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Volumn 7, Issue , 2007, Pages

Prediction of flexible/rigid regions from protein sequences using k-spaced amino acid pairs

Author keywords

[No Author keywords available]

Indexed keywords

ACCURACY; AMINO ACID SEQUENCE; ARTICLE; BAYESIAN LEARNING; CONFORMATIONAL TRANSITION; LOGISTIC REGRESSION ANALYSIS; MACHINE LEARNING; PREDICTION; PROTEIN FOLDING; PROTEIN STRUCTURE; SENSITIVITY ANALYSIS; SUPPORT VECTOR MACHINE; THREE DIMENSIONAL IMAGING; BAYES THEOREM; CHEMISTRY; PHYSIOLOGY; PROTEIN CONFORMATION;

EID: 34249699005     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-7-25     Document Type: Article
Times cited : (119)

References (57)
  • 1
    • 0037453258 scopus 로고    scopus 로고
    • Structural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin
    • 2003 Apr 18. 10.1016/S0022-2836(03)00271-7. 12684008
    • Structural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin. KL Yap T Yuan TK Mal HJ Vogel M Ikura, J Mol Biol 328 193 204 2003 Apr 18 10.1016/S0022-2836(03)00271-7 12684008
    • J Mol Biol , vol.328 , pp. 193-204
    • Yap, K.L.1    Yuan, T.2    Mal, T.K.3    Vogel, H.J.4    Ikura, M.5
  • 2
    • 0035953757 scopus 로고    scopus 로고
    • Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin
    • 10.1038/35074145. 11323678
    • Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin. MA Schumacher AF Rivard HP Bachinger JP Adelman, Nature 2001 410 1120 1124 10.1038/35074145 11323678
    • (2001) Nature , vol.410 , pp. 1120-1124
    • Schumacher, M.A.1    Rivard, A.F.2    Bachinger, H.P.3    Adelman, J.P.4
  • 3
    • 33744459734 scopus 로고    scopus 로고
    • Prediction of three dimensional structure of calmodulin
    • 10.1007/s10930-006-0011-7. 16721661
    • Prediction of three dimensional structure of calmodulin. K Chen J Ruan LA Kurgan, Protein J 2006 25 57 70 10.1007/s10930-006-0011-7 16721661
    • (2006) Protein J , vol.25 , pp. 57-70
    • Chen, K.1    Ruan, J.2    Kurgan, L.A.3
  • 4
    • 30444436194 scopus 로고    scopus 로고
    • Vps9 domain-containing proteins: Activators of Rab5 GTPases from yeast to neurons
    • 10.1016/j.tcb.2005.11.001. 16330212
    • Vps9 domain-containing proteins: activators of Rab5 GTPases from yeast to neurons. DS Carney BA Davies BF Horazdovsky, Trends Cell Biol 2006 16 27 35 10.1016/j.tcb.2005.11.001 16330212
    • (2006) Trends Cell Biol , vol.16 , pp. 27-35
    • Carney, D.S.1    Davies, B.A.2    Horazdovsky, B.F.3
  • 5
    • 0037452545 scopus 로고    scopus 로고
    • A conformational trigger for activation of a G protein by a G protein-coupled receptor
    • 2003 Feb 18. 10.1021/bi0270539. 12578347
    • A conformational trigger for activation of a G protein by a G protein-coupled receptor. PL Yeagle AD Albert, Biochemistry 42 1365 8 2003 Feb 18 10.1021/bi0270539 12578347
    • Biochemistry , vol.42 , pp. 1365-8
    • Yeagle, P.L.1    Albert, A.D.2
  • 6
    • 30844455998 scopus 로고    scopus 로고
    • Walking with myosin V
    • 10.1016/j.ceb.2005.12.014. 16378722
    • Walking with myosin V. JR Sellers C Veigel, Curr Opin Cell Biol 2006 18 68 73 10.1016/j.ceb.2005.12.014 16378722
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 68-73
    • Sellers, J.R.1    Veigel, C.2
  • 7
    • 21544444439 scopus 로고    scopus 로고
    • Molecular mechanism of actomyosin-based motility
    • 10.1007/s00018-005-5015-5. 15924264
    • Molecular mechanism of actomyosin-based motility. MA Geeves R Fedorov DJ Manstein, Cell Mol Life Sci 2005 62 1462 77 10.1007/s00018-005-5015-5 15924264
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1462-77
    • Geeves, M.A.1    Fedorov, R.2    Manstein, D.J.3
  • 8
    • 33745889935 scopus 로고    scopus 로고
    • Nucleoside transporters: From scavengers to novel therapeutic targets
    • 10.1016/j.tips.2006.06.004. 16820221
    • Nucleoside transporters: from scavengers to novel therapeutic targets. AE King MA Ackley CE Cass JD Young SA Baldwin, Trends Pharmacol Sci 2006 27 416 25 10.1016/j.tips.2006.06.004 16820221
    • (2006) Trends Pharmacol Sci , vol.27 , pp. 416-25
    • King, A.E.1    Ackley, M.A.2    Cass, C.E.3    Young, J.D.4    Baldwin, S.A.5
  • 9
    • 33646899303 scopus 로고    scopus 로고
    • Sorting out Toll signals
    • 2006 Jun 2. 10.1016/j.cell.2006.05.014. 16751092
    • Sorting out Toll signals. KA Fitzgerald ZJ Chen, Cell 125 834 6 2006 Jun 2 10.1016/j.cell.2006.05.014 16751092
    • Cell , vol.125 , pp. 834-6
    • Fitzgerald, K.A.1    Chen, Z.J.2
  • 10
    • 33646761687 scopus 로고    scopus 로고
    • Structural basis for diversity of the EF-hand calcium-binding proteins
    • 2006 Jun 9. 10.1016/j.jmb.2006.03.066. 16678204
    • Structural basis for diversity of the EF-hand calcium-binding proteins. Z Grabarek, J Mol Biol 359 509 25 2006 Jun 9 10.1016/j.jmb.2006.03.066 16678204
    • J Mol Biol , vol.359 , pp. 509-25
    • Grabarek, Z.1
  • 11
    • 33646482468 scopus 로고    scopus 로고
    • Karyopherin flexibility in nucleocytoplasmic transport
    • 10.1016/j.sbi.2006.03.010. 16567089
    • Karyopherin flexibility in nucleocytoplasmic transport. E Conti CW Muller M Stewart, Curr Opin Struct Biol 2006 16 237 44 10.1016/j.sbi.2006.03.010 16567089
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 237-44
    • Conti, E.1    Muller, C.W.2    Stewart, M.3
  • 12
    • 33749661703 scopus 로고    scopus 로고
    • Quantitative Analysis of the Conservation of the Tertiary Structure of Protein Segments
    • 10.1007/s10930-006-9016-5. 16957991
    • Quantitative Analysis of the Conservation of the Tertiary Structure of Protein Segments. J Ruan K Chen J Tuszynski L Kurgan, Protein J 2006 25 5 301 15 10.1007/s10930-006-9016-5 16957991
    • (2006) Protein J , vol.25 , Issue.5 , pp. 301-15
    • Ruan, J.1    Chen, K.2    Tuszynski, J.3    Kurgan, L.4
  • 13
    • 33645036616 scopus 로고    scopus 로고
    • The GYF domain
    • 10.1111/j.1742-4658.2005.05078.x. 16403013
    • The GYF domain. MM Kofler C Freund, FEBS J 2006 273 245 56 10.1111/j.1742-4658.2005.05078.x 16403013
    • (2006) FEBS J , vol.273 , pp. 245-56
    • Kofler, M.M.1    Freund, C.2
  • 14
    • 33745941344 scopus 로고    scopus 로고
    • How flexible is alpha-actinin's rod domain?
    • 16783925
    • How flexible is alpha-actinin's rod domain? MH Zaman MR Kaazempur-Mofrad, Mech Chem Biosyst 2004 1 291 302 16783925
    • (2004) Mech Chem Biosyst , vol.1 , pp. 291-302
    • Zaman, M.H.1    Kaazempur-Mofrad, M.R.2
  • 15
    • 33645318436 scopus 로고    scopus 로고
    • The carboxyl-terminal linker is important for chemoreceptor function
    • 10.1111/j.1365-2958.2006.05108.x. 16573695
    • The carboxyl-terminal linker is important for chemoreceptor function. M Li GL Hazelbauer, Mol Microbiol 2006 60 469 79 10.1111/j.1365-2958.2006.05108.x 16573695
    • (2006) Mol Microbiol , vol.60 , pp. 469-79
    • Li, M.1    Hazelbauer, G.L.2
  • 16
    • 0036280693 scopus 로고    scopus 로고
    • Protein and peptide folding explored with molecular simulations
    • 10.1021/ar0100172. 12069630
    • Protein and peptide folding explored with molecular simulations. CL Brooks 3rd, Acc Chem Res 2002 35 447 54 10.1021/ar0100172 12069630
    • (2002) Acc Chem Res , vol.35 , pp. 447-54
    • Brooks III, C.L.1
  • 17
    • 0242267532 scopus 로고    scopus 로고
    • Unfolding of the cold shock protein studied with biased molecular dynamics
    • 2003 Nov 15. 10.1002/prot.10344. 14579351
    • Unfolding of the cold shock protein studied with biased molecular dynamics. G Morra M Hodoscek EW Knapp, Proteins 53 597 606 2003 Nov 15 10.1002/prot.10344 14579351
    • Proteins , vol.53 , pp. 597-606
    • Morra, G.1    Hodoscek, M.2    Knapp, E.W.3
  • 18
    • 33748448474 scopus 로고    scopus 로고
    • A model of local-minima distribution on conformational space and its application to protein structure prediction
    • 2006 Sep 1. 10.1002/prot.21084. 16838344
    • A model of local-minima distribution on conformational space and its application to protein structure prediction. H Li, Proteins 64 985 91 2006 Sep 1 10.1002/prot.21084 16838344
    • Proteins , vol.64 , pp. 985-91
    • Li, H.1
  • 19
    • 0035189024 scopus 로고    scopus 로고
    • Modeling the third loop of short-chain snake venom neurotoxins: Roles of the short-range and long-range interactions
    • 2001 Jan 1. 10.1002/1097-0134(20010101)42:1<6::AID-PROT20>3.0.CO;2- 7. 11093256
    • Modeling the third loop of short-chain snake venom neurotoxins: roles of the short-range and long-range interactions. Z Liu W Li H Zhang Y Han L Lai, Proteins 42 6 16 2001 Jan 1 10.1002/1097-0134(20010101)42:1<6::AID- PROT20>3.0.CO;2-7 11093256
    • Proteins , vol.42 , pp. 6-16
    • Liu, Z.1    Li, W.2    Zhang, H.3    Han, Y.4    Lai, L.5
  • 20
    • 30344442775 scopus 로고    scopus 로고
    • Evaluation of domain prediction in CASP6
    • 10.1002/prot.20736. 16187361
    • Evaluation of domain prediction in CASP6. CH Tai WJ Lee JJ Vincent B Lee, Proteins 2005 61 suppl 7 183 92 10.1002/prot.20736 16187361
    • (2005) Proteins , vol.61 , Issue.7 SUPPL. , pp. 183-92
    • Tai, C.H.1    Lee, W.J.2    Vincent, J.J.3    Lee, B.4
  • 21
    • 0032932375 scopus 로고    scopus 로고
    • A potential smoothing algorithm accurately predicts transmembrane helix packing
    • 10.1038/5891. 9886292
    • A potential smoothing algorithm accurately predicts transmembrane helix packing. RV Pappu GR Marshall JW Ponder, Nat Struct Biol 1999 6 50 5 10.1038/5891 9886292
    • (1999) Nat Struct Biol , vol.6 , pp. 50-5
    • Pappu, R.V.1    Marshall, G.R.2    Ponder, J.W.3
  • 22
    • 0015859467 scopus 로고    scopus 로고
    • Principles that govern the folding of protein chains
    • 1973 Jul 20. 10.1126/science.181.4096.223. 4124164
    • Principles that govern the folding of protein chains. CB Anfinsen, Science 181 223 30 1973 Jul 20 10.1126/science.181.4096.223 4124164
    • Science , vol.181 , pp. 223-30
    • Anfinsen, C.B.1
  • 23
    • 0035314042 scopus 로고    scopus 로고
    • Improving the performance of Rosetta using multiple sequence alignment information and global measures of hydrophobic core formation
    • 2001 Apr 1. 10.1002/1097-0134(20010401)43:1<1::AID-PROT1012>3.0. CO;2-A. 11170209
    • Improving the performance of Rosetta using multiple sequence alignment information and global measures of hydrophobic core formation. R Bonneau CE Strauss D Baker, Proteins 43 1 11 2001 Apr 1 10.1002/1097-0134(20010401)43: 1<1::AID-PROT1012>3.0.CO;2-A 11170209
    • Proteins , vol.43 , pp. 1-11
    • Bonneau, R.1    Strauss, C.E.2    Baker, D.3
  • 24
    • 0023758305 scopus 로고    scopus 로고
    • NMR evidence for an early framework intermediate on the folding pathway of ribonuclease a
    • 1988 Oct 20. 10.1038/335694a0. 2845278
    • NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. JB Udgaonkar RL Baldwin, Nature 335 694 9 1988 Oct 20 10.1038/335694a0 2845278
    • Nature , vol.335 , pp. 694-9
    • Udgaonkar, J.B.1    Baldwin, R.L.2
  • 25
    • 0028944346 scopus 로고    scopus 로고
    • Is burst hydrophobic collapse necessary for protein folding?
    • 1995 Mar 7. 10.1021/bi00009a038. 7893719
    • Is burst hydrophobic collapse necessary for protein folding? AM Gutin VI Abkevich EI Shakhnovich, Biochemistry 34 3066 76 1995 Mar 7 10.1021/bi00009a038 7893719
    • Biochemistry , vol.34 , pp. 3066-76
    • Gutin, A.M.1    Abkevich, V.I.2    Shakhnovich, E.I.3
  • 26
    • 33746102627 scopus 로고    scopus 로고
    • Atom-by-atom analysis of global downhill protein folding
    • 2006 Jul 20. 10.1038/nature04859. 16799571
    • Atom-by-atom analysis of global downhill protein folding. M Sadqi D Fushman V Munoz, Nature 442 317 21 2006 Jul 20 10.1038/nature04859 16799571
    • Nature , vol.442 , pp. 317-21
    • Sadqi, M.1    Fushman, D.2    Munoz, V.3
  • 27
    • 0346753468 scopus 로고    scopus 로고
    • Tools and databases to analyze protein flexibility; Approaches to mapping implied features onto sequences
    • 14696388
    • Tools and databases to analyze protein flexibility; approaches to mapping implied features onto sequences. WG Krebs J Tsai V Alexandrov J Junker J Jansen M Gerstein, Methods Enzymol 2003 374 544 84 14696388
    • (2003) Methods Enzymol , vol.374 , pp. 544-84
    • Krebs, W.G.1    Tsai, J.2    Alexandrov, V.3    Junker, J.4    Jansen, J.5    Gerstein, M.6
  • 28
    • 0032530836 scopus 로고    scopus 로고
    • A database of macromolecular motions
    • 1998 Sep 15. 9722650. 10.1093/nar/26.18.4280
    • A database of macromolecular motions. M Gerstein W Krebs, Nucleic Acids Res 26 18 4280 90 1998 Sep 15 9722650 10.1093/nar/26.18.4280
    • Nucleic Acids Res , vol.26 , Issue.18 , pp. 4280-90
    • Gerstein, M.1    Krebs, W.2
  • 29
    • 33747816204 scopus 로고    scopus 로고
    • Identifying sequence regions undergoing conformational change via predicted continuum secondary structure
    • 2006 Aug 1. 10.1093/bioinformatics/btl198. 16720586
    • Identifying sequence regions undergoing conformational change via predicted continuum secondary structure. M Boden TL Bailey, Bioinformatics 22 15 1809 14 2006 Aug 1 10.1093/bioinformatics/btl198 16720586
    • Bioinformatics , vol.22 , Issue.15 , pp. 1809-14
    • Boden, M.1    Bailey, T.L.2
  • 30
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • 2005 Aug 15
    • IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Z Dosztanyi V Csizmok P Tompa I Simon, Bioinformatics 16 3433 4 2005 Aug 15
    • Bioinformatics , vol.16 , pp. 3433-4
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 31
    • 33746630984 scopus 로고    scopus 로고
    • Wiggle-predicting functionally flexible regions from primary sequence
    • 16839194. 10.1371/journal.pcbi.0020090
    • Wiggle-predicting functionally flexible regions from primary sequence. J Gu M Gribskov PE Bourne, PLoS Comput Biol 2006 2 7 e90 16839194 10.1371/journal.pcbi.0020090
    • (2006) PLoS Comput Biol , vol.2 , Issue.7 , pp. 90
    • Gu, J.1    Gribskov, M.2    Bourne, P.E.3
  • 34
    • 0000545946 scopus 로고    scopus 로고
    • Improvements to Platt's SMO Algorithm for SVM Classifier Design
    • 10.1162/089976601300014493
    • Improvements to Platt's SMO Algorithm for SVM Classifier Design. SS Keerthi SK Shevade C Bhattacharyya RK K, Neural Computation 2001 13 637 649 10.1162/089976601300014493
    • (2001) Neural Computation , vol.13 , pp. 637-649
    • Keerthi, S.S.1    Shevade, S.K.2    Bhattacharyya, C.3    Murphy, K.K.R.4
  • 35
    • 33644655386 scopus 로고    scopus 로고
    • Prediction of protein continuum secondary structure with probabilistic models based on NMR solved structures
    • 16478545. 10.1186/1471-2105-7-68
    • Prediction of protein continuum secondary structure with probabilistic models based on NMR solved structures. M Boden Z Yuan L Bailey, BMC Bioinformatics 2006 7 68 16478545 10.1186/1471-2105-7-68
    • (2006) BMC Bioinformatics , vol.7 , pp. 68
    • Boden, M.1    Yuan, Z.2    Bailey, L.3
  • 38
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • 10.1002/1097-0134(20001115)41:3<415::AID-PROT130>3.0.CO;2-7. 11025552
    • Why are "natively unfolded" proteins unstructured under physiologic conditions? VN Uversky JR Gillespie AL Fink, Proteins 2000 41 415 427 10.1002/1097-0134(20001115)41:3<415::AID-PROT130>3.0.CO;2-7 11025552
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 39
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity-linking function and disorder
    • 10.1038/nbt0901-805. 11533628
    • The protein trinity-linking function and disorder. AK Dunker Z Obradovic, Nat Biotechnol 2001 19 805 6 10.1038/nbt0901-805 11533628
    • (2001) Nat Biotechnol , vol.19 , pp. 805-6
    • Dunker, A.K.1    Obradovic, Z.2
  • 41
    • 0041620131 scopus 로고    scopus 로고
    • NORSp: Predictions of long regions without regular secondary structure
    • 2003 Jul 1. 12824431. 10.1093/nar/gkg515
    • NORSp: Predictions of long regions without regular secondary structure. J Liu B Rost, Nucleic Acids Res 31 3833 5 2003 Jul 1 12824431 10.1093/nar/gkg515
    • Nucleic Acids Res , vol.31 , pp. 3833-5
    • Liu, J.1    Rost, B.2
  • 42
    • 24344503079 scopus 로고    scopus 로고
    • Protein flexibility and rigidity predicted from sequence
    • 2005 Oct 1. 10.1002/prot.20587. 16080156
    • Protein flexibility and rigidity predicted from sequence. A Schlessinger B Rost, Proteins 61 115 26 2005 Oct 1 10.1002/prot.20587 16080156
    • Proteins , vol.61 , pp. 115-26
    • Schlessinger, A.1    Rost, B.2
  • 43
    • 1842450688 scopus 로고    scopus 로고
    • FlexProt: Alignment of flexible protein structures without a predefinition of hinge regions
    • 10.1089/106652704773416902. 15072690
    • FlexProt: alignment of flexible protein structures without a predefinition of hinge regions. M Shatsky R Nussinov HJ Wolfson, J Comput Biol 2004 11 1 83 106 10.1089/106652704773416902 15072690
    • (2004) J Comput Biol , vol.11 , Issue.1 , pp. 83-106
    • Shatsky, M.1    Nussinov, R.2    Wolfson, H.J.3
  • 44
    • 3242887315 scopus 로고    scopus 로고
    • FATCAT: A web server for flexible structure comparison and structure similarity searching
    • 15215455. 10.1093/nar/gkh430
    • FATCAT: a web server for flexible structure comparison and structure similarity searching. Y Ye A Godzik, Nucleic Acids Res 2004 32 Web Server W582 5 15215455 10.1093/nar/gkh430
    • (2004) Nucleic Acids Res , Issue.32 WEB SERVER , pp. 582-5
    • Ye, Y.1    Godzik, A.2
  • 45
    • 0032728082 scopus 로고    scopus 로고
    • Fast detection of common geometric substructure in proteins
    • 10.1089/106652799318292. 10582569
    • Fast detection of common geometric substructure in proteins. LP Chew D Huttenlocher K Kedem J Kleinberg, J Comput Biol 1999 6 313 25 10.1089/106652799318292 10582569
    • (1999) J Comput Biol , vol.6 , pp. 313-25
    • Chew, L.P.1    Huttenlocher, D.2    Kedem, K.3    Kleinberg, J.4
  • 46
    • 0000521473 scopus 로고
    • Ridge Estimators in Logistic Regression
    • 10.2307/2347628
    • Ridge Estimators in Logistic Regression. CS Le JC Houwelingen, Applied Statistics 1992 41 191 201 10.2307/2347628
    • (1992) Applied Statistics , vol.41 , pp. 191-201
    • Le, C.S.1    Houwelingen, J.C.2
  • 47
    • 33750475941 scopus 로고    scopus 로고
    • Using pseudo-amino acid composition and support vector machine to predict protein structural class
    • 10.1016/j.jtbi.2006.06.025. 16908032
    • Using pseudo-amino acid composition and support vector machine to predict protein structural class. C Chen YX Tian XY Zou PX Cai JY Mo, J Theor Biol 2006 243 3 444 8 10.1016/j.jtbi.2006.06.025 16908032
    • (2006) J Theor Biol , vol.243 , Issue.3 , pp. 444-8
    • Chen, C.1    Tian, Y.X.2    Zou, X.Y.3    Cai, P.X.4    Mo, J.Y.5
  • 48
    • 27644490770 scopus 로고    scopus 로고
    • Better prediction of protein contact number using a support vector regression analysis of amino acid sequence
    • 2005 Oct 13. 16221309. 10.1186/1471-2105-6-248
    • Better prediction of protein contact number using a support vector regression analysis of amino acid sequence. Z Yuan, BMC Bioinformatics 6 248 2005 Oct 13 16221309 10.1186/1471-2105-6-248
    • BMC Bioinformatics , vol.6 , pp. 248
    • Yuan, Z.1
  • 49
    • 33747182577 scopus 로고    scopus 로고
    • Classifier ensembles for protein structural class prediction with varying homology
    • 2006 Sep 29. 10.1016/j.bbrc.2006.07.141. 16904630
    • Classifier ensembles for protein structural class prediction with varying homology. KD Kedarisetti L Kurgan S Dick, Biochem Biophys Res Commun 348 981 8 2006 Sep 29 10.1016/j.bbrc.2006.07.141 16904630
    • Biochem Biophys Res Commun , vol.348 , pp. 981-8
    • Kedarisetti, K.D.1    Kurgan, L.2    Dick, S.3
  • 50
    • 33947372576 scopus 로고    scopus 로고
    • PepDist: A new framework for protein-peptide binding prediction based on learning peptide distance functions
    • 2006 Mar 20
    • PepDist: a new framework for protein-peptide binding prediction based on learning peptide distance functions. T Hertz C Yanover, BMC Bioinformatics Suppl 1 S3 2006 Mar 20
    • BMC Bioinformatics , Issue.1 SUPPL. , pp. 3
    • Hertz, T.1    Yanover, C.2
  • 51
    • 33646195908 scopus 로고    scopus 로고
    • Prediction of cis/trans isomerization in proteins using PSI-BLAST profiles and secondary structure information
    • 2006 Mar 9. 16526956. 10.1186/1471-2105-7-124
    • Prediction of cis/trans isomerization in proteins using PSI-BLAST profiles and secondary structure information. J Song K Burrage Z Yuan T Huber, BMC Bioinformatics 7 124 2006 Mar 9 16526956 10.1186/1471-2105-7-124
    • BMC Bioinformatics , vol.7 , pp. 124
    • Song, J.1    Burrage, K.2    Yuan, Z.3    Huber, T.4
  • 53
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • 10.1006/jmbi.1999.3091. 10493868
    • Protein secondary structure prediction based on position-specific scoring matrices. DT Jones, Journal of Molecular Biology 1999 292 195 202 10.1006/jmbi.1999.3091 10493868
    • (1999) Journal of Molecular Biology , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 56
    • 0025725905 scopus 로고
    • Instance-based learning algorithms
    • Instance-based learning algorithms. D Aha D Kibler, Machine Learning 1991 6 37 66
    • (1991) Machine Learning , vol.6 , pp. 37-66
    • Aha, D.1    Kibler, D.2


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