메뉴 건너뛰기




Volumn 16, Issue 1, 2015, Pages

Coevolutionary analyses require phylogenetically deep alignments and better null models to accurately detect inter-protein contacts within and between species

Author keywords

Coevolution; Contact prediction; Cross species; Host virus; Inter protein; Methods comparison; Protein interaction

Indexed keywords

ALIGNMENT; VIRUSES;

EID: 84960426522     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/s12859-015-0677-y     Document Type: Article
Times cited : (13)

References (72)
  • 1
    • 38349135391 scopus 로고    scopus 로고
    • An integrated system for studying residue coevolution in proteins
    • Yip KY, Patel P, Kim PM, Engelman DM, McDermott D, Gerstein M. An integrated system for studying residue coevolution in proteins. Bioinformatics. 2008; 24(2):290-2. doi: 10.1093/bioinformatics/btm584.
    • (2008) Bioinformatics , vol.24 , Issue.2 , pp. 290-292
    • Yip, K.Y.1    Patel, P.2    Kim, P.M.3    Engelman, D.M.4    McDermott, D.5    Gerstein, M.6
  • 2
    • 39649100613 scopus 로고    scopus 로고
    • Detecting groups of coevolving positions in a molecule: a clustering approach
    • Dutheil J, Galtier N. Detecting groups of coevolving positions in a molecule: a clustering approach. BMC Evol Biol. 2007; 7:242. doi: 10.1186/1471-2148-7-242.
    • (2007) BMC Evol Biol , vol.7 , pp. 242
    • Dutheil, J.1    Galtier, N.2
  • 3
    • 84858265857 scopus 로고    scopus 로고
    • Detecting coevolving positions in a molecule: why and how to account for phylogeny
    • Dutheil JY. Detecting coevolving positions in a molecule: why and how to account for phylogeny. Brief Bioinform. 2012; 13(2):228-43. doi: 10.1093/bib/bbr048.
    • (2012) Brief Bioinform , vol.13 , Issue.2 , pp. 228-243
    • Dutheil, J.Y.1
  • 4
    • 84875225476 scopus 로고    scopus 로고
    • Emerging methods in protein co-evolution
    • de Juan D, Pazos F, Valencia A. Emerging methods in protein co-evolution. Nat Rev Genet. 2013; 14(4):249-61. doi: 10.1038/nrg3414.
    • (2013) Nat Rev Genet , vol.14 , Issue.4 , pp. 249-261
    • de Juan, D.1    Pazos, F.2    Valencia, A.3
  • 5
    • 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. Correction for phylogeny, small number of observations and data redundancy improves the identification of coevolving amino acid pairs using mutual information. Bioinformatics. 2009; 25(9):1125-31. 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
  • 6
    • 33744457709 scopus 로고    scopus 로고
    • A novel method for detecting intramolecular coevolution adding a further dimension to selective constraints analyses
    • Fares MA, Travers SA. A novel method for detecting intramolecular coevolution adding a further dimension to selective constraints analyses. Genetics. 2006; 173(1):9-23. doi: 10.1534/genetics.105.053249.
    • (2006) Genetics , vol.173 , Issue.1 , pp. 9-23
    • Fares, M.A.1    Travers, S.A.2
  • 7
    • 79960999556 scopus 로고    scopus 로고
    • Coordinate linkage of HIV evolution reveals regions of immunological vulnerability
    • Dahirel V, Shekhar K, Pereyra F, Miura T, Artyomov M, Talsania S, et al. Coordinate linkage of HIV evolution reveals regions of immunological vulnerability. Proc Natl Acad Sci USA. 1153; 108(28):0-5. doi: 10.1073/pnas.1105315108.
    • Proc Natl Acad Sci USA , vol.108 , Issue.28 , pp. 0-5
    • Dahirel, V.1    Shekhar, K.2    Pereyra, F.3    Miura, T.4    Artyomov, M.5    Talsania, S.6
  • 8
    • 38849115223 scopus 로고    scopus 로고
    • Mutual information without the influence of phylogeny or entropy dramatically improves residue contact prediction
    • Dunn SD, Wahl LM, Gloor GB. Mutual information without the influence of phylogeny or entropy dramatically improves residue contact prediction. Bioinformatics. 2008; 24(3):333-40. doi: 10.1093/bioinformatics/btm604.
    • (2008) Bioinformatics , vol.24 , Issue.3 , pp. 333-340
    • Dunn, S.D.1    Wahl, L.M.2    Gloor, G.B.3
  • 9
    • 83755178457 scopus 로고    scopus 로고
    • Direct-coupling analysis of residue coevolution captures native contacts across many protein families
    • Morcos F, Pagnani A, Lunt B, Bertolino A, Marks DS, Sander C, et al. Direct-coupling analysis of residue coevolution captures native contacts across many protein families. Proc Natl Acad Sci USA. 2011; 108(49):E1293-301. doi: 10.1073/pnas.1111471108.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.49 , pp. E1293-E1301
    • Morcos, F.1    Pagnani, A.2    Lunt, B.3    Bertolino, A.4    Marks, D.S.5    Sander, C.6
  • 10
    • 23944476399 scopus 로고    scopus 로고
    • A model-based approach for detecting coevolving positions in a molecule
    • Dutheil J, Pupko T, Jean-Marie A, Galtier N. A model-based approach for detecting coevolving positions in a molecule. Mol Biol Evol. 2005; 22(9):1919-28. doi: 10.1093/molbev/msi183.
    • (2005) Mol Biol Evol , vol.22 , Issue.9 , pp. 1919-1928
    • Dutheil, J.1    Pupko, T.2    Jean-Marie, A.3    Galtier, N.4
  • 11
    • 0033582946 scopus 로고    scopus 로고
    • Coevolving protein residues: maximum likelihood identification and relationship to structure
    • Pollock DD, Taylor WR, Goldman N. Coevolving protein residues: maximum likelihood identification and relationship to structure. J Mol Biol. 1999; 287(1):187-98. doi: 10.1006/jmbi.1998.2601.
    • (1999) J Mol Biol , vol.287 , Issue.1 , pp. 187-198
    • Pollock, D.D.1    Taylor, W.R.2    Goldman, N.3
  • 12
    • 60249099824 scopus 로고    scopus 로고
    • Detecting coevolution without phylogenetic trees? tree-ignorant metrics of coevolution perform as well as tree-aware metrics
    • Caporaso JG, Smit S, Easton BC, Hunter L, Huttley GA, Knight R. Detecting coevolution without phylogenetic trees? tree-ignorant metrics of coevolution perform as well as tree-aware metrics. BMC Evol Biol. 2008;8(327). doi: 10.1186/1471-2148-8-327.
    • (2008) BMC Evol Biol , vol.8 , Issue.327
    • Caporaso, J.G.1    Smit, S.2    Easton, B.C.3    Hunter, L.4    Huttley, G.A.5    Knight, R.6
  • 13
    • 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. Identification of direct residue contacts in protein-protein interaction by message passing. Proc Natl Acad Sci USA. 2009; 106(1):67-72. doi: 10.1073/pnas.0805923106.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.1 , pp. 67-72
    • Weigt, M.1    White, R.A.2    Szurmant, H.3    Hoch, J.A.4    Hwa, T.5
  • 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. PSICOV: precise structural contact prediction using sparse inverse covariance estimation on large multiple sequence alignments. Bioinformatics. 2012; 28(2):184-90. doi: 10.1093/bioinformatics/btr638.
    • (2012) Bioinformatics , vol.28 , Issue.2 , pp. 184-190
    • Jones, D.T.1    Buchan, D.W.2    Cozzetto, D.3    Pontil, M.4
  • 15
    • 76749112068 scopus 로고    scopus 로고
    • Disentangling direct from indirect co-evolution of residues in protein alignments
    • Burger L, van Nimwegen E. Disentangling direct from indirect co-evolution of residues in protein alignments. PLoS Comput Biol. 2010; 6(1):e1000633. doi: 10.1371/journal.pcbi.1000633.
    • (2010) PLoS Comput Biol , vol.6 , Issue.1 , pp. e1000633
    • Burger, L.1    van Nimwegen, E.2
  • 16
    • 84873617924 scopus 로고    scopus 로고
    • Large measles outbreak in geneva, switzerland, january to august 2011: descriptive epidemiology and demonstration of quarantine effectiveness
    • Delaporte E, Wyler Lazarevic CA, Iten A, Sudre P. Large measles outbreak in geneva, switzerland, january to august 2011: descriptive epidemiology and demonstration of quarantine effectiveness. Euro Surveill Bull. 2013;18(6). http://www.ncbi.nlm.nih.gov/pubmed/23410259.
    • (2013) Euro Surveill Bull. , vol.18 , Issue.6
    • Delaporte, E.1    Wyler Lazarevic, C.A.2    Iten, A.3    Sudre, P.4
  • 17
    • 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. Multidimensional mutual information methods for the analysis of covariation in multiple sequence alignments. BMC Bioinformatics. 2014; 15(1):157. doi: 10.1186/1471-2105-15-157.
    • (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
  • 18
    • 84868365613 scopus 로고    scopus 로고
    • The spatial architecture of protein function and adaptation
    • McLaughlin Jr RN, Poelwijk FJ, Raman A, Gosal WS, Ranganathan R. The spatial architecture of protein function and adaptation. Nature. 2012; 491(7422):138-42. doi: 10.1038/nature11500.
    • (2012) Nature , vol.491 , Issue.7422 , pp. 138-142
    • McLaughlin, R.N.1    Poelwijk, F.J.2    Raman, A.3    Gosal, W.S.4    Ranganathan, R.5
  • 20
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol. 2005; 6(3):197-208. doi: 10.1038/nrm1589.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 22
    • 84857134729 scopus 로고    scopus 로고
    • Molecular architecture of the 26s proteasome holocomplex determined by an integrative approach
    • Lasker K, Forster F, Bohn S, Walzthoeni T, Villa E, Unverdorben P, et al. Molecular architecture of the 26s proteasome holocomplex determined by an integrative approach. Proc Natl Acad Sci USA. 2012; 109(5):1380-7. doi: 10.1073/pnas.1120559109.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.5 , pp. 1380-1387
    • Lasker, K.1    Forster, F.2    Bohn, S.3    Walzthoeni, T.4    Villa, E.5    Unverdorben, P.6
  • 24
    • 84894638006 scopus 로고    scopus 로고
    • Integrating protein-protein interaction networks with phenotypes reveals signs of interactions
    • Vinayagam A, Zirin J, Roesel C, Hu Y, Yilmazel B, Samsonova AA, et al. Integrating protein-protein interaction networks with phenotypes reveals signs of interactions. Nat Methods. 2013; 11(1):94-9. doi: 10.1038/nmeth.2733.
    • (2013) Nat Methods , vol.11 , Issue.1 , pp. 94-99
    • Vinayagam, A.1    Zirin, J.2    Roesel, C.3    Hu, Y.4    Yilmazel, B.5    Samsonova, A.A.6
  • 25
    • 84884603324 scopus 로고
    • Assessing the utility of coevolution-based residue-residue contact predictions in a sequence- and structure-rich era
    • Kamisetty H, Ovchinnikov S, Baker D. Assessing the utility of coevolution-based residue-residue contact predictions in a sequence- and structure-rich era. Proc Natl Acad Sci USA. 1567; 110(39):4-9. doi: 10.1073/pnas.1314045110.
    • (1567) Proc Natl Acad Sci USA , vol.110 , Issue.39 , pp. 4-9
    • Kamisetty, H.1    Ovchinnikov, S.2    Baker, D.3
  • 27
    • 82855163967 scopus 로고    scopus 로고
    • Protein 3d structure computed from evolutionary sequence variation
    • Marks DS, Colwell LJ, Sheridan R, Hopf TA, Pagnani A, Zecchina R, et al. Protein 3d structure computed from evolutionary sequence variation. PloS ONE. 2011; 6(12):e28766. doi: 10.1371/journal.pone.0028766.
    • (2011) PloS ONE , vol.6 , Issue.12 , pp. e28766
    • Marks, D.S.1    Colwell, L.J.2    Sheridan, R.3    Hopf, T.A.4    Pagnani, A.5    Zecchina, R.6
  • 28
    • 84862647180 scopus 로고    scopus 로고
    • Three-dimensional structures of membrane proteins from genomic sequencing
    • Hopf TA, Colwell LJ, Sheridan R, Rost B, Sander C, Marks DS. Three-dimensional structures of membrane proteins from genomic sequencing. Cell. 2012; 149(7):1607-21. doi: 10.1016/j.cell.2012.04.012.
    • (2012) Cell , vol.149 , Issue.7 , pp. 1607-1621
    • Hopf, T.A.1    Colwell, L.J.2    Sheridan, R.3    Rost, B.4    Sander, C.5    Marks, D.S.6
  • 29
    • 84869447010 scopus 로고    scopus 로고
    • Protein structure prediction from sequence variation
    • Marks DS, Hopf TA, Sander C. Protein structure prediction from sequence variation. Nat Biotechnol. 2012; 30(11):1072-80. doi: 10.1038/nbt.2419.
    • (2012) Nat Biotechnol , vol.30 , Issue.11 , pp. 1072-1080
    • Marks, D.S.1    Hopf, T.A.2    Sander, C.3
  • 30
    • 84899847547 scopus 로고    scopus 로고
    • Robust and accurate prediction of residue-residue interactions across protein interfaces using evolutionary information
    • Ovchinnikov S, Kamisetty H, Baker D. Robust and accurate prediction of residue-residue interactions across protein interfaces using evolutionary information. Elife. 2014; 3:e02030. doi: 10.7554/eLife.02030.
    • (2014) Elife , vol.3 , pp. e02030
    • Ovchinnikov, S.1    Kamisetty, H.2    Baker, D.3
  • 31
    • 38949168935 scopus 로고    scopus 로고
    • High-confidence prediction of global interactomes based on genome-wide coevolutionary networks
    • Juan D, Pazos F, Valencia A. High-confidence prediction of global interactomes based on genome-wide coevolutionary networks. Proc Natl Acad Sci USA. 2008; 105(3):934-9. doi: 10.1073/pnas.0709671105.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.3 , pp. 934-939
    • Juan, D.1    Pazos, F.2    Valencia, A.3
  • 32
    • 78049433528 scopus 로고    scopus 로고
    • Coevolution predicts direct interactions between mtDNA-encoded and nDNA-encoded subunits of oxidative phosphorylation complex i
    • Gershoni M, Fuchs A, Shani N, Fridman Y, Corral-Debrinski M, Aharoni A, et al. Coevolution predicts direct interactions between mtDNA-encoded and nDNA-encoded subunits of oxidative phosphorylation complex i. J Mol Biol. 2010; 404(1):158-71. doi: 10.1016/j.jmb.2010.09.029.
    • (2010) J Mol Biol , vol.404 , Issue.1 , pp. 158-171
    • Gershoni, M.1    Fuchs, A.2    Shani, N.3    Fridman, Y.4    Corral-Debrinski, M.5    Aharoni, A.6
  • 34
    • 36949019322 scopus 로고    scopus 로고
    • Detecting coevolution in and among protein domains
    • Yeang CH, Haussler D. Detecting coevolution in and among protein domains. PLoS Comput Biol. 2007; 3(11):e211. doi: 10.1371/journal.pcbi.0030211.
    • (2007) PLoS Comput Biol , vol.3 , Issue.11 , pp. e211
    • Yeang, C.H.1    Haussler, D.2
  • 35
    • 84908219709 scopus 로고    scopus 로고
    • Affinity purification-mass spectrometry and network analysis to understand protein-protein interactions
    • Morris JH, Knudsen GM, Verschueren E, Johnson JR, Cimermancic P, Greninger AL, et al. Affinity purification-mass spectrometry and network analysis to understand protein-protein interactions. Nat Protoc. 2014; 9(11):2539-54. doi: 10.1038/nprot.2014.164.
    • (2014) Nat Protoc , vol.9 , Issue.11 , pp. 2539-2554
    • Morris, J.H.1    Knudsen, G.M.2    Verschueren, E.3    Johnson, J.R.4    Cimermancic, P.5    Greninger, A.L.6
  • 36
    • 67649663886 scopus 로고    scopus 로고
    • Yeast two-hybrid, a powerful tool for systems biology
    • Brückner A, Polge C, Lentze N, Auerbach D, Schlattner U. Yeast two-hybrid, a powerful tool for systems biology. Int J Mol Sci. 2009; 10(6):2763-88. doi: 10.3390/ijms10062763.
    • (2009) Int J Mol Sci , vol.10 , Issue.6 , pp. 2763-2788
    • Brückner, A.1    Polge, C.2    Lentze, N.3    Auerbach, D.4    Schlattner, U.5
  • 37
    • 84925224926 scopus 로고    scopus 로고
    • The yeast two-hybrid assay: still finding connections after 25 years
    • Vidal M, Fields S. The yeast two-hybrid assay: still finding connections after 25 years. Nat Methods. 2014; 11(12):1203-6. http://www.nature.com/articles/nmeth.3182.
    • (2014) Nat Methods , vol.11 , Issue.12 , pp. 1203-1206
    • Vidal, M.1    Fields, S.2
  • 38
    • 80054760401 scopus 로고    scopus 로고
    • Protein-fragment complementation assays for large-scale analysis, functional dissection and dynamic studies of protein-protein interactions in living cells
    • Michnick SW, Ear PH, Landry C, Malleshaiah MK, Messier V. Protein-fragment complementation assays for large-scale analysis, functional dissection and dynamic studies of protein-protein interactions in living cells. Methods Mol Biol. 2011; 756:395-425. doi: 10.1007/978-1-61779-160-4_25.
    • (2011) Methods Mol Biol , vol.756 , pp. 395-425
    • Michnick, S.W.1    Ear, P.H.2    Landry, C.3    Malleshaiah, M.K.4    Messier, V.5
  • 39
    • 72249103485 scopus 로고    scopus 로고
    • A physical and regulatory map of host-influenza interactions reveals pathways in h1n1 infection
    • Shapira SD, Gat-Viks I, Shum BO, Dricot A, de Grace MM, Wu L, et al. A physical and regulatory map of host-influenza interactions reveals pathways in h1n1 infection. Cell. 2009; 139(7):1255-67. doi: 10.1016/j.cell.2009.12.018.
    • (2009) Cell , vol.139 , Issue.7 , pp. 1255-1267
    • Shapira, S.D.1    Gat-Viks, I.2    Shum, B.O.3    Dricot, A.4    de Grace, M.M.5    Wu, L.6
  • 40
    • 84876797103 scopus 로고    scopus 로고
    • Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus
    • Liao HX, Lynch R, Zhou T, Gao F, Alam SM, Boyd SD, et al. Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus. 2013; 496(7446): 469-76. doi: 10.1038/nature12053.
    • (2013) , vol.496 , Issue.7446 , pp. 469-476
    • Liao, H.X.1    Lynch, R.2    Zhou, T.3    Gao, F.4    Alam, S.M.5    Boyd, S.D.6
  • 41
    • 79955792165 scopus 로고    scopus 로고
    • Dissecting the specificity of protein-protein interaction in bacterial two-component signaling: Orphans and crosstalks
    • Procaccini A, Lunt B, Szurmant H, Hwa T, Weigt M. Dissecting the specificity of protein-protein interaction in bacterial two-component signaling: Orphans and crosstalks. PLoS ONE. 2011; 6(5):e19729. doi: 10.1371/journal.pone.0019729.
    • (2011) PLoS ONE , vol.6 , Issue.5 , pp. e19729
    • Procaccini, A.1    Lunt, B.2    Szurmant, H.3    Hwa, T.4    Weigt, M.5
  • 42
    • 76049105937 scopus 로고    scopus 로고
    • High-resolution protein complexes from integrating genomic information with molecular simulation
    • Schug A, Weigt M, Onuchic JN, Hwa T, Szurmant H. High-resolution protein complexes from integrating genomic information with molecular simulation. Proc Natl Acad Sci USA. 2212; 106(52):4-9. doi: 10.1073/pnas.0912100106.
    • Proc Natl Acad Sci USA , vol.106 , Issue.52 , pp. 4-9
    • Schug, A.1    Weigt, M.2    Onuchic, J.N.3    Hwa, T.4    Szurmant, H.5
  • 43
    • 0026499429 scopus 로고
    • Conservation evaluation and phylogenetic diversity
    • Faith DP. Conservation evaluation and phylogenetic diversity. Biol Conserv. 1992; 61(1):1-10. doi: 10.1016/0006-3207(92)91201-3.
    • (1992) Biol Conserv , vol.61 , Issue.1 , pp. 1-10
    • Faith, D.P.1
  • 44
    • 70349795241 scopus 로고    scopus 로고
    • Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
    • Casino P, Rubio V, Marina A. Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction. Cell. 2009; 139(2):325-36. doi: 10.1016/j.cell.2009.08.032.
    • (2009) Cell , vol.139 , Issue.2 , pp. 325-336
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 45
    • 0037447059 scopus 로고    scopus 로고
    • Amino acids determining enzyme-substrate specificity in prokaryotic and eukaryotic protein kinases
    • Li L, Shakhnovich EI, Mirny LA. Amino acids determining enzyme-substrate specificity in prokaryotic and eukaryotic protein kinases. Proc Natl Acad Sci USA. 2003; 100(8):4463-8. doi: 10.1073/pnas.0737647100.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.8 , pp. 4463-4468
    • Li, L.1    Shakhnovich, E.I.2    Mirny, L.A.3
  • 46
    • 0029988249 scopus 로고
    • Altered recognition mutants of the response regulator PhoB: a new genetic strategy for studying protein-protein interactions
    • Haldimann A, Prahalad MK, Fisher SL, Kim SK, Walsh CT, Wanner BL. Altered recognition mutants of the response regulator PhoB: a new genetic strategy for studying protein-protein interactions. Proc Natl Acad Sci USA. 1436; 93(25):1-6. http://www.ncbi.nlm.nih.gov/pubmed/8962056.
    • (1436) Proc Natl Acad Sci USA , vol.93 , Issue.25 , pp. 1-6
    • Haldimann, A.1    Prahalad, M.K.2    Fisher, S.L.3    Kim, S.K.4    Walsh, C.T.5    Wanner, B.L.6
  • 47
    • 44649153450 scopus 로고    scopus 로고
    • Rewiring the specificity of two-component signal transduction systems
    • Skerker JM, Perchuk BS, Siryaporn A, Lubin EA, Ashenberg O, Goulian M, et al. Rewiring the specificity of two-component signal transduction systems. Cell. 2008; 133(6):1043-54. doi: 10.1016/j.cell.2008.04.040.
    • (2008) Cell , vol.133 , Issue.6 , pp. 1043-1054
    • Skerker, J.M.1    Perchuk, B.S.2    Siryaporn, A.3    Lubin, E.A.4    Ashenberg, O.5    Goulian, M.6
  • 48
    • 44449112421 scopus 로고    scopus 로고
    • Specificity in two-component signal transduction pathways
    • Laub MT, Goulian M. Specificity in two-component signal transduction pathways. Annu Rev Genet. 2007; 41:121-45. doi: 10.1146/annurev.genet.41.042007.170548.
    • (2007) Annu Rev Genet , vol.41 , pp. 121-145
    • Laub, M.T.1    Goulian, M.2
  • 49
    • 0037433701 scopus 로고    scopus 로고
    • Using multiple interdependency to separate functional from phylogenetic correlations in protein alignments
    • Tillier ERM, Lui TWH. Using multiple interdependency to separate functional from phylogenetic correlations in protein alignments. Bioinformatics. 2003; 19(6):750-55. doi: 10.1093/bioinformatics/btg072.
    • (2003) Bioinformatics , vol.19 , Issue.6 , pp. 750-755
    • Tillier, E.R.M.1    Lui, T.W.H.2
  • 50
    • 3042842115 scopus 로고    scopus 로고
    • Influence of conservation on calculations of amino acid covariance in multiple sequence alignments
    • Fodor AA, Aldrich RW. Influence of conservation on calculations of amino acid covariance in multiple sequence alignments. Proteins: Structure Function Bioinform. 2004; 56(2):211-21. doi: 10.1002/prot.20098.
    • (2004) Proteins: Structure Function Bioinform , vol.56 , Issue.2 , pp. 211-221
    • Fodor, A.A.1    Aldrich, R.W.2
  • 52
    • 0034724418 scopus 로고    scopus 로고
    • Separation of phylogenetic and functional associations in biological sequences by using the parametric bootstrap
    • Wollenberg KR, Atchley WR. Separation of phylogenetic and functional associations in biological sequences by using the parametric bootstrap. Proc Natl Acad Sci USA. 2000; 97(7):3288-91. doi: 10.1073/pnas.070154797.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.7 , pp. 3288-3291
    • Wollenberg, K.R.1    Atchley, W.R.2
  • 53
    • 24344496951 scopus 로고    scopus 로고
    • An approximation to the distribution of finite sample size mutual information estimates
    • ICC 2005. IEEE International Conference
    • Goebel B, Dawy Z, Hagenauer J, Mueller JC. An approximation to the distribution of finite sample size mutual information estimates. In: Communications, 2005. ICC 2005. IEEE International Conference on, vol. 2. IEEE: 2005. p. 1102-6. https://ieeexplore.ieee.org/ielx5/9996/32110/01494518.pdf , doi: 10.1109/ICC.2005.1494518.
    • (2005) Communications , vol.2 , pp. 102-106
    • Goebel, B.1    Dawy, Z.2    Hagenauer, J.3    Mueller, J.C.4
  • 54
    • 84856017075 scopus 로고    scopus 로고
    • The host restriction factor APOBEC3g and retroviral vif protein coevolve due to ongoing genetic conflict
    • Compton AA, Hirsch VM, Emerman M. The host restriction factor APOBEC3g and retroviral vif protein coevolve due to ongoing genetic conflict. Cell Host Microbe. 2012; 11(1):91-8. doi: 10.1016/j.chom.2011.11.010.
    • (2012) Cell Host Microbe , vol.11 , Issue.1 , pp. 91-98
    • Compton, A.A.1    Hirsch, V.M.2    Emerman, M.3
  • 55
    • 84875064882 scopus 로고    scopus 로고
    • Convergence and divergence in the evolution of the APOBEC3g-vif interaction reveal ancient origins of simian immunodeficiency viruses
    • Compton AA, Emerman M. Convergence and divergence in the evolution of the APOBEC3g-vif interaction reveal ancient origins of simian immunodeficiency viruses. PLoS Pathog. 2013; 9(1):e1003135. doi: 10.1371/journal.ppat.1003135.
    • (2013) PLoS Pathog , vol.9 , Issue.1 , pp. e1003135
    • Compton, A.A.1    Emerman, M.2
  • 56
    • 69249215357 scopus 로고    scopus 로고
    • A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 vif SLVx4yx9y motif influences its interaction with APOBEC3g
    • Chen G, He Z, Wang T, Xu R, Yu XF. A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 vif SLVx4yx9y motif influences its interaction with APOBEC3g. J Virol. 2009; 83(17):8674-82. doi: 10.1128/JVI.00653-09.
    • (2009) J Virol , vol.83 , Issue.17 , pp. 8674-8682
    • Chen, G.1    He, Z.2    Wang, T.3    Xu, R.4    Yu, X.F.5
  • 57
    • 34547119261 scopus 로고    scopus 로고
    • Identification of two distinct human immunodeficiency virus type 1 vif determinants critical for interactions with human APOBEC3g and APOBEC3f
    • Russell RA, Pathak VK. Identification of two distinct human immunodeficiency virus type 1 vif determinants critical for interactions with human APOBEC3g and APOBEC3f. J Virol. 2007; 81(15):8201-10. doi: 10.1128/JVI.00395-07.
    • (2007) J Virol , vol.81 , Issue.15 , pp. 8201-8210
    • Russell, R.A.1    Pathak, V.K.2
  • 58
    • 0033863969 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 vif protein is an integral component of an mRNP complex of viral RNA and could be involved in the viral RNA folding and packaging process
    • Zhang H, Pomerantz RJ, Dornadula G, Sun Y. Human immunodeficiency virus type 1 vif protein is an integral component of an mRNP complex of viral RNA and could be involved in the viral RNA folding and packaging process. J Virol. 2000; 74(18):8252-61. http://www.ncbi.nlm.nih.gov/pubmed/10954522.
    • (2000) J Virol , vol.74 , Issue.18 , pp. 8252-8261
    • Zhang, H.1    Pomerantz, R.J.2    Dornadula, G.3    Sun, Y.4
  • 59
    • 48449104748 scopus 로고    scopus 로고
    • Characterization of conserved motifs in HIV-1 vif required for APOBEC3g and APOBEC3f interaction
    • He Z, Zhang W, Chen G, Xu R, Yu XF. Characterization of conserved motifs in HIV-1 vif required for APOBEC3g and APOBEC3f interaction. J Mol Biol. 2008; 381(4):1000-11. doi: 10.1016/j.jmb.2008.06.061.
    • (2008) J Mol Biol , vol.381 , Issue.4 , pp. 1000-1011
    • He, Z.1    Zhang, W.2    Chen, G.3    Xu, R.4    Yu, X.F.5
  • 60
    • 36549004535 scopus 로고    scopus 로고
    • Function analysis of sequences in human APOBEC3g involved in vif-mediated degradation
    • Zhang L, Saadatmand J, Li X, Guo F, Niu M, Jiang J, et al. Function analysis of sequences in human APOBEC3g involved in vif-mediated degradation. Virology. 2008; 370(1):113-21. doi: 10.1016/j.virol.2007.08.027.
    • (2008) Virology , vol.370 , Issue.1 , pp. 113-121
    • Zhang, L.1    Saadatmand, J.2    Li, X.3    Guo, F.4    Niu, M.5    Jiang, J.6
  • 61
    • 59649118427 scopus 로고    scopus 로고
    • Distinct domains within APOBEC3g and APOBEC3f interact with separate regions of human immunodeficiency virus type 1 vif
    • Russell RA, Smith J, Barr R, Bhattacharyya D, Pathak VK. Distinct domains within APOBEC3g and APOBEC3f interact with separate regions of human immunodeficiency virus type 1 vif. J Virol. 2009; 83(4):1992-2003. doi: 10.1128/JVI.01621-08.
    • (2009) J Virol , vol.83 , Issue.4 , pp. 1992-2003
    • Russell, R.A.1    Smith, J.2    Barr, R.3    Bhattacharyya, D.4    Pathak, V.K.5
  • 62
    • 1842732157 scopus 로고    scopus 로고
    • A single amino acid substitution in human APOBEC3g antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion
    • Xu H, Svarovskaia ES, Barr R, Zhang Y, Khan MA, Strebel K, et al. A single amino acid substitution in human APOBEC3g antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion. Proc Natl Acad Sci USA. 2004; 101(15):5652-7. doi: 10.1073/pnas.0400830101.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.15 , pp. 5652-5657
    • Xu, H.1    Svarovskaia, E.S.2    Barr, R.3    Zhang, Y.4    Khan, M.A.5    Strebel, K.6
  • 63
    • 84892188402 scopus 로고    scopus 로고
    • Structural basis for hijacking CBF-beta and CUL5 e3 ligase complex by HIV-1 vif
    • Guo Y, Dong L, Qiu X, Wang Y, Zhang B, Liu H, et al. Structural basis for hijacking CBF-beta and CUL5 e3 ligase complex by HIV-1 vif. Nature. 2014; 505(7482):229-33. doi: 10.1038/nature12884.
    • (2014) Nature , vol.505 , Issue.7482 , pp. 229-233
    • Guo, Y.1    Dong, L.2    Qiu, X.3    Wang, Y.4    Zhang, B.5    Liu, H.6
  • 64
    • 27944458910 scopus 로고    scopus 로고
    • Using information theory to search for co-evolving residues in proteins
    • Martin LC, Gloor GB, Dunn SD, Wahl LM. Using information theory to search for co-evolving residues in proteins. Bioinformatics. 2005; 21(22):4116-24. doi: 10.1093/bioinformatics/bti671.
    • (2005) Bioinformatics , vol.21 , Issue.22 , pp. 4116-4124
    • Martin, L.C.1    Gloor, G.B.2    Dunn, S.D.3    Wahl, L.M.4
  • 65
    • 33947156744 scopus 로고    scopus 로고
    • Comparing clusterings-an information based distance
    • Meila M. Comparing clusterings-an information based distance. J Multivar Anal. 2007; 98(5):873-95. doi: 10.1016/j.jmva.2006.11.013.
    • (2007) J Multivar Anal , vol.98 , Issue.5 , pp. 873-895
    • Meila, M.1
  • 67
    • 85066389617 scopus 로고    scopus 로고
    • Data from: Robust and accurate prediction of residue-residue interactions across protein interfaces using evolutionary information
    • Ovchinnikov S, Kamisetty H, Baker D. Data from: Robust and accurate prediction of residue-residue interactions across protein interfaces using evolutionary information. 2014. doi: 10.5061/dryad.s00vr.
    • (2014)
    • Ovchinnikov, S.1    Kamisetty, H.2    Baker, D.3
  • 68
    • 84883427400 scopus 로고    scopus 로고
    • From principal component to direct coupling analysis of coevolution in proteins: low-eigenvalue modes are needed for structure prediction
    • Cocco S, Monasson R, Weigt M. From principal component to direct coupling analysis of coevolution in proteins: low-eigenvalue modes are needed for structure prediction. PLoS Comput Biol. 2013; 9(8):e1003176. doi: 10.1371/journal.pcbi.1003176.
    • (2013) PLoS Comput Biol , vol.9 , Issue.8 , pp. e1003176
    • Cocco, S.1    Monasson, R.2    Weigt, M.3
  • 69
    • 74249108517 scopus 로고    scopus 로고
    • Assessment of domain boundary predictions and the prediction of intramolecular contacts in CASP8
    • Ezkurdia I, Graña O, Izarzugaza JMG, Tress ML. Assessment of domain boundary predictions and the prediction of intramolecular contacts in CASP8. Proteins: Structure Function Bioinform. 2009; 77(S9):196-209. doi: 10.1002/prot.22554.
    • (2009) Proteins: Structure Function Bioinform , vol.77 , pp. 196-209
    • Ezkurdia, I.1    Graña, O.2    Izarzugaza, J.M.G.3    Tress, M.L.4
  • 71
    • 84940644968 scopus 로고
    • A mathematical theory of communication
    • Shannon CE. A mathematical theory of communication. Bell Syst Tech J. 1948; 27:379-423. https://dx.doi.org/10.1002%2Fj.1538-7305.1948.tb01338.x.
    • (1948) Bell Syst Tech J , vol.27 , pp. 379-423
    • Shannon, C.E.1
  • 72
    • 84872521100 scopus 로고    scopus 로고
    • Improved contact prediction in proteins: using pseudolikelihoods to infer potts models
    • Ekeberg M, Lovkvist C, Lan Y, Weigt M, Aurell E. Improved contact prediction in proteins: using pseudolikelihoods to infer potts models. Phys Rev E Stat Nonlinear Soft Matter Phys. 2013; 87(1):012707. http://www.ncbi.nlm.nih.gov/pubmed/23410359.
    • (2013) Phys Rev E Stat Nonlinear Soft Matter Phys , vol.87 , Issue.1 , pp. 012707
    • Ekeberg, M.1    Lovkvist, C.2    Lan, Y.3    Weigt, M.4    Aurell, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.