메뉴 건너뛰기




Volumn 52, Issue 4, 2003, Pages 573-584

Flavors of protein disorder

Author keywords

Genomics; Secondary structure; Sequence composition; Signaling and regulatory proteins; Structure prediction; Unfolded proteins

Indexed keywords

AMINO ACID; PROTEIN; PROTEIN C; PROTEIN S; UNCLASSIFIED DRUG; VIRUS PROTEIN V;

EID: 0041418213     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10437     Document Type: Article
Times cited : (337)

References (50)
  • 1
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm
    • Wright PE, Dyson HJ. Intrinsically unstructured proteins: reassessing 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
  • 2
    • 0035022941 scopus 로고    scopus 로고
    • Intrinsically disordered protein
    • Dunker AK, et al. Intrinsically disordered protein. J Mol Graph Model 2001;19:26-59.
    • (2001) J Mol Graph Model , vol.19 , pp. 26-59
    • Dunker, A.K.1
  • 3
    • 0035131438 scopus 로고    scopus 로고
    • Roles of partly unfolded conformations in macromolecular self-assembly
    • Namba K. Roles of partly unfolded conformations in macromolecular self-assembly. Gen. Cells 2001;6:1-12.
    • (2001) Gen Cells , vol.6 , pp. 1-12
    • Namba, K.1
  • 4
    • 0035096292 scopus 로고    scopus 로고
    • Recognition between flexible protein molecules: Induced and assisted folding
    • Demchenke AP. Recognition between flexible protein molecules: induced and assisted folding. J Mol Recognit 2001;14:42-61.
    • (2001) J Mol Recognit , vol.14 , pp. 42-61
    • Demchenke, A.P.1
  • 5
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky VN. 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
  • 6
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson HJ, Wright PE. 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
  • 7
    • 0001443732 scopus 로고
    • Heterogeneity of the binding sites of bovine serum albumin
    • Karush F. Heterogeneity of the binding sites of bovine serum albumin. J Am Chem Soc 1950;72:2705-2713.
    • (1950) J Am Chem Soc , vol.72 , pp. 2705-2713
    • Karush, F.1
  • 8
    • 0017811758 scopus 로고
    • Energy states of proteins, enzymes and membranes
    • Williams RJ. Energy states of proteins, enzymes and membranes. Proc R Soc Lond B Biol Sci 1978;200:353-389.
    • (1978) Proc R Soc Lond B Biol Sci , vol.200 , pp. 353-389
    • Williams, R.J.1
  • 9
    • 0018107732 scopus 로고
    • The conformational mobility of proteins and its functional significance
    • Williams RJ. The conformational mobility of proteins and its functional significance. Biochem Soc Trans 1978;6:1123-1126.
    • (1978) Biochem Soc Trans , vol.6 , pp. 1123-1126
    • Williams, R.J.1
  • 10
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb PH, Zhen Poon WAW, Conway KA, Lansbury PT Jr. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 1996;35:13709-13715.
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen Poon, W.A.W.2    Conway, K.A.3    Lansbury P.T., Jr.4
  • 11
    • 0036402827 scopus 로고    scopus 로고
    • Identification and functions of usefully disordered proteins
    • Dunker AK, Brown CJ, 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
  • 13
    • 0028222021 scopus 로고
    • The molten globule is a third thermodynamical state of protein molecules
    • Ptitsyn OB, Uversky VN. The molten globule is a third thermodynamical state of protein molecules. FEBS Lett 1994;341:15-18.
    • (1994) FEBS Lett , vol.341 , pp. 15-18
    • Ptitsyn, O.B.1    Uversky, V.N.2
  • 14
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity - Linking function and disorder
    • Dunker AK, 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
  • 16
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins
    • Chou PY, Fasman GD. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry 1974;13:211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 17
    • 0018093765 scopus 로고
    • Conformational preferences of amino acids in globular proteins
    • Levitt M. Conformational preferences of amino acids in globular proteins. Biochemistry 1978;17:4277-4285.
    • (1978) Biochemistry , vol.17 , pp. 4277-4285
    • Levitt, M.1
  • 18
    • 0022631926 scopus 로고
    • The folding type of a protein is relevant to the amino acid composition
    • Nakashima H, Nishikawa K, Ooi T. The folding type of a protein is relevant to the amino acid composition. J Biochem (Tokyo) 1986;99:153-162.
    • (1986) J Biochem (Tokyo) , vol.99 , pp. 153-162
    • Nakashima, H.1    Nishikawa, K.2    Ooi, T.3
  • 19
    • 0030955263 scopus 로고    scopus 로고
    • Understanding the recognition of protein structural classes by amino acid composition
    • Bahar I, Atilgan AR, Jernigan RL, Erman B. Understanding the recognition of protein structural classes by amino acid composition. Proteins 1997;29:172-185.
    • (1997) Proteins , vol.29 , pp. 172-185
    • Bahar, I.1    Atilgan, A.R.2    Jernigan, R.L.3    Erman, B.4
  • 20
    • 0036300690 scopus 로고    scopus 로고
    • Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques
    • Choy WY, Mulder FA, Crowhurst KA. Muhandiram DR, Millett IS, Doniach S, Forman-Kay JD, Kay LE. Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques. J Mol Biol 2002;316:101-12.
    • (2002) J Mol Biol , vol.316 , pp. 101-112
    • Choy, W.Y.1    Mulder, F.A.2    Crowhurst, K.A.3    Muhandiram, D.R.4    Millett, I.S.5    Doniach, S.6    Forman-Kay, J.D.7    Kay, L.E.8
  • 22
    • 0000332920 scopus 로고    scopus 로고
    • Sequence data analysis for long disordered regions prediction in the calcineurin family
    • Romero P, Obradovic Z, Dunker AK. Sequence data analysis for long disordered regions prediction in the calcineurin family. Genome Inform. Ser Workshop Genome Inform 1997;8:110-124.
    • (1997) Genome Inform Ser Workshop Genome Inform , vol.8 , pp. 110-124
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 23
    • 0034458146 scopus 로고    scopus 로고
    • Intelligent data analysis for protein disorder prediction
    • Romero P, Obradovic Z, Dunker AK. Intelligent data analysis for protein disorder prediction. Artific Intel Rev 2000;14:447-484.
    • (2000) Artific Intel Rev , vol.14 , pp. 447-484
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 25
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm U, Sander C. Enlarged representative set of protein structures. Protein Sci 1994;3:522-524.
    • (1994) Protein Sci , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 27
    • 0032893084 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999
    • Bairoch A, Apweiler R. The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999. Nucleic Acids Res 1999;27:49-54.
    • (1999) Nucleic Acids Res , vol.27 , pp. 49-54
    • Bairoch, A.1    Apweiler, R.2
  • 30
    • 84856043672 scopus 로고
    • A mathematical theory of communication
    • Shannon CE. A mathematical theory of communication. Bell Syst Tech J 1948;379-423, 623-656.
    • (1948) Bell Syst Tech J , pp. 379-423
    • Shannon, C.E.1
  • 31
    • 0032726594 scopus 로고    scopus 로고
    • Folding minimal sequences: The lower bound for sequence complexity of globular proteins
    • Romero P, Obradovic Z, Dunker AK. Folding minimal sequences: the lower bound for sequence complexity of globular proteins. FEBS Lett 1999;462:363-367.
    • (1999) FEBS Lett , vol.462 , pp. 363-367
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 33
    • 0024861871 scopus 로고
    • Approximation by superpositions of a sigmoidal function
    • Cybenko G. Approximation by superpositions of a sigmoidal function. MCSS, Math. Control Signals Syst 1989;2:303-314.
    • (1989) MCSS, Math Control Signals Syst , vol.2 , pp. 303-314
    • Cybenko, G.1
  • 34
    • 0035340577 scopus 로고    scopus 로고
    • Price-load relationships in California's electricity market
    • Vucetic S, Obradovic Z. Tomsovic K. Price-load relationships in California's electricity market. IEEE Trans Power Syst 2001;16:280-286.
    • (2001) IEEE Trans Power Syst , vol.16 , pp. 280-286
    • Vucetic, S.1    Obradovic, Z.2    Tomsovic, K.3
  • 36
    • 84943274699 scopus 로고
    • A direct adaptive method for faster backpropogation learning: The RPROP algorithm
    • Riedmiller M, Braun H. A direct adaptive method for faster backpropogation learning: the RPROP algorithm. Proc IEEE Int Confon Neural Networks 1993;1:586-591.
    • (1993) Proc IEEE Int Confon Neural Networks , vol.1 , pp. 586-591
    • Riedmiller, M.1    Braun, H.2
  • 38
    • 0028361031 scopus 로고
    • Accuracy of protein flexibility predictions
    • Vihinen M, Torkkila E, Riikonen P. Accuracy of protein flexibility predictions. Proteins 1994;19:141-149.
    • (1994) Proteins , vol.19 , pp. 141-149
    • Vihinen, M.1    Torkkila, E.2    Riikonen, P.3
  • 39
    • 0032486475 scopus 로고    scopus 로고
    • Domain mapping of human apurinic/apyrimidinic endonuclease. Structural and functional evidence for a disordered amino terminus and a tight globular carboxyl domain
    • Strauss PR, Holt CM. Domain mapping of human apurinic/ apyrimidinic endonuclease. Structural and functional evidence for a disordered amino terminus and a tight globular carboxyl domain. J Biol Chem 1998;273:14435-14441.
    • (1998) J Biol Chem , vol.273 , pp. 14435-14441
    • Strauss, P.R.1    Holt, C.M.2
  • 40
    • 0032544230 scopus 로고    scopus 로고
    • Structure of type IIbeta phosphatidylinositol phosphate kinase: A protein kinase fold flattened for interfacial phosphorylation
    • Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH. Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation. Cell 1998;94:829-839.
    • (1998) Cell , vol.94 , pp. 829-839
    • Rao, V.D.1    Misra, S.2    Boronenkov, I.V.3    Anderson, R.A.4    Hurley, J.H.5
  • 44
    • 0002629270 scopus 로고
    • Maximum likelihood from data via the EM algorithm
    • Dempster AP, Laird NM, Rubin DB. Maximum likelihood from data via the EM algorithm. JR Stat Soc 1977;39:1-38.
    • (1977) JR Stat Soc , vol.39 , pp. 1-38
    • Dempster, A.P.1    Laird, N.M.2    Rubin, D.B.3
  • 46
    • 0034808117 scopus 로고    scopus 로고
    • Comparing function and structure between entire proteomes
    • Liu J, Rost B. Comparing function and structure between entire proteomes. Protein Sci 2001;10:1970-1979.
    • (2001) Protein Sci , vol.10 , pp. 1970-1979
    • Liu, J.1    Rost, B.2
  • 49
    • 0031824449 scopus 로고    scopus 로고
    • Structural genomics: Bioinformatics in the driver's seat
    • Gaasterland T. Structural genomics: bioinformatics in the driver's seat. Nat Biotechnol 1998;16:625-627.
    • (1998) Nat Biotechnol , vol.16 , pp. 625-627
    • Gaasterland, T.1
  • 50
    • 0032521199 scopus 로고    scopus 로고
    • The argonne structural genomics workshop: Lamaze class for the birth of a new science
    • Shapiro L, Lima CD. The argonne structural genomics workshop: Lamaze class for the birth of a new science. Structure 1998;6:265-267.
    • (1998) Structure , vol.6 , pp. 265-267
    • Shapiro, L.1    Lima, C.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.