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Volumn 12, Issue 5, 2011, Pages 3205-3219

Novel strategies for drug discovery based on intrinsically disordered proteins (IDPs)

Author keywords

Drug discovery; Interaction networks; Intrinsically disordered proteins; Sequence characterizations; Structural characterizations

Indexed keywords

ALPHA SYNUCLEIN; EXIFONE; INTRINSICALLY DISORDERED PROTEIN; PROTEIN P53; ROTENONE; STRUCTURAL PROTEIN; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 79957846007     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms12053205     Document Type: Review
Times cited : (46)

References (92)
  • 1
    • 0028170411 scopus 로고
    • Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure
    • Schweers, O.; Schonbrunn-Hanebeck, E.; Marx, A.; Mandelkow, E. Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. J. Biol. Chem. 1994, 269, 24290-24297.
    • (1994) J. Biol. Chem , vol.269 , pp. 24290-24297
    • Schweers, O.1    Schonbrunn-Hanebeck, E.2    Marx, A.3    Mandelkow, E.4
  • 2
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V.N. Natively unfolded proteins: A point where biology waits for physics. Protein Sci. 2002, 11, 739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 4
    • 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, 293, 321-331.
    • (1999) J. Mol. Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 5
    • 73449140116 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of Intrinsically Disordered Proteins in Human Diseases
    • Wang, J.H.; Cao, Z.X.; Li, S.Q. Molecular Dynamics Simulations of Intrinsically Disordered Proteins in Human Diseases. Curr. Comput.-Aided Drug Des. 2009, 5, 280-287.
    • (2009) Curr. Comput.-Aided Drug Des , vol.5 , pp. 280-287
    • Wang, J.H.1    Cao, Z.X.2    Li, S.Q.3
  • 6
    • 72449139985 scopus 로고    scopus 로고
    • Intrinsically disordered proteins and their environment: Effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding
    • Uversky, V.N. Intrinsically disordered proteins and their environment: Effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding. Protein J. 2009, 28, 305-325.
    • (2009) Protein J , vol.28 , pp. 305-325
    • Uversky, V.N.1
  • 7
    • 10044261828 scopus 로고    scopus 로고
    • Natively unfolded domains in endocytosis: Hooks, lines and linkers
    • Dafforn, T.R.; Smith, C.J.I. Natively unfolded domains in endocytosis: Hooks, lines and linkers. EMBO Rep. 2004, 5, 1046-1052.
    • (2004) EMBO Rep , vol.5 , pp. 1046-1052
    • Dafforn, T.R.1    Smith, C.J.I.2
  • 8
    • 0015859467 scopus 로고
    • Principles that govern folding of protein chains
    • Anfinsen, C.B. Principles that govern folding of protein chains. Science 1973, 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 11
    • 58949101630 scopus 로고    scopus 로고
    • Leucine-rich hydrophobic clusters promote folding of the N-terminus of the intrinsically disordered transactivation domain of p53
    • Espinoza-Fonseca, L.M. Leucine-rich hydrophobic clusters promote folding of the N-terminus of the intrinsically disordered transactivation domain of p53. FEBS Lett. 2009, 583, 556-560.
    • (2009) FEBS Lett , vol.583 , pp. 556-560
    • Espinoza-Fonseca, L.M.1
  • 12
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. Intrinsically unstructured proteins. Trends Biochem. Sci. 2002, 27, 527-533.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 14
    • 33644865137 scopus 로고    scopus 로고
    • Intrinsic protein disorder, amino acid composition, and histone terminal domains
    • Hansen, J.C.; Lu, X.; Ross, E.D.; Woody, R.W. Intrinsic protein disorder, amino acid composition, and histone terminal domains. J. Biol. Chem. 2006, 281, 1853-1856.
    • (2006) J. Biol. Chem , vol.281 , pp. 1853-1856
    • Hansen, J.C.1    Lu, X.2    Ross, E.D.3    Woody, R.W.4
  • 15
    • 0034669882 scopus 로고    scopus 로고
    • Why are -natively unfolded{norm of matrix} proteins unstructured under physiologic conditions?
    • Uversky, V.N.; Gillespie, J.R.; Fink, A.L. Why are -natively unfolded{norm of matrix} proteins unstructured under physiologic conditions? Proteins 2000, 41, 415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 16
    • 42449154662 scopus 로고    scopus 로고
    • Intrinsically disordered protein from a pathogenic mesophile Mycobacterium tuberculosis adopts structured conformation at high temperature
    • Kumar, N.; Shukla, S.; Kumar, S.; Suryawanshi, A.; Chaudhry, U.; Ramachandran, S.; Maiti, S. Intrinsically disordered protein from a pathogenic mesophile Mycobacterium tuberculosis adopts structured conformation at high temperature. Proteins 2008, 71, 1123-1133.
    • (2008) Proteins , vol.71 , pp. 1123-1133
    • Kumar, N.1    Shukla, S.2    Kumar, S.3    Suryawanshi, A.4    Chaudhry, U.5    Ramachandran, S.6    Maiti, S.7
  • 17
    • 0242267517 scopus 로고    scopus 로고
    • Critical assessment of methods of protein structure prediction (CASP)-round V
    • Moult, J.; Fidelis, K.; Zemla, A.; Hubbard, T. Critical assessment of methods of protein structure prediction (CASP)-round V. Proteins 2003, 53, 334-339.
    • (2003) Proteins , vol.53 , pp. 334-339
    • Moult, J.1    Fidelis, K.2    Zemla, A.3    Hubbard, T.4
  • 20
    • 44349192171 scopus 로고    scopus 로고
    • Prediction of disordered regions in proteins based on the meta approach
    • Ishida, T.; Kinoshita, K. Prediction of disordered regions in proteins based on the meta approach. Bioinformatics 2008, 24, 1344-1348.
    • (2008) Bioinformatics , vol.24 , pp. 1344-1348
    • Ishida, T.1    Kinoshita, K.2
  • 21
    • 52149105815 scopus 로고    scopus 로고
    • Using Bayesian multinomial classifier to predict whether a given protein sequence is intrinsically disordered
    • Bulashevska, A.; Eils, R. Using Bayesian multinomial classifier to predict whether a given protein sequence is intrinsically disordered. J. Theor. Biol. 2008, 254, 799-803.
    • (2008) J. Theor. Biol , vol.254 , pp. 799-803
    • Bulashevska, A.1    Eils, R.2
  • 23
    • 77951174390 scopus 로고    scopus 로고
    • A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR
    • Wang, X.; Zhang, S.; Zhang, J.; Huang, X.; Xu, C.; Wang, W.; Liu, Z.; Wu, J.; Shi, Y. A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. J. Biol. Chem. 2010, 285, 4951-4963.
    • (2010) J. Biol. Chem , vol.285 , pp. 4951-4963
    • Wang, X.1    Zhang, S.2    Zhang, J.3    Huang, X.4    Xu, C.5    Wang, W.6    Liu, Z.7    Wu, J.8    Shi, Y.9
  • 25
    • 67049119327 scopus 로고    scopus 로고
    • Prediction of protein binding regions in disordered proteins
    • Meszaros, B.; Simon, I.; Dosztanyi, Z. Prediction of protein binding regions in disordered proteins. PLoS Comput. Biol. 2009, 5, e1000376.
    • (2009) PLoS Comput. Biol , vol.5
    • Meszaros, B.1    Simon, I.2    Dosztanyi, Z.3
  • 26
    • 70349996473 scopus 로고    scopus 로고
    • ANCHOR: Web server for predicting protein binding regions in disordered proteins
    • Dosztanyi, Z.; Meszaros, B.; Simon, I. ANCHOR: Web server for predicting protein binding regions in disordered proteins. Bioinformatics 2009, 25, 2745-2746.
    • (2009) Bioinformatics , vol.25 , pp. 2745-2746
    • Dosztanyi, Z.1    Meszaros, B.2    Simon, I.3
  • 28
    • 60349087841 scopus 로고    scopus 로고
    • Biophysical characterization of intrinsically disordered proteins
    • Eliezer, D. Biophysical characterization of intrinsically disordered proteins. Curr. Opin. Struct. Biol. 2009, 19, 23-30.
    • (2009) Curr. Opin. Struct. Biol , vol.19 , pp. 23-30
    • Eliezer, D.1
  • 29
    • 33847768609 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions
    • Xie, H.; Vucetic, S.; Iakoucheva, L.M.; Oldfield, C.J.; Dunker, A.K.; Uversky, V.N.; Obradovic, Z. Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions. J. Proteome. Res. 2007, 6, 1882-1898.
    • (2007) J. Proteome. Res , vol.6 , pp. 1882-1898
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Uversky, V.N.6    Obradovic, Z.7
  • 32
    • 0040368216 scopus 로고    scopus 로고
    • Prospects for new restorative and neuroprotective treatments in Parkinson's disease
    • Dunnett, S.B.; Bjorklund, A. Prospects for new restorative and neuroprotective treatments in Parkinson's disease. Nature 1999, 399, A32-A39.
    • (1999) Nature , vol.399
    • Dunnett, S.B.1    Bjorklund, A.2
  • 33
    • 59649110692 scopus 로고    scopus 로고
    • Structural insights on physiological functions and pathological effects of alpha-synuclein
    • Bisaglia, M.; Mammi, S.; Bubacco, L. Structural insights on physiological functions and pathological effects of alpha-synuclein. Faseb. J. 2009, 23, 329-340.
    • (2009) Faseb. J , vol.23 , pp. 329-340
    • Bisaglia, M.1    Mammi, S.2    Bubacco, L.3
  • 34
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human alpha-synuclein
    • Ulmer, T.S.; Bax, A.; Cole, N.B.; Nussbaum, R.L. Structure and dynamics of micelle-bound human alpha-synuclein. J. Biol. Chem. 2005, 280, 9595-9603.
    • (2005) J. Biol. Chem , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 35
  • 36
    • 33746894560 scopus 로고    scopus 로고
    • Inter-helix distances in lysophospholipid micelle-bound alpha-synuclein from pulsed ESR measurements
    • Borbat, P.; Ramlall, T.F.; Freed, J.H.; Eliezer, D. Inter-helix distances in lysophospholipid micelle-bound alpha-synuclein from pulsed ESR measurements. J. Am. Chem. Soc. 2006, 128, 10004-10005.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 10004-10005
    • Borbat, P.1    Ramlall, T.F.2    Freed, J.H.3    Eliezer, D.4
  • 37
    • 58149173445 scopus 로고    scopus 로고
    • Membrane-bound alpha-synuclein forms an extended helix: Long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles
    • Georgieva, E.R.; Ramlall, T.F.; Borbat, P.P.; Freed, J.H.; Eliezer, D. Membrane-bound alpha-synuclein forms an extended helix: Long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles. J. Am. Chem. Soc. 2008, 130, 12856-12857.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 12856-12857
    • Georgieva, E.R.1    Ramlall, T.F.2    Borbat, P.P.3    Freed, J.H.4    Eliezer, D.5
  • 38
    • 58149380718 scopus 로고    scopus 로고
    • Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement
    • Jao, C.C.; Hegde, B.G.; Chen, J.; Haworth, I.S.; Langen, R. Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement. Proc. Natl. Acad. Sci. USA 2008, 105, 19666-19671.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19666-19671
    • Jao, C.C.1    Hegde, B.G.2    Chen, J.3    Haworth, I.S.4    Langen, R.5
  • 39
    • 65249185574 scopus 로고    scopus 로고
    • Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence
    • Ferreon, A.C.; Gambin, Y.; Lemke, E.A.; Deniz, A.A. Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence. Proc. Natl. Acad. Sci. USA 2009, 106, 5645-5650.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5645-5650
    • Ferreon, A.C.1    Gambin, Y.2    Lemke, E.A.3    Deniz, A.A.4
  • 40
    • 64849109238 scopus 로고    scopus 로고
    • Alpha-synuclein binds large unilamellar vesicles as an extended helix
    • Trexler, A.J.; Rhoades, E. Alpha-synuclein binds large unilamellar vesicles as an extended helix. Biochemistry 2009, 48, 2304-2306.
    • (2009) Biochemistry , vol.48 , pp. 2304-2306
    • Trexler, A.J.1    Rhoades, E.2
  • 41
    • 77956258196 scopus 로고    scopus 로고
    • The lipid-binding domain of wild type and mutant alpha-synuclein: Compactness and interconversion between the broken- and extended-helix forms
    • Georgieva, E.R.; Ramlall, T.F.; Borbat, P.P.; Freed, J.H.; Eliezer, D. The lipid-binding domain of wild type and mutant alpha-synuclein: Compactness and interconversion between the broken- and extended-helix forms. J. Biol. Chem. 2010, 285, 18261-18274.
    • (2010) J. Biol. Chem , vol.285 , pp. 18261-18274
    • Georgieva, E.R.1    Ramlall, T.F.2    Borbat, P.P.3    Freed, J.H.4    Eliezer, D.5
  • 42
    • 73549109861 scopus 로고    scopus 로고
    • Characterization of inhibitor-bound alpha-synuclein dimer: Role of alpha-synuclein N-terminal region in dimerization and inhibitor binding
    • Yamaguchi, Y.; Masuda, M.; Sasakawa, H.; Nonaka, T.; Hanashima, S.; Hisanaga, S.; Kato, K.; Hasegawa, M. Characterization of inhibitor-bound alpha-synuclein dimer: Role of alpha-synuclein N-terminal region in dimerization and inhibitor binding. J. Mol. Biol. 2010, 395, 445-456.
    • (2010) J. Mol. Biol , vol.395 , pp. 445-456
    • Yamaguchi, Y.1    Masuda, M.2    Sasakawa, H.3    Nonaka, T.4    Hanashima, S.5    Hisanaga, S.6    Kato, K.7    Hasegawa, M.8
  • 45
    • 0035014892 scopus 로고    scopus 로고
    • NMR spin relaxation methods for characterization of disorder and folding in proteins
    • Bracken, C. NMR spin relaxation methods for characterization of disorder and folding in proteins. J. Mol. Graph. 2001, 19, 3-12.
    • (2001) J. Mol. Graph , vol.19 , pp. 3-12
    • Bracken, C.1
  • 46
    • 34247210096 scopus 로고    scopus 로고
    • Identifying long-range structure in the intrinsically unstructured transactivation domain of p53
    • Vise, P.; Baral, B.; Stancik, A.; Lowry, D.F.; Daughdrill, G.W. Identifying long-range structure in the intrinsically unstructured transactivation domain of p53. Proteins 2007, 67, 526-530.
    • (2007) Proteins , vol.67 , pp. 526-530
    • Vise, P.1    Baral, B.2    Stancik, A.3    Lowry, D.F.4    Daughdrill, G.W.5
  • 47
    • 56749172641 scopus 로고    scopus 로고
    • Detailed Structural Characterization of Unbound Protein Phosphatase 1 Inhibitors
    • Dancheck, B.; Naim, A.C.; Peti, W. Detailed Structural Characterization of Unbound Protein Phosphatase 1 Inhibitors. Biochemistry 2008, 47, 12346-12356.
    • (2008) Biochemistry , vol.47 , pp. 12346-12356
    • Dancheck, B.1    Naim, A.C.2    Peti, W.3
  • 48
    • 72949094878 scopus 로고    scopus 로고
    • Biophysical characterization reveals structural disorder in the developmental transcriptional regulator LBH
    • Al-Ali, H.; Rieger, M.E.; Seldeen, K.L.; Harris, T.K.; Farooq, A.; Briegel, K.J. Biophysical characterization reveals structural disorder in the developmental transcriptional regulator LBH. Biochem. Biophys. Res. Commun. 2010, 391, 1104-1109.
    • (2010) Biochem. Biophys. Res. Commun , vol.391 , pp. 1104-1109
    • Al-Ali, H.1    Rieger, M.E.2    Seldeen, K.L.3    Harris, T.K.4    Farooq, A.5    Briegel, K.J.6
  • 49
    • 0035984339 scopus 로고    scopus 로고
    • Studies of biomolecular conformations and conformational dynamics by mass spectrometry
    • Kaltashov, I.A.; Eyles, S.J. Studies of biomolecular conformations and conformational dynamics by mass spectrometry. Mass Spectrom. Rev. 2002, 21, 37-71.
    • (2002) Mass Spectrom. Rev , vol.21 , pp. 37-71
    • Kaltashov, I.A.1    Eyles, S.J.2
  • 50
    • 33750934185 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions
    • Crick, S.L.; Jayaraman, M.; Frieden, C.; Wetzel, R.; Pappu, R.V. Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions. Proc. Natl. Acad. Sci. USA 2006, 103, 16764-16769.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16764-16769
    • Crick, S.L.1    Jayaraman, M.2    Frieden, C.3    Wetzel, R.4    Pappu, R.V.5
  • 51
    • 67349216108 scopus 로고    scopus 로고
    • H-start for exclusively heteronuclear NMR spectroscopy: The case of intrinsically disordered proteins
    • Bermel, W.; Bertini, I.; Csizmok, V.; Felli, I.C.; Pierattelli, R.; Tompa, P. H-start for exclusively heteronuclear NMR spectroscopy: The case of intrinsically disordered proteins. J. Magn. Reson. 2009, 198, 275-281.
    • (2009) J. Magn. Reson , vol.198 , pp. 275-281
    • Bermel, W.1    Bertini, I.2    Csizmok, V.3    Felli, I.C.4    Pierattelli, R.5    Tompa, P.6
  • 52
    • 65549129174 scopus 로고    scopus 로고
    • PEP-19, an intrinsically disordered regulator of calmodulin signaling
    • Kleerekoper, Q.K.; Putkey, J.A. PEP-19, an intrinsically disordered regulator of calmodulin signaling. J. Biol. Chem. 2009, 284, 7455-7464.
    • (2009) J. Biol. Chem , vol.284 , pp. 7455-7464
    • Kleerekoper, Q.K.1    Putkey, J.A.2
  • 53
    • 45849135972 scopus 로고    scopus 로고
    • Solution NMR and CD spectroscopy of an intrinsically disordered, peripheral membrane protein: Evaluation of aqueous and membrane-mimetic solvent conditions for studying the conformational adaptability of the 18.5 kDa isoform of myelin basic protein (MBP)
    • Libich, D.S.; Harauz, G. Solution NMR and CD spectroscopy of an intrinsically disordered, peripheral membrane protein: Evaluation of aqueous and membrane-mimetic solvent conditions for studying the conformational adaptability of the 18.5 kDa isoform of myelin basic protein (MBP). Eur. Biophys. J 2008, 37, 1015-1029.
    • (2008) Eur. Biophys. J , vol.37 , pp. 1015-1029
    • Libich, D.S.1    Harauz, G.2
  • 54
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: Implications for fibrillation
    • Marsh, J.A.; Singh, V.K.; Jia, Z.; Forman-Kay, J.D. Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: Implications for fibrillation. Protein Sci. 2006, 15, 2795-2804.
    • (2006) Protein Sci , vol.15 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.3    Forman-Kay, J.D.4
  • 55
    • 73249124356 scopus 로고    scopus 로고
    • Determination of the free energy landscape of alpha-synuclein using spin label nuclear magnetic resonance measurements
    • Allison, J.R.; Varnai, P.; Dobson, C.M.; Vendruscolo, M. Determination of the free energy landscape of alpha-synuclein using spin label nuclear magnetic resonance measurements. J. Am. Chem. Soc. 2009, 131, 18314-18326.
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 18314-18326
    • Allison, J.R.1    Varnai, P.2    Dobson, C.M.3    Vendruscolo, M.4
  • 56
    • 41149177142 scopus 로고    scopus 로고
    • Modeling the accessible conformations of the intrinsically unstructured transactivation domain of p53
    • Lowry, D.F.; Stancik, A.; Shrestha, R.M.; Daughdrill, G.W. Modeling the accessible conformations of the intrinsically unstructured transactivation domain of p53. Proteins 2008, 71, 587-598.
    • (2008) Proteins , vol.71 , pp. 587-598
    • Lowry, D.F.1    Stancik, A.2    Shrestha, R.M.3    Daughdrill, G.W.4
  • 57
    • 44949262123 scopus 로고    scopus 로고
    • Role of backbone-Solvent interactions in determining conformational equilibria of intrinsically disordered proteins
    • Tran, H.T.; Mao, A.; Pappu, R.V. Role of backbone-Solvent interactions in determining conformational equilibria of intrinsically disordered proteins. J. Am. Chem. Soc. 2008, 130, 7380-7392.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 7380-7392
    • Tran, H.T.1    Mao, A.2    Pappu, R.V.3
  • 58
    • 79951886900 scopus 로고    scopus 로고
    • Structural and thermodynamics characters of isolated alpha-syn12 peptide: Long-time temperature replica-exchange molecular dynamics in aqueous solution
    • Cao, Z.; Liu, L.; Wu, P.; Wang, J. Structural and thermodynamics characters of isolated alpha-syn12 peptide: Long-time temperature replica-exchange molecular dynamics in aqueous solution. Acta Biochim. Biophys. Sin. 2011, 43, 172-180.
    • (2011) Acta Biochim. Biophys. Sin , vol.43 , pp. 172-180
    • Cao, Z.1    Liu, L.2    Wu, P.3    Wang, J.4
  • 59
    • 78649874973 scopus 로고    scopus 로고
    • Effects of pH and temperature on the structural and thermodynamic character of alpha-syn12 peptide in aqueous solution
    • Cao, Z.; Liu, L.; Wang, J. Effects of pH and temperature on the structural and thermodynamic character of alpha-syn12 peptide in aqueous solution. J. Biomol. Struct. Dyn. 2010, 28, 343-353.
    • (2010) J. Biomol. Struct. Dyn , vol.28 , pp. 343-353
    • Cao, Z.1    Liu, L.2    Wang, J.3
  • 60
    • 38549110665 scopus 로고    scopus 로고
    • Residual structure in disordered peptides and unfolded proteins from multivariate analysis and ab initio simulation of Raman optical activity data
    • Zhu, F.; Kapitan, J.; Tranter, G.E.; Pudney, P.D.A.; Isaacs, N.W.; Hecht, L.; Barron, L.D. Residual structure in disordered peptides and unfolded proteins from multivariate analysis and ab initio simulation of Raman optical activity data. Proteins 2008, 70, 823-833.
    • (2008) Proteins , vol.70 , pp. 823-833
    • Zhu, F.1    Kapitan, J.2    Tranter, G.E.3    Pudney, P.D.A.4    Isaacs, N.W.5    Hecht, L.6    Barron, L.D.7
  • 61
    • 0027474991 scopus 로고
    • Left-handed Polyproline-II helices commonly occur in globular proteins
    • Adzhubei, A.A.; Sternberg, M.J.E. Left-handed Polyproline-II helices commonly occur in globular proteins. J. Mol. Biol. 1993, 229, 472-493.
    • (1993) J. Mol. Biol , vol.229 , pp. 472-493
    • Adzhubei, A.A.1    Sternberg, M.J.E.2
  • 62
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson, M.P. The structure and function of proline-rich regions in proteins. Biochem. J. 1994, 297, 249-260.
    • (1994) Biochem. J , vol.297 , pp. 249-260
    • Williamson, M.P.1
  • 64
    • 67650385638 scopus 로고    scopus 로고
    • Protein disorder in the human diseasome: Unfoldomics of human genetic diseases
    • Midic, U.; Oldfield, C.J.; Dunker, A.K.; Obradovic, Z.; Uversky, V.N. Protein disorder in the human diseasome: unfoldomics of human genetic diseases. BMC Genomics 2009, 10, 1:S12.
    • (2009) BMC Genomics , vol.10 , Issue.1
    • Midic, U.1    Oldfield, C.J.2    Dunker, A.K.3    Obradovic, Z.4    Uversky, V.N.5
  • 65
    • 73449123761 scopus 로고    scopus 로고
    • Unfoldomics of human genetic diseases: Illustrative examples of ordered and intrinsically disordered members of the human diseasome
    • Midic, U.; Oldfield, C.J.; Dunker, A.K.; Obradovic, Z.; Uversky, V.N. Unfoldomics of human genetic diseases: illustrative examples of ordered and intrinsically disordered members of the human diseasome. Protein Pept. Lett. 2009, 16, 1533-1547.
    • (2009) Protein Pept. Lett , vol.16 , pp. 1533-1547
    • Midic, U.1    Oldfield, C.J.2    Dunker, A.K.3    Obradovic, Z.4    Uversky, V.N.5
  • 66
    • 65949097958 scopus 로고    scopus 로고
    • The role of intrinsically unstructured proteins in neurodegenerative diseases
    • Raychaudhuri, S.; Dey, S.; Bhattacharyya, N.P.; Mukhopadhyay, D. The role of intrinsically unstructured proteins in neurodegenerative diseases. PLoS One 2009, 4, e5566.
    • (2009) PLoS One , vol.4
    • Raychaudhuri, S.1    Dey, S.2    Bhattacharyya, N.P.3    Mukhopadhyay, D.4
  • 67
    • 70149097069 scopus 로고    scopus 로고
    • Interaction between intrinsically disordered proteins frequently occurs in a human protein-protein interaction network
    • Shimizu, K.; Toh, H. Interaction between intrinsically disordered proteins frequently occurs in a human protein-protein interaction network. J. Mol. Biol. 2009, 392, 1253-1265.
    • (2009) J. Mol. Biol , vol.392 , pp. 1253-1265
    • Shimizu, K.1    Toh, H.2
  • 68
    • 77951898121 scopus 로고    scopus 로고
    • Hub promiscuity in protein-protein interaction networks
    • Patil, A.; Kinoshita, K.; Nakamura, H. Hub promiscuity in protein-protein interaction networks. Int. J. Mol. Sci. 2010, 11, 1930-1943.
    • (2010) Int. J. Mol. Sci , vol.11 , pp. 1930-1943
    • Patil, A.1    Kinoshita, K.2    Nakamura, H.3
  • 69
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets-The roles of intrinsic disorder in protein interaction networks
    • Dunker, A.K.; Cortese, M.S.; Romero, P.; Iakoucheva, L.M.; Uversky, V.N. Flexible nets-The roles of intrinsic disorder in protein interaction networks. FEBS J. 2005, 272, 5129-5148.
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 70
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure
    • Uversky, V.N.; Li, J.; Fink, A.L. Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure. J. Biol. Chem. 2001, 276, 44284-44296.
    • (2001) J. Biol. Chem , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 71
    • 33847783298 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins
    • Xie, H.; Vucetic, S.; Iakoucheva, L.M.; Oldfield, C.J.; Dunker, A.K.; Obradovic, Z.; Uversky, V.N. Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins. J. Proteome Res. 2007, 6, 1917-1932.
    • (2007) J. Proteome Res , vol.6 , pp. 1917-1932
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Obradovic, Z.6    Uversky, V.N.7
  • 72
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F.; Dobson, C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75, 333-366.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 73
    • 34547631623 scopus 로고    scopus 로고
    • Prevention of amyloid-like aggregation as a driving force of protein evolution
    • Monsellier, E.; Chiti, F. Prevention of amyloid-like aggregation as a driving force of protein evolution. EMBO Rep. 2007, 8, 737-742.
    • (2007) EMBO Rep , vol.8 , pp. 737-742
    • Monsellier, E.1    Chiti, F.2
  • 74
    • 70349662023 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Potential targets for drug discovery
    • Pathan, S.; Chintan, C.; Sriram, S. Intrinsically unstructured proteins: Potential targets for drug discovery. Am. J. Infect. Dis. 2009, 5, 133-141.
    • (2009) Am. J. Infect. Dis , vol.5 , pp. 133-141
    • Pathan, S.1    Chintan, C.2    Sriram, S.3
  • 75
    • 70349086181 scopus 로고    scopus 로고
    • SH2B1 enhances insulin sensitivity by both stimulating the insulin receptor and inhibiting tyrosine dephosphorylation of insulin receptor substrate proteins
    • Morris, D.L.; Cho, K.W.; Zhou, Y.; Rui, L. SH2B1 enhances insulin sensitivity by both stimulating the insulin receptor and inhibiting tyrosine dephosphorylation of insulin receptor substrate proteins. Diabetes 2009, 58, 2039-2047.
    • (2009) Diabetes , vol.58 , pp. 2039-2047
    • Morris, D.L.1    Cho, K.W.2    Zhou, Y.3    Rui, L.4
  • 76
    • 70349662023 scopus 로고    scopus 로고
    • Intrinsically Unstructured Proteins: Potential Targets for Drug Discovery
    • Salma, P.; Chhatbar, C.; Seshadri, S. Intrinsically Unstructured Proteins: Potential Targets for Drug Discovery. Am. J. Infect. Dis. 2009, 5, 133-141.
    • (2009) Am. J. Infect. Dis , vol.5 , pp. 133-141
    • Salma, P.1    Chhatbar, C.2    Seshadri, S.3
  • 77
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: Introducing the D2 concept
    • Uversky, V.N.; Oldfield, C.J.; Dunker, A.K. Intrinsically disordered proteins in human diseases: Introducing the D2 concept. Annu. Rev. Biophys. 2008, 37, 215-246.
    • (2008) Annu. Rev. Biophys , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 78
    • 25144472591 scopus 로고    scopus 로고
    • Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • Uversky, V.N.; Oldfield, C.J.; Dunker, A.K. Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling. J. Mol. Recognit. 2005, 18, 343-384.
    • (2005) J. Mol. Recognit , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3    Showing, Y.I.D.4
  • 81
    • 20444376940 scopus 로고    scopus 로고
    • Protein-protein interactions and cancer: Small molecules going in for the kill
    • Arkin, M. Protein-protein interactions and cancer: Small molecules going in for the kill. Curr. Opin. Chem. Biol. 2005, 9, 317-324.
    • (2005) Curr. Opin. Chem. Biol , vol.9 , pp. 317-324
    • Arkin, M.1
  • 84
    • 34249704608 scopus 로고    scopus 로고
    • Identification of novel proteins associated with both alpha-synuclein and DJ-1
    • Jin, J.H.; Li, G.J.; Davis, J.; Zhu, D.; Wang, Y.; Pan, C.; Zhang, J. Identification of novel proteins associated with both alpha-synuclein and DJ-1. Mol. Cell. Proteomics 2007, 6, 845-859.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 845-859
    • Jin, J.H.1    Li, G.J.2    Davis, J.3    Zhu, D.4    Wang, Y.5    Pan, C.6    Zhang, J.7
  • 86
    • 33750731675 scopus 로고    scopus 로고
    • 100 years and counting: Prospects for defeating Alzheimer's disease
    • Roberson, E.D.; Mucke, L. 100 years and counting: Prospects for defeating Alzheimer's disease. Science 2006, 314, 781-784.
    • (2006) Science , vol.314 , pp. 781-784
    • Roberson, E.D.1    Mucke, L.2
  • 87
    • 34250162541 scopus 로고    scopus 로고
    • Alzheimer's disease-A new take on tau
    • Marx, J. Alzheimer's disease-A new take on tau. Science 2007, 316, 1416-1417.
    • (2007) Science , vol.316 , pp. 1416-1417
    • Marx, J.1
  • 89
    • 0033992478 scopus 로고    scopus 로고
    • p53 and human cancer: The first ten thousand mutations
    • Hainaut, P.; Hollstein, M. p53 and human cancer: The first ten thousand mutations. Adv. Cancer. Res. 2000, 77, 81-137.
    • (2000) Adv. Cancer. Res , vol.77 , pp. 81-137
    • Hainaut, P.1    Hollstein, M.2
  • 90
    • 70249148909 scopus 로고    scopus 로고
    • Redefining cancer research
    • Alberts, B. Redefining cancer research. Science 2009, 325, 1319-1319.
    • (2009) Science , vol.325 , pp. 1319
    • Alberts, B.1
  • 92
    • 1642357706 scopus 로고    scopus 로고
    • The many roles of computation in drug discovery
    • Jorgensen, W.L. The many roles of computation in drug discovery. Science 2004, 303, 1813-1818.
    • (2004) Science , vol.303 , pp. 1813-1818
    • Jorgensen, W.L.1


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