메뉴 건너뛰기




Volumn 19, Issue SUPPL. 2, 2003, Pages

Flexible structure alignment by chaining aligned fragment pairs allowing twists

Author keywords

[No Author keywords available]

Indexed keywords

RIBOSOME PROTEIN;

EID: 3042581007     PISSN: 13674803     EISSN: 13674811     Source Type: Journal    
DOI: 10.1093/bioinformatics/btg1086     Document Type: Conference Paper
Times cited : (497)

References (26)
  • 1
    • 0021314461 scopus 로고
    • Structural and functional aspects of domain motions in proteins
    • Bennett, W. and Huber, R. (1984) Structural and functional aspects of domain motions in proteins. Crit. Rev. Biochem., 15, 291-384.
    • (1984) Crit. Rev. Biochem. , vol.15 , pp. 291-384
    • Bennett, W.1    Huber, R.2
  • 2
    • 0028789439 scopus 로고
    • Optimal protein structure alignments by multiple linkage clustering: Application to distantly related proteins
    • Boutonnet, N.S., Rooman, M.J., Ochagavia, M.E., Richelle, J. and Wodak, S.J. (1995) Optimal protein structure alignments by multiple linkage clustering: application to distantly related proteins. Protein Engng, 8, 647-662.
    • (1995) Protein Engng , vol.8 , pp. 647-662
    • Boutonnet, N.S.1    Rooman, M.J.2    Ochagavia, M.E.3    Richelle, J.4    Wodak, S.J.5
  • 3
    • 0037246863 scopus 로고    scopus 로고
    • Molmovdb: Analysis and visualization of conformational change and structural flexibility
    • Echols, N., Milburn, D. and Gerstein, M. (2003) Molmovdb: analysis and visualization of conformational change and structural flexibility. Nucleic Acids Res., 31, 478-482.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 478-482
    • Echols, N.1    Milburn, D.2    Gerstein, M.3
  • 5
    • 0030334647 scopus 로고    scopus 로고
    • Optimum superimposition of protein structures: Ambiguities and implications
    • Feng, Z.K. and Sippl, M.J. (1996) Optimum superimposition of protein structures: ambiguities and implications. Fold Des., 1, 123-132.
    • (1996) Fold Des. , vol.1 , pp. 123-132
    • Feng, Z.K.1    Sippl, M.J.2
  • 6
    • 0030310317 scopus 로고    scopus 로고
    • Assessing the performance of fold recognition methods by means of a comprehensive benchmark
    • Fischer, D., Elofsson, A., Rice, D. and Eisenberg, D. (1996) Assessing the performance of fold recognition methods by means of a comprehensive benchmark. In Pacific Symposium on Biocomputing. pp. 300-318.
    • (1996) Pacific Symposium on Biocomputing , pp. 300-318
    • Fischer, D.1    Elofsson, A.2    Rice, D.3    Eisenberg, D.4
  • 7
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M., Lesk, A.M. and Chothia, C. (1994) Structural mechanisms for domain movements in proteins. Biochemistry, 33, 6739-6749.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 8
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, E. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol., 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, E.1    Sander, C.2
  • 9
    • 0035427398 scopus 로고    scopus 로고
    • Protein flexibility predictions using graph theory
    • Jacobs, D.J., Rader, A.J., Kuhn, L.A. and Thorpe, M.F. (2001) Protein flexibility predictions using graph theory. Proteins, 44, 150-165.
    • (2001) Proteins , vol.44 , pp. 150-165
    • Jacobs, D.J.1    Rader, A.J.2    Kuhn, L.A.3    Thorpe, M.F.4
  • 10
    • 0036600834 scopus 로고    scopus 로고
    • Evolution of protein structures and functions
    • Kinch, L.N. and Grishin, N.V. (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
  • 12
    • 0037008092 scopus 로고    scopus 로고
    • Caught in the act: The structure of phosphorylated beta- phosphoglucomutase from Lactococcus Lactis
    • Lahiri, S.D., Zhang, G., Dunaway-Mariano, D. and Allen, K.N. (2002) Caught in the act: the structure of phosphorylated beta-phosphoglucomutase from Lactococcus Lactis. Biochemistry, 41, 8351-8359.
    • (2002) Biochemistry , vol.41 , pp. 8351-8359
    • Lahiri, S.D.1    Zhang, G.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 13
    • 0032510975 scopus 로고    scopus 로고
    • Crystal structures of reaction intermediates of 1-2-haloacid dehalogenase and implications for the reaction mechanism
    • Li, Y.F., Hata, Y., Fujii, T., Hisano, T., Nishihara, M., Kurihara, T. and Esaki, N. (1998) Crystal structures of reaction intermediates of 1-2-haloacid dehalogenase and implications for the reaction mechanism. J. Biol. Chem., 273, 15 035-15 044.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15035-15044
    • Li, Y.F.1    Hata, Y.2    Fujii, T.3    Hisano, T.4    Nishihara, M.5    Kurihara, T.6    Esaki, N.7
  • 14
    • 0028838717 scopus 로고
    • Threading a database of protein cores
    • Madej, T., Gibrat, J.F. and Bryant, S.H. (1995) Threading a database of protein cores. Proteins, 23, 356-369.
    • (1995) Proteins , vol.23 , pp. 356-369
    • Madej, T.1    Gibrat, J.F.2    Bryant, S.H.3
  • 15
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T. and 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
  • 16
    • 0035999993 scopus 로고    scopus 로고
    • Advanced pair-wise structure alignments of proteins and analysis of conformational changes
    • Ochagavia, M.E., Richelle, J. and Wodak, S.J. (2002) Advanced pair-wise structure alignments of proteins and analysis of conformational changes. Bioinformatics, 18, 637-640.
    • (2002) Bioinformatics , vol.18 , pp. 637-640
    • Ochagavia, M.E.1    Richelle, J.2    Wodak, S.J.3
  • 17
    • 0030596129 scopus 로고    scopus 로고
    • Crystal structures of adenylosuccinate synthetase from Escherichia Coli complexed with GDP, IMP hadacidin, NO3-, and Mg2 +
    • Poland, B.W., Fromm, H.J. and Honzatko, R.B. (1996) Crystal structures of adenylosuccinate synthetase from Escherichia Coli complexed with GDP, IMP hadacidin, NO3-, and Mg2 +. J. Mol. Biol., 264, 1013-1027.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1013-1027
    • Poland, B.W.1    Fromm, H.J.2    Honzatko, R.B.3
  • 18
    • 0027507711 scopus 로고
    • Packing of secondary structural elements in proteins. Analysis and prediction of inter-helix distances
    • Reddy, B.V. and Blundell, T.L. (1993) Packing of secondary structural elements in proteins. Analysis and prediction of inter-helix distances. J. Mol. Biol., 233, 464-479.
    • (1993) J. Mol. Biol. , vol.233 , pp. 464-479
    • Reddy, B.V.1    Blundell, T.L.2
  • 19
    • 0033016710 scopus 로고    scopus 로고
    • Analysis of interactive packing of secondary structural elements in alpha/beta units in proteins
    • Reddy, B.V., Nagarajaram, H.A. and Blundell, T.L. (1999) Analysis of interactive packing of secondary structural elements in alpha/beta units in proteins. Protein Sci., 8, 573-586.
    • (1999) Protein Sci. , vol.8 , pp. 573-586
    • Reddy, B.V.1    Nagarajaram, H.A.2    Blundell, T.L.3
  • 21
    • 0036681439 scopus 로고    scopus 로고
    • Flexible protein alignment and hinge detection
    • Shatsky, M., Nussinov, R. and Wolfson, H.J. (2002) Flexible protein alignment and hinge detection. Proteins, 48, 242-256.
    • (2002) Proteins , vol.48 , pp. 242-256
    • Shatsky, M.1    Nussinov, R.2    Wolfson, H.J.3
  • 22
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov, I.N. and Bourne, P.E. (1998) Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Engng, 11, 739-747.
    • (1998) Protein Engng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 24
    • 0025744920 scopus 로고
    • Detection of common three-dimensional substructures in proteins
    • Vriend, G. and Sander, C. (1991) Detection of common three-dimensional substructures in proteins. Proteins, 11, 52-58.
    • (1991) Proteins , vol.11 , pp. 52-58
    • Vriend, G.1    Sander, C.2
  • 25
    • 0030883755 scopus 로고    scopus 로고
    • Protein domain movements: Detection of rigid domains and visualization of hinges in comparisons of atomic coordinates
    • Wriggers, W. and Schulten, K. (1997) Protein domain movements: detection of rigid domains and visualization of hinges in comparisons of atomic coordinates. Proteins, 29, 1-14.
    • (1997) Proteins , vol.29 , pp. 1-14
    • Wriggers, W.1    Schulten, K.2
  • 26
    • 0018172628 scopus 로고
    • Internal motion in globular proteins
    • Wuthrich, K. and Wagner, G. (1978) Internal motion in globular proteins. Trends Biochem. Sci., 3, 227-230.
    • (1978) Trends Biochem. Sci. , vol.3 , pp. 227-230
    • Wuthrich, K.1    Wagner, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.