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Volumn 11, Issue 6, 2012, Pages 479-488

Local motifs in proteins combine to generate global functional moves

Author keywords

Allosteric communication; Amino acid contacts; Assortative coordination; Collective dynamics; Redundant links; Weighted networks

Indexed keywords

PROTEIN;

EID: 84870315927     PISSN: 20412649     EISSN: 20412657     Source Type: Journal    
DOI: 10.1093/bfgp/els027     Document Type: Article
Times cited : (18)

References (66)
  • 1
    • 79959704466 scopus 로고    scopus 로고
    • Exploration of the relationship between topology and designability of conformations
    • Leelananda SP, Towfic F, Jernigan RL, et al. Exploration of the relationship between topology and designability of conformations. J Chem Phys 2011;134:235101.
    • (2011) J Chem Phys , vol.134 , pp. 235101
    • Leelananda, S.P.1    Towfic, F.2    Jernigan, R.L.3
  • 2
    • 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. Biophys J 2004;86:85-91.
    • (2004) Biophys J , vol.86 , pp. 85-91
    • Atilgan, A.R.1    Akan, P.2    Baysal, C.3
  • 3
    • 0242720597 scopus 로고    scopus 로고
    • Uncovering network systems within protein structures
    • Greene LH, Higman VA. Uncovering network systems within protein structures. J Mol Biol 2003;334:781-91.
    • (2003) J Mol Biol , vol.334 , pp. 781-791
    • Greene, L.H.1    Higman, V.A.2
  • 4
    • 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
  • 5
    • 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 Des 1997;2:173-81.
    • (1997) Folding Des , vol.2 , pp. 173-181
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 6
    • 0000496772 scopus 로고    scopus 로고
    • Vibrational dynamics of folded proteins: significance of slow and fast motions in relation to function and stability
    • Bahar I, Atilgan AR, Demirel MC, et al. Vibrational dynamics of folded proteins: significance of slow and fast motions in relation to function and stability. Phys Rev Lett 1998; 80:2733-6.
    • (1998) Phys Rev Lett , vol.80 , pp. 2733-2736
    • Bahar, I.1    Atilgan, A.R.2    Demirel, M.C.3
  • 7
    • 34848882812 scopus 로고    scopus 로고
    • Signal propagation in proteins and relation to equilibrium fluctuations
    • Chennubhotla C, Bahar I. Signal propagation in proteins and relation to equilibrium fluctuations. PLoS Comput Biol 2007;3:1716-26.
    • (2007) PLoS Comput Biol , vol.3 , pp. 1716-1726
    • Chennubhotla, C.1    Bahar, I.2
  • 8
    • 12944331889 scopus 로고    scopus 로고
    • Small-world network approach to identify key residues in protein-protein interaction
    • del Sol A, O'Meara P. Small-world network approach to identify key residues in protein-protein interaction. Proteins 2005;58:672-82.
    • (2005) Proteins , vol.58 , pp. 672-682
    • del Sol, A.1    O'Meara, P.2
  • 9
    • 34249308113 scopus 로고    scopus 로고
    • How accurate and statistically robust are catalytic site predictions based on closeness centrality?
    • Chea E, Livesay DR. How accurate and statistically robust are catalytic site predictions based on closeness centrality? BMC Bioinformatics 2007;8:153.
    • (2007) BMC Bioinformatics , vol.8 , pp. 153
    • Chea, E.1    Livesay, D.R.2
  • 10
  • 11
    • 33745024278 scopus 로고    scopus 로고
    • Symmetry, form, and shape: guiding principles for robustness in macromolecular machines
    • Tama F, Brooks CL. Symmetry, form, and shape: guiding principles for robustness in macromolecular machines. Annu Rev Biophys Biomol Struct 2006;35:115-33.
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 115-133
    • Tama, F.1    Brooks, C.L.2
  • 12
    • 34547666968 scopus 로고    scopus 로고
    • How well can we understand large-scale protein motions using normal modes of elastic network models?
    • Yang L, Song G, Jernigan RL. How well can we understand large-scale protein motions using normal modes of elastic network models? Biophys J 2007;93:920-9.
    • (2007) Biophys J , vol.93 , pp. 920-929
    • Yang, L.1    Song, G.2    Jernigan, R.L.3
  • 14
    • 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
  • 15
    • 34247580211 scopus 로고    scopus 로고
    • Screened nonbonded interactions in native proteins manipulate optimal paths for robust residue communication
    • Atilgan AR, Turgut D, Atilgan C. Screened nonbonded interactions in native proteins manipulate optimal paths for robust residue communication. Biophys J 2007;92: 3052-62.
    • (2007) Biophys J , vol.92 , pp. 3052-3062
    • Atilgan, A.R.1    Turgut, D.2    Atilgan, C.3
  • 16
    • 33747843929 scopus 로고    scopus 로고
    • Dependence of single-molecule junction conductance on molecular conformation
    • Venkataraman L, Klare JE, Nuckolls C, et al. Dependence of single-molecule junction conductance on molecular conformation. Nature 2006;442:904-7.
    • (2006) Nature , vol.442 , pp. 904-907
    • Venkataraman, L.1    Klare, J.E.2    Nuckolls, C.3
  • 19
    • 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, et al. Protein cutoff scanning: a comparative analysis of cutoff dependent and cutoff free methods for prospecting contacts in proteins. Proteins 2009;74:727-43.
    • (2009) Proteins , vol.74 , pp. 727-743
    • da Silveira, C.H.1    Pires, D.E.V.2    Minardi, R.C.3
  • 20
    • 0033047710 scopus 로고    scopus 로고
    • A neural network based predictor of residue contacts in proteins
    • Fariselli P, Casadio R. A neural network based predictor of residue contacts in proteins. Protein Eng 1999;12:15-21.
    • (1999) Protein Eng , vol.12 , pp. 15-21
    • Fariselli, P.1    Casadio, R.2
  • 21
    • 0031672563 scopus 로고    scopus 로고
    • Identification of kinetically hot residues in proteins
    • Demirel MC, Atilgan AR, Jernigan RL, et al. Identification of kinetically hot residues in proteins. Protein Sci 1998;7: 2522-32.
    • (1998) Protein Sci , vol.7 , pp. 2522-2532
    • Demirel, M.C.1    Atilgan, A.R.2    Jernigan, R.L.3
  • 22
    • 0034901412 scopus 로고    scopus 로고
    • Are proteins well-packed?
    • Liang J, Dill KA. Are proteins well-packed? Biophys J 2001; 81:751-66.
    • (2001) Biophys J , vol.81 , pp. 751-766
    • Liang, J.1    Dill, K.A.2
  • 23
    • 80054952081 scopus 로고    scopus 로고
    • Combinatorial study of degree assortativity in networks
    • Estrada E. Combinatorial study of degree assortativity in networks. Phys Rev E Stat Nonlin Soft Matter Phys 2011; 84(4 Pt 2):047101.
    • (2011) Phys Rev E Stat Nonlin Soft Matter Phys , vol.84 , Issue.4 PART 2 , pp. 047101
    • Estrada, E.1
  • 24
    • 78650757173 scopus 로고    scopus 로고
    • Assortative mixing in close-packed spatial networks
    • Turgut D, Atilgan AR, Atilgan C. Assortative mixing in close-packed spatial networks. PLoS One 2010;5: e15551.
    • (2010) PLoS One , vol.5
    • Turgut, D.1    Atilgan, A.R.2    Atilgan, C.3
  • 26
    • 55249123363 scopus 로고    scopus 로고
    • Variations in clique and community patterns in protein structures during allosteric communication: investigation of dynamically equilibrated structures of methionyl tRNA synthetase complexes
    • Ghosh A, Vishveshwara S. Variations in clique and community patterns in protein structures during allosteric communication: investigation of dynamically equilibrated structures of methionyl tRNA synthetase complexes. Biochemistry 2008;47:11398-407.
    • (2008) Biochemistry , vol.47 , pp. 11398-11407
    • Ghosh, A.1    Vishveshwara, S.2
  • 27
    • 79955670187 scopus 로고    scopus 로고
    • Network approach for capturing ligand-induced subtle global changes in protein structures
    • Sukhwal A, Bhattacharyya M, Vishveshwara S. Network approach for capturing ligand-induced subtle global changes in protein structures. Acta Crystallogr DBiol Crystallogr 2011; 67:429-39.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 429-439
    • Sukhwal, A.1    Bhattacharyya, M.2    Vishveshwara, S.3
  • 28
    • 70149098505 scopus 로고    scopus 로고
    • Coarse-grained modeling of allosteric regulation in protein receptors
    • Balabin IA, Yang WT, Beratan DN. Coarse-grained modeling of allosteric regulation in protein receptors. Proc Natl Acad Sci USA 2009;106:14253-8.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14253-14258
    • Balabin, I.A.1    Yang, W.T.2    Beratan, D.N.3
  • 29
    • 77955680967 scopus 로고    scopus 로고
    • Manipulation of conformational change in proteins by single-residue perturbations
    • Atilgan C, Gerek ZN, Ozkan SB, et al. Manipulation of conformational change in proteins by single-residue perturbations. Biophys J 2010;99:933-43.
    • (2010) Biophys J , vol.99 , pp. 933-943
    • Atilgan, C.1    Gerek, Z.N.2    Ozkan, S.B.3
  • 30
    • 84857131975 scopus 로고    scopus 로고
    • Disordered proteins and network disorder in network descriptions of protein structure, dynamics and function Hypotheses and a comprehensive review
    • Csermely P, Sandhu KS, Hazai E, et al. Disordered proteins and network disorder in network descriptions of protein structure, dynamics and function. Hypotheses and a comprehensive review. Curr Protein Peptide Sci 2012;13:19-33.
    • (2012) Curr Protein Peptide Sci , vol.13 , pp. 19-33
    • Csermely, P.1    Sandhu, K.S.2    Hazai, E.3
  • 32
    • 73449126303 scopus 로고    scopus 로고
    • Perturbation-response scanning reveals ligand entry-exit mechanisms of ferric binding protein
    • Atilgan C, Atilgan AR. Perturbation-response scanning reveals ligand entry-exit mechanisms of ferric binding protein. PloS Comput Biol 2009;5:14.
    • (2009) PloS Comput Biol , vol.5 , pp. 14
    • Atilgan, C.1    Atilgan, A.R.2
  • 33
    • 84859265748 scopus 로고    scopus 로고
    • Protein folding by 'levels of separation': a hypothesis
    • Greene LH, Grant TM. Protein folding by 'levels of separation': a hypothesis. FEBS Lett 2012;586:962-6.
    • (2012) FEBS Lett , vol.586 , pp. 962-966
    • Greene, L.H.1    Grant, T.M.2
  • 35
    • 0032005126 scopus 로고    scopus 로고
    • Simplified proteins: minimalist solutions to the 'protein folding problem'
    • Plaxco KW, Riddle DS, Grantcharova V, et al. Simplified proteins: minimalist solutions to the 'protein folding problem'. Curr Opin Struct Biol 1998;8:80-5.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 80-85
    • Plaxco, K.W.1    Riddle, D.S.2    Grantcharova, V.3
  • 36
    • 82955201864 scopus 로고    scopus 로고
    • Local and non-local native topologies reveal the underlying folding landscape of proteins
    • Zou TS, Ozkan SB. Local and non-local native topologies reveal the underlying folding landscape of proteins. Phys Biol 2011;8:066011.
    • (2011) Phys Biol , vol.8 , pp. 066011
    • Zou, T.S.1    Ozkan, S.B.2
  • 37
    • 54249105941 scopus 로고    scopus 로고
    • Surface sites for engineering allosteric control in proteins
    • Lee J, Natarajan M, Nashine VC, et al. Surface sites for engineering allosteric control in proteins. Science 2008;322: 438-42.
    • (2008) Science , vol.322 , pp. 438-442
    • Lee, J.1    Natarajan, M.2    Nashine, V.C.3
  • 38
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless SW, Ranganathan R. Evolutionarily conserved pathways of energetic connectivity in protein families. Science 1999;286:295-9.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 39
    • 60849087655 scopus 로고    scopus 로고
    • Distance matrix-based approach to protein structure prediction
    • Kloczkowski A, Jernigan RL, Wu Z, et al. Distance matrix-based approach to protein structure prediction. J Struct Funct Genomics 2009;10:67-81.
    • (2009) J Struct Funct Genomics , vol.10 , pp. 67-81
    • Kloczkowski, A.1    Jernigan, R.L.2    Wu, Z.3
  • 40
    • 65649089458 scopus 로고    scopus 로고
    • Intra and intermolecular communications through protein structure network
    • Vishveshwara S, Ghosh A, Hansia P. Intra and intermolecular communications through protein structure network. Curr Protein Pept Sci 2009;10:146-60.
    • (2009) Curr Protein Pept Sci , vol.10 , pp. 146-160
    • Vishveshwara, S.1    Ghosh, A.2    Hansia, P.3
  • 41
    • 34248185088 scopus 로고    scopus 로고
    • Construction and application of the weighted amino acid network based on energy
    • Jiao X, Chang S, Li CH, et al. Construction and application of the weighted amino acid network based on energy. Phys Rev E Stat Nonlin Soft Matter Phy 2007;75(5 Pt 1):051903.
    • (2007) Phys Rev E Stat Nonlin Soft Matter Phy , vol.75 , Issue.5 PART 1 , pp. 051903
    • Jiao, X.1    Chang, S.2    Li, C.H.3
  • 42
    • 78649883885 scopus 로고    scopus 로고
    • Interaction energy based protein structure networks
    • Vijayabaskar MS, Vishveshwara S. Interaction energy based protein structure networks. Biophys J 2010;99:3704-15.
    • (2010) Biophys J , vol.99 , pp. 3704-3715
    • Vijayabaskar, M.S.1    Vishveshwara, S.2
  • 43
    • 0029919190 scopus 로고    scopus 로고
    • Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading
    • Miyazawa S, Jernigan RL. Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading. J Mol Biol 1996; 256:623-44.
    • (1996) J Mol Biol , vol.256 , pp. 623-644
    • Miyazawa, S.1    Jernigan, R.L.2
  • 44
    • 0029909384 scopus 로고    scopus 로고
    • An iterative method for extracting energy-like quantities from protein structures
    • Thomas PD, Dill KA. An iterative method for extracting energy-like quantities from protein structures. Proc Natl Acad Sci USA 1996;93:11628-33.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11628-11633
    • Thomas, P.D.1    Dill, K.A.2
  • 45
    • 33144476007 scopus 로고    scopus 로고
    • Universal behavior of optimal paths in weighted networks with general disorder
    • Chen YP, Lopez E, Havlin S, et al. Universal behavior of optimal paths in weighted networks with general disorder. Phys Rev Lett 2006;96:068702.
    • (2006) Phys Rev Lett , vol.96 , pp. 068702
    • Chen, Y.P.1    Lopez, E.2    Havlin, S.3
  • 46
    • 33745461893 scopus 로고    scopus 로고
    • Residues crucial for maintaining short paths in network communication mediate signaling in proteins
    • 2006
    • 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: 2006.0019.
    • (2006) Mol Syst Biol , vol.2 , pp. 0019
    • del Sol, A.1    Fujihashi, H.2    Amoros, D.3
  • 47
    • 84861411420 scopus 로고    scopus 로고
    • Network-based models as tools hinting at nonevident protein functionality
    • Atilgan C, Okan OB, Atilgan AR. Network-based models as tools hinting at nonevident protein functionality. Annu Rev Biophys 2012;41:205-25.
    • (2012) Annu Rev Biophys , vol.41 , pp. 205-225
    • Atilgan, C.1    Okan, O.B.2    Atilgan, A.R.3
  • 48
    • 0012015514 scopus 로고    scopus 로고
    • How much sequence variation can the functions of biological molecules tolerate
    • Frauenfelder H, Deisenhofer J, Wolynes PG (eds) Berlin, Germany: Dahlem University Press
    • Baase WA, Gassner NC, Zhang X-J, et al. How much sequence variation can the functions of biological molecules tolerate. In: Frauenfelder H, Deisenhofer J, Wolynes PG (eds). Simplicity and Complexity in Proteins and Nucleic Acids. Berlin, Germany: Dahlem University Press, 1999:297-311.
    • (1999) Simplicity and Complexity in Proteins and Nucleic Acids , pp. 297-311
    • Baase, W.A.1    Gassner, N.C.2    Zhang, X.-J.3
  • 49
    • 65649100094 scopus 로고    scopus 로고
    • Frameworks for understanding longrange intra-protein communication
    • Whitley MJ, Lee AL. Frameworks for understanding longrange intra-protein communication. Curr Protein Pept Sci 2009;10:116-27.
    • (2009) Curr Protein Pept Sci , vol.10 , pp. 116-127
    • Whitley, M.J.1    Lee, A.L.2
  • 50
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel GM, Lockless SW, Wall MA, et al. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat Struct Biol 2003;10:59-69.
    • (2003) Nat Struct Biol , vol.10 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3
  • 51
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • Hilser VJ, Thompson EB. Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. Proc Natl Acad Sci USA 2007;104:8311-15.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 52
    • 34248332629 scopus 로고    scopus 로고
    • Functional residues serve a dominant role in mediating the cooperativity of the protein ensemble
    • Liu T, Whitten ST, Hilser VJ. Functional residues serve a dominant role in mediating the cooperativity of the protein ensemble. Proc Natl Acad Sci USA 2007;104:4347-52.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4347-4352
    • Liu, T.1    Whitten, S.T.2    Hilser, V.J.3
  • 53
    • 33748442882 scopus 로고    scopus 로고
    • Coupling of global and local vibrational modes in dynamic allostery of proteins
    • Hawkins RJ, McLeish TCB. Coupling of global and local vibrational modes in dynamic allostery of proteins. Biophys J 2006;91:2055-62.
    • (2006) Biophys J , vol.91 , pp. 2055-2062
    • Hawkins, R.J.1    McLeish, T.C.B.2
  • 54
    • 0032474444 scopus 로고    scopus 로고
    • Constitutive activation of opsin by mutation of methionine 257 on transmembrane helix 6
    • Han M, Smith SO, Sakmar TP. Constitutive activation of opsin by mutation of methionine 257 on transmembrane helix 6. Biochemistry 1998;37:8253-61.
    • (1998) Biochemistry , vol.37 , pp. 8253-8261
    • Han, M.1    Smith, S.O.2    Sakmar, T.P.3
  • 55
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G protein-coupled receptors: implications of the highresolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • Ballesteros JA, Shi L, Javitch JA. Structural mimicry in G protein-coupled receptors: implications of the highresolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Mol Pharmacol 2001; 60:1-19.
    • (2001) Mol Pharmacol , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 56
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether U. Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocr Rev 2000; 21:90-113.
    • (2000) Endocr Rev , vol.21 , pp. 90-113
    • Gether, U.1
  • 57
    • 79951518651 scopus 로고    scopus 로고
    • Modeling allosteric signal propagation using protein structure networks
    • Park K, Kim D. Modeling allosteric signal propagation using protein structure networks. BMC Bioinformatics 2011; 12.
    • (2011) BMC Bioinformatics , pp. 12
    • Park, K.1    Kim, D.2
  • 58
    • 22444450449 scopus 로고    scopus 로고
    • Intramolecular signaling pathways revealed by modeling anisotropic thermal diffusion
    • Ota N, Agard DA. Intramolecular signaling pathways revealed by modeling anisotropic thermal diffusion. J Mol Biol 2005;351:345-54.
    • (2005) J Mol Biol , vol.351 , pp. 345-354
    • Ota, N.1    Agard, D.A.2
  • 59
    • 53549104402 scopus 로고    scopus 로고
    • Activation of tyrosine kinases by mutation of the gatekeeper threonine
    • Azam M, Seeliger MA, Gray NS, et al. Activation of tyrosine kinases by mutation of the gatekeeper threonine. Nat Struct Mol Biol 2008;15:1109-18.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1109-1118
    • Azam, M.1    Seeliger, M.A.2    Gray, N.S.3
  • 60
    • 79960284776 scopus 로고    scopus 로고
    • Probing the allosteric mechanism in pyrrolysyl-tRNA synthetase using energyweighted network formalism
    • Bhattacharyya M, Vishyeshwara S. Probing the allosteric mechanism in pyrrolysyl-tRNA synthetase using energyweighted network formalism. Biochemistry 2011;50: 6225-36.
    • (2011) Biochemistry , vol.50 , pp. 6225-6236
    • Bhattacharyya, M.1    Vishyeshwara, S.2
  • 61
    • 80054804699 scopus 로고    scopus 로고
    • Allosteric communication in cysteinyl tRNA synthetase: a network of direct and indirect readout
    • Ghosh A, Sakaguchi R, Liu CP, et al. Allosteric communication in cysteinyl tRNA synthetase: a network of direct and indirect readout. J Biol Chem 2011;286:37721-31.
    • (2011) J Biol Chem , vol.286 , pp. 37721-37731
    • Ghosh, A.1    Sakaguchi, R.2    Liu, C.P.3
  • 62
    • 66149086947 scopus 로고    scopus 로고
    • Dynamical networks in tRNA: protein complexes
    • Sethi A, Eargle J, Black AA, et al. Dynamical networks in tRNA: protein complexes. ProcNatlAcad SciUSA 2009;106: 6620-5.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 6620-6625
    • Sethi, A.1    Eargle, J.2    Black, A.A.3
  • 64
    • 80054029334 scopus 로고    scopus 로고
    • h-Degree as a basic measure in weighted networks
    • Zhao SX, Rousseau R, Ye FY. h-Degree as a basic measure in weighted networks. J Informetrics 2011;5:668-77.
    • (2011) J Informetrics , vol.5 , pp. 668-677
    • Zhao, S.X.1    Rousseau, R.2    Ye, F.Y.3
  • 66
    • 84255188571 scopus 로고    scopus 로고
    • Modelling dynamical processes in complex socio-technical systems
    • Vespignani A. Modelling dynamical processes in complex socio-technical systems. Nat Phys 2012;8:32-39.
    • (2012) Nat Phys , vol.8 , pp. 32-39
    • Vespignani, A.1


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