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Volumn 1415, Issue , 2016, Pages 463-476

Protein residue contacts and prediction methods

(2)  Adhikari, Badri a   Cheng, Jianlin a  

a NONE

Author keywords

Deep learning; Protein contact prediction methods

Indexed keywords

AMINO ACID; GLOBULAR PROTEIN; PROTEIN; PROTEIN BINDING;

EID: 84984984288     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-3572-7_24     Document Type: Chapter
Times cited : (24)

References (58)
  • 2
    • 1642464839 scopus 로고    scopus 로고
    • Protein structure prediction using Rosetta
    • Ludwig B, Michael LJ, Academic, Cambridge, MA
    • Rohl CA, Strauss CEM, Misura KMS, Baker D (2004) Protein structure prediction using Rosetta. In: Ludwig B, Michael LJ (eds) Methods in enzymology, vol 383. Academic, Cambridge, MA, pp 66–93, http://dx.doi. org/10.1016/S0076-6879(04)83004-0
    • (2004) Methods in Enzymology , vol.383 , pp. 66-93
    • Rohl, C.A.1    Strauss, C.2    Misura, K.3    Baker, D.4
  • 3
    • 84898619057 scopus 로고    scopus 로고
    • De Novo Structure Prediction of Globular Proteins Aided by Sequence Variation-Derived Contacts
    • Kosciolek T, Jones DT (2014) De Novo Structure Prediction of Globular Proteins Aided by Sequence Variation-Derived Contacts. PLoS One 9 (3): e92197
    • (2014) Plos One , vol.9 , Issue.3
    • Kosciolek, T.1    Jones, D.T.2
  • 6
    • 0033628817 scopus 로고    scopus 로고
    • Protein folding using contact maps
    • Vendruscolo M, Domany E (2000) Protein folding using contact maps. Vitam Horm 58: 171–212
    • (2000) Vitam Horm , vol.58 , pp. 171-212
    • Vendruscolo, M.1    Domany, E.2
  • 7
    • 0030443368 scopus 로고    scopus 로고
    • Protein fold recognition and dynamics in the space of contact maps
    • Mirny L, Domany E (1996) Protein fold recognition and dynamics in the space of contact maps. Protein Struct Funct Bioinform 26 (4): 391–410. doi: 10.1002/(SICI)1097-0134(199612)26:4<391::AID-PROT3>3.0.CO;2-F
    • (1996) Protein Struct Funct Bioinform , vol.26 , Issue.4 , pp. 391-410
    • Mirny, L.1    Domany, E.2
  • 8
    • 1642464839 scopus 로고    scopus 로고
    • Protein structure prediction using Rosetta
    • Rohl CA, Strauss CE, Misura KM, Baker D (2004) Protein structure prediction using Rosetta. Methods Enzymol 383: 66–93. doi: 10.1016/s0076-6879(04)83004-0
    • (2004) Methods Enzymol , vol.383 , pp. 66-93
    • Rohl, C.A.1    Strauss, C.E.2    Misura, K.M.3    Baker, D.4
  • 9
    • 0035698619 scopus 로고    scopus 로고
    • Predicting novel protein folds by using FRAGFOLD
    • Jones DT (2001) Predicting novel protein folds by using FRAGFOLD. Proteins 5: 127–132
    • (2001) Proteins , vol.5 , pp. 127-132
    • Jones, D.T.1
  • 11
    • 47049101751 scopus 로고    scopus 로고
    • Using inferred residue contacts to distinguish between correct and incorrect protein models
    • Miller CS, Eisenberg D (2008) Using inferred residue contacts to distinguish between correct and incorrect protein models. Bioinformatics 24 (14): 1575–1582. doi: 10.1093/bioinformatics/btn248
    • (2008) Bioinformatics , vol.24 , Issue.14 , pp. 1575-1582
    • Miller, C.S.1    Eisenberg, D.2
  • 12
    • 79958078892 scopus 로고    scopus 로고
    • APOLLO: A quality assessment service for single and multiple protein models
    • Wang Z, Eickholt J, Cheng J (2011) APOLLO: a quality assessment service for single and multiple protein models. Bioinformatics 27 (12): 1715–1716. doi: 10.1093/bioinformatics/btr268
    • (2011) Bioinformatics , vol.27 , Issue.12 , pp. 1715-1716
    • Wang, Z.1    Eickholt, J.2    Cheng, J.3
  • 14
    • 84856090271 scopus 로고    scopus 로고
    • PSICOV: Precise structural contact prediction using sparse inverse covariance estimation on large multiple sequence alignments
    • Jones DT, Buchan DW, Cozzetto D, Pontil M (2012) PSICOV: precise structural contact prediction using sparse inverse covariance estimation on large multiple sequence alignments. Bioinformatics 28 (2): 184–190
    • (2012) Bioinformatics , vol.28 , Issue.2 , pp. 184-190
    • Jones, D.T.1    Buchan, D.W.2    Cozzetto, D.3    Pontil, M.4
  • 15
    • 0034635337 scopus 로고    scopus 로고
    • Exploring local and non-local interactions for protein stability by structural motif engineering
    • Niggemann M, Steipe B (2000) Exploring local and non-local interactions for protein stability by structural motif engineering. J Mol Biol 296 (1): 181–195. doi: 10.1006/jmbi.1999.3385
    • (2000) J Mol Biol , vol.296 , Issue.1 , pp. 181-195
    • Niggemann, M.1    Steipe, B.2
  • 18
    • 84885355205 scopus 로고    scopus 로고
    • A study and benchmark of DNcon: A method for protein residueresidue contact prediction using deep networks
    • Eickholt J, Cheng J (2013) A study and benchmark of DNcon: a method for protein residueresidue contact prediction using deep networks. BMC Bioinformatics 14 (Suppl 14): S12
    • (2013) BMC Bioinformatics , vol.14 , pp. S12
    • Eickholt, J.1    Cheng, J.2
  • 21
    • 84870415234 scopus 로고    scopus 로고
    • Predicting protein residue–residue contacts using deep networks and boosting
    • Eickholt J, Cheng J (2012) Predicting protein residue–residue contacts using deep networks and boosting. Bioinformatics 28 (23): 3066–3072
    • (2012) Bioinformatics , vol.28 , Issue.23 , pp. 3066-3072
    • Eickholt, J.1    Cheng, J.2
  • 22
    • 84929144039 scopus 로고    scopus 로고
    • MetaPSICOV: Combining coevolution methods for accurate prediction of contacts and long range hydrogen bonding in proteins
    • Jones DT, Singh T, Kosciolek T, Tetchner S (2015) MetaPSICOV: combining coevolution methods for accurate prediction of contacts and long range hydrogen bonding in proteins. Bioinformatics 31 (7): 999–1006. doi: 10.1093/bioinformatics/btu791
    • (2015) Bioinformatics , vol.31 , Issue.7 , pp. 999-1006
    • Jones, D.T.1    Singh, T.2    Kosciolek, T.3    Tetchner, S.4
  • 23
    • 84908542331 scopus 로고    scopus 로고
    • Combining physicochemical and evolutionary information for protein contact prediction
    • Schneider M, Brock O (2014) Combining physicochemical and evolutionary information for protein contact prediction. PLoS One 9 (10): e108438. doi: 10.1371/journal.pone.0108438
    • (2014) Plos One , vol.9 , Issue.10
    • Schneider, M.1    Brock, O.2
  • 24
    • 84867316765 scopus 로고    scopus 로고
    • Deep architectures for protein contact map prediction
    • Di Lena P, Nagata K, Baldi P (2012) Deep architectures for protein contact map prediction. Bioinformatics 28 (19): 2449–2457. doi: 10.1093/bioinformatics/bts475
    • (2012) Bioinformatics , vol.28 , Issue.19 , pp. 2449-2457
    • Di Lena, P.1    Nagata, K.2    Baldi, P.3
  • 25
    • 65549127269 scopus 로고    scopus 로고
    • Using multi-data hidden Markov models trained on local neighborhoods of protein structure to predict residue–residue contacts
    • Björkholm P, Daniluk P, Kryshtafovych A, Fidelis K, Andersson R, Hvidsten TR (2009) Using multi-data hidden Markov models trained on local neighborhoods of protein structure to predict residue–residue contacts. Bioinformatics 25 (10): 1264–1270. doi: 10.1093/bioinformatics/btp149
    • (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
  • 26
    • 84912100015 scopus 로고    scopus 로고
    • Improved contact predictions using the recognition of protein like contact patterns
    • Skwark MJ, Raimondi D, Michel M, Elofsson A (2014) Improved contact predictions using the recognition of protein like contact patterns. PLoS Comput Biol 10 (11): e1003889
    • (2014) Plos Comput Biol , vol.10 , Issue.11
    • Skwark, M.J.1    Raimondi, D.2    Michel, M.3    Elofsson, A.4
  • 27
    • 84929144039 scopus 로고    scopus 로고
    • MetaPSICOV: Combining coevolution methods for accurate prediction of contacts and long range hydrogen bonding in proteins
    • Jones DT, Singh T, Kosciolek T, Tetchner S (2014) MetaPSICOV: combining coevolution methods for accurate prediction of contacts and long range hydrogen bonding in proteins. Bioinformatics 31 (7): 999–1006, btu791
    • (2014) Bioinformatics , vol.31 , Issue.7 , pp. 999-1006
    • Jones, D.T.1    Singh, T.2    Kosciolek, T.3    Tetchner, S.4
  • 28
    • 67849110005 scopus 로고    scopus 로고
    • NNcon: Improved protein contact map prediction using 2D-recursive neural networks
    • Tegge AN, Wang Z, Eickholt J, Cheng J (2009) NNcon: improved protein contact map prediction using 2D-recursive neural networks. Nucleic Acids Res 37 (suppl 2): W515–W518
    • (2009) Nucleic Acids Res , vol.37 , pp. W515-W518
    • Tegge, A.N.1    Wang, Z.2    Eickholt, J.3    Cheng, J.4
  • 29
    • 66249107719 scopus 로고    scopus 로고
    • Predicting residue–residue contact maps by a two-layer, integrated neural-network method
    • Xue B, Faraggi E, Zhou Y (2009) Predicting residue–residue contact maps by a two-layer, integrated neural-network method. Protein Struct Funct Bioinform 76 (1): 176–183. doi: 10.1002/prot.22329
    • (2009) Protein Struct Funct Bioinform , vol.76 , Issue.1 , pp. 176-183
    • Xue, B.1    Faraggi, E.2    Zhou, Y.3
  • 30
    • 36749031067 scopus 로고    scopus 로고
    • Contact prediction using mutual information and neural nets
    • Shackelford G, Karplus K (2007) Contact prediction using mutual information and neural nets. Protein Struct Funct Bioinform 69 (S8): 159–164. doi: 10.1002/prot.21791
    • (2007) Protein Struct Funct Bioinform , vol.69 , Issue.S8 , pp. 159-164
    • Shackelford, G.1    Karplus, K.2
  • 31
    • 0033047710 scopus 로고    scopus 로고
    • A neural network based predictor of residue contacts in proteins
    • Fariselli P, Casadio R (1999) A neural network based predictor of residue contacts in proteins. Protein Eng 12 (1): 15–21. doi: 10.1093/protein/12.1.15
    • (1999) Protein Eng , vol.12 , Issue.1 , pp. 15-21
    • Fariselli, P.1    Casadio, R.2
  • 32
    • 0035700864 scopus 로고    scopus 로고
    • Progress in predicting inter-residue contacts of proteins with neural networks and correlated mutations
    • Fariselli P, Olmea O, Valencia A, Casadio R (2001) Progress in predicting inter-residue contacts of proteins with neural networks and correlated mutations. Proteins 5: 157–162
    • (2001) Proteins , vol.5 , pp. 157-162
    • Fariselli, P.1    Olmea, O.2    Valencia, A.3    Casadio, R.4
  • 33
    • 24744453057 scopus 로고    scopus 로고
    • Striped sheets and protein contact prediction
    • MacCallum RM (2004) Striped sheets and protein contact prediction. Bioinformatics 20 (Suppl 1): i224–i231. doi: 10.1093/bioinformatics/bth913
    • (2004) Bioinformatics , vol.20 , pp. i224-i231
    • Maccallum, R.M.1
  • 34
    • 77952597524 scopus 로고    scopus 로고
    • Prediction of protein long-range contacts using an ensemble of genetic algorithm classifiers with sequence profile centers
    • Chen P, Li J (2010) Prediction of protein long-range contacts using an ensemble of genetic algorithm classifiers with sequence profile centers. BMC Struct Biol 10 (Suppl 1): S2
    • (2010) BMC Struct Biol , vol.10 , pp. S2
    • Chen, P.1    Li, J.2
  • 35
    • 83255194562 scopus 로고    scopus 로고
    • Predicting residue–residue contacts using random forest models
    • Li Y, Fang Y, Fang J (2011) Predicting residue–residue contacts using random forest models. Bioinformatics 27 (24): 3379–3384. doi: 10.1093/bioinformatics/btr579
    • (2011) Bioinformatics , vol.27 , Issue.24 , pp. 3379-3384
    • Li, Y.1    Fang, Y.2    Fang, J.3
  • 36
    • 69849084410 scopus 로고    scopus 로고
    • Prediction of protein ß-residue contacts by Markov logic networks with grounding-specific weights
    • Lippi M, Frasconi P (2009) Prediction of protein ß-residue contacts by Markov logic networks with grounding-specific weights. Bioinformatics 25 (18): 2326–2333. doi: 10.1093/bioinformatics/btp421
    • (2009) Bioinformatics , vol.25 , Issue.18 , pp. 2326-2333
    • Lippi, M.1    Frasconi, P.2
  • 37
    • 34247247779 scopus 로고    scopus 로고
    • Improved residue contact prediction using support vector machines and a large feature set
    • Cheng J, Baldi P (2007) Improved residue contact prediction using support vector machines and a large feature set. BMC Bioinformatics 8 (1): 113
    • (2007) BMC Bioinformatics , vol.8 , Issue.1 , pp. 113
    • Cheng, J.1    Baldi, P.2
  • 38
    • 41349114023 scopus 로고    scopus 로고
    • A comprehensive assessment of sequence-based and templatebased methods for protein contact prediction
    • Wu S, Zhang Y (2008) A comprehensive assessment of sequence-based and templatebased methods for protein contact prediction. Bioinformatics 24 (7): 924–931. doi: 10.1093/ bioinformatics/btn069
    • (2008) Bioinformatics , vol.24 , Issue.7 , pp. 924-931
    • Wu, S.1    Zhang, Y.2
  • 39
    • 0028084754 scopus 로고
    • Can three-dimensional contacts in protein structures be predicted by analysis of correlated mutations?
    • Shindyalov IN, Kolchanov NA, Sander C (1994) Can three-dimensional contacts in protein structures be predicted by analysis of correlated mutations? Protein Eng 7 (3): 349–358
    • (1994) Protein Eng , vol.7 , Issue.3 , pp. 349-358
    • Shindyalov, I.N.1    Kolchanov, N.A.2    Sander, C.3
  • 40
    • 0028295169 scopus 로고
    • Correlated mutations and residue contacts in proteins
    • Gobel U, Sander C, Schneider R, Valencia A (1994) Correlated mutations and residue contacts in proteins. Proteins 18 (4): 309–317. doi: 10.1002/prot.340180402
    • (1994) Proteins , vol.18 , Issue.4 , pp. 309-317
    • Gobel, U.1    Sander, C.2    Schneider, R.3    Valencia, A.4
  • 41
    • 0030627941 scopus 로고    scopus 로고
    • Improving contact predictions by the combination of correlated mutations and other sources of sequence information
    • Olmea O, Valencia A (1997) Improving contact predictions by the combination of correlated mutations and other sources of sequence information. Folding Des 2 (Suppl 1): S25–S32. doi: 10.1016/S1359-0278(97)00060-6, http://dx.doi.org/
    • (1997) Folding Des , Issue.2 , pp. S25-S32
    • Olmea, O.1    Valencia, A.2
  • 42
    • 0008117663 scopus 로고    scopus 로고
    • Correlated mutations in models of protein sequences: Phylogenetic and structural effects
    • Seillier-Moiseiwitsch F (ed), Lecture Notes--Monograph Series. Institute of Mathematical Statistics, Hayward, CA
    • Lapedes AS, Giraud B, Liu L, Stormo GD (1999) Correlated mutations in models of protein sequences: phylogenetic and structural effects. In: Seillier-Moiseiwitsch F (ed) Statistics in molecular biology and genetics, vol 33, Lecture Notes--Monograph Series. Institute of Mathematical Statistics, Hayward, CA, pp 236–256. doi: 10.1214/lnms/1215455556
    • (1999) Statistics in Molecular Biology and Genetics , vol.33 , pp. 236-256
    • Lapedes, A.S.1    Giraud, B.2    Liu, L.3    Stormo, G.D.4
  • 43
    • 58549114185 scopus 로고    scopus 로고
    • Identification of direct residue contacts in protein–protein interaction by message passing
    • Weigt M, White RA, Szurmant H, Hoch JA, Hwa T (2009) Identification of direct residue contacts in protein–protein interaction by message passing. Proc Natl Acad Sci 106 (1): 67–72. doi: 10.1073/pnas.0805923106
    • (2009) Proc Natl Acad Sci , vol.106 , Issue.1 , pp. 67-72
    • Weigt, M.1    White, R.A.2    Szurmant, H.3    Hoch, J.A.4    Hwa, T.5
  • 44
    • 84977501890 scopus 로고    scopus 로고
    • Opportunities and limitations in applying coevolution-derived contacts to protein structure prediction
    • Tetchner S, Kosciolek T, Jones DT (2014) Opportunities and limitations in applying coevolution-derived contacts to protein structure prediction. Bio Algorithm Med Syst 10 (4): 243–254
    • (2014) Bio Algorithm Med Syst , vol.10 , Issue.4 , pp. 243-254
    • Tetchner, S.1    Kosciolek, T.2    Jones, D.T.3
  • 46
    • 84872521100 scopus 로고    scopus 로고
    • Improved contact prediction in proteins: Using pseudolikelihoods to infer Potts models
    • Ekeberg M, Lövkvist C, Lan Y, Weigt M, Aurell E (2013) Improved contact prediction in proteins: using pseudolikelihoods to infer Potts models. Phys Rev E 87 (1): 012707
    • (2013) Phys Rev E , vol.87 , Issue.1
    • Ekeberg, M.1    Lövkvist, C.2    Lan, Y.3    Weigt, M.4    Aurell, E.5
  • 47
    • 84905637666 scopus 로고    scopus 로고
    • Fast pseudolikelihood maximization for directcoupling analysis of protein structure from many homologous amino-acid sequences
    • Ekeberg M, Hartonen T, Aurell E (2014) Fast pseudolikelihood maximization for directcoupling analysis of protein structure from many homologous amino-acid sequences. J Comput Phys 276: 341–356. doi: 10.1016/j.jcp.2014.07.024, http://dx.doi.org/
    • (2014) J Comput Phys , vol.276 , pp. 341-356
    • Ekeberg, M.1    Hartonen, T.2    Aurell, E.3
  • 48
    • 84908313189 scopus 로고    scopus 로고
    • Improving contact prediction along three dimensions
    • Feinauer C, Skwark MJ, Pagnani A, Aurell E (2014) Improving contact prediction along three dimensions. PLoS Comput Biol 10 (10): e1003847. doi: 10.1371/journal.pcbi.1003847
    • (2014) Plos Comput Biol , vol.10 , Issue.10
    • Feinauer, C.1    Skwark, M.J.2    Pagnani, A.3    Aurell, E.4
  • 49
    • 84884603324 scopus 로고    scopus 로고
    • Assessing the utility of coevolution-based residue–residue contact predictions in a sequenceand structure-rich era
    • Kamisetty H, Ovchinnikov S, Baker D (2013) Assessing the utility of coevolution-based residue–residue contact predictions in a sequenceand structure-rich era. Proc Natl Acad Sci 110 (39): 15674–15679. doi: 10.1073/pnas.1314045110
    • (2013) Proc Natl Acad Sci , vol.110 , Issue.39 , pp. 15674-15679
    • Kamisetty, H.1    Ovchinnikov, S.2    Baker, D.3
  • 50
    • 84902081454 scopus 로고    scopus 로고
    • Multidimensional mutual information methods for the analysis of covariation in multiple sequence alignments
    • Clark GW, Ackerman SH, Tillier ER, Gatti DL (2014) Multidimensional mutual information methods for the analysis of covariation in multiple sequence alignments. BMC Bioinformatics 15 (1): 157
    • (2014) BMC Bioinformatics , vol.15 , Issue.1 , pp. 157
    • Clark, G.W.1    Ackerman, S.H.2    Tillier, E.R.3    Gatti, D.L.4
  • 51
    • 33645792604 scopus 로고    scopus 로고
    • Physically realistic homology models built with ROSETTA can be more accurate than their templates
    • Misura KM, Chivian D, Rohl CA, Kim DE, Baker D (2006) Physically realistic homology models built with ROSETTA can be more accurate than their templates. Proc Natl Acad Sci U S A 103 (14): 5361–5366. doi: 10.1073/pnas.0509355103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.14 , pp. 5361-5366
    • Misura, K.M.1    Chivian, D.2    Rohl, C.A.3    Kim, D.E.4    Baker, D.5
  • 53
    • 84867301175 scopus 로고    scopus 로고
    • Contact map prediction using a largescale ensemble of rule sets and the fusion of multiple predicted structural features
    • Bacardit J, Widera P, Márquez-Chamorro A, Divina F, Aguilar-Ruiz JS, Krasnogor N (2012) Contact map prediction using a largescale ensemble of rule sets and the fusion of multiple predicted structural features. Bioinformatics. doi: 10.1093/bioinformatics/bts472
    • (2012) Bioinformatics
    • Bacardit, J.1    Widera, P.2    Márquez-Chamorro, A.3    Divina, F.4    Aguilar-Ruiz, J.S.5    Krasnogor, N.6
  • 54
    • 33745610096 scopus 로고    scopus 로고
    • A twostage approach for improved prediction of residue contact maps
    • Vullo A, Walsh I, Pollastri G (2006) A twostage approach for improved prediction of residue contact maps. BMC Bioinformatics 7: 180. doi: 10.1186/1471-2105-7-180
    • (2006) BMC Bioinformatics , vol.7 , pp. 180
    • Vullo, A.1    Walsh, I.2    Pollastri, G.3
  • 55
    • 84911444768 scopus 로고    scopus 로고
    • CCMpred—fast and precise prediction of protein residue–residue contacts from correlated mutations
    • Seemayer S, Gruber M, Söding J (2014) CCMpred—fast and precise prediction of protein residue–residue contacts from correlated mutations. Bioinformatics 30 (21): 3128–3130
    • (2014) Bioinformatics , vol.30 , Issue.21 , pp. 3128-3130
    • Seemayer, S.1    Gruber, M.2    Söding, J.3
  • 56
    • 84899072164 scopus 로고    scopus 로고
    • FreeContact: Fast and free software for protein contact prediction from residue co-evolution
    • Kaján L, Hopf TA, Marks DS, Rost B (2014) FreeContact: fast and free software for protein contact prediction from residue co-evolution. BMC Bioinformatics 15 (1): 85
    • (2014) BMC Bioinformatics , vol.15 , Issue.1 , pp. 85
    • Kaján, L.1    Hopf, T.A.2    Marks, D.S.3    Rost, B.4
  • 57
    • 84868563621 scopus 로고    scopus 로고
    • Reliable and robust detection of coevolving protein residues
    • Jeong CS, Kim D (2012) Reliable and robust detection of coevolving protein residues. Protein Eng Des Sel 25 (11): 705–713. doi: 10.1093/protein/gzs081
    • (2012) Protein Eng Des Sel , vol.25 , Issue.11 , pp. 705-713
    • Jeong, C.S.1    Kim, D.2
  • 58
    • 65449172344 scopus 로고    scopus 로고
    • Correction for phylogeny, small number of observations and data redundancy improves the identification of coevolving amino acid pairs using mutual information
    • Buslje CM, Santos J, Delfino JM, Nielsen M (2009) Correction for phylogeny, small number of observations and data redundancy improves the identification of coevolving amino acid pairs using mutual information. Bioinformatics 25 (9): 1125–1131. doi: 10.1093/bioinformatics/btp135
    • (2009) Bioinformatics , vol.25 , Issue.9 , pp. 1125-1131
    • Buslje, C.M.1    Santos, J.2    Delfino, J.M.3    Nielsen, M.4


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