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Volumn 40, Issue 5, 2012, Pages 945-949

Intrinsically disordered proteins: Administration not executive

Author keywords

Flexibility; Globular protein; Intrinsically disordered protein (IDP); Protein evolution; Secondary structure

Indexed keywords

AMINO ACID; GLOBULAR PROTEIN; GLYCINE; INTRINSICALLY DISORDERED PROTEIN; ISOLEUCINE; LEUCINE; POLYPEPTIDE; PROLINE; PROTEIN; UNCLASSIFIED DRUG;

EID: 84866697561     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20120188     Document Type: Review
Times cited : (10)

References (35)
  • 1
    • 79959240249 scopus 로고    scopus 로고
    • Binary classification of protein molecules into intrinsically disordered and ordered segments
    • Fukuchi, S., Hosoda, K., Homma, K., Gojobori, T. and Nishikawa, K. (2011) Binary classification of protein molecules into intrinsically disordered and ordered segments. BMC Struct. Biol. 11, 29
    • (2011) BMC Struct. Biol. , vol.11 , pp. 29
    • Fukuchi, S.1    Hosoda, K.2    Homma, K.3    Gojobori, T.4    Nishikawa, K.5
  • 3
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa, P. (2005) The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett. 579, 3346-3354
    • (2005) FEBS Lett. , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 7
    • 84866714885 scopus 로고    scopus 로고
    • Structures and interactions in 'bottlebrush' neurofilaments: The role of charged disordered proteins in forming hydrogel networks
    • Beck, R., Deek, J. and Safinya, C.R. (2012) Structures and interactions in 'bottlebrush' neurofilaments: the role of charged disordered proteins in forming hydrogel networks. Biochem. Soc. Trans. 40, 1027-1031
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1027-1031
    • Beck, R.1    Deek, J.2    Safinya, C.R.3
  • 11
    • 84866643147 scopus 로고    scopus 로고
    • Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS
    • Sibille, N. and Bernadó, P. (2012) Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS. Biochem. Soc. Trans. 40, 955-962
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 955-962
    • Sibille, N.1    Bernadó, P.2
  • 12
    • 29844433240 scopus 로고    scopus 로고
    • Defining long-range order and disorder in native α-synuclein using residual dipolar couplings
    • Bernadó, P., Bertoncini, C.W., Griesinger, C., Zweckstetter, M. and Blackledge, M. (2005) Defining long-range order and disorder in native α-synuclein using residual dipolar couplings. J. Am. Chem. Soc. 127, 17968-17969
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17968-17969
    • Bernadó, P.1    Bertoncini, C.W.2    Griesinger, C.3    Zweckstetter, M.4    Blackledge, M.5
  • 13
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmerman, S.B. and Minton, A.P. (1993) Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 22, 27-65
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 14
    • 84866671599 scopus 로고    scopus 로고
    • Bacterial in-cell NMR of human α-synuclein: A disordered monomer by nature?
    • Binolfi, A., Theillet, F.-X. and Selenko, P. (2012) Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature? Biochem. Soc. Trans. 40, 950-954
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 950-954
    • Binolfi, A.1    Theillet, F.-X.2    Selenko, P.3
  • 15
    • 0042819915 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins evolve by repeat expansion
    • Tompa, P. (2003) Intrinsically unstructured proteins evolve by repeat expansion. BioEssays 25, 847-855
    • (2003) BioEssays , vol.25 , pp. 847-855
    • Tompa, P.1
  • 16
    • 37249067732 scopus 로고    scopus 로고
    • The origin of protein interactions and allostery in colocalization
    • Kuriyan, J. and Eisenberg, D. (2007) The origin of protein interactions and allostery in colocalization. Nature 450, 983-990
    • (2007) Nature , vol.450 , pp. 983-990
    • Kuriyan, J.1    Eisenberg, D.2
  • 17
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions
    • Tompa, P. and Fuxreiter, M. (2008) Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem. Sci. 33, 2-8
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 18
    • 20444414545 scopus 로고    scopus 로고
    • Linear motifs: Evolutionary interaction switches
    • Neduva, V. and Russell, R.B. (2005) Linear motifs: evolutionary interaction switches. FEBS Lett. 579, 3342-3345
    • (2005) FEBS Lett. , vol.579 , pp. 3342-3345
    • Neduva, V.1    Russell, R.B.2
  • 19
    • 33751248768 scopus 로고    scopus 로고
    • Quantitative relation between intermolecular and intramolecular binding of Pro-rich peptides to SH3 domains
    • Zhou, H.-X. (2006) Quantitative relation between intermolecular and intramolecular binding of Pro-rich peptides to SH3 domains. Biophys. J. 91, 3170-3181
    • (2006) Biophys. J. , vol.91 , pp. 3170-3181
    • Zhou, H.-X.1
  • 20
    • 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. and Babu, M.M. (2012) Tissue-specific splicing of disordered segments that embed binding motifs rewires protein interaction networks. Mol. Cell 46, 871-883
    • (2012) Mol. Cell , vol.46 , pp. 871-883
    • Buljan, M.1    Chalancon, G.2    Eustermann, S.3    Wagner, G.P.4    Fuxreiter, M.5    Bateman, A.6    Babu, M.M.7
  • 21
    • 29144480142 scopus 로고    scopus 로고
    • Intrinsically disordered loops inserted into the structural domains of human proteins
    • Fukuchi, S., Homma, K., Minezaki, Y. and Nishikawa, K. (2006) Intrinsically disordered loops inserted into the structural domains of human proteins. J. Mol. Biol. 355, 845-857
    • (2006) J. Mol. Biol. , vol.355 , pp. 845-857
    • Fukuchi, S.1    Homma, K.2    Minezaki, Y.3    Nishikawa, K.4
  • 22
    • 84866720054 scopus 로고    scopus 로고
    • Interplay between allostery and intrinsic disorder in an ensemble
    • Motlagh, H.N., Li, J., Thompson, E.B. and Hilser, V.J. (2012) Interplay between allostery and intrinsic disorder in an ensemble. Biochem. Soc. Trans. 40, 975-980
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 975-980
    • Motlagh, H.N.1    Li, J.2    Thompson, E.B.3    Hilser, V.J.4
  • 23
    • 84858234186 scopus 로고    scopus 로고
    • Agonism/antagonism switching in allosteric ensembles
    • Motlagh, H.N. and Hilser, V.J. (2012) Agonism/antagonism switching in allosteric ensembles. Proc. Natl. Acad. Sci. U.S.A. 109, 4134-4139
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 4134-4139
    • Motlagh, H.N.1    Hilser, V.J.2
  • 24
    • 84866673529 scopus 로고    scopus 로고
    • An intrinsically disordered protein, CP12: Jack of all trades and master of the Calvin cycle
    • Gontero, B. and Maberly, S.C. (2012) An intrinsically disordered protein, CP12: jack of all trades and master of the Calvin cycle. Biochem. Soc. Trans. 40, 995-999
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 995-999
    • Gontero, B.1    Maberly, S.C.2
  • 25
    • 84866681214 scopus 로고    scopus 로고
    • Native disorder mediates binding of dynein to NudE and dynactin
    • Barbar, E. (2012) Native disorder mediates binding of dynein to NudE and dynactin. Biochem. Soc. Trans. 40, 1009-1013
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1009-1013
    • Barbar, E.1
  • 26
    • 84866689134 scopus 로고    scopus 로고
    • Cell cycle regulation by the intrinsically disordered proteins p21 and p27
    • Yoon, M.-K., Mitrea, D.M., Ou, L. and Kriwacki, R.W. (2012) Cell cycle regulation by the intrinsically disordered proteins p21 and p27. Biochem. Soc. Trans. 40, 981-988
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 981-988
    • Yoon, M.-K.1    Mitrea, D.M.2    Ou, L.3    Kriwacki, R.W.4
  • 27
    • 80055012207 scopus 로고    scopus 로고
    • Expanding the proteome: Disordered and alternatively folded proteins
    • Dyson, H.J. (2011) Expanding the proteome: disordered and alternatively folded proteins. Q. Rev. Biophys. 44, 467-518
    • (2011) Q. Rev. Biophys. , vol.44 , pp. 467-518
    • Dyson, H.J.1
  • 28
    • 84866679293 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 1 by intrinsically disordered proteins
    • Choy, M.S., Page, R. and Peti, W. (2012) Regulation of protein phosphatase 1 by intrinsically disordered proteins. Biochem. Soc. Trans. 40, 969-974
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 969-974
    • Choy, M.S.1    Page, R.2    Peti, W.3
  • 29
    • 84866644698 scopus 로고    scopus 로고
    • Diverse functional manifestations of intrinsic disorder in molecular chaperones
    • Kovacs, D. and Tompa, P. (2012) Diverse functional manifestations of intrinsic disorder in molecular chaperones. Biochem. Soc. Trans. 40, 963-968
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 963-968
    • Kovacs, D.1    Tompa, P.2
  • 30
    • 84866658433 scopus 로고    scopus 로고
    • LEA proteins: IDPs with versatile functions in cellular dehydration tolerance
    • Hincha, D.K. and Thalhammer, A. (2012) LEA proteins: IDPs with versatile functions in cellular dehydration tolerance. Biochem. Soc. Trans. 40, 1000-1003
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1000-1003
    • Hincha, D.K.1    Thalhammer, A.2
  • 31
    • 77951631601 scopus 로고    scopus 로고
    • Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase
    • Mittag, T., Marsh, J., Grishaev, A., Orlicky, S., Lin, H., Sicheri, F., Tyers, M. and Forman-Kay, J.D. (2010) Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. Structure 18, 494-506
    • (2010) Structure , vol.18 , pp. 494-506
    • Mittag, T.1    Marsh, J.2    Grishaev, A.3    Orlicky, S.4    Lin, H.5    Sicheri, F.6    Tyers, M.7    Forman-Kay, J.D.8
  • 33
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker, B.A., Portman, J.J. and Wolynes, P.G. (2000) Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc. Natl. Acad. Sci. U.S.A. 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
  • 34
    • 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. and Sudol, P. (2000) The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14, 231-241
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, P.3
  • 35
    • 84866671396 scopus 로고    scopus 로고
    • Mechanisms of small molecule binding to intrinsically disordered proteins
    • Cuchillo, R. and Michel, J. (2012) Mechanisms of small molecule binding to intrinsically disordered proteins. Biochem. Soc. Trans. 40, 1004-1008
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1004-1008
    • Cuchillo, R.1    Michel, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.