메뉴 건너뛰기




Volumn 16, Issue 4, 2000, Pages 376-382

Wavelet change-point prediction of transmembrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

HELIX LOOP HELIX PROTEIN; MEMBRANE PROTEIN;

EID: 0034084705     PISSN: 13674803     EISSN: None     Source Type: Journal    
DOI: 10.1093/bioinformatics/16.4.376     Document Type: Article
Times cited : (81)

References (28)
  • 1
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: The dense alignment surface method
    • Cserzo, M., Wallin, E., Simon, I., von Heijne, G. and Elofsson, A. (1997) Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method. Protein Eng., 10, 673-676.
    • (1997) Protein Eng. , vol.10 , pp. 673-676
    • Cserzo, M.1    Wallin, E.2    Simon, I.3    Von Heijne, G.4    Elofsson, A.5
  • 3
    • 0032334093 scopus 로고    scopus 로고
    • Minimax estimation via wavelet shrinkage
    • Donoho, D. and Johnstone, I. (1998) Minimax estimation via wavelet shrinkage. Ann. Statist., 26, 879-921.
    • (1998) Ann. Statist. , vol.26 , pp. 879-921
    • Donoho, D.1    Johnstone, I.2
  • 5
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • Engelman, D.M., Steitz, T.A. and Goldman, A. (1986) Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Chem., 15, 321-353.
    • (1986) Annu. Rev. Biophys. Chem. , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 6
    • 0026609104 scopus 로고
    • The distribution of charged amino acids in mitochondrial inner membrane proteins suggests different modes of membrane integration for nuclearly and mitochondrially encoded proteins
    • Gavel, Y. and von Heijne, G. (1992) The distribution of charged amino acids in mitochondrial inner membrane proteins suggests different modes of membrane integration for nuclearly and mitochondrially encoded proteins. Eur. J. Biochem., 205, 1207-1215.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 1207-1215
    • Gavel, Y.1    Von Heijne, G.2
  • 7
    • 0030601801 scopus 로고    scopus 로고
    • Using evolutionary trees in protein secondary structure prediction and other comparative sequence analyses
    • Goldman, N., Thorne, J. and Jones, D.T. (1996) Using evolutionary trees in protein secondary structure prediction and other comparative sequence analyses. J. Mol. Biol., 263, 196-208.
    • (1996) J. Mol. Biol. , vol.263 , pp. 196-208
    • Goldman, N.1    Thorne, J.2    Jones, D.T.3
  • 8
    • 0026716643 scopus 로고
    • Membrane Protein Structure prediction -hydrophobicity analysis and the positive-inside rule
    • von Heijne, G. (1992) Membrane Protein Structure prediction -hydrophobicity analysis and the positive-inside rule. J. Mol. Biol., 225, 487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Heijne, G.1
  • 9
    • 0032971848 scopus 로고    scopus 로고
    • The hydrophobic core of proteins predicted by wavelet analysis
    • Hirakawa, H., Muta, S. and Kuhara, S. (1999) The hydrophobic core of proteins predicted by wavelet analysis. Bioinformatics, 15, 141-148.
    • (1999) Bioinformatics , vol.15 , pp. 141-148
    • Hirakawa, H.1    Muta, S.2    Kuhara, S.3
  • 10
    • 0000207681 scopus 로고
    • TMbase a database of membrane spanning proteins segments
    • Hofmann, K. and Stoffel, W. (1993) TMbase a database of membrane spanning proteins segments. Biol. Chem. Hoppe-Seyler, 347, 166-171.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.347 , pp. 166-171
    • Hofmann, K.1    Stoffel, W.2
  • 11
    • 0028211273 scopus 로고
    • A model recognition approach to the prediction of allhelical membrane protein structure and topology
    • Jones, D.T. (1994) A model recognition approach to the prediction of allhelical membrane protein structure and topology. Biochemistry, 33, 3038-3049.
    • (1994) Biochemistry , vol.33 , pp. 3038-3049
    • Jones, D.T.1
  • 12
    • 0000908693 scopus 로고    scopus 로고
    • The preference functions method for predicting helical turns with membrane propensity
    • Juretic, D. and Lucin, A. (1998) The preference functions method for predicting helical turns with membrane propensity. J. Chem. Inf. Comput Sci., 38, 575-585.
    • (1998) J. Chem. Inf. Comput Sci. , vol.38 , pp. 575-585
    • Juretic, D.1    Lucin, A.2
  • 13
    • 0020475449 scopus 로고
    • A simple method for displaying the hydrophatic character of a protein
    • Kyte, J. and Doolittle, R.F. (1982) A simple method for displaying the hydrophatic character of a protein. J. Mol. Biol., 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 14
    • 0032708723 scopus 로고    scopus 로고
    • Using protein structural information in evolutionary inference: Transmembrane proteins
    • Lio', P. and Goldman, N. (1999) Using protein structural information in evolutionary inference: transmembrane proteins. Mol. Biol. Evol., 16, 1696-1710.
    • (1999) Mol. Biol. Evol. , vol.16 , pp. 1696-1710
    • Lio', P.1    Goldman, N.2
  • 15
    • 0024700097 scopus 로고
    • A theory for multiresolution signal decomposition: The wavelet representation
    • Mallat, S.G. (1989) A theory for multiresolution signal decomposition: the wavelet representation. IEEE Trans. Pattern Anal. Mach. Intell., 11, 674-693.
    • (1989) IEEE Trans. Pattern Anal. Mach. Intell. , vol.11 , pp. 674-693
    • Mallat, S.G.1
  • 17
    • 0030160662 scopus 로고    scopus 로고
    • Data dependent wavelet thresholding in nonparametric regression with change-point applications
    • Ogden, R.T. and Parzen, E. (1996a) Data dependent wavelet thresholding in nonparametric regression with change-point applications. Comput. Stat. Data Anal., 22, 53-70.
    • (1996) Comput. Stat. Data Anal. , vol.22 , pp. 53-70
    • Ogden, R.T.1    Parzen, E.2
  • 18
    • 21344466471 scopus 로고    scopus 로고
    • Change-point approach to data analytic wavelet thresholding
    • Ogden, R.T. and Parzen, E. (1996b) Change-point approach to data analytic wavelet thresholding. Stat. Comput., 6, 93-99.
    • (1996) Stat. Comput. , vol.6 , pp. 93-99
    • Ogden, R.T.1    Parzen, E.2
  • 19
    • 0023055775 scopus 로고
    • New hydrophilicity scale derived from High-Performance Liquid Chromatography peptide retention data: Correlation of predicted surface residues with antigenicity and X-ray derived accessible sites
    • Parker, J.M., Guo, D. and Hodges, R.S. (1986) New hydrophilicity scale derived from High-Performance Liquid Chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray derived accessible sites. Biochemistry, 25, 5425-5432.
    • (1986) Biochemistry , vol.25 , pp. 5425-5432
    • Parker, J.M.1    Guo, D.2    Hodges, R.S.3
  • 20
    • 0027354210 scopus 로고
    • Hydrophobic characteristics of folded proteins
    • Ponnuswamy, P.K. (1993) Hydrophobic characteristics of folded proteins. Prog. Biophys. Molec. Biol., 59, 57-103.
    • (1993) Prog. Biophys. Molec. Biol. , vol.59 , pp. 57-103
    • Ponnuswamy, P.K.1
  • 21
    • 0032352519 scopus 로고    scopus 로고
    • Minimax estimation of sharp change points
    • Raimondo, M. (1998) Minimax estimation of sharp change points. Ann. Stat., 26, 1379-1397.
    • (1998) Ann. Stat. , vol.26 , pp. 1379-1397
    • Raimondo, M.1
  • 22
    • 0023059178 scopus 로고
    • A conformational preference parameter to predict helices in integral membrane proteins
    • Rao, J.K.M. and Argos, P. (1986) A conformational preference parameter to predict helices in integral membrane proteins. Bioch. Biophys. Acta, 869, 197-214.
    • (1986) Bioch. Biophys. Acta , vol.869 , pp. 197-214
    • Rao, J.K.M.1    Argos, P.2
  • 23
    • 0030038634 scopus 로고    scopus 로고
    • Topology prediction for helical transmembrane proteins at 86% accuracy
    • Rost, B., Fariselli, P. and Casadio, R. (1996) Topology prediction for helical transmembrane proteins at 86% accuracy. Protein Sci., 5, 1704-1718.
    • (1996) Protein Sci. , vol.5 , pp. 1704-1718
    • Rost, B.1    Fariselli, P.2    Casadio, R.3
  • 24
    • 0028902788 scopus 로고
    • Transmembrane helices predicted at 95% accuracy
    • Rost, B., Casadio, R., Fariselli, P. and Sander, C. (1995) Transmembrane helices predicted at 95% accuracy. Protein Sci., 4, 521-533.
    • (1995) Protein Sci. , vol.4 , pp. 521-533
    • Rost, B.1    Casadio, R.2    Fariselli, P.3    Sander, C.4
  • 25
    • 0031614678 scopus 로고    scopus 로고
    • A hidden Markov model for predicting transmembrane helices in protein sequences
    • Sonnhammer, E.L. L., von Heijne, G. and Krogh, A. (1998) A hidden Markov model for predicting transmembrane helices in protein sequences. ISMB, 6, 175-182.
    • (1998) ISMB , vol.6 , pp. 175-182
    • Sonnhammer, E.L.L.1    Von Heijne, G.2    Krogh, A.3
  • 26
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: Classification and secondary structure prediction system for membrane proteins
    • Takatsugu, H., Boon-Chieng, S. and Shigeki, M. (1998) SOSUI: Classification and secondary structure prediction system for membrane proteins. Bioinformatics, 14, 378-379.
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Takatsugu, H.1    Boon-Chieng, S.2    Shigeki, M.3
  • 27
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: Application to topology prediction
    • Tusnady, G.E. and Simon, I. (1998) Principles governing amino acid composition of integral membrane proteins: application to topology prediction. J. Mol. Biol., 283, 489-506.
    • (1998) J. Mol. Biol. , vol.283 , pp. 489-506
    • Tusnady, G.E.1    Simon, I.2
  • 28
    • 0000999642 scopus 로고
    • Jump and sharp cusp detection by wavelets
    • Wang, Y. (1995) Jump and sharp cusp detection by wavelets. Biometrika, 82, 385-397.
    • (1995) Biometrika , vol.82 , pp. 385-397
    • Wang, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.