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Volumn 4, Issue 10, 2008, Pages

Protein docking by the underestimation of free energy funnels in the space of encounter complexes

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION REACTIONS; CHAINS; INTERFACE STATES; MONTE CARLO METHODS; PROTEINS; STOCHASTIC SYSTEMS;

EID: 55449101982     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000191     Document Type: Article
Times cited : (38)

References (51)
  • 1
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz P, Giot L, Cagney G, Mansfield TA, Judson RS, et al. (2000) A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403: 623-627.
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1    Giot, L.2    Cagney, G.3    Mansfield, T.A.4    Judson, R.S.5
  • 2
    • 0035836765 scopus 로고    scopus 로고
    • A comprehensive two-hybrid analysis to explore the yeast protein interactome
    • Ito T, Chiba T, Ozawa R, Yoshida M, Hattori M, et al. (2001) A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc Natl Acad Sci U S A 98: 4569-4574.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 4569-4574
    • Ito, T.1    Chiba, T.2    Ozawa, R.3    Yoshida, M.4    Hattori, M.5
  • 3
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin AC, Bosche M, Krause R, Grandi P, Marzioch M, et al. (2002) Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415: 141-147.
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1    Bosche, M.2    Krause, R.3    Grandi, P.4    Marzioch, M.5
  • 4
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y, Gruhler A, Heilbut A, Bader GD, Moore L, et al. (2002) Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415: 180-183.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3    Bader, G.D.4    Moore, L.5
  • 6
    • 0026723063 scopus 로고
    • Protein folding funnels: A kinetic approach to the sequence-structure relationship
    • Leopold PE, Montal M, Onuchic JN (1992) Protein folding funnels: a kinetic approach to the sequence-structure relationship. Proc Natl Acad Sci U S A 89: 8721-8725.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 8721-8725
    • Leopold, P.E.1    Montal, M.2    Onuchic, J.N.3
  • 7
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein-folding: A synthesis
    • Bryngelson J, Onuchic JN, Socci ND, Wolynes PG (1995) Funnels, pathways, and the energy landscape of protein-folding: a synthesis. Proteins 21: 167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 8
    • 0032993447 scopus 로고    scopus 로고
    • Polymer principles and protein folding
    • Dill KA (1999) Polymer principles and protein folding. Protein Sci 8: 1166-1180.
    • (1999) Protein Sci , vol.8 , pp. 1166-1180
    • Dill, K.A.1
  • 9
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai CJ, Kumar S, Ma B, Nussinov R (1999) Folding funnels, binding funnels, and protein function. Protein Sci 8: 1981-1990.
    • (1999) Protein Sci , vol.8 , pp. 1981-1990
    • Tsai, C.J.1    Kumar, S.2    Ma, B.3    Nussinov, R.4
  • 10
    • 0032054612 scopus 로고    scopus 로고
    • Theory of biomolecular recognition
    • McCammon JA (1998) Theory of biomolecular recognition. Curr Opin Struct Biol 8: 245-249.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 245-249
    • McCammon, J.A.1
  • 11
    • 0033081069 scopus 로고    scopus 로고
    • Protein-protein recognition: Exploring the energy funnels near the binding sites
    • Zhang C, Chan J, DeLisi C (1999) Protein-protein recognition: exploring the energy funnels near the binding sites. Proteins 34: 255-267.
    • (1999) Proteins , vol.34 , pp. 255-267
    • Zhang, C.1    Chan, J.2    DeLisi, C.3
  • 12
    • 0034916879 scopus 로고    scopus 로고
    • How common is the funnel-like energy landscape in protein-protein interactions?
    • Tovchigrechko A, Vakser IA (2001) How common is the funnel-like energy landscape in protein-protein interactions? Protein Sci 10: 1572-1583.
    • (2001) Protein Sci , vol.10 , pp. 1572-1583
    • Tovchigrechko, A.1    Vakser, I.A.2
  • 13
    • 0035889692 scopus 로고    scopus 로고
    • New insights into the mechanism of protein-protein association
    • Selzer T, Schreiber G (2001) New insights into the mechanism of protein-protein association. Proteins 45: 190-198.
    • (2001) Proteins , vol.45 , pp. 190-198
    • Selzer, T.1    Schreiber, G.2
  • 14
    • 0032493375 scopus 로고    scopus 로고
    • Reaching the global minimum in docking simulations: A monte carlo energy minimization approach using bezier splines
    • Trosset JY, Scheraga HA (1998) Reaching the global minimum in docking simulations: a monte carlo energy minimization approach using bezier splines. Proc Natl Acad Sci U S A 95: 8011-8015.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 8011-8015
    • Trosset, J.Y.1    Scheraga, H.A.2
  • 15
    • 0032981961 scopus 로고    scopus 로고
    • Free energy landscapes of encounter complexes in protein-protein association
    • Camacho CJ, Weng Z, Vajda S, DeLisi C (1999) Free energy landscapes of encounter complexes in protein-protein association. Biophys J 76: 1166-1178.
    • (1999) Biophys J , vol.76 , pp. 1166-1178
    • Camacho, C.J.1    Weng, Z.2    Vajda, S.3    DeLisi, C.4
  • 16
    • 0034049350 scopus 로고    scopus 로고
    • Kinetics of desolvation-mediated protein-protein binding
    • Camacho CJ, Kimura SR, DeLisi C, Vajda S (2000) Kinetics of desolvation-mediated protein-protein binding. Biophys J 78: 1094-1105.
    • (2000) Biophys J , vol.78 , pp. 1094-1105
    • Camacho, C.J.1    Kimura, S.R.2    DeLisi, C.3    Vajda, S.4
  • 17
    • 0038021436 scopus 로고    scopus 로고
    • Assessment of blind predictions of protein-protein interactions: Current status of docking methods
    • Méndez R, Leplae R, De Maria L, Wodak SJ (2003) Assessment of blind predictions of protein-protein interactions: current status of docking methods. Proteins 52: 51-67.
    • (2003) Proteins , vol.52 , pp. 51-67
    • Méndez, R.1    Leplae, R.2    De Maria, L.3    Wodak, S.J.4
  • 18
    • 21644469377 scopus 로고    scopus 로고
    • Assessment of CAPRI predictions in rounds 3-5 shows progress in docking procedures
    • Méndez R, Leplae R, Lensink MF, Wodak SJ (2005) Assessment of CAPRI predictions in rounds 3-5 shows progress in docking procedures. Proteins 60: 150-169.
    • (2005) Proteins , vol.60 , pp. 150-169
    • Méndez, R.1    Leplae, R.2    Lensink, M.F.3    Wodak, S.J.4
  • 19
    • 36749006579 scopus 로고    scopus 로고
    • Docking and scoring protein complexes: CAPRI 3rd edition
    • Lensink MF, Méndez R, Wodak SJ (2007) Docking and scoring protein complexes: CAPRI 3rd edition. Proteins 69: 704-718.
    • (2007) Proteins , vol.69 , pp. 704-718
    • Lensink, M.F.1    Méndez, R.2    Wodak, S.J.3
  • 20
    • 1242270553 scopus 로고    scopus 로고
    • Protein-protein docking: Is the glass half full or half empty?
    • Vajda S, Camacho CJ (2004) Protein-protein docking: is the glass half full or half empty? Trends Biotechnol 22: 110-116.
    • (2004) Trends Biotechnol , vol.22 , pp. 110-116
    • Vajda, S.1    Camacho, C.J.2
  • 21
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK: An initial-stage protein docking algorithm
    • Chen R, Li L, Weng Z (2003) ZDOCK: an initial-stage protein docking algorithm. Proteins 52: 80-87.
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 22
    • 33749020839 scopus 로고    scopus 로고
    • PIPER: An FFT-based protein docking program with pairwise potentials
    • Kozakov D, Brenke R, Comeau SR, Vajda S (2006) PIPER: an FFT-based protein docking program with pairwise potentials. Proteins 65: 392-406.
    • (2006) Proteins , vol.65 , pp. 392-406
    • Kozakov, D.1    Brenke, R.2    Comeau, S.R.3    Vajda, S.4
  • 23
    • 0029025913 scopus 로고
    • A geometry-based suite of molecular docking processes
    • Fischer D, Lin SL, Wolfson H, Nussinov R (1995) A geometry-based suite of molecular docking processes. J Mol Biol 248: 459-477.
    • (1995) J Mol Biol , vol.248 , pp. 459-477
    • Fischer, D.1    Lin, S.L.2    Wolfson, H.3    Nussinov, R.4
  • 24
    • 0038161052 scopus 로고    scopus 로고
    • Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations
    • Gray JJ, Moughon S, Wang C, Schueler-Furman O, Kuhlman B, et al. (2003) Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations. J Mol Biol 331: 281-299.
    • (2003) J Mol Biol , vol.331 , pp. 281-299
    • Gray, J.J.1    Moughon, S.2    Wang, C.3    Schueler-Furman, O.4    Kuhlman, B.5
  • 25
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • Abagyan R, Totrov M (1994) Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins. J Mol Biol 235: 983-1002.
    • (1994) J Mol Biol , vol.235 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 26
    • 21844461156 scopus 로고    scopus 로고
    • Convex global underestimation for molecular structure prediction
    • Migdalas A, Pardalos PM, Varbrand P, eds. Boston Massachusetts, Kluwer Academic Publishers. pp
    • Phillips AT, Rosen JB, Dill KA (2001) Convex global underestimation for molecular structure prediction. In: From Local to Global Optimization. Migdalas A, Pardalos PM, Varbrand P, eds. Boston (Massachusetts): Kluwer Academic Publishers. pp 1-18.
    • (2001) From Local to Global Optimization , pp. 1-18
    • Phillips, A.T.1    Rosen, J.B.2    Dill, K.A.3
  • 27
    • 0030788883 scopus 로고    scopus 로고
    • Protein structure and energy landscape dependence on sequence using a continuous energy function
    • Dill KA, Phillips AT, Rosen JB (1997) Protein structure and energy landscape dependence on sequence using a continuous energy function. J Comput Biol 4: 227-240.
    • (1997) J Comput Biol , vol.4 , pp. 227-240
    • Dill, K.A.1    Phillips, A.T.2    Rosen, J.B.3
  • 29
    • 0036462492 scopus 로고    scopus 로고
    • Semi-global simplex optimization and its application to deter-mining the preferred solvation sites of proteins
    • Dennis S, Vajda S (2002) Semi-global simplex optimization and its application to deter-mining the preferred solvation sites of proteins. J Comput Chem 23: 319-334.
    • (2002) J Comput Chem , vol.23 , pp. 319-334
    • Dennis, S.1    Vajda, S.2
  • 30
    • 34247207508 scopus 로고    scopus 로고
    • A semi-definite programming-based underestimation method for stochastic global optimization in protein docking
    • Paschalidis IC, Shen Y, Vakili P, Vajda S (2007) A semi-definite programming-based underestimation method for stochastic global optimization in protein docking. IEEE Trans Automat Contr 52: 664-676.
    • (2007) IEEE Trans Automat Contr , vol.52 , pp. 664-676
    • Paschalidis, I.C.1    Shen, Y.2    Vakili, P.3    Vajda, S.4
  • 32
    • 0345832301 scopus 로고    scopus 로고
    • ClusPro: An automated docking and discrimination method for the prediction of protein complexes
    • Comeau SR, Gatchell D, Vajda S, Camacho CJ (2004) ClusPro: an automated docking and discrimination method for the prediction of protein complexes. Bioinformatics 20: 45-50.
    • (2004) Bioinformatics , vol.20 , pp. 45-50
    • Comeau, S.R.1    Gatchell, D.2    Vajda, S.3    Camacho, C.J.4
  • 33
    • 0037331833 scopus 로고    scopus 로고
    • Numerical optimization on the Euclidean group with applications to camera calibration
    • Gwak S, Kim J, Park FC (2003) Numerical optimization on the Euclidean group with applications to camera calibration. IEEE Trans Robot Autom 19: 65-74.
    • (2003) IEEE Trans Robot Autom , vol.19 , pp. 65-74
    • Gwak, S.1    Kim, J.2    Park, F.C.3
  • 35
    • 0031189315 scopus 로고    scopus 로고
    • Smooth invariant interpolation of rotations
    • Park FC, Ravani B (1997) Smooth invariant interpolation of rotations. ACM Trans Graph 16: 277-295.
    • (1997) ACM Trans Graph , vol.16 , pp. 277-295
    • Park, F.C.1    Ravani, B.2
  • 36
    • 0029272466 scopus 로고
    • Distance metrics on the rigid-body motions with applications to mechanism design
    • Park FC (1995) Distance metrics on the rigid-body motions with applications to mechanism design. J Mech Des 117: 48-54.
    • (1995) J Mech Des , vol.117 , pp. 48-54
    • Park, F.C.1
  • 40
    • 0242299200 scopus 로고    scopus 로고
    • RDOCK: Refinement of rigid-body protein docking predictions
    • Li L, Chen R, Weng Z (2003) RDOCK: refinement of rigid-body protein docking predictions. Proteins 53: 629-639.
    • (2003) Proteins , vol.53 , pp. 629-639
    • Li, L.1    Chen, R.2    Weng, Z.3
  • 41
    • 48449105393 scopus 로고    scopus 로고
    • The RosettaDock server for local protein-protein docking
    • Lyskov S, Gray JJ (2008) The RosettaDock server for local protein-protein docking. Nucleic Acids Res 36: W233-W238.
    • (2008) Nucleic Acids Res , vol.36
    • Lyskov, S.1    Gray, J.J.2
  • 42
    • 0038161052 scopus 로고    scopus 로고
    • Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations
    • Gray JJ, Moughon S, Wang C, Schueler-Furman O, Kuhlman B, et al. (2003) Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations. J Mol Biol 331: 281-299.
    • (2003) J Mol Biol , vol.331 , pp. 281-299
    • Gray, J.J.1    Moughon, S.2    Wang, C.3    Schueler-Furman, O.4    Kuhlman, B.5
  • 43
    • 36749050815 scopus 로고    scopus 로고
    • Docking with PIPER and refinement with SDU in rounds 6-11 of CAPRI
    • Shen Y, Brenke R, Kozakov D, Comeau SR, Beglov D, et al. (2007) Docking with PIPER and refinement with SDU in rounds 6-11 of CAPRI. Proteins 69: 734-742.
    • (2007) Proteins , vol.69 , pp. 734-742
    • Shen, Y.1    Brenke, R.2    Kozakov, D.3    Comeau, S.R.4    Beglov, D.5
  • 44
    • 34548124821 scopus 로고    scopus 로고
    • Global optimization in protein docking us-ing convex underestimation and semidefinite programming
    • Marcia RF, Mitchell JC, Wright SJ (2007) Global optimization in protein docking us-ing convex underestimation and semidefinite programming. Optim Methods Softw 22: 803-811.
    • (2007) Optim Methods Softw , vol.22 , pp. 803-811
    • Marcia, R.F.1    Mitchell, J.C.2    Wright, S.J.3
  • 45
    • 23244436580 scopus 로고    scopus 로고
    • Optimal clustering for detecting near-native conformation in protein docking
    • Kozakov D, Clodfelter KH, Vajda S, Camacho CJ (2005) Optimal clustering for detecting near-native conformation in protein docking. Biophys J 89: 867-875.
    • (2005) Biophys J , vol.89 , pp. 867-875
    • Kozakov, D.1    Clodfelter, K.H.2    Vajda, S.3    Camacho, C.J.4
  • 47
    • 0033296299 scopus 로고    scopus 로고
    • Sturm JF (1999) Using SeDuMi 1.02, a MATLAB toolbox for optimization over symmet-ric cones. Optim Methods Softw 11-12: 625-653. Special issue on Interior Point Methods (CD supplement with software).
    • Sturm JF (1999) Using SeDuMi 1.02, a MATLAB toolbox for optimization over symmet-ric cones. Optim Methods Softw 11-12: 625-653. Special issue on Interior Point Methods (CD supplement with software).
  • 48
    • 55449111144 scopus 로고    scopus 로고
    • Fujisawa K, Kojima M, Nakata K, Yamashita M (2002) SDPA (SemiDefinite Programming Algorithm) User's Manual Version 6.00. Department of Mathematical and Com-puting Sciences, Tokyo Institute of Technology. Research Reports on Mathematical and Computing Sciences Series B : Operations Research.
    • Fujisawa K, Kojima M, Nakata K, Yamashita M (2002) SDPA (SemiDefinite Programming Algorithm) User's Manual Version 6.00. Department of Mathematical and Com-puting Sciences, Tokyo Institute of Technology. Research Reports on Mathematical and Computing Sciences Series B : Operations Research.
  • 49
    • 0031552370 scopus 로고    scopus 로고
    • Determination of atomic desolvation energies from the structures of crystallized proteins
    • Zhang C, Vasmatzis G, Cornette J, DeLisi C (1997) Determination of atomic desolvation energies from the structures of crystallized proteins. J Mol Biol 267: 707-726.
    • (1997) J Mol Biol , vol.267 , pp. 707-726
    • Zhang, C.1    Vasmatzis, G.2    Cornette, J.3    DeLisi, C.4
  • 50
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal structures: Quasi-chemical approximation
    • Miyazawa S, Jernigan RL (1985) Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation. Macromolecules 18: 534-552.
    • (1985) Macromolecules , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.L.2


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