메뉴 건너뛰기




Volumn 69, Issue 2, 2014, Pages 275-281

A Model for Small Heat Shock Protein Inhibition of Polyglutamine Aggregation

Author keywords

Ataxin 3; Fibrillar aggregation; PolyQ; SHsp; Small heat shock proteins; Spinocerebellar ataxia; B crystallin

Indexed keywords

ALPHA CRYSTALLIN; ATXN3 PROTEIN, HUMAN; NERVE PROTEIN; NUCLEAR PROTEIN; PEPTIDE; POLYGLUTAMINE; REPRESSOR PROTEIN; SMALL HEAT SHOCK PROTEIN;

EID: 84901235097     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12013-013-9795-1     Document Type: Article
Times cited : (11)

References (31)
  • 1
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor, J. P., Hardy, J., & Fischbeck, K. H. (2002). Toxic proteins in neurodegenerative disease. Science, 296, 1991-1995.
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 2
    • 33745195252 scopus 로고    scopus 로고
    • The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step
    • Ellisdon, A. M., Thomas, B., & Bottomley, S. P. (2006). The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step. Journal of Biological Chemistry, 281, 16888-16896.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 16888-16896
    • Ellisdon, A.M.1    Thomas, B.2    Bottomley, S.P.3
  • 7
    • 0036306310 scopus 로고    scopus 로고
    • Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity
    • Gu, L., Abulimiti, A., Li, W., & Chang, Z. J. (2002). Monodisperse Hsp16. 3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity. Journal of Molecular Biology, 319, 517-526.
    • (2002) Journal of Molecular Biology , vol.319 , pp. 517-526
    • Gu, L.1    Abulimiti, A.2    Li, W.3    Chang, Z.J.4
  • 8
    • 37449009967 scopus 로고    scopus 로고
    • Structure and orientation of T4 lysozyme bound to the small heat shock protein alpha-crystallin
    • Claxton, D. P., Zou, P., & Mchaourab, H. S. (2008). Structure and orientation of T4 lysozyme bound to the small heat shock protein alpha-crystallin. Journal of Molecular Biology, 375, 1026-1039.
    • (2008) Journal of Molecular Biology , vol.375 , pp. 1026-1039
    • Claxton, D.P.1    Zou, P.2    Mchaourab, H.S.3
  • 9
    • 34548241302 scopus 로고    scopus 로고
    • Interactive sequences in the stress protein and molecular chaperone human alphaB crystallin recognize and modulate the assembly of filaments
    • Ghosh, J. G., Houck, S. A., & Clark, J. I. (2007). Interactive sequences in the stress protein and molecular chaperone human alphaB crystallin recognize and modulate the assembly of filaments. International Journal of Biochemistry & Cell Biology, 39, 1804-1815.
    • (2007) International Journal of Biochemistry & Cell Biology , vol.39 , pp. 1804-1815
    • Ghosh, J.G.1    Houck, S.A.2    Clark, J.I.3
  • 10
    • 35949001344 scopus 로고    scopus 로고
    • Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila
    • Bilen, J., & Bonini, N. M. (2007). Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila. PLoS Genetics, 3, 1950-1964.
    • (2007) PLoS Genetics , vol.3 , pp. 1950-1964
    • Bilen, J.1    Bonini, N.M.2
  • 14
    • 84855303488 scopus 로고    scopus 로고
    • The effect of desolvation on nucleophilic halogenase activity
    • Healy, E. F. (2011). The effect of desolvation on nucleophilic halogenase activity. Computational and Theoretical Chemistry, 964, 91-93.
    • (2011) Computational and Theoretical Chemistry , vol.964 , pp. 91-93
    • Healy, E.F.1
  • 16
    • 0041821388 scopus 로고    scopus 로고
    • Dehydron: A structure-encoded signal for protein interactions
    • Fernández, A., & Ridgway, S. (2003). Dehydron: A structure-encoded signal for protein interactions. Biophysical Journal, 85, 1914-1928.
    • (2003) Biophysical Journal , vol.85 , pp. 1914-1928
    • Fernández, A.1    Ridgway, S.2
  • 17
    • 33751250818 scopus 로고    scopus 로고
    • Feature-similarity protein classifier as a ligand engineering tool
    • Maddipati, S., & Fernández, A. (2006). Feature-similarity protein classifier as a ligand engineering tool. Biomolecular Engineering, 23, 307-315.
    • (2006) Biomolecular Engineering , vol.23 , pp. 307-315
    • Maddipati, S.1    Fernández, A.2
  • 18
    • 79959543603 scopus 로고    scopus 로고
    • Nature non-adaptive origins of interactome complexity
    • Fernández, A., & Lynch, M. (2011). Nature non-adaptive origins of interactome complexity. Nature, 474, 502-505.
    • (2011) Nature , vol.474 , pp. 502-505
    • Fernández, A.1    Lynch, M.2
  • 20
    • 84859599030 scopus 로고    scopus 로고
    • A model for heterooligomer formation in the heat shock response of Escherichia coli
    • Healy, E. F. (2012). A model for heterooligomer formation in the heat shock response of Escherichia coli. Biochemical and Biophysical Research Communications, 420, 639-643.
    • (2012) Biochemical and Biophysical Research Communications , vol.420 , pp. 639-643
    • Healy, E.F.1
  • 23
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK: An initial-stage protein-docking algorithm
    • Chen, R., Li, L., & Weng, Z. (2003). ZDOCK: An initial-stage protein-docking algorithm. Proteins, 52, 80-87.
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 24
    • 34248513078 scopus 로고    scopus 로고
    • ZRANK: Reranking protein docking predictions with an optimized energy function
    • Pierce, B., & Weng, Z. (2007). ZRANK: Reranking protein docking predictions with an optimized energy function. Proteins-Structure Function and Genetics, 67, 1078-1086.
    • (2007) Proteins-Structure Function and Genetics , vol.67 , pp. 1078-1086
    • Pierce, B.1    Weng, Z.2
  • 26
    • 84901207991 scopus 로고    scopus 로고
    • AutoDock Tools
    • AutoDock Tools [http://autodock. scripps. edu/resources/adt/index_html].
  • 27
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity-A rapid access to atomic charges
    • Gasteiger, J., & Marsili, M. (1980). Iterative partial equalization of orbital electronegativity-A rapid access to atomic charges. Tetrahedron, 36, 3219-3228.
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 29
    • 0038425042 scopus 로고    scopus 로고
    • Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis
    • Fernández, A., & Berry, R. S. (2003). Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis. Proceedings of the National Academy of Sciences of the USA, 100, 2391-2396.
    • (2003) Proceedings of the National Academy of Sciences of the USA , vol.100 , pp. 2391-2396
    • Fernández, A.1    Berry, R.S.2
  • 31
    • 74049108958 scopus 로고    scopus 로고
    • Protein folding: sticky N17 speeds huntingtin pile-up
    • Liebman, S. W., & Meredith, S. C. (2010). Protein folding: sticky N17 speeds huntingtin pile-up. Nature Chemical Biology, 6, 7-8.
    • (2010) Nature Chemical Biology , vol.6 , pp. 7-8
    • Liebman, S.W.1    Meredith, S.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.