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Volumn 13, Issue 1, 2012, Pages

The MULTICOM toolbox for protein structure prediction

Author keywords

Bioinformatics tool; Contact map; Domain; Fold recognition; Protein disorder; Protein model quality assessment; Protein structure prediction; Secondary structure; Solvent accessibility; Tertiary structure

Indexed keywords

BIOINFORMATICS TOOLS; CONTACT MAPS; DOMAIN; FOLD RECOGNITION; PROTEIN MODELS; PROTEIN STRUCTURE PREDICTION; SECONDARY STRUCTURES; SOLVENT ACCESSIBILITY; TERTIARY STRUCTURES;

EID: 84862182129     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-13-65     Document Type: Article
Times cited : (28)

References (118)
  • 1
    • 36949091243 scopus 로고
    • Structure of myoglobin: a three-dimensional Fourier synthesis at 2å resolution
    • 10.1038/185422a0, 18990802
    • Kendrew J, Dickerson R, Strandberg B, Hart R, Davies D, Phillips D, Shore V. Structure of myoglobin: a three-dimensional Fourier synthesis at 2å resolution. Nature 1960, 185(4711):422-427. 10.1038/185422a0, 18990802.
    • (1960) Nature , vol.185 , Issue.4711 , pp. 422-427
    • Kendrew, J.1    Dickerson, R.2    Strandberg, B.3    Hart, R.4    Davies, D.5    Phillips, D.6    Shore, V.7
  • 2
    • 36949066642 scopus 로고
    • Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5å resolution, obtained by X-ray analysis
    • 10.1038/185416a0, 18990801
    • Perutz M, Rossmann M, Cullis A, Muirhead H, Will G, North A. Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5å resolution, obtained by X-ray analysis. Nature 1960, 185(4711):416-422. 10.1038/185416a0, 18990801.
    • (1960) Nature , vol.185 , Issue.4711 , pp. 416-422
    • Perutz, M.1    Rossmann, M.2    Cullis, A.3    Muirhead, H.4    Will, G.5    North, A.6
  • 3
    • 38749108825 scopus 로고    scopus 로고
    • Structural genomics: from genes to structures with valuable materials and many questions in between
    • 10.1038/nmeth0208-129, 18235432
    • Fox BG, Goulding C, Malkowski MG, Stewart L, Deacon A. Structural genomics: from genes to structures with valuable materials and many questions in between. Nat Methods 2008, 5(2):129-132. 10.1038/nmeth0208-129, 18235432.
    • (2008) Nat Methods , vol.5 , Issue.2 , pp. 129-132
    • Fox, B.G.1    Goulding, C.2    Malkowski, M.G.3    Stewart, L.4    Deacon, A.5
  • 5
    • 17444397116 scopus 로고    scopus 로고
    • Porter: a new, accurate server for protein secondary structure prediction
    • 10.1093/bioinformatics/bti203, 15585524
    • Pollastri G, Mclysaght A. Porter: a new, accurate server for protein secondary structure prediction. Bioinformatics 2005, 21(8):1719-1720. 10.1093/bioinformatics/bti203, 15585524.
    • (2005) Bioinformatics , vol.21 , Issue.8 , pp. 1719-1720
    • Pollastri, G.1    Mclysaght, A.2
  • 7
    • 23144465987 scopus 로고    scopus 로고
    • SCRATCH: a protein structure and structural feature prediction server
    • 1160157, 15980571, Web Server Issue
    • Cheng J, Randall A, Sweredoski M, Baldi P. SCRATCH: a protein structure and structural feature prediction server. Nucleic Acids Res 2005, 33(Web Server Issue):W72-W76. 1160157, 15980571.
    • (2005) Nucleic Acids Res , vol.33
    • Cheng, J.1    Randall, A.2    Sweredoski, M.3    Baldi, P.4
  • 8
    • 33747868721 scopus 로고    scopus 로고
    • Spritz: a server for the prediction of intrinsically disordered regions in protein sequences using kernel machines
    • 10.1093/nar/gkl166, 1538873, 16844983
    • Vullo A, Bortolami O, Pollastri G, Tosatto SCE. Spritz: a server for the prediction of intrinsically disordered regions in protein sequences using kernel machines. Nucleic Acids Res 2006, 34:W164-W168. 10.1093/nar/gkl166, 1538873, 16844983.
    • (2006) Nucleic Acids Res , vol.34
    • Vullo, A.1    Bortolami, O.2    Pollastri, G.3    Tosatto, S.C.E.4
  • 9
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • 10.1093/bioinformatics/16.4.404, 10869041
    • McGuffin L, Bryson K, Jones D. The PSIPRED protein structure prediction server. Bioinformatics 2000, 16(4):404. 10.1093/bioinformatics/16.4.404, 10869041.
    • (2000) Bioinformatics , vol.16 , Issue.4 , pp. 404
    • McGuffin, L.1    Bryson, K.2    Jones, D.3
  • 12
    • 17844381893 scopus 로고    scopus 로고
    • Linear regression models for solvent accessibility prediction in proteins
    • 10.1089/cmb.2005.12.355, 15857247
    • Wagner M, Adamczak R, Porollo A, Meller J. Linear regression models for solvent accessibility prediction in proteins. J Comput Biol 2005, 12(3):355-369. 10.1089/cmb.2005.12.355, 15857247.
    • (2005) J Comput Biol , vol.12 , Issue.3 , pp. 355-369
    • Wagner, M.1    Adamczak, R.2    Porollo, A.3    Meller, J.4
  • 13
    • 50949125397 scopus 로고    scopus 로고
    • Maximum feasibility approach for consensus classifiers: Applications to protein structure prediction
    • Porollo A, Adamczak R, Wagner M, Meller J. Maximum feasibility approach for consensus classifiers: Applications to protein structure prediction. 2003, 2003:75-76.
    • (2003) , vol.2003 , pp. 75-76
    • Porollo, A.1    Adamczak, R.2    Wagner, M.3    Meller, J.4
  • 14
    • 33746267388 scopus 로고    scopus 로고
    • YASSPP: better kernels and coding schemes lead to improvements in protein secondary structure prediction
    • Karypis G. YASSPP: better kernels and coding schemes lead to improvements in protein secondary structure prediction. Proteins: Structure, Function, and Bioinformatics 2006, 64(3):575-586.
    • (2006) Proteins: Structure, Function, and Bioinformatics , vol.64 , Issue.3 , pp. 575-586
    • Karypis, G.1
  • 15
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • 2447793, 18463136
    • Cole C, Barber JD, Barton GJ. The Jpred 3 secondary structure prediction server. Nucleic Acids Res 2008, 36(suppl 2):W197-W201. 2447793, 18463136.
    • (2008) Nucleic Acids Res , vol.36 , Issue.SUPPL. 2
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 16
    • 0029996162 scopus 로고    scopus 로고
    • Incorporation of long-distance interactions into a secondary structure prediction algorithm
    • 10.1093/protein/9.2.133, 9005434
    • Frishman D, Argos P. Incorporation of long-distance interactions into a secondary structure prediction algorithm. Protein Eng 1996, 9(2):133-142. 10.1093/protein/9.2.133, 9005434.
    • (1996) Protein Eng , vol.9 , Issue.2 , pp. 133-142
    • Frishman, D.1    Argos, P.2
  • 18
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • 10.1002/bip.360221211, 6667333
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22(12):2577-2637. 10.1002/bip.360221211, 6667333.
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 19
    • 20744452365 scopus 로고    scopus 로고
    • GOR V server for protein secondary structure prediction
    • 10.1093/bioinformatics/bti408, 2553678, 15797907
    • Sen TZ, Jernigan RL, Garnier J, Kloczkowski A. GOR V server for protein secondary structure prediction. Bioinformatics 2005, 21(11):2787-2788. 10.1093/bioinformatics/bti408, 2553678, 15797907.
    • (2005) Bioinformatics , vol.21 , Issue.11 , pp. 2787-2788
    • Sen, T.Z.1    Jernigan, R.L.2    Garnier, J.3    Kloczkowski, A.4
  • 20
    • 68949213019 scopus 로고    scopus 로고
    • A generic method for assignment of reliability scores applied to solvent accessibility predictions
    • 10.1186/1472-6807-9-51, 2725087, 19646261
    • Petersen B, Petersen TN, Andersen P, Nielsen M, Lundegaard C. A generic method for assignment of reliability scores applied to solvent accessibility predictions. BMC Struct Biol 2009, 9(1):51. 10.1186/1472-6807-9-51, 2725087, 19646261.
    • (2009) BMC Struct Biol , vol.9 , Issue.1 , pp. 51
    • Petersen, B.1    Petersen, T.N.2    Andersen, P.3    Nielsen, M.4    Lundegaard, C.5
  • 22
    • 61449123967 scopus 로고    scopus 로고
    • Improving the prediction accuracy of residue solvent accessibility and real-value backbone torsion angles of proteins by guided-learning through a two-layer neural network
    • Faraggi E, Xue B, Zhou Y. Improving the prediction accuracy of residue solvent accessibility and real-value backbone torsion angles of proteins by guided-learning through a two-layer neural network. Proteins: Structure, Function, and Bioinformatics 2009, 74(4):847-856.
    • (2009) Proteins: Structure, Function, and Bioinformatics , vol.74 , Issue.4 , pp. 847-856
    • Faraggi, E.1    Xue, B.2    Zhou, Y.3
  • 25
    • 77956502766 scopus 로고    scopus 로고
    • Improved sequence-based prediction of disordered regions with multilayer fusion of multiple information sources
    • 10.1093/bioinformatics/btq373, 2935446, 20823312
    • Mizianty MJ, Stach W, Chen K, Kedarisetti KD, Disfani FM, Kurgan L. Improved sequence-based prediction of disordered regions with multilayer fusion of multiple information sources. Bioinformatics 2010, 26(18):i489-i496. 10.1093/bioinformatics/btq373, 2935446, 20823312.
    • (2010) Bioinformatics , vol.26 , Issue.18
    • Mizianty, M.J.1    Stach, W.2    Chen, K.3    Kedarisetti, K.D.4    Disfani, F.M.5    Kurgan, L.6
  • 26
    • 3242891318 scopus 로고    scopus 로고
    • The DISOPRED server for the prediction of protein disorder
    • 10.1093/bioinformatics/bth195, 15044227
    • Ward JJ, McGuffin LJ, Bryson K, Buxton BF, Jones DT. The DISOPRED server for the prediction of protein disorder. Bioinformatics 2004, 20(13):2138-2139. 10.1093/bioinformatics/bth195, 15044227.
    • (2004) Bioinformatics , vol.20 , Issue.13 , pp. 2138-2139
    • Ward, J.J.1    McGuffin, L.J.2    Bryson, K.3    Buxton, B.F.4    Jones, D.T.5
  • 27
    • 84855184716 scopus 로고    scopus 로고
    • SPINE-D: Accurate Prediction of Short and Long Disordered Regions by a Single Neural-Network Based Method
    • 10.1080/073911012010525022, 3297974, 22208280
    • Zhang T, Faraggi E, Xue B, Dunker A, Uversky VN, Zhou Y. SPINE-D: Accurate Prediction of Short and Long Disordered Regions by a Single Neural-Network Based Method. J Biomol Struct Dyn 2012, 29(4):799-813. 10.1080/073911012010525022, 3297974, 22208280.
    • (2012) J Biomol Struct Dyn , vol.29 , Issue.4 , pp. 799-813
    • Zhang, T.1    Faraggi, E.2    Xue, B.3    Dunker, A.4    Uversky, V.N.5    Zhou, Y.6
  • 28
    • 34547588389 scopus 로고    scopus 로고
    • PrDOS: prediction of disordered protein regions from amino acid sequence
    • 1933209, 17567614
    • Ishida T, Kinoshita K. PrDOS: prediction of disordered protein regions from amino acid sequence. Nucleic Acids Res 2007, 35(suppl 2):W460-W464. 1933209, 17567614.
    • (2007) Nucleic Acids Res , vol.35 , Issue.SUPPL. 2
    • Ishida, T.1    Kinoshita, K.2
  • 29
    • 34548738213 scopus 로고    scopus 로고
    • POODLE-S: web application for predicting protein disorder by using physicochemical features and reduced amino acid set of a position-specific scoring matrix
    • 10.1093/bioinformatics/btm330, 17599940
    • Shimizu K, Hirose S, Noguchi T. POODLE-S: web application for predicting protein disorder by using physicochemical features and reduced amino acid set of a position-specific scoring matrix. Bioinformatics 2007, 23(17):2337-2338. 10.1093/bioinformatics/btm330, 17599940.
    • (2007) Bioinformatics , vol.23 , Issue.17 , pp. 2337-2338
    • Shimizu, K.1    Hirose, S.2    Noguchi, T.3
  • 30
    • 34548567232 scopus 로고    scopus 로고
    • POODLE-L: a two-level SVM prediction system for reliably predicting long disordered regions
    • 10.1093/bioinformatics/btm302, 17545177
    • Hirose S, Shimizu K, Kanai S, Kuroda Y, Noguchi T. POODLE-L: a two-level SVM prediction system for reliably predicting long disordered regions. Bioinformatics 2007, 23(16):2046-2053. 10.1093/bioinformatics/btm302, 17545177.
    • (2007) Bioinformatics , vol.23 , Issue.16 , pp. 2046-2053
    • Hirose, S.1    Shimizu, K.2    Kanai, S.3    Kuroda, Y.4    Noguchi, T.5
  • 31
    • 34748854289 scopus 로고    scopus 로고
    • Predicting mostly disordered proteins by using structure-unknown protein data
    • Shimizu K, Muraoka Y, Hirose S, Tomii K, Noguchi T. Predicting mostly disordered proteins by using structure-unknown protein data. BMC Bioinforma 2007, 8(1):78.
    • (2007) BMC Bioinforma , vol.8 , Issue.1 , pp. 78
    • Shimizu, K.1    Muraoka, Y.2    Hirose, S.3    Tomii, K.4    Noguchi, T.5
  • 32
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • 10.1016/j.jmb.2005.01.071, 15769473
    • Dosztányi Z, Csizmok V, Tompa P, Simon I. The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J Mol Biol 2005, 347(4):827-839. 10.1016/j.jmb.2005.01.071, 15769473.
    • (2005) J Mol Biol , vol.347 , Issue.4 , pp. 827-839
    • Dosztányi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 33
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • 10.1093/bioinformatics/bti541, 15955779
    • Dosztányi Z, Csizmok V, Tompa P, Simon I. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 2005, 21(16):3433-3434. 10.1093/bioinformatics/bti541, 15955779.
    • (2005) Bioinformatics , vol.21 , Issue.16 , pp. 3433-3434
    • Dosztányi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 34
    • 39149099199 scopus 로고    scopus 로고
    • The ModFOLD server for the quality assessment of protein structural models
    • 10.1093/bioinformatics/btn014, 18184684
    • McGuffin L. The ModFOLD server for the quality assessment of protein structural models. Bioinformatics 2008, 24(4):586. 10.1093/bioinformatics/btn014, 18184684.
    • (2008) Bioinformatics , vol.24 , Issue.4 , pp. 586
    • McGuffin, L.1
  • 35
    • 79959564695 scopus 로고    scopus 로고
    • The IntFOLD server: an integrated web resource for protein fold recognition, 3D model quality assessment, intrinsic disorder prediction, domain prediction and ligand binding site prediction
    • 3125722, 21459847
    • Roche DB, Buenavista MT, Tetchner SJ, McGuffin LJ. The IntFOLD server: an integrated web resource for protein fold recognition, 3D model quality assessment, intrinsic disorder prediction, domain prediction and ligand binding site prediction. Nucleic Acids Res 2011, 39(suppl 2):W171-W176. 3125722, 21459847.
    • (2011) Nucleic Acids Res , vol.39 , Issue.SUPPL. 2
    • Roche, D.B.1    Buenavista, M.T.2    Tetchner, S.J.3    McGuffin, L.J.4
  • 36
    • 0036893072 scopus 로고    scopus 로고
    • Rapid protein domain assignment from amino acid sequence using predicted secondary structure
    • 2373756, 12441380
    • Marsden RL, McGuffin LJ, Jones DT. Rapid protein domain assignment from amino acid sequence using predicted secondary structure. Protein Sci 2002, 11(12):2814-2824. 2373756, 12441380.
    • (2002) Protein Sci , vol.11 , Issue.12 , pp. 2814-2824
    • Marsden, R.L.1    McGuffin, L.J.2    Jones, D.T.3
  • 37
    • 77956938868 scopus 로고    scopus 로고
    • DomSVR: domain boundary prediction with support vector regression from sequence information alone
    • 10.1007/s00726-010-0506-6, 2909371, 20165918
    • Chen P, Liu C, Burge L, Li J, Mohammad M, Southerland W, Gloster C, Wang B. DomSVR: domain boundary prediction with support vector regression from sequence information alone. Amino Acids 2010, 39(3):713-726. 10.1007/s00726-010-0506-6, 2909371, 20165918.
    • (2010) Amino Acids , vol.39 , Issue.3 , pp. 713-726
    • Chen, P.1    Liu, C.2    Burge, L.3    Li, J.4    Mohammad, M.5    Southerland, W.6    Gloster, C.7    Wang, B.8
  • 38
  • 39
    • 3042810008 scopus 로고    scopus 로고
    • Sequence-based prediction of protein domains
    • 10.1093/nar/gkh684, 484172, 15240828
    • Liu J, Rost B. Sequence-based prediction of protein domains. Nucleic Acids Res 2004, 32(12):3522-3530. 10.1093/nar/gkh684, 484172, 15240828.
    • (2004) Nucleic Acids Res , vol.32 , Issue.12 , pp. 3522-3530
    • Liu, J.1    Rost, B.2
  • 40
    • 79351469227 scopus 로고    scopus 로고
    • DoBo: Protein domain boundary prediction by integrating evolutionary signals and machine learning
    • Eickholt J, Deng X, Cheng J. DoBo: Protein domain boundary prediction by integrating evolutionary signals and machine learning. BMC Bioinforma 2011, 12:43.
    • (2011) BMC Bioinforma , vol.12 , pp. 43
    • Eickholt, J.1    Deng, X.2    Cheng, J.3
  • 41
    • 32144434539 scopus 로고    scopus 로고
    • SSEP-Domain: protein domain prediction by alignment of secondary structure elements and profiles
    • 10.1093/bioinformatics/bti751, 16267083
    • Gewehr JE, Zimmer R. SSEP-Domain: protein domain prediction by alignment of secondary structure elements and profiles. Bioinformatics 2006, 22(2):181-187. 10.1093/bioinformatics/bti751, 16267083.
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 181-187
    • Gewehr, J.E.1    Zimmer, R.2
  • 42
    • 3242885293 scopus 로고    scopus 로고
    • The predictprotein server
    • 441515, 15215403
    • Rost B, Yachdav G, Liu J. The predictprotein server. Nucleic Acids Res 2004, 32(suppl 2):W321-W326. 441515, 15215403.
    • (2004) Nucleic Acids Res , vol.32 , Issue.SUPPL. 2
    • Rost, B.1    Yachdav, G.2    Liu, J.3
  • 43
    • 33749139123 scopus 로고    scopus 로고
    • Distill: a suite of web servers for the prediction of one-, two-, and three-dimensional structural features of proteins
    • Baú D, Martin A, Mooney C, Vullo A, Walsh I, Pollastri G. Distill: a suite of web servers for the prediction of one-, two-, and three-dimensional structural features of proteins. BMC Bioinforma 2006, 7(1):402.
    • (2006) BMC Bioinforma , vol.7 , Issue.1 , pp. 402
    • Baú, D.1    Martin, A.2    Mooney, C.3    Vullo, A.4    Walsh, I.5    Pollastri, G.6
  • 44
    • 38349104051 scopus 로고    scopus 로고
    • SVM-BetaPred: prediction of right-handed ß-helix fold from protein sequence using SVM
    • Singh S, Hajela K, Ramani A. SVM-BetaPred: prediction of right-handed ß-helix fold from protein sequence using SVM. Pattern Recognition in Bioinformatics 2007, 108-119.
    • (2007) Pattern Recognition in Bioinformatics , pp. 108-119
    • Singh, S.1    Hajela, K.2    Ramani, A.3
  • 45
    • 21444454088 scopus 로고    scopus 로고
    • PROFcon: novel prediction of long-range contacts
    • 10.1093/bioinformatics/bti454, 15890748
    • Punta M, Rost B. PROFcon: novel prediction of long-range contacts. Bioinformatics 2005, 21(13):2960-2968. 10.1093/bioinformatics/bti454, 15890748.
    • (2005) Bioinformatics , vol.21 , Issue.13 , pp. 2960-2968
    • Punta, M.1    Rost, B.2
  • 46
    • 61449245515 scopus 로고    scopus 로고
    • Prediction of helix-helix contacts and interacting helices in polytopic membrane proteins using neural networks
    • Fuchs A, Kirschner A, Frishman D. Prediction of helix-helix contacts and interacting helices in polytopic membrane proteins using neural networks. Proteins: Structure, Function, and Bioinformatics 2009, 74(4):857-871.
    • (2009) Proteins: Structure, Function, and Bioinformatics , vol.74 , Issue.4 , pp. 857-871
    • Fuchs, A.1    Kirschner, A.2    Frishman, D.3
  • 47
    • 23144437891 scopus 로고    scopus 로고
    • DiANNA: a web server for disulfide connectivity prediction
    • 1160173, 15980459
    • Ferre F, Clote P. DiANNA: a web server for disulfide connectivity prediction. Nucleic Acids Res 2005, 33(suppl 2):W230-W232. 1160173, 15980459.
    • (2005) Nucleic Acids Res , vol.33 , Issue.SUPPL. 2
    • Ferre, F.1    Clote, P.2
  • 48
    • 3242886780 scopus 로고    scopus 로고
    • GDAP: a web tool for genome-wide protein disulfide bond prediction
    • 441514, 15215411
    • O'Connor BD, Yeates TO. GDAP: a web tool for genome-wide protein disulfide bond prediction. Nucleic Acids Res 2004, 32(suppl 2):W360-W364. 441514, 15215411.
    • (2004) Nucleic Acids Res , vol.32 , Issue.SUPPL. 2
    • O'Connor, B.D.1    Yeates, T.O.2
  • 49
    • 0033566578 scopus 로고    scopus 로고
    • Role of evolutionary information in predicting the disulfide-bonding state of cysteine in proteins
    • Fariselli P, Riccobelli P, Casadio R. Role of evolutionary information in predicting the disulfide-bonding state of cysteine in proteins. Proteins: Structure, Function, and Bioinformatics 1999, 36(3):340-346.
    • (1999) Proteins: Structure, Function, and Bioinformatics , vol.36 , Issue.3 , pp. 340-346
    • Fariselli, P.1    Riccobelli, P.2    Casadio, R.3
  • 50
    • 0035910068 scopus 로고    scopus 로고
    • Betawrap: Successful prediction of parallel β-helices from primary sequence reveals an association with many microbial pathogens
    • 10.1073/pnas.251267298, 64942, 11752429
    • Bradley P, Cowen L, Menke M, King J, Berger B. Betawrap: Successful prediction of parallel β-helices from primary sequence reveals an association with many microbial pathogens. Proc Natl Acad Sci 2001, 98(26):14819-14824. 10.1073/pnas.251267298, 64942, 11752429.
    • (2001) Proc Natl Acad Sci , vol.98 , Issue.26 , pp. 14819-14824
    • Bradley, P.1    Cowen, L.2    Menke, M.3    King, J.4    Berger, B.5
  • 51
    • 38149087243 scopus 로고    scopus 로고
    • BETTY: Prediction of β-Strand Type from Sequence
    • Zimmermann O, Wang L, Hansmann UHE. BETTY: Prediction of β-Strand Type from Sequence. In Silico Biol 2007, 7(4):535-542.
    • (2007) In Silico Biol , vol.7 , Issue.4 , pp. 535-542
    • Zimmermann, O.1    Wang, L.2    Hansmann, U.H.E.3
  • 52
    • 83255194562 scopus 로고    scopus 로고
    • Predicting residue-residue contacts using random forest models
    • 10.1093/bioinformatics/btr579, 22016406
    • Li Y, Fang Y, Fang J. Predicting residue-residue contacts using random forest models. Bioinformatics 2011, 27(24):3379-3384. 10.1093/bioinformatics/btr579, 22016406.
    • (2011) Bioinformatics , vol.27 , Issue.24 , pp. 3379-3384
    • Li, Y.1    Fang, Y.2    Fang, J.3
  • 53
    • 65549127269 scopus 로고    scopus 로고
    • Using multi-data hidden Markov models trained on local neighborhoods of protein structure to predict residue-residue contacts
    • 10.1093/bioinformatics/btp149, 2677742, 19289446
    • Björkholm P, Daniluk P, Kryshtafovych A, Fidelis K, Andersson R, Hvidsten TR. Using multi-data hidden Markov models trained on local neighborhoods of protein structure to predict residue-residue contacts. Bioinformatics 2009, 25(10):1264-1270. 10.1093/bioinformatics/btp149, 2677742, 19289446.
    • (2009) Bioinformatics , vol.25 , Issue.10 , pp. 1264-1270
    • Björkholm, P.1    Daniluk, P.2    Kryshtafovych, A.3    Fidelis, K.4    Andersson, R.5    Hvidsten, T.R.6
  • 54
    • 41349114023 scopus 로고    scopus 로고
    • A comprehensive assessment of sequence-based and template-based methods for protein contact prediction
    • 10.1093/bioinformatics/btn069, 2648832, 18296462
    • Wu S, Zhang Y. A comprehensive assessment of sequence-based and template-based methods for protein contact prediction. Bioinformatics 2008, 24(7):924-931. 10.1093/bioinformatics/btn069, 2648832, 18296462.
    • (2008) Bioinformatics , vol.24 , Issue.7 , pp. 924-931
    • Wu, S.1    Zhang, Y.2
  • 56
    • 12844288890 scopus 로고    scopus 로고
    • The protein structure prediction problem could be solved using the current PDB library
    • 10.1073/pnas.0407152101, 545829, 15653774
    • Zhang Y, Skolnick J. The protein structure prediction problem could be solved using the current PDB library. Proc Natl Acad Sci 2005, 102(4):1029-1034. 10.1073/pnas.0407152101, 545829, 15653774.
    • (2005) Proc Natl Acad Sci , vol.102 , Issue.4 , pp. 1029-1034
    • Zhang, Y.1    Skolnick, J.2
  • 57
    • 0035812694 scopus 로고    scopus 로고
    • Protein structure prediction and structural genomics
    • 10.1126/science.1065659, 11588250
    • Baker D, Sali A. Protein structure prediction and structural genomics. Science 2001, 294(5540):93-96. 10.1126/science.1065659, 11588250.
    • (2001) Science , vol.294 , Issue.5540 , pp. 93-96
    • Baker, D.1    Sali, A.2
  • 58
    • 44949145113 scopus 로고    scopus 로고
    • Progress and challenges in protein structure prediction
    • 10.1016/j.sbi.2008.02.004, 2680823, 18436442
    • Zhang Y. Progress and challenges in protein structure prediction. Curr Opin Struct Biol 2008, 18(3):342-348. 10.1016/j.sbi.2008.02.004, 2680823, 18436442.
    • (2008) Curr Opin Struct Biol , vol.18 , Issue.3 , pp. 342-348
    • Zhang, Y.1
  • 59
    • 24644512819 scopus 로고    scopus 로고
    • SPEM: improving multiple sequence alignment with sequence profiles and predicted secondary structures
    • 10.1093/bioinformatics/bti582, 16020471
    • Zhou H, Zhou Y. SPEM: improving multiple sequence alignment with sequence profiles and predicted secondary structures. Bioinformatics 2005, 21(18):3615-3621. 10.1093/bioinformatics/bti582, 16020471.
    • (2005) Bioinformatics , vol.21 , Issue.18 , pp. 3615-3621
    • Zhou, H.1    Zhou, Y.2
  • 60
    • 0242369082 scopus 로고    scopus 로고
    • RAPTOR: optimal protein threading by linear programming
    • Xu J, Li M, Kim D, Xu Y. RAPTOR: optimal protein threading by linear programming. J Bioinforma Comput Biol 2003, 1(1):95-117.
    • (2003) J Bioinforma Comput Biol , vol.1 , Issue.1 , pp. 95-117
    • Xu, J.1    Li, M.2    Kim, D.3    Xu, Y.4
  • 61
    • 0031585984 scopus 로고    scopus 로고
    • Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions
    • 10.1006/jmbi.1997.0959, 9149153
    • Simons K, Kooperberg C, Huang E, Baker D. Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions. J Mol Biol 1997, 268(1):209-225. 10.1006/jmbi.1997.0959, 9149153.
    • (1997) J Mol Biol , vol.268 , Issue.1 , pp. 209-225
    • Simons, K.1    Kooperberg, C.2    Huang, E.3    Baker, D.4
  • 62
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • 10.1038/nprot.2010.5, 2849174, 20360767
    • Roy A, Kucukural A, Zhang Y. I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 2010, 5(4):725-738. 10.1038/nprot.2010.5, 2849174, 20360767.
    • (2010) Nat Protoc , vol.5 , Issue.4 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 63
    • 74249106219 scopus 로고    scopus 로고
    • I-TASSER: Fully automated protein structure prediction in CASP8
    • Zhang Y. I-TASSER: Fully automated protein structure prediction in CASP8. Proteins: Structure, Function, and Bioinformatics 2009, 77(S9):100-113.
    • (2009) Proteins: Structure, Function, and Bioinformatics , vol.77 , Issue.S9 , pp. 100-113
    • Zhang, Y.1
  • 64
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y. I-TASSER server for protein 3D structure prediction. BMC Bioinforma 2008, 9(1):40.
    • (2008) BMC Bioinforma , vol.9 , Issue.1 , pp. 40
    • Zhang, Y.1
  • 66
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: generation and refinement of homology-based protein structure models
    • Fiser A, Sali A. Modeller: generation and refinement of homology-based protein structure models. Methods Enzymol 2003, 374:461-491.
    • (2003) Methods Enzymol , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 67
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • 1160169, 15980461, Web Server Issue
    • Soding J, Biegert A, Lupas A. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 2005, 33(Web Server Issue):W244-W248. 1160169, 15980461.
    • (2005) Nucleic Acids Res , vol.33
    • Soding, J.1    Biegert, A.2    Lupas, A.3
  • 68
    • 84862225232 scopus 로고    scopus 로고
    • Ab initio protein structure assembly using continuous structure fragments and optimized knowledge-based force field
    • Xu D, Zhang Y. Ab initio protein structure assembly using continuous structure fragments and optimized knowledge-based force field. Proteins: Structure, Function, and Bioinformatics 2012,
    • (2012) Proteins: Structure, Function, and Bioinformatics
    • Xu, D.1    Zhang, Y.2
  • 69
    • 34548608483 scopus 로고    scopus 로고
    • Ab initio protein structure prediction using chunk-TASSER
    • 10.1529/biophysj.107.109959, 1948038, 17496016
    • Zhou H, Skolnick J. Ab initio protein structure prediction using chunk-TASSER. Biophys J 2007, 93(5):1510-1518. 10.1529/biophysj.107.109959, 1948038, 17496016.
    • (2007) Biophys J , vol.93 , Issue.5 , pp. 1510-1518
    • Zhou, H.1    Skolnick, J.2
  • 70
    • 34547612652 scopus 로고    scopus 로고
    • Pcons. net: protein structure prediction meta server
    • 1933226, 17584798
    • Wallner B, Larsson P, Elofsson A. Pcons. net: protein structure prediction meta server. Nucleic Acids Res 2007, 35(suppl 2):W369-W374. 1933226, 17584798.
    • (2007) Nucleic Acids Res , vol.35 , Issue.SUPPL. 2
    • Wallner, B.1    Larsson, P.2    Elofsson, A.3
  • 71
    • 0032438987 scopus 로고    scopus 로고
    • Hidden Markov models for detecting remote protein homologies
    • 10.1093/bioinformatics/14.10.846, 9927713
    • Karplus K, Barrett C, Hughey R. Hidden Markov models for detecting remote protein homologies. Bioinformatics 1998, 14(10):846-856. 10.1093/bioinformatics/14.10.846, 9927713.
    • (1998) Bioinformatics , vol.14 , Issue.10 , pp. 846-856
    • Karplus, K.1    Barrett, C.2    Hughey, R.3
  • 72
    • 77954196482 scopus 로고    scopus 로고
    • Low-homology protein threading
    • 10.1093/bioinformatics/btq192, 2881377, 20529920
    • Peng J, Xu J. Low-homology protein threading. Bioinformatics 2010, 26(12):i294-i300. 10.1093/bioinformatics/btq192, 2881377, 20529920.
    • (2010) Bioinformatics , vol.26 , Issue.12
    • Peng, J.1    Xu, J.2
  • 73
    • 79960394811 scopus 로고    scopus 로고
    • Improving protein fold recognition and template-based modeling by employing probabilistic-based matching between predicted one-dimensional structural properties of query and corresponding native properties of templates
    • 10.1093/bioinformatics/btr350, 21666270
    • Yang Y, Faraggi E, Zhao H, Zhou Y. Improving protein fold recognition and template-based modeling by employing probabilistic-based matching between predicted one-dimensional structural properties of query and corresponding native properties of templates. Bioinformatics 2011, 27(15):2076-2082. 10.1093/bioinformatics/btr350, 21666270.
    • (2011) Bioinformatics , vol.27 , Issue.15 , pp. 2076-2082
    • Yang, Y.1    Faraggi, E.2    Zhao, H.3    Zhou, Y.4
  • 75
    • 80054685109 scopus 로고    scopus 로고
    • Critical assessment of methods of protein strucutre prediction - round IX
    • Moult J, Fidelis K, Kryshtafovych A, Tramontano A. Critical assessment of methods of protein strucutre prediction - round IX. Protiens 2011, 79(S10):1-5.
    • (2011) Protiens , vol.79 , Issue.S10 , pp. 1-5
    • Moult, J.1    Fidelis, K.2    Kryshtafovych, A.3    Tramontano, A.4
  • 76
    • 80855132586 scopus 로고    scopus 로고
    • Evaluation of disorder predictions in CASP9
    • 10.1002/prot.23161, 21928402
    • Monastyrskyy B, Fidelis K, Moult J, Tramontano A, Kryshtafovych A. Evaluation of disorder predictions in CASP9. Proteins 2011, 79(S10):107-118. 10.1002/prot.23161, 21928402.
    • (2011) Proteins , vol.79 , Issue.S10 , pp. 107-118
    • Monastyrskyy, B.1    Fidelis, K.2    Moult, J.3    Tramontano, A.4    Kryshtafovych, A.5
  • 77
    • 80855132587 scopus 로고    scopus 로고
    • Evaluation of residue-residue contact prediction in CASP9
    • 10.1002/prot.23160, 21928322
    • Monastyrskyy B, Fidelis K, Tramontano A, Kryshtafovych A. Evaluation of residue-residue contact prediction in CASP9. Proteins 2011, 79(S10):119-125. 10.1002/prot.23160, 21928322.
    • (2011) Proteins , vol.79 , Issue.S10 , pp. 119-125
    • Monastyrskyy, B.1    Fidelis, K.2    Tramontano, A.3    Kryshtafovych, A.4
  • 79
    • 80855132939 scopus 로고    scopus 로고
    • Assessment of template based protein structure predictions in CASP9
    • 10.1002/prot.23177, 22002823
    • Mariani V, Kiefer F, Schmidt T, Haas J, Schwede T. Assessment of template based protein structure predictions in CASP9. Proteins 2011, 79(S10):37-58. 10.1002/prot.23177, 22002823.
    • (2011) Proteins , vol.79 , Issue.S10 , pp. 37-58
    • Mariani, V.1    Kiefer, F.2    Schmidt, T.3    Haas, J.4    Schwede, T.5
  • 80
    • 80855133462 scopus 로고    scopus 로고
    • CASP9 assessment of free modeling target predictions
    • 10.1002/prot.23181, 21997521
    • Kinch L, Shi SY, Cong Q, Cheng H, Liao Y, Grishin NV. CASP9 assessment of free modeling target predictions. Proteins 2011, 79(S10):59-73. 10.1002/prot.23181, 21997521.
    • (2011) Proteins , vol.79 , Issue.S10 , pp. 59-73
    • Kinch, L.1    Shi, S.Y.2    Cong, Q.3    Cheng, H.4    Liao, Y.5    Grishin, N.V.6
  • 81
    • 40549141792 scopus 로고    scopus 로고
    • QMEAN: a comprehensive scoring function for model quality assessment
    • Benkert P, Tosatto S, Schomburg D. QMEAN: a comprehensive scoring function for model quality assessment. Proteins 2008, 71(1).
    • (2008) Proteins , vol.71 , Issue.1
    • Benkert, P.1    Tosatto, S.2    Schomburg, D.3
  • 83
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: assessment of protein models with three-dimensional profiles
    • Eisenberg D, Luthy R, Bowie J. VERIFY3D: assessment of protein models with three-dimensional profiles. Methods Enzymol 1997, 277:396-404.
    • (1997) Methods Enzymol , vol.277 , pp. 396-404
    • Eisenberg, D.1    Luthy, R.2    Bowie, J.3
  • 84
    • 74249103622 scopus 로고    scopus 로고
    • Assessment of global and local model quality in CASP8 using Pcons and ProQ
    • 10.1002/prot.22476, 19544566
    • Larsson P, Skwark M, Wallner B, Elofsson A. Assessment of global and local model quality in CASP8 using Pcons and ProQ. Proteins 2009, 77(S9):167-172. 10.1002/prot.22476, 19544566.
    • (2009) Proteins , vol.77 , Issue.S9 , pp. 167-172
    • Larsson, P.1    Skwark, M.2    Wallner, B.3    Elofsson, A.4
  • 85
    • 77950478720 scopus 로고    scopus 로고
    • Rapid model quality assessment for protein structure predictions using the comparison of multiple models without structural alignments
    • 10.1093/bioinformatics/btp629, 19897565
    • McGuffin L, Roche D. Rapid model quality assessment for protein structure predictions using the comparison of multiple models without structural alignments. Bioinformatics 2010, 26(2):182-188. 10.1093/bioinformatics/btp629, 19897565.
    • (2010) Bioinformatics , vol.26 , Issue.2 , pp. 182-188
    • McGuffin, L.1    Roche, D.2
  • 86
    • 66149084059 scopus 로고    scopus 로고
    • Model Quality Assessment using Distance Constraints from Alignments
    • Paluszewski M, Karplus K. Model Quality Assessment using Distance Constraints from Alignments. Proteins 2008, 75:540-549.
    • (2008) Proteins , vol.75 , pp. 540-549
    • Paluszewski, M.1    Karplus, K.2
  • 87
    • 80855131663 scopus 로고    scopus 로고
    • Evaluation of model quality predictions in CASP9
    • 10.1002/prot.23180, 21997462
    • Kryshtafovych A, Fidelis K, Tramontano A. Evaluation of model quality predictions in CASP9. Proteins 2011, 79(S10):91-109. 10.1002/prot.23180, 21997462.
    • (2011) Proteins , vol.79 , Issue.S10 , pp. 91-109
    • Kryshtafovych, A.1    Fidelis, K.2    Tramontano, A.3
  • 88
    • 85152601164 scopus 로고    scopus 로고
    • Critical assessment of methods of protein structure prediction (CASP)-round VIII
    • (Accpeted)
    • Moult J, Fidelis K, Kryshtafovych A, Rost B, Tramontano A. Critical assessment of methods of protein structure prediction (CASP)-round VIII. 2009, (Accpeted).
    • (2009)
    • Moult, J.1    Fidelis, K.2    Kryshtafovych, A.3    Rost, B.4    Tramontano, A.5
  • 89
    • 80855147416 scopus 로고    scopus 로고
    • Assessment of protein structure refinement in CASP9
    • 10.1002/prot.23131, 22069034
    • MacCallum JL, Perez A, Schnieders MJ, Hua L, Jacobson MP, Dill KA. Assessment of protein structure refinement in CASP9. Proteins 2011, 79(S10):74-90. 10.1002/prot.23131, 22069034.
    • (2011) Proteins , vol.79 , Issue.S10 , pp. 74-90
    • MacCallum, J.L.1    Perez, A.2    Schnieders, M.J.3    Hua, L.4    Jacobson, M.P.5    Dill, K.A.6
  • 90
    • 2542420004 scopus 로고    scopus 로고
    • The principled design of large-scale recursive neural network architectures-DAG-RNNs and the protein structure prediction problem
    • Baldi P, Pollastri G. The principled design of large-scale recursive neural network architectures-DAG-RNNs and the protein structure prediction problem. J Mach Learn Res 2003, 4:575-602.
    • (2003) J Mach Learn Res , vol.4 , pp. 575-602
    • Baldi, P.1    Pollastri, G.2
  • 91
    • 0017411710 scopus 로고
    • The protein data bank: A computer-based archival file for macromolecular structures
    • 10.1016/S0022-2836(77)80200-3, 875032
    • Bernstein FC, Koetzle TF, Williams GJB, Meyer EF. The protein data bank: A computer-based archival file for macromolecular structures*. J Mol Biol 1977, 112(3):535-542. 10.1016/S0022-2836(77)80200-3, 875032.
    • (1977) J Mol Biol , vol.112 , Issue.3 , pp. 535-542
    • Bernstein, F.C.1    Koetzle, T.F.2    Williams, G.J.B.3    Meyer, E.F.4
  • 92
    • 75149164436 scopus 로고    scopus 로고
    • PreDisorder: ab initio sequence-based prediction of protein disordered regions
    • Deng X, Eickholt J, Cheng J. PreDisorder: ab initio sequence-based prediction of protein disordered regions. BMC Bioinforma 2009, 10(1):436.
    • (2009) BMC Bioinforma , vol.10 , Issue.1 , pp. 436
    • Deng, X.1    Eickholt, J.2    Cheng, J.3
  • 93
    • 84864510883 scopus 로고    scopus 로고
    • A comprehensive overview of computational protein disorder prediction methods
    • Deng X, Eickholt J, Cheng J. A comprehensive overview of computational protein disorder prediction methods. Mol BioSyst 2011, 8.
    • (2011) Mol BioSyst , pp. 8
    • Deng, X.1    Eickholt, J.2    Cheng, J.3
  • 94
    • 80051490632 scopus 로고    scopus 로고
    • Improving protein structure prediction using multiple sequence-based contact predictions
    • 10.1016/j.str.2011.05.004, 21827953
    • Wu S, Szilagyi A, Zhang Y. Improving protein structure prediction using multiple sequence-based contact predictions. Structure 2011, 19(8):1182-1191. 10.1016/j.str.2011.05.004, 21827953.
    • (2011) Structure , vol.19 , Issue.8 , pp. 1182-1191
    • Wu, S.1    Szilagyi, A.2    Zhang, Y.3
  • 95
    • 67849110005 scopus 로고    scopus 로고
    • NNcon: improved protein contact map prediction using 2D-recursive neural networks
    • 2703959, 19420062
    • Tegge AN, Wang Z, Eickholt J, Cheng J. NNcon: improved protein contact map prediction using 2D-recursive neural networks. Nucleic Acids Res 2009, 37(suppl 2):W515-W518. 2703959, 19420062.
    • (2009) Nucleic Acids Res , vol.37 , Issue.SUPPL. 2
    • Tegge, A.N.1    Wang, Z.2    Eickholt, J.3    Cheng, J.4
  • 96
    • 34247247779 scopus 로고    scopus 로고
    • Improved residue contact prediction using support vector machines and a large feature set
    • Cheng J, Baldi P. Improved residue contact prediction using support vector machines and a large feature set. BMC Bioinforma 2007, 8(1):113.
    • (2007) BMC Bioinforma , vol.8 , Issue.1 , pp. 113
    • Cheng, J.1    Baldi, P.2
  • 99
    • 31944444347 scopus 로고    scopus 로고
    • Large scale prediction of disulphide bridges using kernel methods, two dimensional recursive neural networks, and weighted graph matching
    • Cheng J, Saigo H, Baldi P. Large scale prediction of disulphide bridges using kernel methods, two dimensional recursive neural networks, and weighted graph matching. Proteins: Structure, Function, and Bioinformatics 2006, 62(3):617-629.
    • (2006) Proteins: Structure, Function, and Bioinformatics , vol.62 , Issue.3 , pp. 617-629
    • Cheng, J.1    Saigo, H.2    Baldi, P.3
  • 101
    • 84860507958 scopus 로고    scopus 로고
    • Three-stage prediction of protein β-sheets by neural networks, alignments and graph algorithms
    • 10.1093/bioinformatics/bti1004, 15961501
    • Cheng J, Baldi P. Three-stage prediction of protein β-sheets by neural networks, alignments and graph algorithms. Bioinformatics 2005, 21(suppl 1):i75-i84. 10.1093/bioinformatics/bti1004, 15961501.
    • (2005) Bioinformatics , vol.21 , Issue.SUPPL. 1
    • Cheng, J.1    Baldi, P.2
  • 102
    • 77951941264 scopus 로고    scopus 로고
    • MULTICOM: a multi-level combination approach to protein structure prediction and its assessments in CASP8
    • 10.1093/bioinformatics/btq058, 2844995, 20150411
    • Wang Z, Eickholt J, Cheng J. MULTICOM: a multi-level combination approach to protein structure prediction and its assessments in CASP8. Bioinformatics 2010, 26(7):882-888. 10.1093/bioinformatics/btq058, 2844995, 20150411.
    • (2010) Bioinformatics , vol.26 , Issue.7 , pp. 882-888
    • Wang, Z.1    Eickholt, J.2    Cheng, J.3
  • 103
    • 10344232638 scopus 로고    scopus 로고
    • Scoring function for automated assessment of protein structure template quality
    • Zhang Y, Skolnick J. Scoring function for automated assessment of protein structure template quality. Proteins: Structure, Function, and Bioinformatics 2004, 57(4):702-710.
    • (2004) Proteins: Structure, Function, and Bioinformatics , vol.57 , Issue.4 , pp. 702-710
    • Zhang, Y.1    Skolnick, J.2
  • 105
    • 0042622381 scopus 로고    scopus 로고
    • LGA: a method for finding 3D similarities in protein structures
    • 10.1093/nar/gkg571, 168977, 12824330
    • Zemla A. LGA: a method for finding 3D similarities in protein structures. Nucleic Acids Res 2003, 31(13):3370-3374. 10.1093/nar/gkg571, 168977, 12824330.
    • (2003) Nucleic Acids Res , vol.31 , Issue.13 , pp. 3370-3374
    • Zemla, A.1
  • 106
    • 79958078892 scopus 로고    scopus 로고
    • APOLLO: a quality assessment service for single and multiple protein models
    • 10.1093/bioinformatics/btr268, 3106203, 21546397
    • Wang Z, Eickholt J, Cheng J. APOLLO: a quality assessment service for single and multiple protein models. Bioinformatics 2011, 27(12):1715-1716. 10.1093/bioinformatics/btr268, 3106203, 21546397.
    • (2011) Bioinformatics , vol.27 , Issue.12 , pp. 1715-1716
    • Wang, Z.1    Eickholt, J.2    Cheng, J.3
  • 107
    • 66149156968 scopus 로고    scopus 로고
    • Evaluating the absolute quality of a single protein model using structural features and support vector machines
    • Wang Z, Tegge AN, Cheng J. Evaluating the absolute quality of a single protein model using structural features and support vector machines. Proteins: Structure, Function, and Bioinformatics 2009, 75(3):638-647.
    • (2009) Proteins: Structure, Function, and Bioinformatics , vol.75 , Issue.3 , pp. 638-647
    • Wang, Z.1    Tegge, A.N.2    Cheng, J.3
  • 108
    • 74249120024 scopus 로고    scopus 로고
    • Prediction of global and local quality of CASP8 models by MULTICOM series
    • 10.1002/prot.22487, 19544564
    • Cheng J, Wang Z, Tegge A, Eickholt J. Prediction of global and local quality of CASP8 models by MULTICOM series. Proteins 2009, 77(S9):181-184. 10.1002/prot.22487, 19544564.
    • (2009) Proteins , vol.77 , Issue.S9 , pp. 181-184
    • Cheng, J.1    Wang, Z.2    Tegge, A.3    Eickholt, J.4
  • 109
    • 84455168000 scopus 로고    scopus 로고
    • An iterative self-refining and self-evaluating approach for protein model quality estimation
    • 10.1002/pro.764, 22057943
    • Wang Z, Cheng J. An iterative self-refining and self-evaluating approach for protein model quality estimation. Protein Sci 2012, 21(1):142-151. 10.1002/pro.764, 22057943.
    • (2012) Protein Sci , vol.21 , Issue.1 , pp. 142-151
    • Wang, Z.1    Cheng, J.2
  • 110
    • 33644847172 scopus 로고    scopus 로고
    • Prediction of protein stability changes for single site mutations using support vector machines
    • Cheng J, Randall A, Baldi P. Prediction of protein stability changes for single site mutations using support vector machines. Proteins: Structure, Function, and Bioinformatics 2006, 62(4):1125-1132.
    • (2006) Proteins: Structure, Function, and Bioinformatics , vol.62 , Issue.4 , pp. 1125-1132
    • Cheng, J.1    Randall, A.2    Baldi, P.3
  • 111
    • 0034460414 scopus 로고    scopus 로고
    • PoPMuSiC, an algorithm for predicting protein mutant stability changes. Application to prion proteins
    • 10.1093/protein/13.12.849, 11239084
    • Gilis D, Rooman M. PoPMuSiC, an algorithm for predicting protein mutant stability changes. Application to prion proteins. Protein Engineering 2000, 13(12):849-856. 10.1093/protein/13.12.849, 11239084.
    • (2000) Protein Engineering , vol.13 , Issue.12 , pp. 849-856
    • Gilis, D.1    Rooman, M.2
  • 112
    • 79959942908 scopus 로고    scopus 로고
    • SDM-a server for predicting effects of mutations on protein stability and malfunction
    • 3125769, 21593128
    • Worth CL, Preissner R, Blundell TL. SDM-a server for predicting effects of mutations on protein stability and malfunction. Nucleic Acids Res 2011, 39(suppl 2):W215-W222. 3125769, 21593128.
    • (2011) Nucleic Acids Res , vol.39 , Issue.SUPPL. 2
    • Worth, C.L.1    Preissner, R.2    Blundell, T.L.3
  • 113
    • 23144461249 scopus 로고    scopus 로고
    • I-Mutant2. 0: predicting stability changes upon mutation from the protein sequence or structure
    • 1160136, 15980478
    • Capriotti E, Fariselli P, Casadio R. I-Mutant2. 0: predicting stability changes upon mutation from the protein sequence or structure. Nucleic Acids Res 2005, 33(suppl 2):W306-W310. 1160136, 15980478.
    • (2005) Nucleic Acids Res , vol.33 , Issue.SUPPL. 2
    • Capriotti, E.1    Fariselli, P.2    Casadio, R.3
  • 114
    • 33747838537 scopus 로고    scopus 로고
    • CUPSAT: prediction of protein stability upon point mutations
    • 1538884, 16845001
    • Parthiban V, Gromiha MM, Schomburg D. CUPSAT: prediction of protein stability upon point mutations. Nucleic Acids Res 2006, 34(suppl 2):W239-W242. 1538884, 16845001.
    • (2006) Nucleic Acids Res , vol.34 , Issue.SUPPL. 2
    • Parthiban, V.1    Gromiha, M.M.2    Schomburg, D.3
  • 115
    • 77952279379 scopus 로고    scopus 로고
    • SeqRate: sequence-based protein folding type classification and rates prediction
    • Lin G, Wang Z, Xu D, Cheng J. SeqRate: sequence-based protein folding type classification and rates prediction. BMC Bioinforma 2010, 11(Suppl 3):S1.
    • (2010) BMC Bioinforma , vol.11 , Issue.SUPPL. 3
    • Lin, G.1    Wang, Z.2    Xu, D.3    Cheng, J.4
  • 116
    • 83355164022 scopus 로고    scopus 로고
    • MSACompro: Protein Multiple Sequence Alignment Using Predicted Secondary Structure, Solvent Accessibility, and Residue-Residue Contacts
    • Deng X, Cheng J. MSACompro: Protein Multiple Sequence Alignment Using Predicted Secondary Structure, Solvent Accessibility, and Residue-Residue Contacts. BMC Bioinforma 2011, 12:472.
    • (2011) BMC Bioinforma , vol.12 , pp. 472
    • Deng, X.1    Cheng, J.2
  • 118
    • 44449173642 scopus 로고    scopus 로고
    • HMMEditor: a visual editing tool for profile hidden Markov model
    • 10.1186/1471-2164-9-S1-S8, 2559898, 18831799
    • Dai J, Cheng J. HMMEditor: a visual editing tool for profile hidden Markov model. BMC genomics 2008, 9(Suppl 1):S8. 10.1186/1471-2164-9-S1-S8, 2559898, 18831799.
    • (2008) BMC genomics , vol.9 , Issue.SUPPL. 1
    • Dai, J.1    Cheng, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.