메뉴 건너뛰기




Volumn 43, Issue W1, 2015, Pages W331-W337

PrionW: A server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PROTEIN; ASPARAGINE; GLUTAMINE; PRION PROTEIN; PROTEOME; AMYLOID; FUNGAL PROTEIN; PRION;

EID: 84964334339     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkv490     Document Type: Article
Times cited : (62)

References (23)
  • 1
    • 84874638938 scopus 로고    scopus 로고
    • Prions, prionoids and pathogenic proteins in Alzheimer disease
    • Ashe,K.H. and Aguzzi,A. (2013) Prions, prionoids and pathogenic proteins in Alzheimer disease. Prion, 7, 55-59.
    • (2013) Prion , vol.7 , pp. 55-59
    • Ashe, K.H.1    Aguzzi, A.2
  • 2
    • 84864381145 scopus 로고    scopus 로고
    • Multiple substitutions of methionine 129 in human prion protein reveal its importance in the amyloid fibrillation pathway
    • Nystrom,S., Mishra,R., Hornemann,S., Aguzzi,A., Nilsson,K.P. and Hammarstrom,P. (2012) Multiple substitutions of methionine 129 in human prion protein reveal its importance in the amyloid fibrillation pathway. J. Biol. Chem., 287, 25975-25984.
    • (2012) J. Biol. Chem. , vol.287 , pp. 25975-25984
    • Nystrom, S.1    Mishra, R.2    Hornemann, S.3    Aguzzi, A.4    Nilsson, K.P.5    Hammarstrom, P.6
  • 5
    • 78049285236 scopus 로고    scopus 로고
    • Prion-like aggregates: Infectious agents in human disease
    • Westermark,G.T. and Westermark,P. (2010) Prion-like aggregates: infectious agents in human disease. Trends Mol. Med., 16, 501-507.
    • (2010) Trends Mol. Med. , vol.16 , pp. 501-507
    • Westermark, G.T.1    Westermark, P.2
  • 6
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg,D. and Jucker,M. (2012) The amyloid state of proteins in human diseases. Cell, 148, 1188-1203.
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 7
    • 77957782470 scopus 로고    scopus 로고
    • Biology of amyloid: Structure, function, and regulation
    • Greenwald,J. and Riek,R. (2010) Biology of amyloid: structure, function, and regulation. Structure (London, England : 1993), 18, 1244-1260.
    • (2010) Structure (London, England : 1993). , vol.18 , pp. 1244-1260
    • Greenwald, J.1    Riek, R.2
  • 8
    • 84876288161 scopus 로고    scopus 로고
    • Protein disorder, prion propensities, and self-organizing macromolecular collectives
    • Malinovska,L., Kroschwald,S. and Alberti,S. (2013) Protein disorder, prion propensities, and self-organizing macromolecular collectives. Biochim. Biophys. Acta, 1834, 918-931.
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 918-931
    • Malinovska, L.1    Kroschwald, S.2    Alberti, S.3
  • 10
    • 73549115633 scopus 로고    scopus 로고
    • Compositional determinants of prion formation in yeast
    • Toombs,J.A., McCarty,B.R. and Ross,E.D. (2010) Compositional determinants of prion formation in yeast. Mol. Cell. Biol., 30, 319-332.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 319-332
    • Toombs, J.A.1    McCarty, B.R.2    Ross, E.D.3
  • 13
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti,S., Halfmann,R., King,O., Kapila,A. and Lindquist,S. (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell, 137, 146-158.
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 14
    • 84877834389 scopus 로고    scopus 로고
    • Discovering putative prion sequences in complete proteomes using probabilistic representations of q/n-rich domains
    • Espinosa Angarica,V., Ventura,S. and Sancho,J. (2013) Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains. BMC Genomics, 14, 316.
    • (2013) BMC Genomics , vol.14 , pp. 316
    • Espinosa Angarica, V.1    Ventura, S.2    Sancho, J.3
  • 17
    • 29444444251 scopus 로고    scopus 로고
    • How evolutionary pressure against protein aggregation shaped chaperone specificity
    • Rousseau,F., Serrano,L. and Schymkowitz,J.W. (2006) How evolutionary pressure against protein aggregation shaped chaperone specificity. J. Mol. Biol., 355, 1037-1047.
    • (2006) J. Mol. Biol. , vol.355 , pp. 1037-1047
    • Rousseau, F.1    Serrano, L.2    Schymkowitz, J.W.3
  • 18
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/asparagine-rich regions: Implications for their conserved function and the prediction of novel prions
    • Michelitsch,M.D. and Weissman,J.S. (2000) A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc. Natl. Acad. Sci. U.S.A., 97, 11910-11915.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 19
    • 0038576863 scopus 로고    scopus 로고
    • A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes
    • Harrison,P.M. and Gerstein,M. (2003) A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes. Genome Biol., 4, R40.
    • (2003) Genome Biol. , vol.4 , pp. R40
    • Harrison, P.M.1    Gerstein, M.2
  • 20
    • 20744437001 scopus 로고    scopus 로고
    • Ronn: The bio-basis function neural network technique applied to the detection of natively disordered regions in proteins
    • Yang,Z.R., Thomson,R., McNeil,P. and Esnouf,R.M. (2005) RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics, 21, 3369-3376.
    • (2005) Bioinformatics , vol.21 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4
  • 21
    • 33751381791 scopus 로고    scopus 로고
    • Foldunfold: Web server for the prediction of disordered regions in protein chain
    • Galzitskaya,O.V., Garbuzynskiy,S.O. and Lobanov,M.Y. (2006) FoldUnfold: web server for the prediction of disordered regions in protein chain. Bioinformatics, 22, 2948-2949.
    • (2006) Bioinformatics , vol.22 , pp. 2948-2949
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2    Lobanov, M.Y.3
  • 22
    • 78651083450 scopus 로고    scopus 로고
    • In sup35p filaments (the [psi+] prion), the globular c-Terminal domains are widely offset from the amyloid fibril backbone
    • Baxa,U., Keller,P.W., Cheng,N., Wall,J.S. and Steven,A.C. (2011) In Sup35p filaments (the [PSI+] prion), the globular C-Terminal domains are widely offset from the amyloid fibril backbone. Mol. Microbiol., 79, 523-532.
    • (2011) Mol. Microbiol. , vol.79 , pp. 523-532
    • Baxa, U.1    Keller, P.W.2    Cheng, N.3    Wall, J.S.4    Steven, A.C.5
  • 23
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Low complexity sequence domains form dynamic fibers within hydrogels
    • Kato,M., Han,T.W., Xie,S., Shi,K., Du,X., Wu,L.C., Mirzaei,H., Goldsmith,E.J., Longgood,J., Pei,J. et al. (2012) Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. Cell, 149, 753-767.
    • (2012) Cell , vol.149 , pp. 753-767
    • Kato, M.1    Han, T.W.2    Xie, S.3    Shi, K.4    Du, X.5    Wu, L.C.6    Mirzaei, H.7    Goldsmith, E.J.8    Longgood, J.9    Pei, J.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.