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Volumn 26, Issue 1, 2014, Pages 62-72

Controlling entropy to tune the functions of intrinsically disordered regions

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; INTRINSICALLY DISORDERED PROTEIN;

EID: 84902500178     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2014.05.007     Document Type: Review
Times cited : (112)

References (98)
  • 3
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward J.J., Sodhi J.S., McGuffin L.J., Buxton B.F., Jones D.T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 2004, 337635-337645.
    • (2004) J Mol Biol , pp. 337635-337645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 5
    • 84902446852 scopus 로고    scopus 로고
    • Short linear motifs: ubiquitous and functionally diverse protein interaction modules directing cell regulation
    • (in press)
    • Van Roey K., Uyar B., Weatheritt R.J., Dinkel H., Seiler M., Budd A., Gibson T.J., Davey N.E. Short linear motifs: ubiquitous and functionally diverse protein interaction modules directing cell regulation. Chem Rev 2014, (in press).
    • (2014) Chem Rev
    • Van Roey, K.1    Uyar, B.2    Weatheritt, R.J.3    Dinkel, H.4    Seiler, M.5    Budd, A.6    Gibson, T.J.7    Davey, N.E.8
  • 6
    • 4143107222 scopus 로고    scopus 로고
    • Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers
    • Gunasekaran K., Tsai C.J., Nussinov R. Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers. J Mol Biol 2004, 3411327-3411341.
    • (2004) J Mol Biol , pp. 3411327-3411341
    • Gunasekaran, K.1    Tsai, C.J.2    Nussinov, R.3
  • 7
    • 84902446853 scopus 로고    scopus 로고
    • Unusual biophysics of intrinsically disordered proteins
    • Uversky V.N. Unusual biophysics of intrinsically disordered proteins. Biochim Biophys Acta 2013, 1834932-1834951.
    • (2013) Biochim Biophys Acta , pp. 1834932-1834951
    • Uversky, V.N.1
  • 8
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr D.D., Nussinov R., Wright P.E. The role of dynamic conformational ensembles in biomolecular recognition. Nat Chem Biol 2009, 5789-5796.
    • (2009) Nat Chem Biol , pp. 5789-5796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 9
    • 82455179494 scopus 로고    scopus 로고
    • Understanding biomolecular motion, recognition, and allostery by use of conformational ensembles
    • Fenwick R.B., Esteban-Martin S., Salvatella X. Understanding biomolecular motion, recognition, and allostery by use of conformational ensembles. Eur Biophys J 2011, 401339-401355.
    • (2011) Eur Biophys J , pp. 401339-401355
    • Fenwick, R.B.1    Esteban-Martin, S.2    Salvatella, X.3
  • 10
    • 84863522650 scopus 로고    scopus 로고
    • Biomolecular dynamics: order-disorder transitions and energy landscapes
    • Whitford P.C., Sanbonmatsu K.Y., Onuchic J.N. Biomolecular dynamics: order-disorder transitions and energy landscapes. Rep Prog Phys 2012, 75076601.
    • (2012) Rep Prog Phys , pp. 75076601
    • Whitford, P.C.1    Sanbonmatsu, K.Y.2    Onuchic, J.N.3
  • 12
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright P.E., Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 1999, 293321-293331.
    • (1999) J Mol Biol , pp. 293321-293331
    • Wright, P.E.1    Dyson, H.J.2
  • 14
    • 84856708599 scopus 로고    scopus 로고
    • Intrinsic disorder: signaling via highly specific but short-lived association
    • Zhou H.X. Intrinsic disorder: signaling via highly specific but short-lived association. Trends Biochem Sci 2012, 3743-3748.
    • (2012) Trends Biochem Sci , pp. 3743-3748
    • Zhou, H.X.1
  • 16
    • 82655180384 scopus 로고    scopus 로고
    • Fuzziness: linking regulation to protein dynamics
    • Fuxreiter M. Fuzziness: linking regulation to protein dynamics. Mol Biosyst 2012, 8168-8177.
    • (2012) Mol Biosyst , pp. 8168-8177
    • Fuxreiter, M.1
  • 18
    • 75849126506 scopus 로고    scopus 로고
    • The structural basis of peptide-protein binding strategies
    • London N., Movshovitz-Attias D., Schueler-Furman O. The structural basis of peptide-protein binding strategies. Structure 2010, 18188-18199.
    • (2010) Structure , pp. 18188-18199
    • London, N.1    Movshovitz-Attias, D.2    Schueler-Furman, O.3
  • 19
    • 49749117432 scopus 로고    scopus 로고
    • Contextual specificity in peptide-mediated protein interactions
    • Stein A., Aloy P. Contextual specificity in peptide-mediated protein interactions. PLoS ONE 2008, 3e2524.
    • (2008) PLoS ONE
    • Stein, A.1    Aloy, P.2
  • 20
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay B.K., Williamson M.P., Sudol M. The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J 2000, 14231-14241.
    • (2000) FASEB J , pp. 14231-14241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 26
    • 84876018623 scopus 로고    scopus 로고
    • The tandem beta-zipper: modular binding of tandem domains and linear motifs
    • Matthews J.M., Potts J.R. The tandem beta-zipper: modular binding of tandem domains and linear motifs. FEBS Lett 2013, 5871164-5871171.
    • (2013) FEBS Lett , pp. 5871164-5871171
    • Matthews, J.M.1    Potts, J.R.2
  • 27
    • 84876266689 scopus 로고    scopus 로고
    • Allostery in disease and in drug discovery
    • Nussinov R., Tsai C.J. Allostery in disease and in drug discovery. Cell 2013, 153293-153305.
    • (2013) Cell , pp. 153293-153305
    • Nussinov, R.1    Tsai, C.J.2
  • 29
    • 84879161353 scopus 로고    scopus 로고
    • The roles of conditional disorder in redox proteins
    • Reichmann D., Jakob U. The roles of conditional disorder in redox proteins. Curr Opin Struct Biol 2013, 23436-23442.
    • (2013) Curr Opin Struct Biol , pp. 23436-23442
    • Reichmann, D.1    Jakob, U.2
  • 30
    • 22844435320 scopus 로고    scopus 로고
    • Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation
    • Hong W., Jiao W., Hu J., Zhang J., Liu C., Fu X., Shen D., Xia B., Chang Z. Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation. J Biol Chem 2005, 28027029-28027034.
    • (2005) J Biol Chem , pp. 28027029-28027034
    • Hong, W.1    Jiao, W.2    Hu, J.3    Zhang, J.4    Liu, C.5    Fu, X.6    Shen, D.7    Xia, B.8    Chang, Z.9
  • 31
    • 11444262208 scopus 로고    scopus 로고
    • Beyond transcription-new mechanisms for the regulation of molecular chaperones
    • Winter J., Jakob U. Beyond transcription-new mechanisms for the regulation of molecular chaperones. Crit Rev Biochem Mol Biol 2004, 39297-39317.
    • (2004) Crit Rev Biochem Mol Biol , pp. 39297-39317
    • Winter, J.1    Jakob, U.2
  • 32
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • Tompa P., Csermely P. The role of structural disorder in the function of RNA and protein chaperones. FASEB J 2004, 181169-181175.
    • (2004) FASEB J , pp. 181169-181175
    • Tompa, P.1    Csermely, P.2
  • 34
    • 84902446848 scopus 로고    scopus 로고
    • Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function
    • Jakob U., Kriwacki R., Uversky V.N. Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function. Chem Rev 2014.
    • (2014) Chem Rev
    • Jakob, U.1    Kriwacki, R.2    Uversky, V.N.3
  • 36
    • 70149109136 scopus 로고    scopus 로고
    • Computation of conformational coupling in allosteric proteins
    • Kidd B.A., Baker D., Thomas W.E. Computation of conformational coupling in allosteric proteins. PLoS Comput Biol 2009, 5e1000484.
    • (2009) PLoS Comput Biol
    • Kidd, B.A.1    Baker, D.2    Thomas, W.E.3
  • 37
    • 84864651001 scopus 로고    scopus 로고
    • Protein activity regulation by conformational entropy
    • Tzeng S.R., Kalodimos C.G. Protein activity regulation by conformational entropy. Nature 2012, 488236-488240.
    • (2012) Nature , pp. 488236-488240
    • Tzeng, S.R.1    Kalodimos, C.G.2
  • 38
    • 84876356757 scopus 로고    scopus 로고
    • Allosteric interactions after 50 years
    • Edelstein S.J. Allosteric interactions after 50 years. J Mol Biol 2013, 4251391-4251395.
    • (2013) J Mol Biol , pp. 4251391-4251395
    • Edelstein, S.J.1
  • 39
    • 48249141040 scopus 로고    scopus 로고
    • Allostery and cooperativity revisited
    • Cui Q., Karplus M. Allostery and cooperativity revisited. Protein Sci 2008, 171295-171307.
    • (2008) Protein Sci , pp. 171295-171307
    • Cui, Q.1    Karplus, M.2
  • 40
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel G.M., Lockless S.W., Wall M.A., Ranganathan R. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat Struct Biol 2003, 1059-1069.
    • (2003) Nat Struct Biol , pp. 1059-1069
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 42
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • Hilser V.J., Thompson E.B. Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. Proc Natl Acad Sci U S A 2007, 1048311-1048315.
    • (2007) Proc Natl Acad Sci U S A , pp. 1048311-1048315
    • Hilser, V.J.1    Thompson, E.B.2
  • 44
    • 84879327823 scopus 로고    scopus 로고
    • Modulation of allostery by protein intrinsic disorder
    • Ferreon A.C., Ferreon J.C., Wright P.E., Deniz A.A. Modulation of allostery by protein intrinsic disorder. Nature 2013, 498390-498394.
    • (2013) Nature , pp. 498390-498394
    • Ferreon, A.C.1    Ferreon, J.C.2    Wright, P.E.3    Deniz, A.A.4
  • 45
    • 84879392599 scopus 로고    scopus 로고
    • Structural biology: signalling from disordered proteins
    • Hilser V.J. Structural biology: signalling from disordered proteins. Nature 2013, 498308-498310.
    • (2013) Nature , pp. 498308-498310
    • Hilser, V.J.1
  • 46
    • 82655179921 scopus 로고    scopus 로고
    • How do dynamic cellular signals travel long distances?
    • Nussinov R. How do dynamic cellular signals travel long distances?. Mol Biosyst 2012, 822-826.
    • (2012) Mol Biosyst , pp. 822-826
    • Nussinov, R.1
  • 48
    • 84858234186 scopus 로고    scopus 로고
    • Agonism/antagonism switching in allosteric ensembles
    • Motlagh H.N., Hilser V.J. Agonism/antagonism switching in allosteric ensembles. Proc Natl Acad Sci U S A 2012, 1094134-1094139.
    • (2012) Proc Natl Acad Sci U S A , pp. 1094134-1094139
    • Motlagh, H.N.1    Hilser, V.J.2
  • 49
    • 84876158670 scopus 로고    scopus 로고
    • The switches.ELM resource: a compendium of conditional regulatory interaction interfaces
    • Van Roey K., Dinkel H., Weatheritt R.J., Gibson T.J., Davey N.E. The switches.ELM resource: a compendium of conditional regulatory interaction interfaces. Sci Signal 2013, 6rs7.
    • (2013) Sci Signal
    • Van Roey, K.1    Dinkel, H.2    Weatheritt, R.J.3    Gibson, T.J.4    Davey, N.E.5
  • 50
    • 0037318720 scopus 로고    scopus 로고
    • Adaptors as central mediators of signal transduction in immune cells
    • Jordan M.S., Singer A.L., Koretzky G.A. Adaptors as central mediators of signal transduction in immune cells. Nat Immunol 2003, 4110-4116.
    • (2003) Nat Immunol , pp. 4110-4116
    • Jordan, M.S.1    Singer, A.L.2    Koretzky, G.A.3
  • 51
    • 84862992463 scopus 로고    scopus 로고
    • Tissue-specific splicing of disordered segments that embed binding motifs rewires protein interaction networks
    • Buljan M., Chalancon G., Eustermann S., Wagner G.P., Fuxreiter M., Bateman A., Babu M.M. Tissue-specific splicing of disordered segments that embed binding motifs rewires protein interaction networks. Mol Cell 2012, 46871-46883.
    • (2012) Mol Cell , pp. 46871-46883
    • Buljan, M.1    Chalancon, G.2    Eustermann, S.3    Wagner, G.P.4    Fuxreiter, M.5    Bateman, A.6    Babu, M.M.7
  • 54
    • 84863928687 scopus 로고    scopus 로고
    • Linear motifs confer functional diversity onto splice variants
    • Weatheritt R.J., Davey N.E., Gibson T.J. Linear motifs confer functional diversity onto splice variants. Nucleic Acids Res 2012, 407123-407131.
    • (2012) Nucleic Acids Res , pp. 407123-407131
    • Weatheritt, R.J.1    Davey, N.E.2    Gibson, T.J.3
  • 55
  • 57
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels
    • Kato M., Han T.W., Xie S., Shi K., Du X., Wu L.C., Mirzaei H., Goldsmith E.J., Longgood J., Pei J., et al. Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. Cell 2012, 149753-149767.
    • (2012) Cell , pp. 149753-149767
    • Kato, M.1    Han, T.W.2    Xie, S.3    Shi, K.4    Du, X.5    Wu, L.C.6    Mirzaei, H.7    Goldsmith, E.J.8    Longgood, J.9    Pei, J.10
  • 60
    • 84878136082 scopus 로고    scopus 로고
    • Blessings in disguise: biological benefits of prion-like mechanisms
    • Newby G.A., Lindquist S. Blessings in disguise: biological benefits of prion-like mechanisms. Trends Cell Biol 2013, 23251-23259.
    • (2013) Trends Cell Biol , pp. 23251-23259
    • Newby, G.A.1    Lindquist, S.2
  • 61
    • 80053441923 scopus 로고    scopus 로고
    • Dynamic protein-DNA recognition: beyond what can be seen
    • Fuxreiter M., Simon I., Bondos S. Dynamic protein-DNA recognition: beyond what can be seen. Trends Biochem Sci 2011, 36415-36423.
    • (2011) Trends Biochem Sci , pp. 36415-36423
    • Fuxreiter, M.1    Simon, I.2    Bondos, S.3
  • 62
    • 84864545860 scopus 로고    scopus 로고
    • Thermodynamic dissection of the intrinsically disordered N-terminal domain of human glucocorticoid receptor
    • Li J., Motlagh H.N., Chakuroff C., Thompson E.B., Hilser V.J. Thermodynamic dissection of the intrinsically disordered N-terminal domain of human glucocorticoid receptor. J Biol Chem 2012, 28726777-28726787.
    • (2012) J Biol Chem , pp. 28726777-28726787
    • Li, J.1    Motlagh, H.N.2    Chakuroff, C.3    Thompson, E.B.4    Hilser, V.J.5
  • 63
    • 84862274751 scopus 로고    scopus 로고
    • Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly
    • Fermani S., Trivelli X., Sparla F., Thumiger A., Calvaresi M., Marri L., Falini G., Zerbetto F., Trost P. Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly. J Biol Chem 2012, 28721372-28721383.
    • (2012) J Biol Chem , pp. 28721372-28721383
    • Fermani, S.1    Trivelli, X.2    Sparla, F.3    Thumiger, A.4    Calvaresi, M.5    Marri, L.6    Falini, G.7    Zerbetto, F.8    Trost, P.9
  • 64
    • 38349085008 scopus 로고    scopus 로고
    • Spontaneous assembly of photosynthetic supramolecular complexes as mediated by the intrinsically unstructured protein CP12
    • Marri L., Trost P., Trivelli X., Gonnelli L., Pupillo P., Sparla F. Spontaneous assembly of photosynthetic supramolecular complexes as mediated by the intrinsically unstructured protein CP12. J Biol Chem 2008, 2831831-2831838.
    • (2008) J Biol Chem , pp. 2831831-2831838
    • Marri, L.1    Trost, P.2    Trivelli, X.3    Gonnelli, L.4    Pupillo, P.5    Sparla, F.6
  • 67
    • 84866403056 scopus 로고    scopus 로고
    • Sweeping away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression
    • Santner A.A., Croy C.H., Vasanwala F.H., Uversky V.N., Van Y.Y., Dunker A.K. Sweeping away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression. Biochemistry 2012, 517250-517262.
    • (2012) Biochemistry , pp. 517250-517262
    • Santner, A.A.1    Croy, C.H.2    Vasanwala, F.H.3    Uversky, V.N.4    Van, Y.Y.5    Dunker, A.K.6
  • 69
    • 84876432757 scopus 로고    scopus 로고
    • Marked variability in the extent of protein disorder within and between viral families
    • Pushker R., Mooney C., Davey N.E., Jacque J.M., Shields D.C. Marked variability in the extent of protein disorder within and between viral families. PLoS ONE 2013, 8e60724.
    • (2013) PLoS ONE
    • Pushker, R.1    Mooney, C.2    Davey, N.E.3    Jacque, J.M.4    Shields, D.C.5
  • 70
    • 84859701551 scopus 로고    scopus 로고
    • Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life
    • Xue B., Dunker A.K., Uversky V.N. Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life. J Biomol Struct Dyn 2012, 30137-30149.
    • (2012) J Biomol Struct Dyn , pp. 30137-30149
    • Xue, B.1    Dunker, A.K.2    Uversky, V.N.3
  • 73
    • 84892876722 scopus 로고    scopus 로고
    • Signatures of pleiotropy, economy and convergent evolution in a domain-resolved map of human-virus protein-protein interaction networks
    • Garamszegi S., Franzosa E.A., Xia Y. Signatures of pleiotropy, economy and convergent evolution in a domain-resolved map of human-virus protein-protein interaction networks. PLoS Pathog 2013, 9e1003778.
    • (2013) PLoS Pathog
    • Garamszegi, S.1    Franzosa, E.A.2    Xia, Y.3
  • 74
    • 84902318220 scopus 로고    scopus 로고
    • Use of host-like peptide motifs in viral proteins is a prevalent strategy in host-virus interactions
    • (in press)
    • Hagai T., Azia A., Babu M.M., Andino R. Use of host-like peptide motifs in viral proteins is a prevalent strategy in host-virus interactions. Cell Reports 2014, 7(5). (in press). 10.1016/j.celrep.2014.04.052.
    • (2014) Cell Reports , vol.7 , Issue.5
    • Hagai, T.1    Azia, A.2    Babu, M.M.3    Andino, R.4
  • 77
    • 84859780045 scopus 로고    scopus 로고
    • Spatial organization of enzymes for metabolic engineering
    • Lee H., DeLoache W.C., Dueber J.E. Spatial organization of enzymes for metabolic engineering. Metab Eng 2012, 14242-14251.
    • (2012) Metab Eng , pp. 14242-14251
    • Lee, H.1    DeLoache, W.C.2    Dueber, J.E.3
  • 78
    • 0141757323 scopus 로고    scopus 로고
    • Reprogramming control of an allosteric signaling switch through modular recombination
    • Dueber J.E., Yeh B.J., Chak K., Lim W.A. Reprogramming control of an allosteric signaling switch through modular recombination. Science 2003, 3011904-3011908.
    • (2003) Science , pp. 3011904-3011908
    • Dueber, J.E.1    Yeh, B.J.2    Chak, K.3    Lim, W.A.4
  • 79
    • 77952944052 scopus 로고    scopus 로고
    • Designing customized cell signalling circuits
    • Lim W.A. Designing customized cell signalling circuits. Nat Rev Mol Cell Biol 2010, 11393-11403.
    • (2010) Nat Rev Mol Cell Biol , pp. 11393-11403
    • Lim, W.A.1
  • 80
    • 84874245248 scopus 로고    scopus 로고
    • Injectable protease-operated depots of glucagon-like peptide-1 provide extended and tunable glucose control
    • Amiram M., Luginbuhl K.M., Li X., Feinglos M.N., Chilkoti A. Injectable protease-operated depots of glucagon-like peptide-1 provide extended and tunable glucose control. Proc Natl Acad Sci U S A 2013, 1102792-1102797.
    • (2013) Proc Natl Acad Sci U S A , pp. 1102792-1102797
    • Amiram, M.1    Luginbuhl, K.M.2    Li, X.3    Feinglos, M.N.4    Chilkoti, A.5
  • 82
    • 84864709161 scopus 로고    scopus 로고
    • Structural biology: dynamic binding
    • Baldwin A.J., Kay L.E. Structural biology: dynamic binding. Nature 2012, 488165-488166.
    • (2012) Nature , pp. 488165-488166
    • Baldwin, A.J.1    Kay, L.E.2
  • 83
    • 84873526289 scopus 로고    scopus 로고
    • Molten globules, entropy-driven conformational change and protein folding
    • Baldwin R.L., Rose G.D. Molten globules, entropy-driven conformational change and protein folding. Curr Opin Struct Biol 2013, 234-310.
    • (2013) Curr Opin Struct Biol , pp. 234-310
    • Baldwin, R.L.1    Rose, G.D.2
  • 84
    • 84873526287 scopus 로고    scopus 로고
    • The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation
    • Wand A.J. The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation. Curr Opin Struct Biol 2013, 2375-2381.
    • (2013) Curr Opin Struct Biol , pp. 2375-2381
    • Wand, A.J.1
  • 86
    • 84873527015 scopus 로고    scopus 로고
    • Single-molecule spectroscopy of protein folding dynamics-expanding scope and timescales
    • Schuler B., Hofmann H. Single-molecule spectroscopy of protein folding dynamics-expanding scope and timescales. Curr Opin Struct Biol 2013, 2336-2347.
    • (2013) Curr Opin Struct Biol , pp. 2336-2347
    • Schuler, B.1    Hofmann, H.2
  • 87
    • 84886930646 scopus 로고    scopus 로고
    • Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding
    • Kumar R., Moure C.M., Khan S.H., Callaway C., Grimm S.L., Goswami D., Griffin P.R., Edwards D.P. Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. J Biol Chem 2013, 28830285-28830299.
    • (2013) J Biol Chem , pp. 28830285-28830299
    • Kumar, R.1    Moure, C.M.2    Khan, S.H.3    Callaway, C.4    Grimm, S.L.5    Goswami, D.6    Griffin, P.R.7    Edwards, D.P.8
  • 88
    • 84889583170 scopus 로고    scopus 로고
    • Pleomorphic ensembles: formation of large clusters composed of weakly interacting multivalent molecules
    • Falkenberg C.V., Blinov M.L., Loew L.M. Pleomorphic ensembles: formation of large clusters composed of weakly interacting multivalent molecules. Biophys J 2013, 1052451-1052460.
    • (2013) Biophys J , pp. 1052451-1052460
    • Falkenberg, C.V.1    Blinov, M.L.2    Loew, L.M.3
  • 89
    • 84871427941 scopus 로고    scopus 로고
    • Describing sequence-ensemble relationships for intrinsically disordered proteins
    • Mao A.H., Lyle N., Pappu R.V. Describing sequence-ensemble relationships for intrinsically disordered proteins. Biochem J 2013, 449307-449318.
    • (2013) Biochem J , pp. 449307-449318
    • Mao, A.H.1    Lyle, N.2    Pappu, R.V.3
  • 90
    • 84884282981 scopus 로고    scopus 로고
    • Mapping protein conformational energy landscapes using NMR and molecular simulation
    • Guerry P., Mollica L., Blackledge M. Mapping protein conformational energy landscapes using NMR and molecular simulation. Chemphyschem 2013, 143046-143058.
    • (2013) Chemphyschem , pp. 143046-143058
    • Guerry, P.1    Mollica, L.2    Blackledge, M.3
  • 92
    • 84876221513 scopus 로고    scopus 로고
    • Higher-order assemblies in a new paradigm of signal transduction
    • Wu H. Higher-order assemblies in a new paradigm of signal transduction. Cell 2013, 153287-153292.
    • (2013) Cell , pp. 153287-153292
    • Wu, H.1
  • 93
    • 0041845285 scopus 로고    scopus 로고
    • Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha
    • Fontes M.R., Teh T., Jans D., Brinkworth R.I., Kobe B. Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha. J Biol Chem 2003, 27827981-27827987.
    • (2003) J Biol Chem , pp. 27827981-27827987
    • Fontes, M.R.1    Teh, T.2    Jans, D.3    Brinkworth, R.I.4    Kobe, B.5
  • 95
    • 79960742369 scopus 로고    scopus 로고
    • Endocytic sorting of transmembrane protein cargo
    • Kelly B.T., Owen D.J. Endocytic sorting of transmembrane protein cargo. Curr Opin Cell Biol 2011, 23404-23412.
    • (2011) Curr Opin Cell Biol , pp. 23404-23412
    • Kelly, B.T.1    Owen, D.J.2
  • 97
    • 33846822002 scopus 로고    scopus 로고
    • Ligand configurational entropy and protein binding
    • Chang C.E., Chen W., Gilson M.K. Ligand configurational entropy and protein binding. Proc Natl Acad Sci U S A 2007, 1041534-1041539.
    • (2007) Proc Natl Acad Sci U S A , pp. 1041534-1041539
    • Chang, C.E.1    Chen, W.2    Gilson, M.K.3
  • 98
    • 0023475026 scopus 로고
    • Configurational entropy of native proteins
    • Karplus M., Ichiye T., Pettitt B.M. Configurational entropy of native proteins. Biophys J 1987, 521083-521085.
    • (1987) Biophys J , pp. 521083-521085
    • Karplus, M.1    Ichiye, T.2    Pettitt, B.M.3


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