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Volumn 102, Issue 2-3, 2010, Pages 73-84

The protein kingdom extended: Ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation

Author keywords

Amorphous aggregates; Amyloid fibrils; Functional amyloid; Globular proteins; Inter and intramolecular contacts; Natively disordered proteins; Protein folding; Protein protein and DNA protein complexes

Indexed keywords

AMYLOID; PROTEIN;

EID: 77954217602     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbiomolbio.2010.01.003     Document Type: Review
Times cited : (177)

References (138)
  • 1
    • 0016669719 scopus 로고
    • Genetical aspects of [URE3], a non-mitochondrial, cytoplasmically inherited mutation in yeast
    • Aigle M., Lacroute F. Genetical aspects of [URE3], a non-mitochondrial, cytoplasmically inherited mutation in yeast. Mol. Gen. Genet. 1975, 136:327-335.
    • (1975) Mol. Gen. Genet. , vol.136 , pp. 327-335
    • Aigle, M.1    Lacroute, F.2
  • 2
    • 58749116660 scopus 로고    scopus 로고
    • Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin
    • Altschuler G.M., Willison K.R. Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin. J. R. Soc. Interface 2008, 5:1391-1408.
    • (2008) J. R. Soc. Interface , vol.5 , pp. 1391-1408
    • Altschuler, G.M.1    Willison, K.R.2
  • 3
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science 1973, 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 4
    • 0035717504 scopus 로고    scopus 로고
    • Catalysis of disulfide bond formation and isomerization in Escherichia coli
    • Bader M.W., Bardwell J.C. Catalysis of disulfide bond formation and isomerization in Escherichia coli. Adv. Protein Chem. 2001, 59:283-301.
    • (2001) Adv. Protein Chem. , vol.59 , pp. 283-301
    • Bader, M.W.1    Bardwell, J.C.2
  • 6
    • 0034254189 scopus 로고    scopus 로고
    • Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell
    • van den Berg B., Wain R., Dobson C.M., Ellis R.J. Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell. EMBO J. 2000, 19:3870-3875.
    • (2000) EMBO J. , vol.19 , pp. 3870-3875
    • van den Berg, B.1    Wain, R.2    Dobson, C.M.3    Ellis, R.J.4
  • 11
    • 4544363334 scopus 로고    scopus 로고
    • Effect of molecular crowding on self-association of phosphorylase kinase and its interaction with phosphorylase b and glycogen
    • Chebotareva N.A., Andreeva I.E., Makeeva V.F., Livanova N.B., Kurganov B.I. Effect of molecular crowding on self-association of phosphorylase kinase and its interaction with phosphorylase b and glycogen. J. Mol. Recognit. 2004, 17:426-432.
    • (2004) J. Mol. Recognit. , vol.17 , pp. 426-432
    • Chebotareva, N.A.1    Andreeva, I.E.2    Makeeva, V.F.3    Livanova, N.B.4    Kurganov, B.I.5
  • 12
    • 33748280715 scopus 로고    scopus 로고
    • Abundance of intrinsic disorder in protein associated with cardiovascular disease
    • Cheng Y., LeGall T., Oldfield C.J., Dunker A.K., Uversky V.N. Abundance of intrinsic disorder in protein associated with cardiovascular disease. Biochemistry 2006, 45:10448-10460.
    • (2006) Biochemistry , vol.45 , pp. 10448-10460
    • Cheng, Y.1    LeGall, T.2    Oldfield, C.J.3    Dunker, A.K.4    Uversky, V.N.5
  • 13
    • 36749037699 scopus 로고    scopus 로고
    • Mining alpha-helix-forming molecular recognition features with cross species sequence alignments
    • Cheng Y., Oldfield C.J., Meng J., Romero P., Uversky V.N., Dunker A.K. Mining alpha-helix-forming molecular recognition features with cross species sequence alignments. Biochemistry 2007, 46:13468-13477.
    • (2007) Biochemistry , vol.46 , pp. 13468-13477
    • Cheng, Y.1    Oldfield, C.J.2    Meng, J.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 14
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • Chien P., Weissman J.S., DePace A.H. Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem. 2004, 73:617-656.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    DePace, A.H.3
  • 15
    • 0035826236 scopus 로고    scopus 로고
    • Conformational diversity in a yeast prion dictates its seeding specificity
    • Chien P., Weissman J.S. Conformational diversity in a yeast prion dictates its seeding specificity. Nature 2001, 410:223-227.
    • (2001) Nature , vol.410 , pp. 223-227
    • Chien, P.1    Weissman, J.S.2
  • 16
    • 77954219081 scopus 로고    scopus 로고
    • Relative importance of hydrophobicity, net charge and secondary structure propensities in protein aggregation. In protein misfolding, aggregation and conformational diseases
    • Springer Science+Business Media, LLC, New York, V.N. Uversky, A.L. Fink (Eds.)
    • Chiti F. Relative importance of hydrophobicity, net charge and secondary structure propensities in protein aggregation. In protein misfolding, aggregation and conformational diseases. Protein Aggregation and Conformational Diseases 2006, vol. I:43-59. Springer Science+Business Media, LLC, New York. V.N. Uversky, A.L. Fink (Eds.).
    • (2006) Protein Aggregation and Conformational Diseases , vol.1 , pp. 43-59
    • Chiti, F.1
  • 17
    • 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
  • 19
    • 38349190735 scopus 로고    scopus 로고
    • Versatile functions of p53 protein in multicellular organisms
    • Chumakov P.M. Versatile functions of p53 protein in multicellular organisms. Biochemistry (Mosc) 2007, 72:1399-1421.
    • (2007) Biochemistry (Mosc) , vol.72 , pp. 1399-1421
    • Chumakov, P.M.1
  • 20
    • 0031711595 scopus 로고    scopus 로고
    • Pathologic conformations of prion proteins
    • Cohen F.E., Prusiner S.B. Pathologic conformations of prion proteins. Annu. Rev. Biochem. 1998, 67:793-819.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 793-819
    • Cohen, F.E.1    Prusiner, S.B.2
  • 21
    • 0025959235 scopus 로고
    • The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases
    • Coschigano P.W., Magasanik B. The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases. Mol. Cell Biol. 1991, 11:822-832.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 822-832
    • Coschigano, P.W.1    Magasanik, B.2
  • 22
    • 0023954446 scopus 로고
    • Regulation of nitrogen assimilation in Saccharomyces cerevisiae: roles of the URE2 and GLN3 genes
    • Courchesne W.E., Magasanik B. Regulation of nitrogen assimilation in Saccharomyces cerevisiae: roles of the URE2 and GLN3 genes. J. Bacteriol. 1988, 170:708-713.
    • (1988) J. Bacteriol. , vol.170 , pp. 708-713
    • Courchesne, W.E.1    Magasanik, B.2
  • 23
    • 0030885650 scopus 로고    scopus 로고
    • The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog
    • Coustou V., Deleu C., Saupe S., Begueret J. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:9773-9778.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 9773-9778
    • Coustou, V.1    Deleu, C.2    Saupe, S.3    Begueret, J.4
  • 24
    • 0027234098 scopus 로고
    • A single amino acid difference is sufficient to elicit vegetative incompatibility in the fungus Podospora anserina
    • Deleu C., Clave C., Begueret J. A single amino acid difference is sufficient to elicit vegetative incompatibility in the fungus Podospora anserina. Genetics 1993, 135:45-52.
    • (1993) Genetics , vol.135 , pp. 45-52
    • Deleu, C.1    Clave, C.2    Begueret, J.3
  • 25
    • 0032568793 scopus 로고    scopus 로고
    • A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion
    • DePace A.H., Santoso A., Hillner P., Weissman J.S. A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 1998, 93:1241-1252.
    • (1998) Cell , vol.93 , pp. 1241-1252
    • DePace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 26
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 1999, 24:329-332.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 31
    • 0036402827 scopus 로고    scopus 로고
    • Identification and functions of usefully disordered proteins
    • Dunker A.K., Brown C.J., Obradovic Z. Identification and functions of usefully disordered proteins. Adv. Protein Chem. 2002, 62:25-49.
    • (2002) Adv. Protein Chem. , vol.62 , pp. 25-49
    • Dunker, A.K.1    Brown, C.J.2    Obradovic, Z.3
  • 32
    • 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
  • 35
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity-linking function and disorder
    • Dunker A.K., Obradovic Z. The protein trinity-linking function and disorder. Nat. Biotechnol. 2001, 19:805-806.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 805-806
    • Dunker, A.K.1    Obradovic, Z.2
  • 36
    • 40949105259 scopus 로고    scopus 로고
    • Signal transduction via unstructured protein conduits
    • Dunker A.K., Uversky V.N. Signal transduction via unstructured protein conduits. Nat. Chem. Biol. 2008, 4:229-230.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 229-230
    • Dunker, A.K.1    Uversky, V.N.2
  • 37
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson H.J., Wright P.E. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 2002, 12:54-60.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 38
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., Wright P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 2005, 6:197-208.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 39
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: obvious but underappreciated
    • Ellis R.J. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 2001, 26:597-604.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 40
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fandrich M., Fletcher M.A., Dobson C.M. Amyloid fibrils from muscle myoglobin. Nature 2001, 410:165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 41
    • 0033953974 scopus 로고    scopus 로고
    • Protein folding in vivo: the importance of molecular chaperones
    • Feldman D.E., Frydman J. Protein folding in vivo: the importance of molecular chaperones. Curr. Opin. Struct. Biol. 2000, 10:26-33.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 26-33
    • Feldman, D.E.1    Frydman, J.2
  • 42
    • 33748258328 scopus 로고    scopus 로고
    • A practical overview of protein disorder prediction methods
    • Ferron F., Longhi S., Canard B., Karlin D. A practical overview of protein disorder prediction methods. Proteins 2006, 65:1-14.
    • (2006) Proteins , vol.65 , pp. 1-14
    • Ferron, F.1    Longhi, S.2    Canard, B.3    Karlin, D.4
  • 43
    • 0032924105 scopus 로고    scopus 로고
    • Chaperone-mediated protein folding
    • Fink A.L. Chaperone-mediated protein folding. Physiol. Rev. 1999, 79:425-449.
    • (1999) Physiol. Rev. , vol.79 , pp. 425-449
    • Fink, A.L.1
  • 45
    • 84892166712 scopus 로고
    • Einfluss der Configuration auf die Wirkung der Enzyme
    • Fischer E. Einfluss der Configuration auf die Wirkung der Enzyme. Ber. Dt. Chem. Ges. 1894, 27:2985-2993.
    • (1894) Ber. Dt. Chem. Ges. , vol.27 , pp. 2985-2993
    • Fischer, E.1
  • 48
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: a formulation challenge
    • Frokjaer S., Otzen D.E. Protein drug stability: a formulation challenge. Nat. Rev. Drug Discov. 2005, 4:298-306.
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 49
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • Fuxreiter M., Simon I., Friedrich P., Tompa P. Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J. Mol. Biol. 2004, 338:1015-1026.
    • (2004) J. Mol. Biol. , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 51
    • 0027938897 scopus 로고
    • Protein chaperones and protein folding
    • Gilbert H.F. Protein chaperones and protein folding. Curr. Opin. Biotechnol. 1994, 5:534-539.
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 534-539
    • Gilbert, H.F.1
  • 55
    • 69949105161 scopus 로고    scopus 로고
    • The rules of disorder or why disorder rules
    • Gsponer J., Babu M.M. The rules of disorder or why disorder rules. Prog. Biophys. Mol. Biol. 2009, 99:94-103.
    • (2009) Prog. Biophys. Mol. Biol. , vol.99 , pp. 94-103
    • Gsponer, J.1    Babu, M.M.2
  • 56
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: from transcript synthesis to protein degradation
    • Gsponer J., Futschik M.E., Teichmann S.A., Babu M.M. Tight regulation of unstructured proteins: from transcript synthesis to protein degradation. Science 2008, 322:1365-1368.
    • (2008) Science , vol.322 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 58
    • 0029740071 scopus 로고    scopus 로고
    • Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein
    • Hamada D., Segawa S., Goto Y. Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein. Nat. Struct. Biol. 1996, 3:868-873.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 868-873
    • Hamada, D.1    Segawa, S.2    Goto, Y.3
  • 61
    • 70350012289 scopus 로고    scopus 로고
    • Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: a critical assessment of the " fly-casting" mechanism
    • Huang Y., Liu Z. Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: a critical assessment of the " fly-casting" mechanism. J. Mol. Biol. 2009, 393:1143-1159.
    • (2009) J. Mol. Biol. , vol.393 , pp. 1143-1159
    • Huang, Y.1    Liu, Z.2
  • 64
    • 28244437028 scopus 로고    scopus 로고
    • The Yin and Yang of protein folding
    • Jahn T.R., Radford S.E. The Yin and Yang of protein folding. FEBS J. 2005, 272:5962-5970.
    • (2005) FEBS J. , vol.272 , pp. 5962-5970
    • Jahn, T.R.1    Radford, S.E.2
  • 65
    • 34047174813 scopus 로고    scopus 로고
    • Structural biology of the tumor suppressor p53 and cancer-associated mutants
    • Joerger A.C., Fersht A.R. Structural biology of the tumor suppressor p53 and cancer-associated mutants. Adv. Cancer Res. 2007, 97:1-23.
    • (2007) Adv. Cancer Res. , vol.97 , pp. 1-23
    • Joerger, A.C.1    Fersht, A.R.2
  • 66
    • 34047224955 scopus 로고    scopus 로고
    • Structure-function-rescue: the diverse nature of common p53 cancer mutants
    • Joerger A.C., Fersht A.R. Structure-function-rescue: the diverse nature of common p53 cancer mutants. Oncogene 2007, 26:2226-2242.
    • (2007) Oncogene , vol.26 , pp. 2226-2242
    • Joerger, A.C.1    Fersht, A.R.2
  • 67
    • 47649096991 scopus 로고    scopus 로고
    • Structural biology of the tumor suppressor p53
    • Joerger A.C., Fersht A.R. Structural biology of the tumor suppressor p53. Annu. Rev. Biochem. 2008, 77:557-582.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 557-582
    • Joerger, A.C.1    Fersht, A.R.2
  • 68
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly J.W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 1998, 8:101-106.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 69
    • 0030917006 scopus 로고    scopus 로고
    • Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
    • King C.Y., Tittmann P., Gross H., Gebert R., Aebi M., Wuthrich K. Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:6618-6622.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 6618-6622
    • King, C.Y.1    Tittmann, P.2    Gross, H.3    Gebert, R.4    Aebi, M.5    Wuthrich, K.6
  • 70
    • 43249121694 scopus 로고    scopus 로고
    • A regulatory role of the Rnq1 nonprion domain for prion propagation and polyglutamine aggregates
    • Kurahashi H., Ishiwata M., Shibata S., Nakamura Y. A regulatory role of the Rnq1 nonprion domain for prion propagation and polyglutamine aggregates. Mol. Cell Biol. 2008, 28:3313-3323.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 3313-3323
    • Kurahashi, H.1    Ishiwata, M.2    Shibata, S.3    Nakamura, Y.4
  • 72
    • 33745497323 scopus 로고    scopus 로고
    • Structural dynamics, stability and folding of proteins
    • Kuznetsova I.M., Forge V., Turoverov K.K. Structural dynamics, stability and folding of proteins. Tsitologiia 2005, 47:943-952.
    • (2005) Tsitologiia , vol.47 , pp. 943-952
    • Kuznetsova, I.M.1    Forge, V.2    Turoverov, K.K.3
  • 74
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal C. Are there pathways for protein folding?. J. Chim. Phys. 1968, 65:44-45.
    • (1968) J. Chim. Phys. , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 80
    • 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(Suppl. 1):S12.
    • (2009) BMC Genomics , vol.10 , Issue.1 SUPPL.
    • Midic, U.1    Oldfield, C.J.2    Dunker, A.K.3    Obradovic, Z.4    Uversky, V.N.5
  • 81
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • Minton A.P. Implications of macromolecular crowding for protein assembly. Curr. Opin. Struct. Biol. 2000, 10:34-39.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 82
    • 77954215778 scopus 로고    scopus 로고
    • MoRFs: a dataset of molecular recognition features
    • Indiana University, Indianapolis
    • Mohan A. MoRFs: a dataset of molecular recognition features. The School of Informatics 2006, 59. Indiana University, Indianapolis.
    • (2006) The School of Informatics , pp. 59
    • Mohan, A.1
  • 83
    • 33846566217 scopus 로고    scopus 로고
    • Nanoscale mechanical characterisation of amyloid fibrils discovered in a natural adhesive
    • Mostaert A.S., Higgins M.J., Fukuma T., Rindi F., Jarvis S.P. Nanoscale mechanical characterisation of amyloid fibrils discovered in a natural adhesive. J. Biol. Phys. 2006, 32:393-401.
    • (2006) J. Biol. Phys. , vol.32 , pp. 393-401
    • Mostaert, A.S.1    Higgins, M.J.2    Fukuma, T.3    Rindi, F.4    Jarvis, S.P.5
  • 84
    • 4444311182 scopus 로고    scopus 로고
    • Conformational prerequisites for formation of amyloid fibrils from histones
    • Munishkina L.A., Fink A.L., Uversky V.N. Conformational prerequisites for formation of amyloid fibrils from histones. J. Mol. Biol. 2004, 342:1305-1324.
    • (2004) J. Mol. Biol. , vol.342 , pp. 1305-1324
    • Munishkina, L.A.1    Fink, A.L.2    Uversky, V.N.3
  • 85
    • 28844496012 scopus 로고    scopus 로고
    • Actin interacts with CCT via discrete binding sites: a binding transition-release model for CCT-mediated actin folding
    • Neirynck K., Waterschoot D., Vandekerckhove J., Ampe C., Rommelaere H. Actin interacts with CCT via discrete binding sites: a binding transition-release model for CCT-mediated actin folding. J. Mol. Biol. 2006, 355:124-138.
    • (2006) J. Mol. Biol. , vol.355 , pp. 124-138
    • Neirynck, K.1    Waterschoot, D.2    Vandekerckhove, J.3    Ampe, C.4    Rommelaere, H.5
  • 87
    • 0021114569 scopus 로고
    • 'Molten-globule state': a compact form of globular proteins with mobile side-chains
    • Ohgushi M., Wada A. 'Molten-globule state': a compact form of globular proteins with mobile side-chains. FEBS Lett. 1983, 164:21-24.
    • (1983) FEBS Lett. , vol.164 , pp. 21-24
    • Ohgushi, M.1    Wada, A.2
  • 88
  • 89
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • Patino M.M., Liu J.J., Glover J.R., Lindquist S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 1996, 273:622-626.
    • (1996) Science , vol.273 , pp. 622-626
    • Patino, M.M.1    Liu, J.J.2    Glover, J.R.3    Lindquist, S.4
  • 91
    • 33947597626 scopus 로고    scopus 로고
    • Different disturbances - one pathway of protein unfolding. Actin folding-unfolding and misfolding
    • Povarova O.I., Kuznetsova I.M., Turoverov K.K. Different disturbances - one pathway of protein unfolding. Actin folding-unfolding and misfolding. Cell Biol. Int. 2007, 31:405-412.
    • (2007) Cell Biol. Int. , vol.31 , pp. 405-412
    • Povarova, O.I.1    Kuznetsova, I.M.2    Turoverov, K.K.3
  • 92
    • 0015920746 scopus 로고
    • Stages in the mechanism of self-organization of protein molecules
    • Ptitsyn O.B. Stages in the mechanism of self-organization of protein molecules. Dokl Akad Nauk SSSR 1973, 210:1213-1215.
    • (1973) Dokl Akad Nauk SSSR , vol.210 , pp. 1213-1215
    • Ptitsyn, O.B.1
  • 93
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 1995, 47:83-229.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 94
    • 0034383950 scopus 로고    scopus 로고
    • Protein folding: progress made and promises ahead
    • Radford S.E. Protein folding: progress made and promises ahead. Trends Biochem. Sci. 2000, 25:611-618.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 611-618
    • Radford, S.E.1
  • 97
    • 0035962921 scopus 로고    scopus 로고
    • HMGI/Y proteins: flexible regulators of transcription and chromatin structure
    • Reeves R., Beckerbauer L. HMGI/Y proteins: flexible regulators of transcription and chromatin structure. Biochim. Biophys. Acta 2001, 1519:13-29.
    • (2001) Biochim. Biophys. Acta , vol.1519 , pp. 13-29
    • Reeves, R.1    Beckerbauer, L.2
  • 98
    • 0030691703 scopus 로고    scopus 로고
    • Identifying disordered regions in proteins from amino acid sequences. IEEE Int. Conf. Neural Netw.
    • Romero, P., Obradovic, Z., Kissinger, C.R., Villafranca, J.E., Dunker, A.K., 1997. Identifying disordered regions in proteins from amino acid sequences. IEEE Int. Conf. Neural Netw., vol. 1, pp. 90-95.
    • (1997) , vol.1 , pp. 90-95
    • Romero, P.1    Obradovic, Z.2    Kissinger, C.R.3    Villafranca, J.E.4    Dunker, A.K.5
  • 100
    • 0035715945 scopus 로고    scopus 로고
    • Prolyl isomerases
    • Schmid F.X. Prolyl isomerases. Adv. Protein Chem. 2001, 59:243-282.
    • (2001) Adv. Protein Chem. , vol.59 , pp. 243-282
    • Schmid, F.X.1
  • 101
    • 0033989157 scopus 로고    scopus 로고
    • Illuminating folding intermediates
    • Schultz C.P. Illuminating folding intermediates. Nat. Struct. Biol. 2000, 7:7-10.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 7-10
    • Schultz, C.P.1
  • 102
    • 0033280801 scopus 로고    scopus 로고
    • [PSI+]: an epigenetic modulator of translation termination efficiency
    • Serio T.R., Lindquist S.L. [PSI+]: an epigenetic modulator of translation termination efficiency. Annu. Rev. Cell Dev. Biol. 1999, 15:661-703.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 661-703
    • Serio, T.R.1    Lindquist, S.L.2
  • 104
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: the fly-casting mechanism
    • Shoemaker B.A., Portman J.J., Wolynes P.G. Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:8868-8873.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 105
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: an epigenetic modifier of protein function in yeast
    • Sondheimer N., Lindquist S. Rnq1: an epigenetic modifier of protein function in yeast. Mol. Cell 2000, 5:163-172.
    • (2000) Mol. Cell , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 107
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. Protein denaturation. Adv. Protein Chem. 1968, 23:121-282.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 108
    • 0028200770 scopus 로고
    • The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae
    • Ter-Avanesyan M.D., Dagkesamanskaya A.R., Kushnirov V.V., Smirnov V.N. The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae. Genetics 1994, 137:671-676.
    • (1994) Genetics , vol.137 , pp. 671-676
    • Ter-Avanesyan, M.D.1    Dagkesamanskaya, A.R.2    Kushnirov, V.V.3    Smirnov, V.N.4
  • 109
    • 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
  • 110
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett. 2005, 579:3346-3354.
    • (2005) FEBS Lett. , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 111
    • 4544235083 scopus 로고    scopus 로고
    • Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits
    • True H.L., Berlin I., Lindquist S.L. Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature 2004, 431:184-187.
    • (2004) Nature , vol.431 , pp. 184-187
    • True, H.L.1    Berlin, I.2    Lindquist, S.L.3
  • 112
    • 0034727077 scopus 로고    scopus 로고
    • A yeast prion provides a mechanism for genetic variation and phenotypic diversity
    • True H.L., Lindquist S.L. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 2000, 407:477-483.
    • (2000) Nature , vol.407 , pp. 477-483
    • True, H.L.1    Lindquist, S.L.2
  • 113
    • 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
  • 114
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky V.N. What does it mean to be natively unfolded?. Eur. J. Biochem. 2002, 269:2-12.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 115
    • 0141861067 scopus 로고    scopus 로고
    • Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go?
    • Uversky V.N. Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go?. Cell Mol. Life Sci. 2003, 60:1852-1871.
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 1852-1871
    • Uversky, V.N.1
  • 116
    • 55949092886 scopus 로고    scopus 로고
    • Alpha-synuclein misfolding and neurodegenerative diseases
    • Uversky V.N. Alpha-synuclein misfolding and neurodegenerative diseases. Curr. Protein Pept. Sci. 2008, 9:507-540.
    • (2008) Curr. Protein Pept. Sci. , vol.9 , pp. 507-540
    • Uversky, V.N.1
  • 117
    • 69149103558 scopus 로고    scopus 로고
    • Intrinsic disorder in proteins associated with neurodegenerative diseases
    • Uversky V.N. Intrinsic disorder in proteins associated with neurodegenerative diseases. Frontiers in Bioscience 2009, 14:5188-5238.
    • (2009) Frontiers in Bioscience , vol.14 , pp. 5188-5238
    • Uversky, V.N.1
  • 118
    • 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
  • 119
    • 0037181497 scopus 로고    scopus 로고
    • Accelerated alpha-synuclein fibrillation in crowded milieu
    • Uversky V.N., Cooper E.M., Bower K.S., Li J., Fink A.L. Accelerated alpha-synuclein fibrillation in crowded milieu. FEBS Lett. 2002, 515:99-103.
    • (2002) FEBS Lett. , vol.515 , pp. 99-103
    • Uversky, V.N.1    Cooper, E.M.2    Bower, K.S.3    Li, J.4    Fink, A.L.5
  • 120
    • 57149085681 scopus 로고    scopus 로고
    • Biochemistry. Controlled chaos
    • Uversky V.N., Dunker A.K. Biochemistry. Controlled chaos. Science 2008, 322:1340-1341.
    • (2008) Science , vol.322 , pp. 1340-1341
    • Uversky, V.N.1    Dunker, A.K.2
  • 121
    • 36749104448 scopus 로고    scopus 로고
    • Structural and conformational prerequisites of amyloidogenesis
    • Springer Science+Business Media, LLC, New York, V.N. Uversky, A.L. Fink (Eds.) Protein Misfolding, Aggregation and Conformational Diseases
    • Uversky V.N., Fernandez A., Fink A.L. Structural and conformational prerequisites of amyloidogenesis. Protein Aggregation and Conformational Diseases 2006, vol. I:1-20. Springer Science+Business Media, LLC, New York. V.N. Uversky, A.L. Fink (Eds.).
    • (2006) Protein Aggregation and Conformational Diseases , vol.1 , pp. 1-20
    • Uversky, V.N.1    Fernandez, A.2    Fink, A.L.3
  • 122
    • 0034669882 scopus 로고    scopus 로고
    • Why are " natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky V.N., Gillespie J.R., Fink A.L. Why are " natively unfolded" 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
  • 123
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: 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
  • 124
    • 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
  • 128
    • 34249282661 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions
    • Vucetic S., Xie H., Iakoucheva L.M., Oldfield C.J., Dunker A.K., Obradovic Z., Uversky V.N. Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions. J. Proteome Res. 2007, 6:1899-1916.
    • (2007) J. Proteome Res. , vol.6 , pp. 1899-1916
    • Vucetic, S.1    Xie, H.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Obradovic, Z.6    Uversky, V.N.7
  • 129
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W. Protein aggregation and its inhibition in biopharmaceutics. Int. J. Pharm. 2005, 289:1-30.
    • (2005) Int. J. Pharm. , vol.289 , pp. 1-30
    • Wang, W.1
  • 130
    • 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, 337:635-645.
    • (2004) J. Mol. Biol. , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 131
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner R.B. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 1994, 264:566-569.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 132
    • 0001856130 scopus 로고    scopus 로고
    • The role of cytosolic chaperonin, CCT, in normal eukaryotic cell growth
    • Oxford University Press, Oxford, P. Lund (Ed.)
    • Willison K.R., Grantham J. The role of cytosolic chaperonin, CCT, in normal eukaryotic cell growth. Molecular Chaperones in the Cell: Frontiers in Molecular Biology 2001, 90-118. Oxford University Press, Oxford. P. Lund (Ed.).
    • (2001) Molecular Chaperones in the Cell: Frontiers in Molecular Biology , pp. 90-118
    • Willison, K.R.1    Grantham, J.2
  • 134
    • 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
  • 136
    • 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
  • 137
    • 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
  • 138
    • 0027318513 scopus 로고
    • Macromolecular crowding: biochemical, biophysical, and physiological consequences
    • Zimmerman S.B., Minton A.P. Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 1993, 22:27-65.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2


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