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Volumn 8, Issue 4, 2016, Pages 751-760

Length-independent structural similarities enrich the antibody CDR canonical class model

Author keywords

Canonical class; Clustering; Complementarity determining regions; Length independent; Loop modeling

Indexed keywords

ANTIBODY COMBINING SITE; AREA UNDER THE CURVE; ARTICLE; CANONICAL ANALYSIS; CLUSTER ANALYSIS; COMPLEMENTARITY DETERMINING REGION; DYNAMIC TIME WARPING; GERMLINE STEM CELL; HUMAN; HUMAN CELL; INFORMATION PROCESSING; METHODOLOGY; MODEL; NEXT GENERATION SEQUENCING; NONHUMAN; PREDICTION; RECEIVER OPERATING CHARACTERISTIC; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; CLASSIFICATION; HIGH THROUGHPUT SCREENING; MOLECULAR GENETICS; MOLECULAR MODEL;

EID: 84971384297     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.1080/19420862.2016.1158370     Document Type: Article
Times cited : (44)

References (57)
  • 2
    • 84893831480 scopus 로고    scopus 로고
    • The promise and challenge of high-throughput sequencing of the antibody repertoire
    • 24441474
    • G.Georgiou, G.C.Ippolito, J.Beausang, C.E.Busse, H.Wardemann, S.R.Quake. The promise and challenge of high-throughput sequencing of the antibody repertoire. Nat Biotechnol 2014; 32:158-68; PMID:24441474; PMID:24214988; http://dx.doi.org/10.1038/nbt.2782
    • (2014) Nat Biotechnol , vol.32 , pp. 158-168
    • Georgiou, G.1    Ippolito, G.C.2    Beausang, J.3    Busse, C.E.4    Wardemann, H.5    Quake, S.R.6
  • 3
    • 0035171080 scopus 로고    scopus 로고
    • Kabat Database and its applications: future directions
    • 11125092
    • G.Johnson, T.T.Wu. Kabat Database and its applications: future directions. Nucleic Acids Res 2001; 29:205-6; PMID:11125092; http://dx.doi.org/10.1093/nar/29.1.205
    • (2001) Nucleic Acids Res , vol.29 , pp. 205-206
    • Johnson, G.1    Wu, T.T.2
  • 4
    • 33644874839 scopus 로고    scopus 로고
    • IMGT/LIGM-DB, the IMGT comprehensive database of immunoglobulin and T cell receptor nucleotide sequences
    • 16381979
    • V.Giudicelli, P.Duroux, C.Ginestoux, G.Folch, J.Jabado-Michaloud, D.Chaume, M.-P.Lefranc. IMGT/LIGM-DB, the IMGT comprehensive database of immunoglobulin and T cell receptor nucleotide sequences. Nucleic Acids Res 2006; 34:D781-4; PMID:16381979; http://dx.doi.org/10.1093/nar/gkj088
    • (2006) Nucleic Acids Res , vol.34 , pp. D781-D784
    • Giudicelli, V.1    Duroux, P.2    Ginestoux, C.3    Folch, G.4    Jabado-Michaloud, J.5    Chaume, D.6    Lefranc, M.-P.7
  • 6
    • 13444301423 scopus 로고    scopus 로고
    • VBASE2, an integrative V gene database
    • I.Retter, H.H.Althaus, R.Münch, W.Müller. VBASE2, an integrative V gene database. Nucleic Acids Res 2005; 33:671-4; PMID:15608286; http://dx.doi.org/10.1093/nar/gki088
    • (2005) Nucleic Acids Res , vol.33 , pp. 671-674
    • Retter, I.1    Althaus, H.H.2    Münch, R.3    Müller, W.4
  • 7
    • 84859572771 scopus 로고    scopus 로고
    • A database of immunoglobulins with integrated tools: DIGIT
    • A.Chailyan, A.Tramontano, P.Marcatili. A database of immunoglobulins with integrated tools: DIGIT. Nucleic Acids Res 2012; 40:1230-4; PMID:22080506; http://dx.doi.org/10.1093/nar/gkr806
    • (2012) Nucleic Acids Res , vol.40 , pp. 1230-1234
    • Chailyan, A.1    Tramontano, A.2    Marcatili, P.3
  • 8
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • 3681981
    • C.Chothia, A.M.Lesk. Canonical structures for the hypervariable regions of immunoglobulins. J Mol Biol 1987; 196:901-17; PMID:3681981; http://dx.doi.org/10.1016/0022-2836(87)90412-8
    • (1987) J Mol Biol , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 11
    • 0028676261 scopus 로고
    • Structural conservation of hypervariable regions in immunoglobulins evolution
    • 7773781
    • S.Barre, A.S.Greenberg, M.F.Flajnik, C.Chothia. Structural conservation of hypervariable regions in immunoglobulins evolution. Nat Struct Biol 1994; 1:915-20; PMID:7773781; http://dx.doi.org/10.1038/nsb1294-915
    • (1994) Nat Struct Biol , vol.1 , pp. 915-920
    • Barre, S.1    Greenberg, A.S.2    Flajnik, M.F.3    Chothia, C.4
  • 12
    • 0029159770 scopus 로고
    • The structural repertoire of the human V kappa domain
    • 7556106
    • I.M.Tomlinson, J.P.Cox, E.Gherardi, A.M.Lesk, C.Chothia. The structural repertoire of the human V kappa domain. EMBO J 1995; 14:4628-38; PMID:7556106
    • (1995) EMBO J , vol.14 , pp. 4628-4638
    • Tomlinson, I.M.1    Cox, J.P.2    Gherardi, E.3    Lesk, A.M.4    Chothia, C.5
  • 13
    • 0030589039 scopus 로고    scopus 로고
    • Structural families in loops of homologous proteins: automatic classification, modelling and application to antibodies
    • 8947577
    • A.C.R.Martin, J.M.Thornton. Structural families in loops of homologous proteins: automatic classification, modelling and application to antibodies. J Mol Biol 1996; 263:800-15; PMID:8947577; http://dx.doi.org/10.1006/jmbi.1996.0617
    • (1996) J Mol Biol , vol.263 , pp. 800-815
    • Martin, A.C.R.1    Thornton, J.M.2
  • 14
    • 0031405336 scopus 로고    scopus 로고
    • Antibody structure, prediction and redesign
    • 9468606
    • V.Morea, A.Tramontano, M.Rustici, C.Chothia, A.M.Lesk. Antibody structure, prediction and redesign. Biophys Chem 1997; 68:9-16; PMID:9468606; http://dx.doi.org/10.1016/S0301-4622(96)02266-1
    • (1997) Biophys Chem , vol.68 , pp. 9-16
    • Morea, V.1    Tramontano, A.2    Rustici, M.3    Chothia, C.4    Lesk, A.M.5
  • 15
    • 0031558798 scopus 로고    scopus 로고
    • Standard conformations for the canonical structures of immunoglobulins
    • 9367782
    • B.Al-Lazikani, A.M.Lesk, C.Chothia. Standard conformations for the canonical structures of immunoglobulins. J Mol Biol 1997; 273:927-48; PMID:9367782; http://dx.doi.org/10.1006/jmbi.1997.1354
    • (1997) J Mol Biol , vol.273 , pp. 927-948
    • Al-Lazikani, B.1    Lesk, A.M.2    Chothia, C.3
  • 16
    • 0034426867 scopus 로고    scopus 로고
    • Antibody modeling: implications for engineering and design
    • 10694450
    • V.Morea, A.M.Lesk, A.Tramontano. Antibody modeling: implications for engineering and design. Methods 2000; 20:267-79; PMID:10694450; http://dx.doi.org/10.1006/meth.1999.0921
    • (2000) Methods , vol.20 , pp. 267-279
    • Morea, V.1    Lesk, A.M.2    Tramontano, A.3
  • 17
    • 79251598995 scopus 로고    scopus 로고
    • A new clustering of antibody CDR loop conformations
    • 21035459
    • B.North, A.Lehmann, R.L.DunbrackJr. A new clustering of antibody CDR loop conformations. J Mol Biol 2011; 406:228-56; PMID:21035459; http://dx.doi.org/10.1016/j.jmb.2010.10.030
    • (2011) J Mol Biol , vol.406 , pp. 228-256
    • North, B.1    Lehmann, A.2    Dunbrack, R.L.3
  • 18
    • 84903838044 scopus 로고    scopus 로고
    • A complete, multi-level conformational clustering of antibody complementarity-determining regions
    • 25071986
    • D.Nikoloudis, J.E.Pitts, J.W.Saldanha. A complete, multi-level conformational clustering of antibody complementarity-determining regions. PeerJ 2014; 2:e456; PMID:25071986; http://dx.doi.org/10.7717/peerj.456
    • (2014) PeerJ , vol.2
    • Nikoloudis, D.1    Pitts, J.E.2    Saldanha, J.W.3
  • 19
    • 84946071579 scopus 로고    scopus 로고
    • PyIgClassify: a database of antibody CDR structural classifications
    • J.Adolf-Bryfogle, Q.Xu, B.North, A.Lehmann, R.L.DunbrackJr. PyIgClassify: a database of antibody CDR structural classifications. Nucleic Acids Res 2015; 43:432-8; http://dx.doi.org/10.1093/nar/gku1106
    • (2015) Nucleic Acids Res , vol.43 , pp. 432-438
    • Adolf-Bryfogle, J.1    Xu, Q.2    North, B.3    Lehmann, A.4    Dunbrack, R.L.5
  • 22
    • 65249106714 scopus 로고    scopus 로고
    • Systematic classification of CDR-L3 in antibodies: Implications of the light chain subtypes and the VL-VH interface
    • D.Kuroda, H.Shirai, M.Kobori, H.Nakamura. Systematic classification of CDR-L3 in antibodies: Implications of the light chain subtypes and the VL-VH interface. Proteins Struct Funct Bioinforma 2009; 75:139-46; PMID:18798566; http://dx.doi.org/10.1002/prot.22230
    • (2009) Proteins Struct Funct Bioinforma , vol.75 , pp. 139-146
    • Kuroda, D.1    Shirai, H.2    Kobori, M.3    Nakamura, H.4
  • 23
    • 84904464590 scopus 로고    scopus 로고
    • Canonical structures of short CDR-L3 in antibodies
    • A.Teplyakov, G.L.Gilliland. Canonical structures of short CDR-L3 in antibodies. Proteins Struct Funct Bioinforma 2014; 82:1668-73; http://dx.doi.org/10.1002/prot.24559
    • (2014) Proteins Struct Funct Bioinforma , vol.82 , pp. 1668-1673
    • Teplyakov, A.1    Gilliland, G.L.2
  • 24
    • 0028984808 scopus 로고
    • Prediction of hypervariable CDR-H3 loop structures in antibodies
    • 7567924
    • M.Reczko, A.C.R.Martin, H.Bohr, S.Suhai. Prediction of hypervariable CDR-H3 loop structures in antibodies. Protein Eng 1995; 8:389-95; PMID:7567924; http://dx.doi.org/10.1093/protein/8.4.389
    • (1995) Protein Eng , vol.8 , pp. 389-395
    • Reczko, M.1    Martin, A.C.R.2    Bohr, H.3    Suhai, S.4
  • 25
    • 0030577371 scopus 로고    scopus 로고
    • Structural classification of CDR-H3 in antibodies
    • 8980108
    • H.Shirai, A.Kidera, H.Nakamura. Structural classification of CDR-H3 in antibodies. FEBS Lett 1996; 399:1-8; PMID:8980108; http://dx.doi.org/10.1016/S0014-5793(96)01252-5
    • (1996) FEBS Lett , vol.399 , pp. 1-8
    • Shirai, H.1    Kidera, A.2    Nakamura, H.3
  • 26
    • 0032568959 scopus 로고    scopus 로고
    • Automated classification of antibody complementarity determining region 3 of the heavy chain (H3) loops into canonical forms and its application to protein structure prediction
    • 9642095
    • B.Oliva, P.A.Bates, E.Querol, F.X.Avilés, M.J.Sternberg. Automated classification of antibody complementarity determining region 3 of the heavy chain (H3) loops into canonical forms and its application to protein structure prediction. J Mol Biol 1998; 279:1193-210; PMID:9642095; http://dx.doi.org/10.1006/jmbi.1998.1847
    • (1998) J Mol Biol , vol.279 , pp. 1193-1210
    • Oliva, B.1    Bates, P.A.2    Querol, E.3    Avilés, F.X.4    Sternberg, M.J.5
  • 27
    • 0032536197 scopus 로고    scopus 로고
    • Conformations of the third hypervariable region in the VH domain of immunoglobulins
    • 9466909
    • V.Morea, A.Tramontano, M.Rustici, C.Chothia, A.M.Lesk. Conformations of the third hypervariable region in the VH domain of immunoglobulins. J Mol Biol 1998; 275:269-94; PMID:9466909; http://dx.doi.org/10.1006/jmbi.1997.1442
    • (1998) J Mol Biol , vol.275 , pp. 269-294
    • Morea, V.1    Tramontano, A.2    Rustici, M.3    Chothia, C.4    Lesk, A.M.5
  • 28
    • 0033058759 scopus 로고    scopus 로고
    • H3-rules: identification of CDR-H3 structures in antibodies
    • 10428499
    • H.Shirai, A.Kidera, H.Nakamura. H3-rules: identification of CDR-H3 structures in antibodies. FEBS Lett 1999; 455:188-97; PMID:10428499; http://dx.doi.org/10.1016/S0014-5793(99)00821-2
    • (1999) FEBS Lett , vol.455 , pp. 188-197
    • Shirai, H.1    Kidera, A.2    Nakamura, H.3
  • 29
    • 0035920123 scopus 로고    scopus 로고
    • A role of the third complementarity-determining region in the affinity maturation of an antibody
    • K.Furukawa, H.Shirai, T.Azuma, H.Nakamura. A role of the third complementarity-determining region in the affinity maturation of an antibody. J Biol Chem 2001; 276:22—8; PMID:11375987
    • (2001) J Biol Chem , vol.276 , pp. 22
    • Furukawa, K.1    Shirai, H.2    Azuma, T.3    Nakamura, H.4
  • 30
    • 57349097173 scopus 로고    scopus 로고
    • Structural classification of CDR-H3 revisited: A lesson in antibody modeling
    • D.Kuroda, H.Shirai, M.Kobori, H.Nakamura. Structural classification of CDR-H3 revisited: A lesson in antibody modeling. Proteins Struct Funct Bioinforma 2008; 73:608-20; PMID:18473362; http://dx.doi.org/10.1002/prot.22087
    • (2008) Proteins Struct Funct Bioinforma , vol.73 , pp. 608-620
    • Kuroda, D.1    Shirai, H.2    Kobori, M.3    Nakamura, H.4
  • 31
    • 84930190530 scopus 로고    scopus 로고
    • The Origin of CDR H3 Structural Diversity
    • 25579815
    • B.D.Weitzner, R.L.DunbrackJr, J.J.Gray. The Origin of CDR H3 Structural Diversity. Structure 2015; 23:302-11; PMID:25579815; http://dx.doi.org/10.1016/j.str.2014.11.010
    • (2015) Structure , vol.23 , pp. 302-311
    • Weitzner, B.D.1    Dunbrack, R.L.2    Gray, J.J.3
  • 32
    • 50549090182 scopus 로고    scopus 로고
    • PIGS: automatic prediction of antibody structures
    • 18641403
    • P.Marcatili, A.Rosi, A.Tramontano. PIGS: automatic prediction of antibody structures. Bioinformatics 2008; 24:1953-4; PMID:18641403; http://dx.doi.org/10.1093/bioinformatics/btn341
    • (2008) Bioinformatics , vol.24 , pp. 1953-1954
    • Marcatili, P.1    Rosi, A.2    Tramontano, A.3
  • 34
    • 84867015346 scopus 로고    scopus 로고
    • Computer-aided antibody design
    • 22661385
    • D.Kuroda, H.Shirai, M.P.Jacobson, H.Nakamura. Computer-aided antibody design. Protein Eng Des Sel 2012; 25(10):507-22; PMID:22661385; http://dx.doi.org/10.1093/protein/gzs024
    • (2012) Protein Eng Des Sel , vol.25 , Issue.10 , pp. 507-522
    • Kuroda, D.1    Shirai, H.2    Jacobson, M.P.3    Nakamura, H.4
  • 35
    • 77958157337 scopus 로고    scopus 로고
    • OptCDR: a general computational method for the design of antibody complementarity determining regions for targeted epitope binding
    • 20847101
    • R.J.Pantazes, C.D.Maranas. OptCDR: a general computational method for the design of antibody complementarity determining regions for targeted epitope binding. Protein Eng Des Sel 2010; 23:849-58; PMID:20847101; http://dx.doi.org/10.1093/protein/gzq061
    • (2010) Protein Eng Des Sel , vol.23 , pp. 849-858
    • Pantazes, R.J.1    Maranas, C.D.2
  • 36
    • 84937737866 scopus 로고    scopus 로고
    • OptMAVEn–a new framework for the de novo design of antibody variable region models targeting specific antigen epitopes
    • 25153121
    • T.Li, R.J.Pantazes, C.D.Maranas. OptMAVEn–a new framework for the de novo design of antibody variable region models targeting specific antigen epitopes. PLoS One 2014; 9(8):e105954; PMID:25153121; http://dx.doi.org/10.1371/journal.pone.0105954
    • (2014) PLoS One , vol.9 , Issue.8
    • Li, T.1    Pantazes, R.J.2    Maranas, C.D.3
  • 37
    • 84937736814 scopus 로고    scopus 로고
    • AbDesign: An algorithm for combinatorial backbone design guided by natural conformations and sequences
    • 25670500
    • G.D.Lapidoth, D.Baran, G.M.Pszolla, C.Norn, A.Alon, M.D.Tyka, S.J.Fleishman. AbDesign: An algorithm for combinatorial backbone design guided by natural conformations and sequences. Proteins 2015; 83:1385-406; PMID:25670500; http://dx.doi.org/10.1002/prot.24779
    • (2015) Proteins , vol.83 , pp. 1385-1406
    • Lapidoth, G.D.1    Baran, D.2    Pszolla, G.M.3    Norn, C.4    Alon, A.5    Tyka, M.D.6    Fleishman, S.J.7
  • 38
    • 84925284996 scopus 로고    scopus 로고
    • In-depth determination and analysis of the human paired heavy- and light-chain antibody repertoire
    • 25501908
    • B.J.DeKosky, T.Kojima, A.Rodin, W.Charab, G.C.Ippolito, A.D.Ellington, G.Georgiou. In-depth determination and analysis of the human paired heavy- and light-chain antibody repertoire. Nat Med 2014; 21:86-91; PMID:25501908; http://dx.doi.org/10.1038/nm.3743
    • (2014) Nat Med , vol.21 , pp. 86-91
    • DeKosky, B.J.1    Kojima, T.2    Rodin, A.3    Charab, W.4    Ippolito, G.C.5    Ellington, A.D.6    Georgiou, G.7
  • 39
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • S.R.Eddy. Profile hidden Markov models. Bioinformatics 1998; 14:755-63. 8; PMID:9918945; http://dx.doi.org/10.1093/bioinformatics/14.9.755
    • (1998) Bioinformatics , vol.14 , pp. 755
    • Eddy, S.R.1
  • 40
    • 0020534965 scopus 로고
    • Somatic generation of antibody diversity
    • 6300689
    • S.Tonegawa. Somatic generation of antibody diversity. Nature 1983; 302:575-81; PMID:6300689; http://dx.doi.org/10.1038/302575a0
    • (1983) Nature , vol.302 , pp. 575-581
    • Tonegawa, S.1
  • 41
    • 39049145798 scopus 로고    scopus 로고
    • Immunoglobulin Somatic Hypermutation
    • 17576170
    • G.Teng, F.N.Papavasiliou. Immunoglobulin Somatic Hypermutation. Annu Rev Genet 2007; 41:107-20; PMID:17576170; http://dx.doi.org/10.1146/annurev.genet.41.110306.130340
    • (2007) Annu Rev Genet , vol.41 , pp. 107-120
    • Teng, G.1    Papavasiliou, F.N.2
  • 42
    • 0347758541 scopus 로고    scopus 로고
    • The generation of antibody diversity through somatic hypermutation and class switch recombination
    • 14724175
    • Z.Li, C.J.Woo, M.D.Iglesias-Ussel, D.Ronai, M.D.Scharff. The generation of antibody diversity through somatic hypermutation and class switch recombination. Genes Dev 2004; 18:1-11; PMID:14724175; http://dx.doi.org/10.1101/gad.1161904
    • (2004) Genes Dev , vol.18 , pp. 1-11
    • Li, Z.1    Woo, C.J.2    Iglesias-Ussel, M.D.3    Ronai, D.4    Scharff, M.D.5
  • 43
    • 0031983725 scopus 로고    scopus 로고
    • Somatic hypermutation introduces insertions and deletions into immunoglobulin V genes
    • 9419211
    • P.C.Wilson, O.de Bouteiller, Y.J.Liu, K.Potter, J.Banchereau, J.D.Capra, V.Pascual. Somatic hypermutation introduces insertions and deletions into immunoglobulin V genes. J Exp Med 1998; 187:59-70; PMID:9419211; http://dx.doi.org/10.1084/jem.187.1.59
    • (1998) J Exp Med , vol.187 , pp. 59-70
    • Wilson, P.C.1    de Bouteiller, O.2    Liu, Y.J.3    Potter, K.4    Banchereau, J.5    Capra, J.D.6    Pascual, V.7
  • 44
    • 84867742557 scopus 로고    scopus 로고
    • Location and length distribution of somatic hypermutation-associated DNA insertions and deletions reveals regions of antibody structural plasticity
    • 22717702
    • B.S.Briney, J.R.Willis, J.E.Crowe. Location and length distribution of somatic hypermutation-associated DNA insertions and deletions reveals regions of antibody structural plasticity. Genes Immun 2012; 13:523-9; PMID:22717702; http://dx.doi.org/10.1038/gene.2012.28
    • (2012) Genes Immun , vol.13 , pp. 523-529
    • Briney, B.S.1    Willis, J.R.2    Crowe, J.E.3
  • 45
    • 0025063143 scopus 로고
    • Framework residue 71 is a major determinant of the position and conformation of the second hypervariable region in the VH domains of immunoglobulins
    • 2118959
    • A.Tramontano, C.Chothia, A.M.Lesk. Framework residue 71 is a major determinant of the position and conformation of the second hypervariable region in the VH domains of immunoglobulins. J Mol Biol 1990; 215:175-82; PMID:2118959; http://dx.doi.org/10.1016/S0022-2836(05)80102-0
    • (1990) J Mol Biol , vol.215 , pp. 175-182
    • Tramontano, A.1    Chothia, C.2    Lesk, A.M.3
  • 49
    • 84938011869 scopus 로고
    • On adaptive control processes
    • R.Bellman, R.Kalaba. On adaptive control processes. IRE Trans Autom Control 1959; 4:1-9; http://dx.doi.org/10.1109/TAC.1959.1104847
    • (1959) IRE Trans Autom Control , vol.4 , pp. 1-9
    • Bellman, R.1    Kalaba, R.2
  • 51
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • 5420325
    • S.B.Needleman, C.D.Wunsch. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol 1970; 48:443-53; PMID:5420325; http://dx.doi.org/10.1016/0022-2836(70)90057-4
    • (1970) J Mol Biol , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 53
    • 0000825481 scopus 로고
    • A statistical method for evaluating systematic relationships
    • R.R.Sokal, C.D.Michener. A statistical method for evaluating systematic relationships. Univ Kansas Sci Bull 1958; 38:1409-38
    • (1958) Univ Kansas Sci Bull , vol.38 , pp. 1409-1438
    • Sokal, R.R.1    Michener, C.D.2
  • 56
    • 2142738304 scopus 로고    scopus 로고
    • WebLogo: a sequence logo generator
    • 15173120
    • G.E.Crooks, G.Hon, J.-M.Chandonia, S.E.Brenner. WebLogo: a sequence logo generator. Genome Res 2004; 14:1188-90; PMID:15173120; http://dx.doi.org/10.1101/gr.849004
    • (2004) Genome Res , vol.14 , pp. 1188-1190
    • Crooks, G.E.1    Hon, G.2    Chandonia, J.-M.3    Brenner, S.E.4


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