메뉴 건너뛰기




Volumn 8, Issue 3, 2013, Pages

Global Conformational Selection and Local Induced Fit for the Recognition between Intrinsic Disordered p53 and CBP

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; NUCLEAR RECEPTOR COACTIVATOR; PROTEIN P53;

EID: 84875469274     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0059627     Document Type: Article
Times cited : (14)

References (64)
  • 1
    • 0030570961 scopus 로고    scopus 로고
    • Transcription. A growing coactivator network
    • Janknecht R, Hunter T, (1996) Transcription. A growing coactivator network. Nature 383: 22-23.
    • (1996) Nature , vol.383 , pp. 22-23
    • Janknecht, R.1    Hunter, T.2
  • 2
    • 0343417089 scopus 로고    scopus 로고
    • The p300/CBP family: integrating signals with transcription factors and chromatin
    • Shiama N, (1997) The p300/CBP family: integrating signals with transcription factors and chromatin. Trends Cell Biol 7: 230-236.
    • (1997) Trends Cell Biol , vol.7 , pp. 230-236
    • Shiama, N.1
  • 3
    • 0037203771 scopus 로고    scopus 로고
    • Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators
    • Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, et al. (2002) Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. Nature 415: 549-553.
    • (2002) Nature , vol.415 , pp. 549-553
    • Demarest, S.J.1    Martinez-Yamout, M.2    Chung, J.3    Chen, H.4    Xu, W.5
  • 4
    • 0034785837 scopus 로고    scopus 로고
    • A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies
    • Lin CH, Hare BJ, Wagner G, Harrison SC, Maniatis T, et al. (2001) A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies. Mol Cell 8: 581-590.
    • (2001) Mol Cell , vol.8 , pp. 581-590
    • Lin, C.H.1    Hare, B.J.2    Wagner, G.3    Harrison, S.C.4    Maniatis, T.5
  • 5
    • 0346733326 scopus 로고    scopus 로고
    • Packing, specificity, and mutability at the binding interface between the p160 coactivator and CREB-binding protein
    • Demarest SJ, Deechongkit S, Jane Dyson H, Evans RM, Wright PE, (2004) Packing, specificity, and mutability at the binding interface between the p160 coactivator and CREB-binding protein. Protein science 13: 203-210.
    • (2004) Protein Science , vol.13 , pp. 203-210
    • Demarest, S.J.1    Deechongkit, S.2    Jane Dyson, H.3    Evans, R.M.4    Wright, P.E.5
  • 6
    • 10744233648 scopus 로고    scopus 로고
    • Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation
    • Mujtaba S, He Y, Zeng L, Yan S, Plotnikova O, et al. (2004) Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation. Mol Cell 13: 251-263.
    • (2004) Mol Cell , vol.13 , pp. 251-263
    • Mujtaba, S.1    He, Y.2    Zeng, L.3    Yan, S.4    Plotnikova, O.5
  • 7
    • 66149124079 scopus 로고    scopus 로고
    • Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2
    • Ferreon JC, Lee CW, Arai M, Martinez-Yamout MA, Dyson HJ, et al. (2009) Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2. Proc Natl Acad Sci U S A 106: 6591-6596.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 6591-6596
    • Ferreon, J.C.1    Lee, C.W.2    Arai, M.3    Martinez-Yamout, M.A.4    Dyson, H.J.5
  • 8
    • 0026535237 scopus 로고
    • p53: a transdominant regulator of transcription whose function is ablated by mutations occurring in human cancer
    • Unger T, Nau MM, Segal S, Minna JD, (1992) p53: a transdominant regulator of transcription whose function is ablated by mutations occurring in human cancer. EMBO J 11: 1383-1390.
    • (1992) EMBO J , vol.11 , pp. 1383-1390
    • Unger, T.1    Nau, M.M.2    Segal, S.3    Minna, J.D.4
  • 9
    • 0028303752 scopus 로고
    • Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein
    • Lin J, Chen J, Elenbaas B, Levine AJ, (1994) Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein. Genes Dev 8: 1235-1246.
    • (1994) Genes Dev , vol.8 , pp. 1235-1246
    • Lin, J.1    Chen, J.2    Elenbaas, B.3    Levine, A.J.4
  • 10
    • 78649284498 scopus 로고    scopus 로고
    • Structure of the p53 transactivation domain in complex with the nuclear receptor coactivator binding domain of CREB binding protein
    • Lee CW, Martinez-Yamout MA, Dyson HJ, Wright PE, (2010) Structure of the p53 transactivation domain in complex with the nuclear receptor coactivator binding domain of CREB binding protein. Biochemistry 49: 9964-9971.
    • (2010) Biochemistry , vol.49 , pp. 9964-9971
    • Lee, C.W.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 11
    • 73949144611 scopus 로고    scopus 로고
    • Toward a quantitative theory of intrinsically disordered proteins and their function
    • Liu J, Faeder JR, Camacho CJ, (2009) Toward a quantitative theory of intrinsically disordered proteins and their function. Proc Natl Acad Sci U S A 106: 19819-19823.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19819-19823
    • Liu, J.1    Faeder, J.R.2    Camacho, C.J.3
  • 12
    • 44449116120 scopus 로고    scopus 로고
    • Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
    • Wells M, Tidow H, Rutherford TJ, Markwick P, Jensen MR, et al. (2008) Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain. Proc Natl Acad Sci U S A 105: 5762-5767.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5762-5767
    • Wells, M.1    Tidow, H.2    Rutherford, T.J.3    Markwick, P.4    Jensen, M.R.5
  • 13
    • 33745428137 scopus 로고    scopus 로고
    • Ligation-state hydrogen exchange: coupled binding and folding equilibria in ribonuclease P protein
    • Henkels CH, Oas TG, (2006) Ligation-state hydrogen exchange: coupled binding and folding equilibria in ribonuclease P protein. J Am Chem Soc 128: 7772-7781.
    • (2006) J Am Chem Soc , vol.128 , pp. 7772-7781
    • Henkels, C.H.1    Oas, T.G.2
  • 14
    • 0037154980 scopus 로고    scopus 로고
    • Protein folding and unfolding at atomic resolution
    • Fersht AR, Daggett V, (2002) Protein folding and unfolding at atomic resolution. Cell 108: 573-582.
    • (2002) Cell , vol.108 , pp. 573-582
    • Fersht, A.R.1    Daggett, V.2
  • 15
    • 64649101249 scopus 로고    scopus 로고
    • Long-timescale molecular dynamics simulations of protein structure and function
    • Klepeis JL, Lindorff-Larsen K, Dror RO, Shaw DE, (2009) Long-timescale molecular dynamics simulations of protein structure and function. Curr Opin Struct Biol 19: 120-127.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 120-127
    • Klepeis, J.L.1    Lindorff-Larsen, K.2    Dror, R.O.3    Shaw, D.E.4
  • 16
    • 0034743155 scopus 로고    scopus 로고
    • From folding theories to folding proteins: a review and assessment of simulation studies of protein folding and unfolding
    • Shea JE, Brooks CL, (2001) From folding theories to folding proteins: a review and assessment of simulation studies of protein folding and unfolding. Annu Rev Phys Chem 52: 499-535.
    • (2001) Annu Rev Phys Chem , vol.52 , pp. 499-535
    • Shea, J.E.1    Brooks, C.L.2
  • 17
    • 0042511005 scopus 로고    scopus 로고
    • A graph-theory algorithm for rapid protein side-chain prediction
    • Canutescu AA, Shelenkov AA, Dunbrack RL, (2003) A graph-theory algorithm for rapid protein side-chain prediction. Protein Sci 12: 2001-2014.
    • (2003) Protein Sci , vol.12 , pp. 2001-2014
    • Canutescu, A.A.1    Shelenkov, A.A.2    Dunbrack, R.L.3
  • 20
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N{dot operator}log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L, (1993) Particle mesh Ewald: An N{dot operator}log(N) method for Ewald sums in large systems. The Journal of Chemical Physics 98: 10089.
    • (1993) The Journal of Chemical Physics , vol.98 , pp. 10089
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 21
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules
    • Wang JM, Cieplak P, Kollman PA, (2000) How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules. J Comput Chem 21: 1049-1074.
    • (2000) J Comput Chem , vol.21 , pp. 1049-1074
    • Wang, J.M.1    Cieplak, P.2    Kollman, P.A.3
  • 22
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes
    • Ryckaert JP, Ciccotti G, Berendsen HJC, (1977) Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. Journal of Computational Physics 23: 327-341.
    • (1977) Journal of Computational Physics , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 23
    • 0021104755 scopus 로고
    • Molecular dynamics of native protein. II. Analysis and nature of motion
    • Levitt M, (1983) Molecular dynamics of native protein. II. Analysis and nature of motion. J Mol Biol 168: 621-657.
    • (1983) J Mol Biol , vol.168 , pp. 621-657
    • Levitt, M.1
  • 24
    • 84887006810 scopus 로고
    • A nonlinear mapping for data structure analysis
    • Sammon JW, (1969) A nonlinear mapping for data structure analysis. Computers, IEEE Transactions on 100: 401-409.
    • (1969) Computers, IEEE Transactions on , vol.100 , pp. 401-409
    • Sammon, J.W.1
  • 25
    • 33947252405 scopus 로고    scopus 로고
    • Binding induced folding in p53-MDM2 complex
    • Chen HF, Luo R, (2007) Binding induced folding in p53-MDM2 complex. J Am Chem Soc 129: 2930-2937.
    • (2007) J Am Chem Soc , vol.129 , pp. 2930-2937
    • Chen, H.F.1    Luo, R.2
  • 26
    • 84863181653 scopus 로고    scopus 로고
    • Identified hadron compositions in p+p and Au+Au collisions at high transverse momenta at radicalS(NN) = 200 GeV
    • Agakishiev G, Aggarwal MM, Ahammed Z, Alakhverdyants AV, Alekseev I, et al. (2012) Identified hadron compositions in p+p and Au+Au collisions at high transverse momenta at radicalS(NN) = 200 GeV. Phys Rev Lett 108: 072302.
    • (2012) Phys Rev Lett , vol.108 , pp. 072302
    • Agakishiev, G.1    Aggarwal, M.M.2    Ahammed, Z.3    Alakhverdyants, A.V.4    Alekseev, I.5
  • 27
    • 84860384642 scopus 로고    scopus 로고
    • Regulation of the fate of human mesenchymal stem cells by mechanical and stereo-topographical cues provided by silicon nanowires
    • Kuo SW, Lin HI, Ho JH, Shih YR, Chen HF, et al. (2012) Regulation of the fate of human mesenchymal stem cells by mechanical and stereo-topographical cues provided by silicon nanowires. Biomaterials 33: 5013-5022.
    • (2012) Biomaterials , vol.33 , pp. 5013-5022
    • Kuo, S.W.1    Lin, H.I.2    Ho, J.H.3    Shih, Y.R.4    Chen, H.F.5
  • 28
    • 84862110832 scopus 로고    scopus 로고
    • Risk of Parkinson disease onset in patients with diabetes: a 9-year population-based cohort study with age and sex stratifications
    • Sun Y, Chang YH, Chen HF, Su YH, Su HF, et al. (2012) Risk of Parkinson disease onset in patients with diabetes: a 9-year population-based cohort study with age and sex stratifications. Diabetes Care 35: 1047-1049.
    • (2012) Diabetes Care , vol.35 , pp. 1047-1049
    • Sun, Y.1    Chang, Y.H.2    Chen, H.F.3    Su, Y.H.4    Su, H.F.5
  • 29
    • 84861012177 scopus 로고    scopus 로고
    • Insight into the stability of cross-beta amyloid fibril from VEALYL short peptide with molecular dynamics simulation
    • Ye W, Chen Y, Wang W, Yu Q, Li Y, et al. (2012) Insight into the stability of cross-beta amyloid fibril from VEALYL short peptide with molecular dynamics simulation. PLoS One 7: e36382.
    • (2012) PLoS One , vol.7
    • Ye, W.1    Chen, Y.2    Wang, W.3    Yu, Q.4    Li, Y.5
  • 30
    • 77951170511 scopus 로고    scopus 로고
    • Induced fit or conformational selection for RNA/U1A folding
    • Qin F, Chen Y, Wu M, Li Y, Zhang J, et al. (2010) Induced fit or conformational selection for RNA/U1A folding. RNA 16: 1053-1061.
    • (2010) RNA , vol.16 , pp. 1053-1061
    • Qin, F.1    Chen, Y.2    Wu, M.3    Li, Y.4    Zhang, J.5
  • 31
    • 84865442439 scopus 로고    scopus 로고
    • Atomistic Mechanism of MicroRNA Translation Upregulation via Molecular Dynamics Simulations
    • Ye W, Qin F, Zhang J, Luo R, Chen HF, (2012) Atomistic Mechanism of MicroRNA Translation Upregulation via Molecular Dynamics Simulations. PLoS One 7: e43788.
    • (2012) PLoS One , vol.7
    • Ye, W.1    Qin, F.2    Zhang, J.3    Luo, R.4    Chen, H.F.5
  • 32
    • 0025283002 scopus 로고
    • Electrostatic interactions in macromolecules: theory and applications
    • Sharp KA, Honig B, (1990) Electrostatic interactions in macromolecules: theory and applications. Annu Rev Biophys Biophys Chem 19: 301-332.
    • (1990) Annu Rev Biophys Biophys Chem , vol.19 , pp. 301-332
    • Sharp, K.A.1    Honig, B.2
  • 33
    • 0028264860 scopus 로고
    • Molecular dynamics simulation of protein denaturation: solvation of the hydrophobic cores and secondary structure of barnase
    • Caflisch A, Karplus M, (1994) Molecular dynamics simulation of protein denaturation: solvation of the hydrophobic cores and secondary structure of barnase. Proc Natl Acad Sci U S A 91: 1746-1750.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1746-1750
    • Caflisch, A.1    Karplus, M.2
  • 34
    • 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, Karplus M, (2001) Three key residues form a critical contact network in a protein folding transition state. Nature 409: 641-645.
    • (2001) Nature , vol.409 , pp. 641-645
    • Vendruscolo, M.1    Paci, E.2    Dobson, C.M.3    Karplus, M.4
  • 35
    • 0037076334 scopus 로고    scopus 로고
    • Molecular dynamics simulations of protein folding from the transition state
    • Gsponer J, Caflisch A, (2002) Molecular dynamics simulations of protein folding from the transition state. Proc Natl Acad Sci U S A 99: 6719-6724.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 6719-6724
    • Gsponer, J.1    Caflisch, A.2
  • 36
    • 73349117207 scopus 로고    scopus 로고
    • Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin
    • Wlodarski T, Zagrovic B, (2009) Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin. Proc Natl Acad Sci U S A 106: 19346-19351.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19346-19351
    • Wlodarski, T.1    Zagrovic, B.2
  • 39
    • 26444608613 scopus 로고    scopus 로고
    • Ensemble versus single-molecule protein unfolding
    • Day R, Daggett V, (2005) Ensemble versus single-molecule protein unfolding. Proc Natl Acad Sci U S A 102: 13445-13450.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 13445-13450
    • Day, R.1    Daggett, V.2
  • 40
    • 43349097327 scopus 로고    scopus 로고
    • Analyzing molecular interactions
    • Chapter 8: Unit8 1
    • Petsko GA (2003) Analyzing molecular interactions. Curr Protoc Bioinformatics Chapter 8: Unit8 1.
    • (2003) Curr Protoc Bioinformatics
    • Petsko, G.A.1
  • 41
    • 0037109040 scopus 로고    scopus 로고
    • A two-state kinetic model for the unfolding of single molecules by mechanical force
    • Ritort F, Bustamante C, Tinoco I, (2002) A two-state kinetic model for the unfolding of single molecules by mechanical force. Proc Natl Acad Sci U S A 99: 13544-13548.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 13544-13548
    • Ritort, F.1    Bustamante, C.2    Tinoco, I.3
  • 42
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Matouschek A, Kellis JT, Serrano L, Fersht AR, (1989) Mapping the transition state and pathway of protein folding by protein engineering. Nature 340: 122-126.
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek, A.1    Kellis, J.T.2    Serrano, L.3    Fersht, A.R.4
  • 43
    • 0027171034 scopus 로고
    • Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding
    • Matouschek A, Fersht AR, (1993) Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding. Proc Natl Acad Sci U S A 90: 7814-7818.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 7814-7818
    • Matouschek, A.1    Fersht, A.R.2
  • 44
    • 0027948175 scopus 로고
    • Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding
    • Otzen DE, Itzhaki LS, elMasry NF, Jackson SE, Fersht AR, (1994) Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding. Proc Natl Acad Sci U S A 91: 10422-10425.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10422-10425
    • Otzen, D.E.1    Itzhaki, L.S.2    elMasry, N.F.3    Jackson, S.E.4    Fersht, A.R.5
  • 45
    • 0028143603 scopus 로고
    • Characterization of the transition state of protein unfolding by use of molecular dynamics: chymotrypsin inhibitor 2
    • Li A, Daggett V, (1994) Characterization of the transition state of protein unfolding by use of molecular dynamics: chymotrypsin inhibitor 2. Proc Natl Acad Sci U S A 91: 10430-10434.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10430-10434
    • Li, A.1    Daggett, V.2
  • 46
    • 0034652206 scopus 로고    scopus 로고
    • Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism
    • Fersht AR, (2000) Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism. Proc Natl Acad Sci U S A 97: 1525-1529.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 1525-1529
    • Fersht, A.R.1
  • 48
    • 2542599277 scopus 로고    scopus 로고
    • Phi-value analysis and the nature of protein-folding transition states
    • Fersht AR, Sato S, (2004) Phi-value analysis and the nature of protein-folding transition states. Proc Natl Acad Sci U S A 101: 7976-7981.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 7976-7981
    • Fersht, A.R.1    Sato, S.2
  • 50
    • 34249863018 scopus 로고    scopus 로고
    • Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53
    • Teufel DP, Freund SM, Bycroft M, Fersht AR, (2007) Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53. Proc Natl Acad Sci U S A 104: 7009-7014.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7009-7014
    • Teufel, D.P.1    Freund, S.M.2    Bycroft, M.3    Fersht, A.R.4
  • 51
    • 0036771626 scopus 로고    scopus 로고
    • Accelerated Poisson-Boltzmann calculations for static and dynamic systems
    • Luo R, David L, Gilson MK, (2002) Accelerated Poisson-Boltzmann calculations for static and dynamic systems. J Comput Chem 23: 1244-1253.
    • (2002) J Comput Chem , vol.23 , pp. 1244-1253
    • Luo, R.1    David, L.2    Gilson, M.K.3
  • 52
    • 45849095234 scopus 로고    scopus 로고
    • Biochemistry. How do proteins interact?
    • Boehr DD, Wright PE, (2008) Biochemistry. How do proteins interact? Science 320: 1429-1430.
    • (2008) Science , vol.320 , pp. 1429-1430
    • Boehr, D.D.1    Wright, P.E.2
  • 53
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H, Sligar SG, Wolynes PG, (1991) The energy landscapes and motions of proteins. Science 254: 1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 54
    • 0033621104 scopus 로고    scopus 로고
    • Folding and binding cascades: shifts in energy landscapes
    • Tsai CJ, Ma B, Nussinov R, (1999) Folding and binding cascades: shifts in energy landscapes. Proc Natl Acad Sci U S A 96: 9970-9972.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 9970-9972
    • Tsai, C.J.1    Ma, B.2    Nussinov, R.3
  • 55
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • Boehr DD, McElheny D, Dyson HJ, Wright PE, (2006) The dynamic energy landscape of dihydrofolate reductase catalysis. Science 313: 1638-1642.
    • (2006) Science , vol.313 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wright, P.E.4
  • 56
    • 65249090946 scopus 로고    scopus 로고
    • Selected-fit versus induced-fit protein binding: kinetic differences and mutational analysis
    • Weikl TR, von Deuster C, (2009) Selected-fit versus induced-fit protein binding: kinetic differences and mutational analysis. Proteins 75: 104-110.
    • (2009) Proteins , vol.75 , pp. 104-110
    • Weikl, T.R.1    von Deuster, C.2
  • 57
    • 0001858251 scopus 로고
    • Application of a Theory of Enzyme Specificity to Protein Synthesis
    • Koshland DE, (1958) Application of a Theory of Enzyme Specificity to Protein Synthesis. Proc Natl Acad Sci U S A 44: 98-104.
    • (1958) Proc Natl Acad Sci U S A , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 58
    • 0026587998 scopus 로고
    • Structural evidence for induced fit as a mechanism for antibody-antigen recognition
    • Rini JM, Schulze-Gahmen U, Wilson IA, (1992) Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science 255: 959-965.
    • (1992) Science , vol.255 , pp. 959-965
    • Rini, J.M.1    Schulze-Gahmen, U.2    Wilson, I.A.3
  • 59
  • 60
    • 70350131719 scopus 로고    scopus 로고
    • Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins
    • Schrank TP, Bolen DW, Hilser VJ, (2009) Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins. Proc Natl Acad Sci U S A 106: 16984-16989.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 16984-16989
    • Schrank, T.P.1    Bolen, D.W.2    Hilser, V.J.3
  • 61
    • 77957231785 scopus 로고    scopus 로고
    • Induced fit, conformational selection and independent dynamic segments: an extended view of binding events
    • Csermely P, Palotai R, Nussinov R, (2010) Induced fit, conformational selection and independent dynamic segments: an extended view of binding events. Trends Biochem Sci 35: 539-546.
    • (2010) Trends Biochem Sci , vol.35 , pp. 539-546
    • Csermely, P.1    Palotai, R.2    Nussinov, R.3
  • 62
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution-a 60-year-old hypothesis revisited
    • James LC, Tawfik DS, (2003) Conformational diversity and protein evolution-a 60-year-old hypothesis revisited. Trends Biochem Sci 28: 361-368.
    • (2003) Trends Biochem Sci , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 63
    • 49649084492 scopus 로고    scopus 로고
    • Dynamic energy landscape view of coupled binding and protein conformational change: induced-fit versus population-shift mechanisms
    • Okazaki K, Takada S, (2008) Dynamic energy landscape view of coupled binding and protein conformational change: induced-fit versus population-shift mechanisms. Proc Natl Acad Sci U S A 105: 11182-11187.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 11182-11187
    • Okazaki, K.1    Takada, S.2
  • 64
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P, (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27: 527-533.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.