메뉴 건너뛰기




Volumn 20, Issue 15, 2004, Pages 2345-2354

Proteins associated with diseases show enhanced sequence correlation between charged residues

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; HEAT SHOCK PROTEIN; NUCLEOCAPSID PROTEIN; PRION PROTEIN; RNA BINDING PROTEIN;

EID: 7244253098     PISSN: 13674803     EISSN: 13674811     Source Type: Journal    
DOI: 10.1093/bioinformatics/bth245     Document Type: Article
Times cited : (24)

References (32)
  • 1
    • 0023660022 scopus 로고
    • Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacoo mosaic virus
    • Altschuh,D., Lesk,A.M., Bloomer,A.C. and Klug,A. (1987) Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacoo mosaic virus. J. Mol. Biol., 193, 693-707.
    • (1987) J. Mol. Biol. , vol.193 , pp. 693-707
    • Altschuh, D.1    Lesk, A.M.2    Bloomer, A.C.3    Klug, A.4
  • 7
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti,F., Stefani,M., Taddei,N., Ramponi,G. and Dobson,C.M. (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature, 424, 805-808.
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 8
    • 0035966046 scopus 로고    scopus 로고
    • DNA converts cellular prion protein into the β-sheet conformation and inhibits prion peptide aggregation
    • Cordeiro,Y., Machado,F., Juliano,L., Juliano,M.A., Brentani,R.R., Foguel,D. and Silva,J.L. (2001) DNA converts cellular prion protein into the β-sheet conformation and inhibits prion peptide aggregation. J. Biol. Chem., 276, 49400-49409.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49400-49409
    • Cordeiro, Y.1    Machado, F.2    Juliano, L.3    Juliano, M.A.4    Brentani, R.R.5    Foguel, D.6    Silva, J.L.7
  • 10
    • 0036708438 scopus 로고    scopus 로고
    • C to form β sheet using NMR structures and sequence alignments
    • C to form β sheet using NMR structures and sequence alignments. Biophys. J., 83, 1268-1280.
    • (2002) Biophys. J. , vol.83 , pp. 1268-1280
    • Dima, R.I.1    Thirumalai, D.2
  • 11
    • 0033047710 scopus 로고    scopus 로고
    • A neural network based predictor of residue contacts in proteins
    • Fariselli,P. and Casadio,R. (1999) A neural network based predictor of residue contacts in proteins. Protein Eng., 12, 15-21.
    • (1999) Protein Eng. , vol.12 , pp. 15-21
    • Fariselli, P.1    Casadio, R.2
  • 16
    • 0029117163 scopus 로고
    • Statistical significance of sequence patterns in proteins
    • Karlin,S. (1995) Statistical significance of sequence patterns in proteins. Curr. Opin. Struct. Biol., 5, 360-371.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 360-371
    • Karlin, S.1
  • 18
    • 0037337271 scopus 로고    scopus 로고
    • Dissecting the assembly of Aβ(16-22) amyloid peptides into antiparallel β sheets
    • Klimov,D.K. and Thirumalai,D. (2003) Dissecting the assembly of Aβ(16-22) amyloid peptides into antiparallel β sheets. Structure, 11, 295-307.
    • (2003) Structure , vol.11 , pp. 295-307
    • Klimov, D.K.1    Thirumalai, D.2
  • 19
    • 0035853280 scopus 로고    scopus 로고
    • Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins
    • Landgraf,R., Xenarios,I. and Eisenberg,D. (2001) Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins. J. Mol. Biol., 307, 1487-1502.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1487-1502
    • Landgraf, R.1    Xenarios, I.2    Eisenberg, D.3
  • 20
    • 0019332167 scopus 로고
    • How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins
    • Lesk,A.M. and Chothia,C. (1980) How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins. J. Mol. Biol., 136, 225-270.
    • (1980) J. Mol. Biol. , vol.136 , pp. 225-270
    • Lesk, A.M.1    Chothia, C.2
  • 21
    • 0000702165 scopus 로고
    • Mutual information functions versus correlation functions
    • Li,W. (1990) Mutual information functions versus correlation functions. J. Stat. Phys., 60, 823-837.
    • (1990) J. Stat. Phys. , vol.60 , pp. 823-837
    • Li, W.1
  • 22
    • 0036468670 scopus 로고    scopus 로고
    • Evolutionary predictions of binding surfaces and interactions
    • Lichtarge,O. and Sowa,M.E. (2002) Evolutionary predictions of binding surfaces and interactions. Curr. Opin. Struct. Biol., 12 21-27.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 21-27
    • Lichtarge, O.1    Sowa, M.E.2
  • 23
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionary conserved pathways of energetic connectivity in protein families
    • Lockless,S.W. and Ranganathan,R. (1999) Evolutionary conserved pathways of energetic connectivity in protein families. Science, 286, 295-299.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 24
    • 0036081257 scopus 로고    scopus 로고
    • Charge states rather than propensity for beta-structure determine enhanced fibrillogenesis in wild-type Alzheimer's beta-amyloid peptide compared to E22Q Dutch mutant
    • Massi,F., Klimov,D.K., Thirumalai,D. and Straub,J.E. (2002) Charge states rather than propensity for beta-structure determine enhanced fibrillogenesis in wild-type Alzheimer's beta-amyloid peptide compared to E22Q Dutch mutant. Protein Sci., 11, 1639-1647.
    • (2002) Protein Sci. , vol.11 , pp. 1639-1647
    • Massi, F.1    Klimov, D.K.2    Thirumalai, D.3    Straub, J.E.4
  • 26
    • 0028125904 scopus 로고
    • How frequent are correlated changes in families of protein sequences?
    • Neher,E. (1994) How frequent are correlated changes in families of protein sequences? Proc. Natl Acad. Sci., USA, 91 98-102.
    • (1994) Proc. Natl. Acad. Sci., USA , vol.91 , pp. 98-102
    • Neher, E.1
  • 27
    • 0033550256 scopus 로고    scopus 로고
    • Effective use of sequence correlation and conservation in fold recognition
    • Olmea,O., Rost,B. and Valencia,A. (1999) Effective use of sequence correlation and conservation in fold recognition. J. Mol. Biol., 295, 1221-1239.
    • (1999) J. Mol. Biol. , vol.295 , pp. 1221-1239
    • Olmea, O.1    Rost, B.2    Valencia, A.3
  • 28
    • 0030821675 scopus 로고    scopus 로고
    • Correlated mutations contain information about protein-protein interaction
    • Pazos,F., Helmer-Citterich,M., Ausiello,G. and Valencia,A. (1997) Correlated mutations contain information about protein-protein interaction. J. Mol. Biol., 271, 511-523.
    • (1997) J. Mol. Biol. , vol.271 , pp. 511-523
    • Pazos, F.1    Helmer-Citterich, M.2    Ausiello, G.3    Valencia, A.4
  • 29
    • 0030743758 scopus 로고    scopus 로고
    • Effectiveness of correlation analysis in identifying protein residues undergoing correlated evolution
    • Pollock,D.D. and Taylor,W.R. (1997) Effectiveness of correlation analysis in identifying protein residues undergoing correlated evolution. Protein Eng., 10, 647-657.
    • (1997) Protein Eng. , vol.10 , pp. 647-657
    • Pollock, D.D.1    Taylor, W.R.2
  • 30
    • 0027194968 scopus 로고
    • Nucleic acids binding proteins in highly purified Creutzfeldt-Jakob disease preparations
    • Sklaviadis,T., Akowitz,A., Manuelidis,E.E. and Manuelidis,L. (1993) Nucleic acids binding proteins in highly purified Creutzfeldt-Jakob disease preparations. Proc. Natl Acad. Sci., USA, 90, 5713-5717.
    • (1993) Proc. Natl. Acad. Sci., USA , vol.90 , pp. 5713-5717
    • Sklaviadis, T.1    Akowitz, A.2    Manuelidis, E.E.3    Manuelidis, L.4
  • 31
    • 0027952860 scopus 로고
    • Compensating changes in protein multiple sequence alignments
    • Taylor,W.R. and Hatrick,K. (1994) Compensating changes in protein multiple sequence alignments. Protein Eng., 7, 341-348.
    • (1994) Protein Eng. , vol.7 , pp. 341-348
    • Taylor, W.R.1    Hatrick, K.2
  • 32
    • 0037397705 scopus 로고    scopus 로고
    • Emerging ideas on the molecular basis of protein and peptide aggregation
    • Thirumalai,D., Klimov,D.K. and Dima,R.I. (2003) Emerging ideas on the molecular basis of protein and peptide aggregation. Curr. Opin. Struct. Biol., 13, 146-159.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 146-159
    • Thirumalai, D.1    Klimov, D.K.2    Dima, R.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.