitemid 38016660)
    • (2003) Bioinformatics , vol.19 , Issue.18 , pp. 2500-2501
    • Fiser, A.1    Sali, A.2
  • 23
    • 0023906547 scopus 로고
    • Protein disulphide-isomerase: A homologue of thioredoxin implicated in the biosynthesis of secretory proteins
    • R.B. Freedman, H.C. Hawkins, S.J. Murant, and L. Reid Protein disulphide-isomerase: a homologue of thioredoxin implicated in the biosynthesis of secretory proteins Biochem. Soc. Trans. 16 1988 96 99 (Pubitemid 18092697)
    • (1988) Biochemical Society Transactions , vol.16 , Issue.2 , pp. 96-99
    • Freedman, R.B.1    Hawkins, H.C.2    Murant, S.J.3    Reid, L.4
  • 25
    • 0018780591 scopus 로고
    • Side-chain torsional potentials: Effect of dipeptide, protein, and solvent environment
    • B.R. Gelin, and M. Karplus Side-chain torsional potentials: effect of dipeptide, protein, and solvent environment Biochemistry 18 1979 1256 1268
    • (1979) Biochemistry , vol.18 , pp. 1256-1268
    • Gelin, B.R.1    Karplus, M.2
  • 26
    • 33746664765 scopus 로고    scopus 로고
    • Can sequence determine function?
    • J.A. Gerlt, and P.C. Babbitt Can sequence determine function? Genome Biol. 1 2000 REVIEWS0005
    • (2000) Genome Biol. , vol.1
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 27
    • 67650150099 scopus 로고    scopus 로고
    • Improving structure-based function prediction using molecular dynamics
    • D.S. Glazer, R.J. Radmer, and R.B. Altman Improving structure-based function prediction using molecular dynamics Structure 17 2009 919 929
    • (2009) Structure , vol.17 , pp. 919-929
    • Glazer, D.S.1    Radmer, R.J.2    Altman, R.B.3
  • 29
    • 0032526690 scopus 로고    scopus 로고
    • Crystal structures of reduced and oxidized DsbA: Investigation of domain motion and thiolate stabilization
    • L.W. Guddat, J.C. Bardwell, and J.L. Martin Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization Structure 6 1998 757 767 (Pubitemid 28301209)
    • (1998) Structure , vol.6 , Issue.6 , pp. 757-767
    • Guddat, L.W.1    Bardwell, J.C.A.2    Martin, J.L.3
  • 30
    • 0037249633 scopus 로고    scopus 로고
    • The TIGRFAMs database of protein families
    • DOI 10.1093/nar/gkg128
    • D.H. Haft, J.D. Selengut, and O. White The TIGRFAMs database of protein families Nucleic Acids Res. 31 2003 371 373 (Pubitemid 36150405)
    • (2003) Nucleic Acids Research , vol.31 , Issue.1 , pp. 371-373
    • Haft, D.H.1    Selengut, J.D.2    White, O.3
  • 31
    • 52249116089 scopus 로고    scopus 로고
    • The FEATURE framework for protein function annotation: Modeling new functions, improving performance, and extending to novel applications
    • I. Halperin, D.S. Glazer, S. Wu, and R.B. Altman The FEATURE framework for protein function annotation: modeling new functions, improving performance, and extending to novel applications BMC Genomics 9 Suppl 2 2008 S2
    • (2008) BMC Genomics , vol.9 , Issue.SUPPL. 2 , pp. 2
    • Halperin, I.1    Glazer, D.S.2    Wu, S.3    Altman, R.B.4
  • 32
    • 0037375799 scopus 로고    scopus 로고
    • Efficient identification of side-chain patterns using a multidimensional index tree
    • DOI 10.1002/prot.10338
    • T. Hamelryck Efficient identification of side-chain patterns using a multidimensional index tree Proteins 51 2003 96 108 (Pubitemid 36293036)
    • (2003) Proteins: Structure, Function and Genetics , vol.51 , Issue.1 , pp. 96-108
    • Hamelryck, T.1
  • 33
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • DOI 10.1038/nature06522, PII NATURE06522
    • K. Henzler-Wildman, and D. Kern Dynamic personalities of proteins Nature 450 2007 964 972 (Pubitemid 350273626)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 34
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • DOI 10.1093/bioinformatics/btn507
    • L. Holm, S. Kaariainen, P. Rosenstrom, and A. Schenkel Searching protein structure databases with DaliLite v.3 Bioinformatics 24 2008 2780 2781 (Pubitemid 352722625)
    • (2008) Bioinformatics , vol.24 , Issue.23 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 35
    • 0018080325 scopus 로고
    • Glutathione-dependent enzyme reactions of the phage T4 ribonucleotide reductase system
    • A. Holmgren Glutathione-dependent enzyme reactions of the phage T4 ribonucleotide reductase system J. Biol. Chem. 253 1978 7424 7430 (Pubitemid 9045230)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.20 , pp. 7424-7430
    • Holmgren, A.1
  • 37
    • 0023937750 scopus 로고
    • Thioredoxin and glutaredoxin: Small multi-functional redox proteins with active-site disulphide bonds
    • A. Holmgren Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds Biochem. Soc. Trans. 16 1988 95 96 (Pubitemid 18092696)
    • (1988) Biochemical Society Transactions , vol.16 , Issue.2 , pp. 95-96
    • Holmgren, A.1
  • 39
    • 49549119981 scopus 로고    scopus 로고
    • The disulfide bond formation (Dsb) system
    • K. Ito, and K. Inaba The disulfide bond formation (Dsb) system Curr. Opin. Struct. Biol. 18 2008 450 458
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 450-458
    • Ito, K.1    Inaba, K.2
  • 40
    • 0036310711 scopus 로고    scopus 로고
    • On the role of the crystal environment in determining protein side-chain conformations
    • DOI 10.1016/S0022-2836(02)00470-9
    • M.P. Jacobson, R.A. Friesner, Z. Xiang, and B. Honig On the role of the crystal environment in determining protein side-chain conformations J. Mol. Biol. 320 2002 597 608 (Pubitemid 34753983)
    • (2002) Journal of Molecular Biology , vol.320 , Issue.3 , pp. 597-608
    • Jacobson, M.P.1    Friesner, R.A.2    Xiang, Z.3    Honig, B.4
  • 42
    • 0036434640 scopus 로고    scopus 로고
    • Identification and characterization of thioredoxin and thioredoxin reductase from Aeropyrum pernix K1
    • DOI 10.1046/j.1432-1033.2002.03231.x
    • S.J. Jeon, and K. Ishikawa Identification and characterization of thioredoxin and thioredoxin reductase from Aeropyrum pernix K1 Eur. J. Biochem. 269 2002 5423 5430 (Pubitemid 35370026)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.22 , pp. 5423-5430
    • Jeon, S.-J.1    Ishikawa, K.2
  • 43
    • 0032438987 scopus 로고    scopus 로고
    • Hidden Markov models for detecting remote protein homologies
    • DOI 10.1093/bioinformatics/14.10.846
    • K. Karplus, C. Barrett, and R. Hughey Hidden Markov models for detecting remote protein homologies Bioinformatics 14 1998 846 856 (Pubitemid 29041540)
    • (1998) Bioinformatics , vol.14 , Issue.10 , pp. 846-856
    • Karplus, K.1    Barrett, C.2    Hughey, R.3
  • 44
    • 0033613813 scopus 로고    scopus 로고
    • Recognition of spatial motifs in protein structures
    • DOI 10.1006/jmbi.1998.2393
    • G.J. Kleywegt Recognition of spatial motifs in protein structures J. Mol. Biol. 285 1999 1887 1897 (Pubitemid 29060478)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.4 , pp. 1887-1897
    • Kleywegt, G.J.1
  • 45
    • 0026645602 scopus 로고
    • Variability of conformations at crystal contacts in BPTI represent true low-energy structures: Correspondence among lattice packing and molecular dynamics structures
    • A.A. Kossiakoff, M. Randal, J. Guenot, and C. Eigenbrot Variability of conformations at crystal contacts in BPTI represent true low-energy structures: correspondence among lattice packing and molecular dynamics structures Proteins 14 1992 65 74
    • (1992) Proteins , vol.14 , pp. 65-74
    • Kossiakoff, A.A.1    Randal, M.2    Guenot, J.3    Eigenbrot, C.4
  • 47
    • 0029165589 scopus 로고
    • Thioredoxin: A fold for all reasons
    • J.L. Martin Thioredoxin: a fold for all reasons Structure 3 1995 245 250
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 48
    • 75549084894 scopus 로고    scopus 로고
    • PANTHER version 7: Improved phylogenetic trees, orthologs and collaboration with the Gene Ontology Consortium
    • H. Mi, Q. Dong, A. Muruganujan, P. Gaudet, S. Lewis, and P.D. Thomas PANTHER version 7: improved phylogenetic trees, orthologs and collaboration with the Gene Ontology Consortium Nucleic Acids Res. 38 2010 D204 D210
    • (2010) Nucleic Acids Res. , vol.38
    • Mi, H.1    Dong, Q.2    Muruganujan, A.3    Gaudet, P.4    Lewis, S.5    Thomas, P.D.6
  • 49
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • A.G. Murzin, S.E. Brenner, T. Hubbard, and C. Chothia SCOP: a structural classification of proteins database for the investigation of sequences and structures J. Mol. Biol. 247 1995 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
  • 50
    • 1842479952 scopus 로고    scopus 로고
    • Exploring Protein Native States and Large-Scale Conformational Changes with a Modified Generalized Born Model
    • DOI 10.1002/prot.20033
    • A. Onufriev, D. Bashford, and D.A. Case Exploring protein native states and large-scale conformational changes with a modified generalized born model Proteins 55 2004 383 394 (Pubitemid 38437495)
    • (2004) Proteins: Structure, Function and Genetics , vol.55 , Issue.2 , pp. 383-394
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 51
    • 70350465128 scopus 로고    scopus 로고
    • Structural relationships among proteins with different global topologies and their implications for function annotation strategies
    • D. Petrey, M. Fischer, and B. Honig Structural relationships among proteins with different global topologies and their implications for function annotation strategies Proc. Natl. Acad. Sci. USA 106 2009 17377 17382
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 17377-17382
    • Petrey, D.1    Fischer, M.2    Honig, B.3
  • 52
    • 66549120787 scopus 로고    scopus 로고
    • Is protein classification necessary? Toward alternative approaches to function annotation
    • D. Petrey, and B. Honig Is protein classification necessary? Toward alternative approaches to function annotation Curr. Opin. Struct. Biol. 19 2009 363 368
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 363-368
    • Petrey, D.1    Honig, B.2
  • 53
    • 33645098516 scopus 로고    scopus 로고
    • Automated discovery of 3D motifs for protein function annotation
    • B.J. Polacco, and P.C. Babbitt Automated discovery of 3D motifs for protein function annotation Bioinformatics 22 2006 723 730
    • (2006) Bioinformatics , vol.22 , pp. 723-730
    • Polacco, B.J.1    Babbitt, P.C.2
  • 54
    • 4043171970 scopus 로고    scopus 로고
    • The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate Born radii
    • D. Qiu, P.S. Shenkin, F.P. Hollinger, and W.C. Still The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate Born radii J. Phys. Chem. A 101 1997 3005 3014 (Pubitemid 127580882)
    • (1997) Journal of Physical Chemistry A , vol.101 , Issue.16 , pp. 3005-3014
    • Qiu, D.1    Shenkin, P.S.2    Hollinger, F.P.3    Still, W.C.4
  • 55
    • 33646940952 scopus 로고
    • Numerical-integration of Cartesian equations of motion of a system with constraints: Molecular-dynamics of N-alkanes
    • J.P. Ryckaert, G. Ciccotti, and H.J.C. Berendsen Numerical-integration of Cartesian equations of motion of a system with constraints: molecular-dynamics of N-alkanes J. Comp. Physiol. 23 1977 327 341
    • (1977) J. Comp. Physiol. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 56
    • 35748982413 scopus 로고    scopus 로고
    • Geometry-Based Sampling of Conformational Transitions in Proteins
    • DOI 10.1016/j.str.2007.09.017, PII S0969212607003681
    • D. Seeliger, J. Haas, and B.L. de Groot Geometry-based sampling of conformational transitions in proteins Structure 15 2007 1482 1492 (Pubitemid 350051928)
    • (2007) Structure , vol.15 , Issue.11 , pp. 1482-1492
    • Seeliger, D.1    Haas, J.2    De Groot, B.L.3
  • 58
    • 0031813130 scopus 로고    scopus 로고
    • Pfam: Multiple sequence alignments and HMM-profiles of protein domains
    • DOI 10.1093/nar/26.1.320
    • E.L. Sonnhammer, S.R. Eddy, E. Birney, A. Bateman, and R. Durbin Pfam: multiple sequence alignments and HMM-profiles of protein domains Nucleic Acids Res. 26 1998 320 322 (Pubitemid 28291550)
    • (1998) Nucleic Acids Research , vol.26 , Issue.1 , pp. 320-322
    • Sonnhammer, E.L.L.1    Eddy, S.R.2    Birney, E.3    Bateman, A.4    Durbin, R.5
  • 59
    • 0344778061 scopus 로고
    • Semianalytical Treatment of Solvation for Molecular Mechanics and Dynamics
    • W.C. Still, A. Tempczyk, R.C. Hawley, and T. Hendrickson Semianalytical Treatment of Solvation for Molecular Mechanics and Dynamics J. Am. Chem. Soc. 112 1990 6127 6129
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6127-6129
    • Still, W.C.1    Tempczyk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 60
    • 33646044990 scopus 로고    scopus 로고
    • High-resolution structures of Escherichia coli cDsbD in different redox states: A combined crystallographic, biochemical and computational study
    • C.U. Stirnimann, A. Rozhkova, U. Grauschopf, R.A. Bockmann, R. Glockshuber, G. Capitani, and M.G. Grutter High-resolution structures of Escherichia coli cDsbD in different redox states: a combined crystallographic, biochemical and computational study J. Mol. Biol. 358 2006 829 845
    • (2006) J. Mol. Biol. , vol.358 , pp. 829-845
    • Stirnimann, C.U.1    Rozhkova, A.2    Grauschopf, U.3    Bockmann, R.A.4    Glockshuber, R.5    Capitani, G.6    Grutter, M.G.7
  • 62
    • 34250206320 scopus 로고    scopus 로고
    • A conserved cis-proline precludes metal binding by the active site thiolates in members of the thioredoxin family of proteins
    • DOI 10.1021/bi700152b
    • D. Su, C. Berndt, D.E. Fomenko, A. Holmgren, and V.N. Gladyshev A conserved cis-proline precludes metal binding by the active site thiolates in members of the thioredoxin family of proteins Biochemistry 46 2007 6903 6910 (Pubitemid 46906419)
    • (2007) Biochemistry , vol.46 , Issue.23 , pp. 6903-6910
    • Su, D.1    Berndt, C.2    Fomenko, D.E.3    Holmgren, A.4    Gladyshev, V.N.5
  • 63
    • 0037075039 scopus 로고    scopus 로고
    • Secret life of genes
    • G. Theissen Secret life of genes Nature 415 2002 741 (Pubitemid 34150481)
    • (2002) Nature , vol.415 , Issue.6873 , pp. 741
    • Theissen, G.1
  • 64
    • 0035252651 scopus 로고    scopus 로고
    • Structural genomics takes off
    • DOI 10.1016/S0968-0004(00)01765-5, PII S0968000400017655
    • J. Thornton Structural genomics takes off Trends Biochem. Sci. 26 2001 88 89 (Pubitemid 32144741)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.2 , pp. 88-89
    • Thornton, J.1
  • 65
    • 58149352993 scopus 로고    scopus 로고
    • Thioredoxin system inhibitors as mediators of apoptosis for cancer therapy
    • K.F. Tonissen, and G. Di Trapani Thioredoxin system inhibitors as mediators of apoptosis for cancer therapy Mol. Nutr. Food Res. 53 2009 87 103
    • (2009) Mol. Nutr. Food Res. , vol.53 , pp. 87-103
    • Tonissen, K.F.1    Di Trapani, G.2
  • 66
    • 75849153303 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt) in 2010
    • UniProtKB/TrEMBL
    • UniProtKB/TrEMBL The Universal Protein Resource (UniProt) in 2010 Nucleic Acids Res. 38 2010 D142 D148
    • (2010) Nucleic Acids Res. , vol.38
  • 69
    • 0030724039 scopus 로고    scopus 로고
    • Tess: A geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases. Application to enzyme active sites
    • A.C. Wallace, N. Borkakoti, and J.M. Thornton TESS: a geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases. Application to enzyme active sites Protein Sci. 6 1997 2308 2323 (Pubitemid 27490741)
    • (1997) Protein Science , vol.6 , Issue.11 , pp. 2308-2323
    • Wallace, A.C.1    Borkakoti, N.2    Thornton, J.M.3
  • 70
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2: A multiple sequence alignment editor and analysis workbench
    • A.M. Waterhouse, J.B. Procter, D.M. Martin, M. Clamp, and G.J. Barton Jalview Version 2: a multiple sequence alignment editor and analysis workbench Bioinformatics 25 2009 1189 1191
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 71
    • 0030585429 scopus 로고    scopus 로고
    • Crystal structures of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer
    • A. Weichsel, J.R. Gasdaska, G. Powis, and W.R. Montfort Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer Structure 4 1996 735 751 (Pubitemid 126661296)
    • (1996) Structure , vol.4 , Issue.6 , pp. 735-751
    • Weichsel, A.1    Gasdaska, J.R.2    Powis, G.3    Montfort, W.R.4
  • 72
    • 0034677669 scopus 로고    scopus 로고
    • Assessing annotation transfer for genomics: Quantifying the relations between protein sequence, structure and function through traditional and probabilistic scores
    • C.A. Wilson, J. Kreychman, and M. Gerstein Assessing annotation transfer for genomics: quantifying the relations between protein sequence, structure and function through traditional and probabilistic scores J. Mol. Biol. 297 2000 233 249
    • (2000) J. Mol. Biol. , vol.297 , pp. 233-249
    • Wilson, C.A.1    Kreychman, J.2    Gerstein, M.3
  • 73
    • 34547298869 scopus 로고    scopus 로고
    • Can a physics-based, all-atom potential find a protein's native structure among misfolded structures? I. Large scale AMBER benchmarking
    • DOI 10.1002/jcc.20720
    • L. Wroblewska, and J. Skolnick Can a physics-based, all-atom potential find a protein's native structure among misfolded structures? I. Large scale AMBER benchmarking J. Comput. Chem. 28 2007 2059 2066 (Pubitemid 47153603)
    • (2007) Journal of Computational Chemistry , vol.28 , Issue.12 , pp. 2059-2066
    • Wroblewska, L.1    Skolnick, J.2
  • 74
    • 46249116234 scopus 로고    scopus 로고
    • The SeqFEATURE library of 3D functional site models: Comparison to existing methods and applications to protein function annotation
    • S. Wu, M.P. Liang, and R.B. Altman The SeqFEATURE library of 3D functional site models: comparison to existing methods and applications to protein function annotation Genome Biol. 9 2008 R8
    • (2008) Genome Biol. , vol.9 , pp. 8
    • Wu, S.1    Liang, M.P.2    Altman, R.B.3
  • 75
    • 77749314813 scopus 로고    scopus 로고
    • Identification of recurring protein structure microenvironments and discovery of novel functional sites around CYS residues
    • S. Wu, T. Liu, and R.B. Altman Identification of recurring protein structure microenvironments and discovery of novel functional sites around CYS residues BMC Struct. Biol. 10 2010 4
    • (2010) BMC Struct. Biol. , vol.10 , pp. 4
    • Wu, S.1    Liu, T.2    Altman, R.B.3
  • 76
    • 36849085295 scopus 로고    scopus 로고
    • Crystal structure of an unusual thioredoxin protein with a zinc finger domain
    • DOI 10.1074/jbc.M704044200
    • J. Ye, S.H. Cho, J. Fuselier, W. Li, J. Beckwith, and T.A. Rapoport Crystal structure of an unusual thioredoxin protein with a zinc finger domain J. Biol. Chem. 282 2007 34945 34951 (Pubitemid 350232423)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.48 , pp. 34945-34951
    • Ye, J.1    Cho, S.-H.2    Fuselier, J.3    Li, W.4    Beckwith, J.5    Rapoport, T.A.6
  • 77
    • 8644224198 scopus 로고    scopus 로고
    • Secondary-structure preferences of force fields for proteins evaluated by generalized-ensemble simulations
    • T. Yoda, Y. Sugita, and Y. Okamoto Secondary-structure preferences of force fields for proteins evaluated by generalized-ensemble simulations Chem. Phys. 307 2004 269 283
    • (2004) Chem. Phys. , vol.307 , pp. 269-283
    • Yoda, T.1    Sugita, Y.2    Okamoto, Y.3


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