메뉴 건너뛰기




Volumn 11, Issue 6, 2012, Pages 469-478

Protein structure networks

Author keywords

Allostery; Graph theory; Long range interactions; Networks; Protein folding; Protein structure

Indexed keywords

AMINO ACID;

EID: 84870336885     PISSN: 20412649     EISSN: 20412657     Source Type: Journal    
DOI: 10.1093/bfgp/els039     Document Type: Article
Times cited : (61)

References (68)
  • 2
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright PE, Dyson HJ. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 1999;293:321-31.
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 3
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett 2005;579: 3346-54.
    • (2005) FEBS Lett , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 4
    • 52249085709 scopus 로고    scopus 로고
    • The unfoldomics decade: an update on intrinsically disordered proteins
    • Dunker AK, Oldfield C, Meng J, et al. The unfoldomics decade: an update on intrinsically disordered proteins. BMCGenomics 2008;9:S1.
    • (2008) BMC Genomics , vol.9
    • Dunker, A.K.1    Oldfield, C.2    Meng, J.3
  • 5
    • 0001266102 scopus 로고
    • A threedimensional model of the myoglobin molecule obtained by x-ray analysis
    • Kendrew JC, Bodo G, Dintzis HM, et al. A threedimensional model of the myoglobin molecule obtained by x-ray analysis. Nature 1958;181:662-66.
    • (1958) Nature , vol.181 , pp. 662-666
    • Kendrew, J.C.1    Bodo, G.2    Dintzis, H.M.3
  • 6
    • 36949066642 scopus 로고
    • Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis
    • Perutz MF, Rossmann MG, Cullis AF, et al. Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis. Nature 1960;185:416-22.
    • (1960) Nature , vol.185 , pp. 416-422
    • Perutz, M.F.1    Rossmann, M.G.2    Cullis, A.F.3
  • 7
    • 0013890819 scopus 로고
    • The crystal structure of insulin II. An investigation of rhombohedral zinc insulin crystals and a report of other crystalline forms
    • Harding MM, Hodgkin DC, Kennedy AF, et al. The crystal structure of insulin. II. An investigation of rhombohedral zinc insulin crystals and a report of other crystalline forms. JMol Biol 1966;16:212-26.
    • (1966) JMol Biol , vol.16 , pp. 212-226
    • Harding, M.M.1    Hodgkin, D.C.2    Kennedy, A.F.3
  • 8
    • 0016160014 scopus 로고
    • Two-angstrom crystal structure of oxidized chromatium high potential iron protein
    • Carter CW, Kraut J, Freer ST, et al. Two-angstrom crystal structure of oxidized chromatium high potential iron protein. J Biol Chem 1974;249:4212-25.
    • (1974) J Biol Chem , vol.249 , pp. 4212-4225
    • Carter, C.W.1    Kraut, J.2    Freer, S.T.3
  • 9
    • 0033887401 scopus 로고    scopus 로고
    • Early ribbon drawings of proteins
    • Richardson JS. Early ribbon drawings of proteins. NatStruct Mol Biol 2000;7:624-25.
    • (2000) NatStruct Mol Biol , vol.7 , pp. 624-625
    • Richardson, J.S.1
  • 10
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson JS. The anatomy and taxonomy of protein structure. Adv Protien Chem 1981;34:168-339.
    • (1981) Adv Protien Chem , vol.34 , pp. 168-339
    • Richardson, J.S.1
  • 11
    • 0022331151 scopus 로고
    • Schematic drawings of protein structures
    • Richardson J. Schematic drawings of protein structures. Methods Enzymol 1985;115:359-80.
    • (1985) Methods Enzymol , vol.115 , pp. 359-380
    • Richardson, J.1
  • 12
    • 0034284122 scopus 로고    scopus 로고
    • Recent changes to RasMol, recombining the variants
    • Bernstein HJ. Recent changes to RasMol, recombining the variants. Trends Biochem Sci 2000;25:453-55.
    • (2000) Trends Biochem Sci , vol.25 , pp. 453-455
    • Bernstein, H.J.1
  • 13
    • 4444221565 scopus 로고    scopus 로고
    • UCSF chimera- a visualization system for exploratory research and analysis
    • Pettersen EF, Goddard TD, Huang CC, et al. UCSF chimera- a visualization system for exploratory research and analysis. JComputat Chem 2004;25:1605-12.
    • (2004) JComputat Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3
  • 14
    • 0027049243 scopus 로고
    • The kinemage: a tool for scientific communication
    • Richardson DC, Richardson JS. The kinemage: a tool for scientific communication. Protein Sci 1992;1:3-9.
    • (1992) Protein Sci , vol.1 , pp. 3-9
    • Richardson, D.C.1    Richardson, J.S.2
  • 16
    • 41349118690 scopus 로고    scopus 로고
    • Small-world view of the amino acids that play a key role in protein folding
    • Vendruscolo M, Dokholyan NV, Paci E, et al. Small-world view of the amino acids that play a key role in protein folding. Phys Rev E 2002;65:061910.
    • (2002) Phys Rev E , vol.65 , pp. 061910
    • Vendruscolo, M.1    Dokholyan, N.V.2    Paci, E.3
  • 17
    • 0242720597 scopus 로고    scopus 로고
    • Uncovering network systems within protein structures
    • Greene LH, Higman VA. Uncovering network systems within protein structures. JMol Biol 2003;334:781-91.
    • (2003) JMol Biol , vol.334 , pp. 781-791
    • Greene, L.H.1    Higman, V.A.2
  • 18
    • 9944223645 scopus 로고    scopus 로고
    • Network properties of protein structures
    • Bagler G, Sinha S. Network properties of protein structures. Physica A 2005;346:27-33.
    • (2005) Physica A , vol.346 , pp. 27-33
    • Bagler, G.1    Sinha, S.2
  • 20
    • 77749318502 scopus 로고    scopus 로고
    • Universality in protein residue networks
    • Estrada E. Universality in protein residue networks. Biophys J 2010;98:890-900.
    • (2010) Biophys J , vol.98 , pp. 890-900
    • Estrada, E.1
  • 21
    • 0346057951 scopus 로고    scopus 로고
    • Small-world communication of residues and significance for protein dynamics
    • Atilgan AR, Akan P, Baysal C. Small-world communication of residues and significance for protein dynamics. BiophysJ 2004;86:85-91.
    • (2004) BiophysJ , vol.86 , pp. 85-91
    • Atilgan, A.R.1    Akan, P.2    Baysal, C.3
  • 22
    • 0037173002 scopus 로고    scopus 로고
    • Topological determinants of protein folding
    • Dokholyan NV, Li L, Ding F, et al. Topological determinants of protein folding. Proc Natl Acad Sci USA 2002;99: 8637-41.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8637-8641
    • Dokholyan, N.V.1    Li, L.2    Ding, F.3
  • 23
    • 70350031205 scopus 로고    scopus 로고
    • Understanding protein structure from a percolation perspective
    • Deb D, Vishveshwara S, Vishveshwara S. Understanding protein structure from a percolation perspective. Biophys J 2009;97:1787-94.
    • (2009) Biophys J , vol.97 , pp. 1787-1794
    • Deb, D.1    Vishveshwara, S.2    Vishveshwara, S.3
  • 24
    • 78349249413 scopus 로고    scopus 로고
    • A Topological description of hubs in amino acid interaction networks
    • Gaci O. A Topological description of hubs in amino acid interaction networks. Adv Bioinformatics 2010; 1-9.
    • (2010) Adv Bioinformatics , pp. 1-9
    • Gaci, O.1
  • 25
    • 79551587720 scopus 로고    scopus 로고
    • Cytoscape 2 8: new features for data integration and network visualization
    • Smoot ME, Ono K, Ruscheinski J, etal. Cytoscape 2.8: new features for data integration and network visualization. Bioinformatics 2011;27:431-32.
    • (2011) Bioinformatics , vol.27 , pp. 431-432
    • Smoot, M.E.1    Ono, K.2    Ruscheinski, J.3
  • 26
    • 79954415213 scopus 로고    scopus 로고
    • Analyzing and visualizing residue networks of protein structures
    • Doncheva NT, Klein K, Domingues FS, et al. Analyzing and visualizing residue networks of protein structures. Trends Biochem Sci 2011;36:179-82.
    • (2011) Trends Biochem Sci , vol.36 , pp. 179-182
    • Doncheva, N.T.1    Klein, K.2    Domingues, F.S.3
  • 27
    • 0033578690 scopus 로고    scopus 로고
    • Identification of side-chain clusters in protein structures by a graph spectral method
    • Kannan N, Vishveshwara S. Identification of side-chain clusters in protein structures by a graph spectral method. J Mol Biol 1999;292:441-64.
    • (1999) J Mol Biol , vol.292 , pp. 441-464
    • Kannan, N.1    Vishveshwara, S.2
  • 28
    • 0034491038 scopus 로고    scopus 로고
    • Protein domain decomposition using a graph-theoretic approach
    • Xu Y, Xu D, Gabow HN. Protein domain decomposition using a graph-theoretic approach. Bioinformatics 2000;16: 1091-104.
    • (2000) Bioinformatics , vol.16 , pp. 1091-1104
    • Xu, Y.1    Xu, D.2    Gabow, H.N.3
  • 29
    • 0037324306 scopus 로고    scopus 로고
    • Improving the performance of DomainParser for structural domain partition using neural network
    • Guo JT, Xu D, Kim D, et al. Improving the performance of DomainParser for structural domain partition using neural network. Nucleic Acids Res 2003;31:944-52.
    • (2003) Nucleic Acids Res , vol.31 , pp. 944-952
    • Guo, J.T.1    Xu, D.2    Kim, D.3
  • 30
    • 1842464687 scopus 로고    scopus 로고
    • Inter-residue interactions in protein folding and stability
    • Gromiha MM, Selvaraj S. Inter-residue interactions in protein folding and stability. Progr Biophys Mol Biol 2004;86: 235-77.
    • (2004) Progr Biophys Mol Biol , vol.86 , pp. 235-277
    • Gromiha, M.M.1    Selvaraj, S.2
  • 31
    • 59849093382 scopus 로고    scopus 로고
    • Protein cutoff scanning: a comparative analysis of cutoff dependent and cutoff free methods for prospecting contacts in proteins
    • Da Silveira CH, Pires DEV, Minardi RC, etal. Protein cutoff scanning: a comparative analysis of cutoff dependent and cutoff free methods for prospecting contacts in proteins. Proteins Struct Funct Bioinformatics 2009;74:727-43.
    • (2009) Proteins Struct Funct Bioinformatics , vol.74 , pp. 727-743
    • Da Silveira, C.H.1    Pires, D.E.V.2    Minardi, R.C.3
  • 32
    • 75149155238 scopus 로고    scopus 로고
    • Comparative analysis of thermophilic and mesophilic proteins using protein energy networks
    • Vijayabaskar M, Vishveshwara S. Comparative analysis of thermophilic and mesophilic proteins using protein energy networks. BMC Bioinformatics 2010;11:S49.
    • (2010) BMC Bioinformatics , vol.11
    • Vijayabaskar, M.1    Vishveshwara, S.2
  • 33
    • 79955024796 scopus 로고    scopus 로고
    • Mapping allostery through the covariance analysis of NMR chemical shifts
    • Selvaratnam R, Chowdhury S, Vanschouwen B, etal. Mapping allostery through the covariance analysis of NMR chemical shifts. ProcNatlAcad SciUSA 2011;108:6133-8.
    • (2011) ProcNatlAcad SciUSA , vol.108 , pp. 6133-6138
    • Selvaratnam, R.1    Chowdhury, S.2    Vanschouwen, B.3
  • 34
    • 0141571360 scopus 로고    scopus 로고
    • Conserved signature proposed for folding in the lipocalin superfamily
    • Greene LH, Hamada D, Eyles SJ, et al. Conserved signature proposed for folding in the lipocalin superfamily. FEBS Lett 2003;553:39-44.
    • (2003) FEBS Lett , vol.553 , pp. 39-44
    • Greene, L.H.1    Hamada, D.2    Eyles, S.J.3
  • 35
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • Bahar I, Atilgan AR, Erman B. Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. Folding Design 1997;2:173-81.
    • (1997) Folding Design , vol.2 , pp. 173-181
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 36
    • 46449101584 scopus 로고    scopus 로고
    • Discrete breathers in protein structures
    • Piazza F, Sanejouand Y-H. Discrete breathers in protein structures. Phys Biol 2008;5:1-14.
    • (2008) Phys Biol , vol.5 , pp. 1-14
    • Piazza, F.1    Sanejouand, Y.-H.2
  • 37
  • 38
    • 80455143537 scopus 로고    scopus 로고
    • Network analysis of transmembrane protein structures
    • Emerson IA, Gothandam KM. Network analysis of transmembrane protein structures. PhysicaAStatMechAppl 2012; 391:905-16.
    • (2012) Physica A Stat Mech Appl , vol.391 , pp. 905-916
    • Emerson, I.A.1    Gothandam, K.M.2
  • 39
    • 0038483826 scopus 로고    scopus 로고
    • Emergence of scaling in random networks
    • Barabasi Al AR. Emergence of scaling in random networks. Nature 1999;286:509-12.
    • (1999) Nature , vol.286 , pp. 509-512
    • Barabasi Al, A.R.1
  • 40
    • 33744827386 scopus 로고    scopus 로고
    • Elucidation of conserved long-range interaction networks in proteins and their significance in determining protein topology
    • Higman VA, Greene LH. Elucidation of conserved long-range interaction networks in proteins and their significance in determining protein topology. Physica A Stat Mech Appl 2006;368:595-606.
    • (2006) Physica A Stat Mech Appl , vol.368 , pp. 595-606
    • Higman, V.A.1    Greene, L.H.2
  • 41
    • 8544221118 scopus 로고    scopus 로고
    • Network analysis of protein structures identifies functional residues
    • Amitai G, Shemesh A, Sitbon E, et al. Network analysis of protein structures identifies functional residues. J Mol Biol 2004;344:1135-46.
    • (2004) J Mol Biol , vol.344 , pp. 1135-1146
    • Amitai, G.1    Shemesh, A.2    Sitbon, E.3
  • 42
    • 33745461893 scopus 로고    scopus 로고
    • Residues crucial for maintaining short paths in network communication mediate signaling in proteins
    • del Sol A, Fujihashi H, Amoros D, et al. Residues crucial for maintaining short paths in network communication mediate signaling in proteins. Mol Syst Biol 2006;2.
    • (2006) Mol Syst Biol , pp. 2
    • del Sol, A.1    Fujihashi, H.2    Amoros, D.3
  • 43
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionary conserved networks of residues mediate allosteric communication in proteins
    • Suel GM, Lockless SW, Wall MA, et al. Evolutionary conserved networks of residues mediate allosteric communication in proteins. Nat Struct Biol 2002;10:59-69.
    • (2002) Nat Struct Biol , vol.10 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3
  • 44
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionary conserved pathways of energetic connectivity in protein families
    • Lockless SW, Ranganathan R. Evolutionary conserved pathways of energetic connectivity in protein families. Science 1999;286:295-99.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 45
    • 34548815693 scopus 로고    scopus 로고
    • Modular architecture of protein structures and allosteric communications: potential implications for signaling proteins and regulatory linkages
    • Del Sol A, Arauzo-Bravo M, Amoros D, et al. Modular architecture of protein structures and allosteric communications: potential implications for signaling proteins and regulatory linkages. Genome Biol 2007;8:R92.
    • (2007) Genome Biol , vol.8
    • Del Sol, A.1    Arauzo-Bravo, M.2    Amoros, D.3
  • 46
    • 41949141017 scopus 로고    scopus 로고
    • Proteins as networks: usefulness of graph theory in protein science
    • Krishnan A, Zbilut JP, Tomita M, et al. Proteins as networks: usefulness of graph theory in protein science. Curr Protein Peptide Sci 2008;9:28-38.
    • (2008) Curr Protein Peptide Sci , vol.9 , pp. 28-38
    • Krishnan, A.1    Zbilut, J.P.2    Tomita, M.3
  • 47
    • 80052687731 scopus 로고    scopus 로고
    • Protein multi-scale organization through graph partitioning and robustness analysis: application to the myosin-myosin light chain interaction
    • Delmotte A, Tate EW, Yaliraki SN, et al. Protein multi-scale organization through graph partitioning and robustness analysis: application to the myosin-myosin light chain interaction. Phys Biol 2011;8:055010.
    • (2011) Phys Biol , vol.8 , pp. 055010
    • Delmotte, A.1    Tate, E.W.2    Yaliraki, S.N.3
  • 48
    • 68749107059 scopus 로고    scopus 로고
    • Protein sectors: evolutionary units of three-dimensional structure
    • Halabi N, Rivoire O, Leibler S, et al. Protein sectors: evolutionary units of three-dimensional structure. Cell 2009; 138:774-86.
    • (2009) Cell , vol.138 , pp. 774-786
    • Halabi, N.1    Rivoire, O.2    Leibler, S.3
  • 50
    • 84865075440 scopus 로고    scopus 로고
    • ModuLand plug-in for Cytoscape: determination of hierarchical layers of overlapping network modules and community centrality
    • Szalay-Bekö M, Palotai R, Szappanos B, et al. ModuLand plug-in for Cytoscape: determination of hierarchical layers of overlapping network modules and community centrality. Bioinformatics 2012;28:2202-04.
    • (2012) Bioinformatics , vol.28 , pp. 2202-2204
    • Szalay-Bekö, M.1    Palotai, R.2    Szappanos, B.3
  • 51
    • 0017309766 scopus 로고
    • Structural patterns in globular proteins
    • Levitt M, Chothia C. Structural patterns in globular proteins. Nature 1976;261:552-58.
    • (1976) Nature , vol.261 , pp. 552-558
    • Levitt, M.1    Chothia, C.2
  • 52
    • 84857982668 scopus 로고    scopus 로고
    • The Protein Data Bank at 40 reflecting on the Past to Prepare for the Future
    • Berman HM, Kleywegt GJ, Nakamura H, etal. The Protein Data Bank at 40: reflecting on the Past to Prepare for the Future. Structure 2012;20:391-96.
    • (2012) Structure , vol.20 , pp. 391-396
    • Berman, H.M.1    Kleywegt, G.J.2    Nakamura, H.3
  • 53
    • 78651345652 scopus 로고    scopus 로고
    • The RCSB Protein Data Bank: redesigned web site and web services
    • Rose PW, Beran B, Bi C, et al. The RCSB Protein Data Bank: redesigned web site and web services. Nucleic Acids Res 2011;39:D392-401.
    • (2011) Nucleic Acids Res , vol.39
    • Rose, P.W.1    Beran, B.2    Bi, C.3
  • 54
    • 0030777303 scopus 로고    scopus 로고
    • CATH-a hierarchic classification of protein domain structures
    • Orengo CA, Michie AD, Jones S, et al. CATH-a hierarchic classification of protein domain structures. Structure 1997;5: 1093-108.
    • (1997) Structure , vol.5 , pp. 1093-1108
    • Orengo, C.A.1    Michie, A.D.2    Jones, S.3
  • 55
    • 0028961335 scopus 로고
    • SCOP: a structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, et al. SCOP: a structural classification of proteins database for the investigation of sequences and structures. JMolBiol 1995;247:536-40.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3
  • 56
    • 33744805069 scopus 로고    scopus 로고
    • Protein structure comparison: implications for the nature of 'fold space', and structure and function prediction
    • Kolodny R, Petrey D, Honig B. Protein structure comparison: implications for the nature of 'fold space', and structure and function prediction. Curr Opin Struct Biol 2006;16: 393-98.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 393-398
    • Kolodny, R.1    Petrey, D.2    Honig, B.3
  • 57
    • 68249149510 scopus 로고    scopus 로고
    • The CATH hierarchy revisited-structural divergence in domain superfamilies and the continuity of fold space
    • Cuff A, Redfern OC, Greene L, et al. The CATH hierarchy revisited-structural divergence in domain superfamilies and the continuity of fold space. Structure 2009;17:1051-62.
    • (2009) Structure , vol.17 , pp. 1051-1062
    • Cuff, A.1    Redfern, O.C.2    Greene, L.3
  • 59
    • 0035252350 scopus 로고    scopus 로고
    • Three key residues form a critical contact network in a protein folding transition state
    • Vendruscolo M, Paci E, Dobson CM, et al. Three key residues form a critical contact network in a protein folding transition state. Nature 2001;409:641-45.
    • (2001) Nature , vol.409 , pp. 641-645
    • Vendruscolo, M.1    Paci, E.2    Dobson, C.M.3
  • 60
    • 4143090730 scopus 로고    scopus 로고
    • The protein folding network
    • Rao F, Caflisch A. The protein folding network. JMolBiol 2004;342:299-306.
    • (2004) JMolBiol , vol.342 , pp. 299-306
    • Rao, F.1    Caflisch, A.2
  • 61
    • 84859265748 scopus 로고    scopus 로고
    • Protein folding by 'levels of separation': a hypothesis
    • Greene LH, Grant T. Protein folding by 'levels of separation': a hypothesis. FEBS Lett 2012;586:962-66.
    • (2012) FEBS Lett , vol.586 , pp. 962-966
    • Greene, L.H.1    Grant, T.2
  • 62
    • 44349106520 scopus 로고    scopus 로고
    • Identifying folding nucleus based on residue contact networks of proteins
    • Li J, Wang J, Wang W. Identifying folding nucleus based on residue contact networks of proteins. Proteins Struct Funct Bioinformatics 2008;71:1899-907.
    • (2008) Proteins Struct Funct Bioinformatics , vol.71 , pp. 1899-1907
    • Li, J.1    Wang, J.2    Wang, W.3
  • 63
    • 78649309080 scopus 로고    scopus 로고
    • Folding network of villin headpiece subdomain
    • Lei H, Su Y, Jin L, et al. Folding network of villin headpiece subdomain. BiophysJ 2010;99:3374-84.
    • (2010) Biophys J , vol.99 , pp. 3374-3384
    • Lei, H.1    Su, Y.2    Jin, L.3
  • 64
    • 34047195261 scopus 로고    scopus 로고
    • Dynamics of lysozyme structure network: probing the process of unfolding
    • Ghosh A, Brinda KV, Vishveshwara S. Dynamics of lysozyme structure network: probing the process of unfolding. BiophysJ 2007;92:2523-35.
    • (2007) Biophys J , vol.92 , pp. 2523-2535
    • Ghosh, A.1    Brinda, K.V.2    Vishveshwara, S.3
  • 66
    • 0038718854 scopus 로고    scopus 로고
    • The structure and function of complex networks
    • Newman MEJ. The structure and function of complex networks. SIAMRev 2003;45:167-256.
    • (2003) SIAMRev , vol.45 , pp. 167-256
    • Newman, M.E.J.1
  • 67
    • 84859330193 scopus 로고
    • A Set of measures of centrality based on betweenness
    • Linton CF. A Set of measures of centrality based on betweenness. Sociometry 1977;40:35-41.
    • (1977) Sociometry , vol.40 , pp. 35-41
    • Linton, C.F.1
  • 68
    • 34249910312 scopus 로고    scopus 로고
    • Network analysis of protein dynamics
    • Böde C, Kovács IA, Szalay MS, et al. Network analysis of protein dynamics. FEBS Lett 2007;581:2776-82.
    • (2007) FEBS Lett , vol.581 , pp. 2776-2782
    • Böde, C.1    Kovács, I.A.2    Szalay, M.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.