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Volumn 2005, Issue , 2005, Pages

Intrinsic disorder and prote in modifications: Building an SVM predictor for methylation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; AUTOMATA THEORY; BIOTECHNOLOGY; CHEMICAL MODIFICATION; LEARNING SYSTEMS;

EID: 33847215114     PISSN: None     EISSN: None     Source Type: Conference Proceeding    
DOI: 10.1109/cibcb.2005.1594957     Document Type: Conference Paper
Times cited : (50)

References (48)
  • 1
    • 0014200317 scopus 로고
    • Enzymatic methylation of protein pabp 1 identified as an arginine fractions from calf thymus nuclei
    • Paik, W.K. and S. Kim, Enzymatic methylation of protein pabp 1 identified as an arginine fractions from calf thymus nuclei. Biochem. Biophys. Res. Commun., 1967, 29: p. 14-20.
    • (1967) Biochem. Biophys. Res. Commun , vol.29 , pp. 14-20
    • Paik, W.K.1    Kim, S.2
  • 2
    • 19944430267 scopus 로고    scopus 로고
    • DisProt: A database of protein disorder
    • Vucetic, S., et al., DisProt: a database of protein disorder. Bioinformatics, 2005, 21(1): p. 137-140.
    • (2005) Bioinformatics , vol.21 , Issue.1 , pp. 137-140
    • Vucetic, S.1
  • 3
    • 0023016261 scopus 로고
    • Enzymology of protein methylation
    • Paik, W.K. and S. Kim, Enzymology of protein methylation. Yonsei Medical Journal, 1986, 25(3): p. 159-177.
    • (1986) Yonsei Medical Journal , vol.25 , Issue.3 , pp. 159-177
    • Paik, W.K.1    Kim, S.2
  • 4
    • 0032032823 scopus 로고    scopus 로고
    • Protein methylation: A signal event in post-translational modification
    • Aletta, J.M., T.R. Cimato, and M.J. Ettinger, Protein methylation: a signal event in post-translational modification. Trends Biochem. Sciences, 1998, 23(3): p. 89-91.
    • (1998) Trends Biochem. Sciences , vol.23 , Issue.3 , pp. 89-91
    • Aletta, J.M.1    Cimato, T.R.2    Ettinger, M.J.3
  • 5
    • 0025291029 scopus 로고
    • Diversity of methyl acceptor proteins in rat pheochromocytoma (PC12) cells revealed after treatment with adenosine dialdehyde
    • Najbauer, J. and D. Aswad, Diversity of methyl acceptor proteins in rat pheochromocytoma (PC12) cells revealed after treatment with adenosine dialdehyde. J. Biol. Chem., 1990, 265: p. 12717-12721.
    • (1990) J. Biol. Chem , vol.265 , pp. 12717-12721
    • Najbauer, J.1    Aswad, D.2
  • 6
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Shi, Y., et al., Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell, 2004, 119: p. 941-953.
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1
  • 7
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation: An emerging regulator of protein function
    • Bedford, M.T. and S. Richard, Arginine methylation: an emerging regulator of protein function. Mol. Cell, 2005, 18: p. 263-272.
    • (2005) Mol. Cell , vol.18 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 8
    • 0034687558 scopus 로고    scopus 로고
    • Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene
    • Scorilas, A., et al., Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene. Biochem. Biophys. Res. Commun., 2000, 278: p. 349-359.
    • (2000) Biochem. Biophys. Res. Commun , vol.278 , pp. 349-359
    • Scorilas, A.1
  • 9
    • 0027156138 scopus 로고
    • Peptides with sequences similar to glycine, argininerich motifs in proteins interacting with rna are efficiently recognized by methyltransferase(s) modifying arginine in numerous proteins
    • Najbauer, J., et al., Peptides with sequences similar to glycine, argininerich motifs in proteins interacting with rna are efficiently recognized by methyltransferase(s) modifying arginine in numerous proteins. J. Biol. Chem., 1993, 268: p. 10501-10509.
    • (1993) J. Biol. Chem , vol.268 , pp. 10501-10509
    • Najbauer, J.1
  • 10
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • Lachner, M. and T. Jenuwein, The many faces of histone lysine methylation. Curr. Opin. Cell. Bio, 2002, 14(3): p. 286-298.
    • (2002) Curr. Opin. Cell. Bio , vol.14 , Issue.3 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 11
    • 0035197005 scopus 로고    scopus 로고
    • The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins
    • Friesen, W.J., et al., The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins. Mol. Cell. Biol., 2001, 21: p. 8289-8300.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 8289-8300
    • Friesen, W.J.1
  • 12
    • 2642551574 scopus 로고    scopus 로고
    • Small molecule regulators of protein arginine methyltransferases
    • Cheng, D., et al., Small molecule regulators of protein arginine methyltransferases. J. Biol. Chem., 2004, 279: p. 23892-23899.
    • (2004) J. Biol. Chem , vol.279 , pp. 23892-23899
    • Cheng, D.1
  • 13
    • 13444273448 scopus 로고    scopus 로고
    • Bairoch, A., et al., The Universal Protein Resource (UniProt). Nucleic Acids Res, 2005, 33 Database Issue: p. D154-9.
    • Bairoch, A., et al., The Universal Protein Resource (UniProt). Nucleic Acids Res, 2005, 33 Database Issue: p. D154-9.
  • 14
    • 33947482638 scopus 로고
    • The occurrence of var epsilon-n-methyl lysine in histones
    • Murray, K., The occurrence of var epsilon-n-methyl lysine in histones. Biochemistry, 1964, 3: p. 10-15.
    • (1964) Biochemistry , vol.3 , pp. 10-15
    • Murray, K.1
  • 15
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B.D. and C.D. Allis, The language of covalent histone modifications. Nature, 2000, 403(6765): p. 41-45.
    • (2000) Nature , vol.403 , Issue.6765 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 16
    • 0003903126 scopus 로고
    • New York: Springer-Verlag
    • van Holde, K., Chromatin. 1988, New York: Springer-Verlag.
    • (1988) Chromatin
    • van Holde, K.1
  • 17
    • 9244247669 scopus 로고    scopus 로고
    • Regulation of p53 activity through lysine methylation
    • Chuikov, S., et al., Regulation of p53 activity through lysine methylation. Nature, 2004, 432: p. 353-360.
    • (2004) Nature , vol.432 , pp. 353-360
    • Chuikov, S.1
  • 18
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H.J. and P.E. Wright, Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol, 2005, 6(3): p. 197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 19
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink, A.L., Natively unfolded proteins. Curr Opin Struct Biol, 2005, 15(1): p. 35-41.
    • (2005) Curr Opin Struct Biol , vol.15 , Issue.1 , pp. 35-41
    • Fink, A.L.1
  • 20
    • 0035022941 scopus 로고    scopus 로고
    • Intrinsically disordered protein
    • Dunker, A.K., et al., Intrinsically disordered protein. J. Mol. Graph. Model., 2001, 19(1): p. 26-59.
    • (2001) J. Mol. Graph. Model , vol.19 , Issue.1 , pp. 26-59
    • Dunker, A.K.1
  • 21
    • 0036792049 scopus 로고    scopus 로고
    • FlgMgains structure in living cells
    • Dedmon, M.M., et al., FlgMgains structure in living cells. Proc. Natl. Acad. Sci. U. S. A., 2002, 99(20): p. 12681-12684.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , Issue.20 , pp. 12681-12684
    • Dedmon, M.M.1
  • 22
    • 33847211930 scopus 로고    scopus 로고
    • personal communication
    • Pielaok, C., personal communication. 2005.
    • (2005)
    • Pielaok, C.1
  • 23
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity - linking function and disorder
    • Dunker, A.K. and Z. Obradovic, The protein trinity - linking function and disorder. Nat. Biotechnol., 2001, 19(9): p. 805-806.
    • (2001) Nat. Biotechnol , vol.19 , Issue.9 , pp. 805-806
    • Dunker, A.K.1    Obradovic, Z.2
  • 24
    • 0037188377 scopus 로고    scopus 로고
    • Intrinsic disorder and protein function
    • Dunker, A.K., et al., Intrinsic disorder and protein function. Biochemistry, 2002, 41(21): p. 6573-6582.
    • (2002) Biochemistry , vol.41 , Issue.21 , pp. 6573-6582
    • Dunker, A.K.1
  • 25
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P., Intrinsically unstructured proteins. Trends Biochem Sci, 2002, 27(527-533).
    • (2002) Trends Biochem Sci , vol.27 , Issue.527-533
    • Tompa, P.1
  • 26
    • 33847203438 scopus 로고    scopus 로고
    • personal communication
    • Tompa, P., personal communication. 2004.
    • (2004)
    • Tompa, P.1
  • 27
    • 24944511034 scopus 로고    scopus 로고
    • Natively disordered protein
    • J. Buchner and T. Kiefhaber, Editors, Wiley-VCH: Verlag GmbH & Co. KGaA: Weinheim, p
    • Daughdrill, G.W., et al., Natively disordered protein, in Protein Folding Handbook, J. Buchner and T. Kiefhaber, Editors. 2005, Wiley-VCH: Verlag GmbH & Co. KGaA: Weinheim, p. 271-353.
    • (2005) Protein Folding Handbook , pp. 271-353
    • Daughdrill, G.W.1
  • 28
    • 19544394729 scopus 로고    scopus 로고
    • AutoMotif server: Prediction of single residue post-translational modifications in proteins
    • Plewczynski, D., et al., AutoMotif server: prediction of single residue post-translational modifications in proteins. Bioinformatics, 2005, 21(10): p. 2525-7.
    • (2005) Bioinformatics , vol.21 , Issue.10 , pp. 2525-2527
    • Plewczynski, D.1
  • 29
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl silac
    • Ong, S.-E., G. Mittler, and M. Mann, Identifying and quantifying in vivo methylation sites by heavy methyl silac. Nat. Methods, 2004, 1: p. 119-126.
    • (2004) Nat. Methods , vol.1 , pp. 119-126
    • Ong, S.-E.1    Mittler, G.2    Mann, M.3
  • 30
    • 0028361031 scopus 로고
    • Accuracy of protein flexibility predictions
    • Vihinen, M., E. Torkkila, and P. Riikonen, Accuracy of protein flexibility predictions. Proteins, 1994, 19: p. 141-149.
    • (1994) Proteins , vol.19 , pp. 141-149
    • Vihinen, M.1    Torkkila, E.2    Riikonen, P.3
  • 31
    • 0000929505 scopus 로고
    • The hydrophobic moment detects periodicity in protein hydrophobicity
    • Eisenberg, D., R.M. Weiss, and T.C. Terwilliger, The hydrophobic moment detects periodicity in protein hydrophobicity. Proc. Natl. Acad. Sci. U.S. A., 1984, 81: p. 140-144.
    • (1984) Proc. Natl. Acad. Sci. U.S. A , vol.81 , pp. 140-144
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 32
    • 0029901640 scopus 로고    scopus 로고
    • Analysis of compositionally biased regions in sequence databases
    • Wootton, J.C. and S. Federhen, Analysis of compositionally biased regions in sequence databases. Methods Enzymol, 1996, 266: p. 554-571.
    • (1996) Methods Enzymol , vol.266 , pp. 554-571
    • Wootton, J.C.1    Federhen, S.2
  • 33
    • 0014747331 scopus 로고
    • Generalized information functions
    • Daróczy, Z., Generalized information functions. Information and Control, 1970, 16: p. 36-51.
    • (1970) Information and Control , vol.16 , pp. 36-51
    • Daróczy, Z.1
  • 34
    • 0041418213 scopus 로고    scopus 로고
    • Flavors of protein disorder
    • Vucetic, S., et al., Flavors of protein disorder. Proteins, 2003, 52: p. 573-584.
    • (2003) Proteins , vol.52 , pp. 573-584
    • Vucetic, S.1
  • 35
    • 0242267500 scopus 로고    scopus 로고
    • Predicting intrinsic disorder from amino acid sequence
    • Obradovic, Z., et al., Predicting intrinsic disorder from amino acid sequence. Proteins, 2003, 53(S6): p. 566-572.
    • (2003) Proteins , vol.53 , Issue.S6 , pp. 566-572
    • Obradovic, Z.1
  • 36
    • 0347364621 scopus 로고    scopus 로고
    • Protein flexibility and intrinsic disorder
    • Radivojac, P., et al., Protein flexibility and intrinsic disorder. Protein Science, 2004, 13(1): p. 71-80.
    • (2004) Protein Science , vol.13 , Issue.1 , pp. 71-80
    • Radivojac, P.1
  • 37
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul, S.F., et al., Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res., 1997, 25: p. 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 39
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: Tool for the unification of biology. The Gene Ontology Consortium
    • Ashburner, M., et al., Gene ontology: tool for the unification of biology. The Gene Ontology Consortium. Nat. Genet., 2000, 25(1): p. 25-29.
    • (2000) Nat. Genet , vol.25 , Issue.1 , pp. 25-29
    • Ashburner, M.1
  • 40
    • 0033954256 scopus 로고    scopus 로고
    • The protein data bank
    • Berman, H.M., et al., The protein data bank. Nucleic Acids Res., 2000, 28(1): p. 235-242.
    • (2000) Nucleic Acids Res , vol.28 , Issue.1 , pp. 235-242
    • Berman, H.M.1
  • 41
    • 0346731042 scopus 로고    scopus 로고
    • Automatic prediction of protein function
    • Rost, B., et al., Automatic prediction of protein function. Cell Mol Life Sci, 2003, 60(12): p. 2637-2650.
    • (2003) Cell Mol Life Sci , vol.60 , Issue.12 , pp. 2637-2650
    • Rost, B.1
  • 42
    • 13044272912 scopus 로고    scopus 로고
    • Automated analysis of interatomic contacts in proteins
    • Sobolev, V., et al., Automated analysis of interatomic contacts in proteins. Bioinformatics, 1999, 15(4): p. 327-32.
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 327-332
    • Sobolev, V.1
  • 43
    • 0015526732 scopus 로고
    • Participation of the protein ligands in the folding of cytochromec
    • Babul, J. and E. Stell wagen, Participation of the protein ligands in the folding of cytochromec. Biochemistry, 1972, 11(7): p. 1195-200.
    • (1972) Biochemistry , vol.11 , Issue.7 , pp. 1195-1200
    • Babul, J.1    Stell wagen, E.2
  • 44
    • 0015919686 scopus 로고
    • On the role of heme in the formation of the structure of cytochrome c
    • Fisher, W.R., H. Taniuchi, and C.B. Anfinsen, On the role of heme in the formation of the structure of cytochrome c. J Biol Chem, 1973, 248(9): p. 3188-95.
    • (1973) J Biol Chem , vol.248 , Issue.9 , pp. 3188-3195
    • Fisher, W.R.1    Taniuchi, H.2    Anfinsen, C.B.3
  • 45
    • 2342473198 scopus 로고    scopus 로고
    • The importance of intrinsic disorder for protein phosphorylation
    • Iakoucheva, L.M., et al., The importance of intrinsic disorder for protein phosphorylation. Nucleic Acids Res., 2004, 32(3): p. 1037-1049.
    • (2004) Nucleic Acids Res , vol.32 , Issue.3 , pp. 1037-1049
    • Iakoucheva, L.M.1
  • 46
    • 0035413607 scopus 로고    scopus 로고
    • Structural basis for control by phosphorylation
    • Johnson, L.N. and R.J. Lewis, Structural basis for control by phosphorylation. Chem. Rev., 2001, 101: p. 2209-2242.
    • (2001) Chem. Rev , vol.101 , pp. 2209-2242
    • Johnson, L.N.1    Lewis, R.J.2
  • 47
    • 0001079105 scopus 로고
    • On the use of sequence homologies to predict protein structure: Identical pentapeptides can have completely different conformations
    • Kabsch, W. and C. Sander, On the use of sequence homologies to predict protein structure: identical pentapeptides can have completely different conformations. Proc. Natl. Acad. Sci. U. S. A., 1984, 81(4): p. 1075-8.
    • (1984) Proc. Natl. Acad. Sci. U. S. A , vol.81 , Issue.4 , pp. 1075-1078
    • Kabsch, W.1    Sander, C.2
  • 48
    • 6344222803 scopus 로고    scopus 로고
    • Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes
    • Pal, S., et al., Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol. Cell. Biol., 2004, 24: p. 9630-9645.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 9630-9645
    • Pal, S.1


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