메뉴 건너뛰기




Volumn 9, Issue 4, 1998, Pages 383-389

Protein structure prediction

Author keywords

[No Author keywords available]

Indexed keywords

ACCURACY; ALGORITHM; AMINO ACID SEQUENCE; GENOME; MODEL; PREDICTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; REVIEW;

EID: 0032145543     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(98)80012-8     Document Type: Article
Times cited : (30)

References (69)
  • 1
    • 0030581145 scopus 로고    scopus 로고
    • The use of amino acid patterns of classified helices and strands in secondary structure prediction
    • Zhu ZY, Blundell TL. The use of amino acid patterns of classified helices and strands in secondary structure prediction. J Mol Biol. 260:1996;261-276.
    • (1996) J Mol Biol , vol.260 , pp. 261-276
    • Zhu, Z.Y.1    Blundell, T.L.2
  • 2
    • 0029984070 scopus 로고    scopus 로고
    • Improving prediction of protein secondary structure using neural networks and multiple sequence alignments
    • Riis SK, Krough A. Improving prediction of protein secondary structure using neural networks and multiple sequence alignments. J Comp Biol. 3:1996;163-183.
    • (1996) J Comp Biol , vol.3 , pp. 163-183
    • Riis, S.K.1    Krough, A.2
  • 3
    • 0030601801 scopus 로고    scopus 로고
    • Using evolutionary trees in protein secondary structure prediction and other comparative sequence analyses
    • Goldman N, Thorne JL, Jones DT. Using evolutionary trees in protein secondary structure prediction and other comparative sequence analyses. J Mol Biol. 263:1996;196-208.
    • (1996) J Mol Biol , vol.263 , pp. 196-208
    • Goldman, N.1    Thorne, J.L.2    Jones, D.T.3
  • 4
    • 0029804192 scopus 로고    scopus 로고
    • Identification and application of the concepts important for accurate and reliable secondary structure prediction
    • King RD, Sternberg MJE. Identification and application of the concepts important for accurate and reliable secondary structure prediction. Protein Sci. 5:1996;2298-2310.
    • (1996) Protein Sci , vol.5 , pp. 2298-2310
    • King, R.D.1    Sternberg, M.J.E.2
  • 5
    • 0031022743 scopus 로고    scopus 로고
    • Improvement of protein secondary structure prediction using binary word encoding
    • Kawabata T, Doi J. Improvement of protein secondary structure prediction using binary word encoding. Proteins. 27:1997;36-46.
    • (1997) Proteins , vol.27 , pp. 36-46
    • Kawabata, T.1    Doi, J.2
  • 6
    • 0030719433 scopus 로고    scopus 로고
    • Improved method for prediction of protein backbone U-turn positions and major secondary structural elements between U-turns
    • Hu W-P, Kolinski A, Skolnick J. Improved method for prediction of protein backbone U-turn positions and major secondary structural elements between U-turns. Proteins. 29:1997;443-460.
    • (1997) Proteins , vol.29 , pp. 443-460
    • Hu, W.-P.1    Kolinski, A.2    Skolnick, J.3
  • 7
    • 0029996162 scopus 로고    scopus 로고
    • Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence
    • Frishman D, Argos P. Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence. Protein Eng. 9:1996;133-142.
    • (1996) Protein Eng , vol.9 , pp. 133-142
    • Frishman, D.1    Argos, P.2
  • 8
    • 0030931336 scopus 로고    scopus 로고
    • Seventy five percent accuracy in protein secondary structure prediction
    • Frishman D, Argos P. Seventy five percent accuracy in protein secondary structure prediction. Protein. 27:1997;329-335.
    • (1997) Protein , vol.27 , pp. 329-335
    • Frishman, D.1    Argos, P.2
  • 9
    • 0030628191 scopus 로고    scopus 로고
    • The future of protein secondary structure prediction accuracy
    • Frishman D, Argos P. The future of protein secondary structure prediction accuracy. Fold Des. 2:1997;159-162.
    • (1997) Fold Des , vol.2 , pp. 159-162
    • Frishman, D.1    Argos, P.2
  • 10
    • 0031585987 scopus 로고    scopus 로고
    • Protein secondary structure prediction using local alignments
    • Salomov AA, Solovyev VV. Protein secondary structure prediction using local alignments. J Mol Biol. 268:1997;31-36.
    • (1997) J Mol Biol , vol.268 , pp. 31-36
    • Salomov, A.A.1    Solovyev, V.V.2
  • 11
    • 0030777763 scopus 로고    scopus 로고
    • Exploring the limits of nearest neighbour secondary structure prediction
    • Levin JM. Exploring the limits of nearest neighbour secondary structure prediction. Protein Eng. 10:1997;771-776.
    • (1997) Protein Eng , vol.10 , pp. 771-776
    • Levin, J.M.1
  • 12
    • 0031454515 scopus 로고    scopus 로고
    • Secondary structure prediction using segment similarity
    • Rychlewski L, Godzik A. Secondary structure prediction using segment similarity. Protein Eng. 10:1997;1143-1153.
    • (1997) Protein Eng , vol.10 , pp. 1143-1153
    • Rychlewski, L.1    Godzik, A.2
  • 13
    • 0030874702 scopus 로고    scopus 로고
    • Predicting protein secondary structure with probabilistic schemata of evolutionary derived information
    • Thompson MJ, Goldstein RA. Predicting protein secondary structure with probabilistic schemata of evolutionary derived information. Protein Sci. 6:1997;1963-1975.
    • (1997) Protein Sci , vol.6 , pp. 1963-1975
    • Thompson, M.J.1    Goldstein, R.A.2
  • 14
    • 0030774720 scopus 로고    scopus 로고
    • Prediction of protein secondary structure using the 3D-1D compatibility algorithm
    • Ito M, Matsuo Y, Nishikawa K. Prediction of protein secondary structure using the 3D-1D compatibility algorithm. Comput Appl Biosci. 13:1997;473-474.
    • (1997) Comput Appl Biosci , vol.13 , pp. 473-474
    • Ito, M.1    Matsuo, Y.2    Nishikawa, K.3
  • 15
    • 0031518366 scopus 로고    scopus 로고
    • The prediction of protein secondary structure with a cascade correlation learning architecture of neural networks
    • Vivarelli F, Fariselli P, Casadio R. The prediction of protein secondary structure with a cascade correlation learning architecture of neural networks. Neural Comp Appl. 6:1997;57-62.
    • (1997) Neural Comp Appl , vol.6 , pp. 57-62
    • Vivarelli, F.1    Fariselli, P.2    Casadio, R.3
  • 16
    • 0031269127 scopus 로고    scopus 로고
    • Predicting protein secondary structure using stochastic tree grammars
    • Abe M, Mamitsuka H. Predicting protein secondary structure using stochastic tree grammars. Machine Learning. 29:1997;275-301.
    • (1997) Machine Learning , vol.29 , pp. 275-301
    • Abe, M.1    Mamitsuka, H.2
  • 17
    • 0031301753 scopus 로고    scopus 로고
    • Blind predictions of local protein structure in CASP2 targets using the I-sites library
    • Bystroff C, Baker D. Blind predictions of local protein structure in CASP2 targets using the I-sites library. Proteins. 1997;167-171.
    • (1997) Proteins , pp. 167-171
    • Bystroff, C.1    Baker, D.2
  • 18
    • 0030855217 scopus 로고    scopus 로고
    • Three dimensional structures and contexts associated with recurrent amino-acid sequence patterns
    • Han KF, Bystroff C, Baker D. Three dimensional structures and contexts associated with recurrent amino-acid sequence patterns. Protein Sci. 6:1997;1587-1590.
    • (1997) Protein Sci , vol.6 , pp. 1587-1590
    • Han, K.F.1    Bystroff, C.2    Baker, D.3
  • 19
    • 0023660653 scopus 로고
    • Prediction of protein secondary structure and active sites using the alignment of homologous sequences
    • Zvelebil MJ, Barton GJ, Taylor WR, Sternberg MJE. Prediction of protein secondary structure and active sites using the alignment of homologous sequences. J Mol Biol. 195:1987;957-961.
    • (1987) J Mol Biol , vol.195 , pp. 957-961
    • Zvelebil, M.J.1    Barton, G.J.2    Taylor, W.R.3    Sternberg, M.J.E.4
  • 20
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B, Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins. 19:1994;55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 22
    • 0031566432 scopus 로고    scopus 로고
    • Recognition of analogous and homologous protein folds: Analysis of sequence and structure conservation
    • Russell RB, Saqi M, Sayle RA, Bates PA, Sternberg MJE. Recognition of analogous and homologous protein folds: analysis of sequence and structure conservation. J Mol Biol. 269:1997.
    • (1997) J Mol Biol , vol.269
    • Russell, R.B.1    Saqi, M.2    Sayle, R.A.3    Bates, P.A.4    Sternberg, M.J.E.5
  • 23
    • 0030595366 scopus 로고    scopus 로고
    • Multiple sequence information for threading
    • Defay TR, Cohen FE. Multiple sequence information for threading. J Mol Biol. 262:1996;314-323.
    • (1996) J Mol Biol , vol.262 , pp. 314-323
    • Defay, T.R.1    Cohen, F.E.2
  • 24
    • 0031588007 scopus 로고    scopus 로고
    • Multiple sequence threading: An analysis of alignment quality and stability
    • Taylor WR. Multiple sequence threading: an analysis of alignment quality and stability. J Mol Biol. 269:1997;902-943.
    • (1997) J Mol Biol , vol.269 , pp. 902-943
    • Taylor, W.R.1
  • 25
    • 0028818340 scopus 로고
    • Protein structure prediction by threading methods
    • Lemer CM-R, Rooman MJ, Wodak SJ. Protein structure prediction by threading methods. Proteins. 23:1995;337-355.
    • (1995) Proteins , vol.23 , pp. 337-355
    • Lemer, C.M.-R.1    Rooman, M.J.2    Wodak, S.J.3
  • 26
    • 0029951995 scopus 로고    scopus 로고
    • Protein fold recognition by mapping predicted secondary structures
    • Russell RB, Copley RR, Barton GJ. Protein fold recognition by mapping predicted secondary structures. J Mol Biol. 259:1996;349-365.
    • (1996) J Mol Biol , vol.259 , pp. 349-365
    • Russell, R.B.1    Copley, R.R.2    Barton, G.J.3
  • 27
    • 0031577260 scopus 로고    scopus 로고
    • Protein fold recognition by prediction based threading
    • Rost B, Schneider R, Sander C. Protein fold recognition by prediction based threading. J Mol Biol. 270:1997;471-480.
    • (1997) J Mol Biol , vol.270 , pp. 471-480
    • Rost, B.1    Schneider, R.2    Sander, C.3
  • 28
    • 0029874551 scopus 로고    scopus 로고
    • Protein fold recognition using sequence derived predictions
    • Fischer D, Eisenberg D. Protein fold recognition using sequence derived predictions. Protein Sci. 5:1996;947-955.
    • (1996) Protein Sci , vol.5 , pp. 947-955
    • Fischer, D.1    Eisenberg, D.2
  • 29
    • 0031564630 scopus 로고    scopus 로고
    • A 3D/1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence
    • Rice DW, Eisenberg D. A 3D/1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence. J Mol Biol. 267:1997;1026-1038.
    • (1997) J Mol Biol , vol.267 , pp. 1026-1038
    • Rice, D.W.1    Eisenberg, D.2
  • 30
    • 0031588960 scopus 로고    scopus 로고
    • Protein topology recognition from secondary structure sequences
    • Di Francesco V, Garnier J, Munson PJ. Protein topology recognition from secondary structure sequences. J Mol Biol. 267:1997;446-463.
    • (1997) J Mol Biol , vol.267 , pp. 446-463
    • Di Francesco, V.1    Garnier, J.2    Munson, P.J.3
  • 32
    • 0031302793 scopus 로고    scopus 로고
    • Distant homology recognition using structural classification of proteins
    • Murzin AG, Bateman A. Distant homology recognition using structural classification of proteins. Proteins. 1997;105-112.
    • (1997) Proteins , pp. 105-112
    • Murzin, A.G.1    Bateman, A.2
  • 33
    • 0030443368 scopus 로고    scopus 로고
    • Protein fold recognition and dynamics in the space of contact maps
    • Mirny L, Domany E. Protein fold recognition and dynamics in the space of contact maps. Proteins. 26:1996;391-410.
    • (1996) Proteins , vol.26 , pp. 391-410
    • Mirny, L.1    Domany, E.2
  • 34
    • 0031557390 scopus 로고    scopus 로고
    • Factors affecting the ability of energy functions to discriminate correct from incorrect folds
    • Park BH, Huang ES, Levitt M. Factors affecting the ability of energy functions to discriminate correct from incorrect folds. J Mol Biol. 266:1997;831-846.
    • (1997) J Mol Biol , vol.266 , pp. 831-846
    • Park, B.H.1    Huang, E.S.2    Levitt, M.3
  • 35
    • 0030806961 scopus 로고    scopus 로고
    • Statistical significance of hierarchical multibody potentials based on Delauney tessellation and their application in sequence-structure alignment
    • Munson PJ, Singh RK. Statistical significance of hierarchical multibody potentials based on Delauney tessellation and their application in sequence-structure alignment. Protein Sci. 6:1997;1467-1481.
    • (1997) Protein Sci , vol.6 , pp. 1467-1481
    • Munson, P.J.1    Singh, R.K.2
  • 36
    • 0030759746 scopus 로고    scopus 로고
    • Protein sequence-structure compatibility criteria in terms of statistical hypothesis testing
    • Sunyaev S, Kuznetsov E, Rodchenkov I, Tumanyan V. Protein sequence-structure compatibility criteria in terms of statistical hypothesis testing. Protein Eng. 10:1997;635-646.
    • (1997) Protein Eng , vol.10 , pp. 635-646
    • Sunyaev, S.1    Kuznetsov, E.2    Rodchenkov, I.3    Tumanyan, V.4
  • 37
    • 0029895539 scopus 로고    scopus 로고
    • Self-consistently optimized statistical-mechanical energy functions for sequence structure alignment
    • Koretke KK, Luthyschulten Z, Wolynes PG. Self-consistently optimized statistical-mechanical energy functions for sequence structure alignment. Protein Sci. 5:1996;1043-1059.
    • (1996) Protein Sci , vol.5 , pp. 1043-1059
    • Koretke, K.K.1    Luthyschulten, Z.2    Wolynes, P.G.3
  • 38
    • 0029974002 scopus 로고    scopus 로고
    • Evaluation of threading specificity and accuracy
    • Bryant SH. Evaluation of threading specificity and accuracy. Proteins. 26:1996;167-171.
    • (1996) Proteins , vol.26 , pp. 167-171
    • Bryant, S.H.1
  • 39
    • 0030446755 scopus 로고    scopus 로고
    • A polynomial time algorithm for a class of protein threading problems
    • Xu Y, Uberbacher EC. A polynomial time algorithm for a class of protein threading problems. Comput Appl Biosci. 12:1996;511-517.
    • (1996) Comput Appl Biosci , vol.12 , pp. 511-517
    • Xu, Y.1    Uberbacher, E.C.2
  • 40
    • 0030627408 scopus 로고    scopus 로고
    • Similarities and differences between non-homologous proteins with similar folds
    • Zhang BH, Jaroszewski L, Rychlewski L, Godzik A. Similarities and differences between non-homologous proteins with similar folds. Fold Des. 2:1997;307-317.
    • (1997) Fold Des , vol.2 , pp. 307-317
    • Zhang, B.H.1    Jaroszewski, L.2    Rychlewski, L.3    Godzik, A.4
  • 41
    • 0030781040 scopus 로고    scopus 로고
    • Residue-residue mean force potentials for protien structure recognition
    • Reva BA, Finkelstein AV, Sanner MF, Olsen AJ. Residue-residue mean force potentials for protien structure recognition. Protein Eng. 10:1997;865-876.
    • (1997) Protein Eng , vol.10 , pp. 865-876
    • Reva, B.A.1    Finkelstein, A.V.2    Sanner, M.F.3    Olsen, A.J.4
  • 42
    • 0031892528 scopus 로고    scopus 로고
    • Protein fold recognition without Boltzmann statistics or explicit physical basis
    • Huber T, Torda AE. Protein fold recognition without Boltzmann statistics or explicit physical basis. Protein Sci. 7:1998;142-149.
    • (1998) Protein Sci , vol.7 , pp. 142-149
    • Huber, T.1    Torda, A.E.2
  • 43
    • 0030220165 scopus 로고    scopus 로고
    • The current state of the art in protein structure prediction
    • Moult J. The current state of the art in protein structure prediction. Curr Opin Biotechnol. 7:1996;422-427.
    • (1996) Curr Opin Biotechnol , vol.7 , pp. 422-427
    • Moult, J.1
  • 44
    • 0030908273 scopus 로고    scopus 로고
    • Advances in comparative protein modelling
    • Sanchez R, Sali A. Advances in comparative protein modelling. Curr Opin Struct Biol. 7:1997;206-214.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 206-214
    • Sanchez, R.1    Sali, A.2
  • 46
    • 0000064343 scopus 로고
    • Protein model building using structral homology
    • Lee RH. Protein model building using structral homology. Nature. 356:1992;543-544.
    • (1992) Nature , vol.356 , pp. 543-544
    • Lee, R.H.1
  • 47
    • 0026320025 scopus 로고
    • Comparative modelling of homologous proteins
    • Greer J. Comparative modelling of homologous proteins. Methods Enzymol. 202:1992;239-252.
    • (1992) Methods Enzymol , vol.202 , pp. 239-252
    • Greer, J.1
  • 48
    • 0029004590 scopus 로고
    • Protein modelling by E-mail
    • Peitsch MC. Protein modelling by E-mail. Bio/Technology. 13:1995;658-660.
    • (1995) Bio/Technology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 49
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling
    • Peitsch MC. ProMod and Swiss-Model: internet-based tools for automated comparative protein modelling. Biochem Soc Trans. 24:1996;279-660.
    • (1996) Biochem Soc Trans , vol.24 , pp. 279-660
    • Peitsch, M.C.1
  • 50
    • 0030449155 scopus 로고    scopus 로고
    • Conformational analysis and clustering of short and medium sized loops connecting regular secondary structures: A database for modelling and prediction
    • Donate LE, Rufino SD, Canard LHJ, Blundell T. Conformational analysis and clustering of short and medium sized loops connecting regular secondary structures: a database for modelling and prediction. Protein Sci. 5:1996;2600-2616.
    • (1996) Protein Sci , vol.5 , pp. 2600-2616
    • Donate, L.E.1    Rufino, S.D.2    Canard, L.H.J.3    Blundell, T.4
  • 52
    • 0031588926 scopus 로고    scopus 로고
    • Predicting the conformational class of short and medium sized loops connecting regular secondary structures: Application to comparative modelling
    • Rufino SD, Donate LE, Canard LHC, Blundell T. Predicting the conformational class of short and medium sized loops connecting regular secondary structures: application to comparative modelling. J Mol Biol. 267:1997;352-367.
    • (1997) J Mol Biol , vol.267 , pp. 352-367
    • Rufino, S.D.1    Donate, L.E.2    Canard, L.H.C.3    Blundell, T.4
  • 53
    • 0031564640 scopus 로고    scopus 로고
    • PDB-based protein loop prediction: Parameters for selection and methods for optimization
    • van Vlijman HWT, Karplus M. PDB-based protein loop prediction: parameters for selection and methods for optimization. J Mol Biol. 267:1997;975-1001.
    • (1997) J Mol Biol , vol.267 , pp. 975-1001
    • Van Vlijman, H.W.T.1    Karplus, M.2
  • 54
    • 0030589039 scopus 로고    scopus 로고
    • Structural families in loops of homologous proteins: Automatic modelling and application to antibodies
    • Martin ACR, Thornton JM. Structural families in loops of homologous proteins: automatic modelling and application to antibodies. J Mol Biol. 263:1996;800-815.
    • (1996) J Mol Biol , vol.263 , pp. 800-815
    • Martin, A.C.R.1    Thornton, J.M.2
  • 55
    • 0030767954 scopus 로고    scopus 로고
    • Creation and characterization of a new, non-redundant fragment databank
    • Lessel U, Schomburg D. Creation and characterization of a new, non-redundant fragment databank. Protein Eng. 10:1997;659-664.
    • (1997) Protein Eng , vol.10 , pp. 659-664
    • Lessel, U.1    Schomburg, D.2
  • 56
    • 0030623575 scopus 로고    scopus 로고
    • All in one: A highly detailed rotamer library improves both accuracy and speed in the modelling of sidechains by dead-end-elimination
    • De Maeyer M, Desmet J, Lasters I. All in one: a highly detailed rotamer library improves both accuracy and speed in the modelling of sidechains by dead-end-elimination. Fold Des. 2:1997;53-56.
    • (1997) Fold Des , vol.2 , pp. 53-56
    • De Maeyer, M.1    Desmet, J.2    Lasters, I.3
  • 57
    • 0031576989 scopus 로고    scopus 로고
    • Prediction of protein side chain rotamers from a backbone-dependent rotamer library: A new homology modelling tool
    • Bower MJ, Cohen FE, Dunbrack RL Jr. Prediction of protein side chain rotamers from a backbone-dependent rotamer library: a new homology modelling tool. J Mol Biol. 267:1997;1268-1282.
    • (1997) J Mol Biol , vol.267 , pp. 1268-1282
    • Bower, M.J.1    Cohen, F.E.2    Dunbrack R.L., Jr.3
  • 58
    • 1842326139 scopus 로고    scopus 로고
    • Bayesian statistical analysis of protein side-chain rotamer preferences
    • Dunbrack RL Jr, Cohen FE. Bayesian statistical analysis of protein side-chain rotamer preferences. Protein Sci. 6:1997;1661-1681.
    • (1997) Protein Sci , vol.6 , pp. 1661-1681
    • Dunbrack R.L., Jr.1    Cohen, F.E.2
  • 59
    • 0030955505 scopus 로고    scopus 로고
    • Prediction of protein side-chain conformations by principal component analysis for fixed main chain atoms
    • Ogata K, Umeyama H. Prediction of protein side-chain conformations by principal component analysis for fixed main chain atoms. Protein Eng. 10:1997;353-359.
    • (1997) Protein Eng , vol.10 , pp. 353-359
    • Ogata, K.1    Umeyama, H.2
  • 60
    • 0142140800 scopus 로고    scopus 로고
    • Prediction of protein side chain conformations: A study on the influence of backbone accuracy on conformation stability in the rotamer space
    • Tuffery P, Etchebest C, Hazout S. Prediction of protein side chain conformations: a study on the influence of backbone accuracy on conformation stability in the rotamer space. Protein Eng. 10:1997;361-372.
    • (1997) Protein Eng , vol.10 , pp. 361-372
    • Tuffery, P.1    Etchebest, C.2    Hazout, S.3
  • 61
    • 0030310218 scopus 로고    scopus 로고
    • How similar must a template protein be for homology modelling by side-chain packing methods
    • L. Hunter, Klein T.E. Hawaii, USA: World Scientific
    • Chung SY, Subbiah S. How similar must a template protein be for homology modelling by side-chain packing methods. Hunter L, Klein TE. Pacific Symposium on Biocomputing. 1996;126-141 World Scientific, Hawaii, USA.
    • (1996) Pacific Symposium on Biocomputing , pp. 126-141
    • Chung, S.Y.1    Subbiah, S.2
  • 62
    • 0031303336 scopus 로고    scopus 로고
    • Protein modelling by multiple sequence threading and distance geometry
    • Aszodi A, Munro REJ, Taylor WR. Protein modelling by multiple sequence threading and distance geometry. Proteins. 1997;38-42.
    • (1997) Proteins , pp. 38-42
    • Aszodi, A.1    Munro, R.E.J.2    Taylor, W.R.3
  • 63
    • 0030322828 scopus 로고    scopus 로고
    • Homology modelling by distance geometry
    • Aszodi A, Taylor WR. Homology modelling by distance geometry. Fold Des. 1:1996;325-334.
    • (1996) Fold Des , vol.1 , pp. 325-334
    • Aszodi, A.1    Taylor, W.R.2
  • 64
    • 0030623726 scopus 로고    scopus 로고
    • Distance geometry based comparative modelling
    • Aszodi A, Munro REJ, Taylor WR. Distance geometry based comparative modelling. Fold Des. 2:1997;S3-S6.
    • (1997) Fold Des , vol.2
    • Aszodi, A.1    Munro, R.E.J.2    Taylor, W.R.3
  • 65
    • 0030956593 scopus 로고    scopus 로고
    • Homology modelling using simulated annealing of restrained molecular dynamics and conformational search calculations with CONGEN: Application in predicting the three-dimensional structure of murine homeodomain Msx-1
    • Li H, Tejero R, Monleon D, Bassolino-Klimas D, Abate-Shen C, Bruccoleri RE, Montelione GT. Homology modelling using simulated annealing of restrained molecular dynamics and conformational search calculations with CONGEN: application in predicting the three-dimensional structure of murine homeodomain Msx-1. Protein Sci. 6:1997;956-970.
    • (1997) Protein Sci , vol.6 , pp. 956-970
    • Li, H.1    Tejero, R.2    Monleon, D.3    Bassolino-Klimas, D.4    Abate-Shen, C.5    Bruccoleri, R.E.6    Montelione, G.T.7
  • 66
    • 0031915862 scopus 로고    scopus 로고
    • Alignment algorithm for homology modelling and threading
    • Alexandrov NN, Luethy R. Alignment algorithm for homology modelling and threading. Protein Sci. 7:1998;254-258.
    • (1998) Protein Sci , vol.7 , pp. 254-258
    • Alexandrov, N.N.1    Luethy, R.2
  • 67
    • 0031560777 scopus 로고    scopus 로고
    • Contact area difference (CAD): A robust measure to evaluate accuracy of protein models
    • Abagyan RA, Totrov MM. Contact area difference (CAD): a robust measure to evaluate accuracy of protein models. J Mol Biol. 268:1997;678-685.
    • (1997) J Mol Biol , vol.268 , pp. 678-685
    • Abagyan, R.A.1    Totrov, M.M.2
  • 68
    • 0032521218 scopus 로고    scopus 로고
    • Marrying structure and genomics
    • Rost B. Marrying structure and genomics. Structure. 6:1998;259-263.
    • (1998) Structure , vol.6 , pp. 259-263
    • Rost, B.1
  • 69
    • 0032521199 scopus 로고    scopus 로고
    • The Argonne structural genomics workshop: Lamaze class for the birth of a new science
    • Shapiro L, Lima CD. The Argonne structural genomics workshop: Lamaze class for the birth of a new science. Structure. 6:1998;265-267.
    • (1998) Structure , vol.6 , pp. 265-267
    • Shapiro, L.1    Lima, C.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.