메뉴 건너뛰기




Volumn 5 b, Issue , 2008, Pages 325-344

Tools for Protein Technologies

Author keywords

Bioinformatics; Electrophoresis; Multiparametric; Proteomics; Spectrometric

Indexed keywords

ELECTROPHORESIS; MOLECULAR BIOLOGY;

EID: 84952905895     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527620876.ch14     Document Type: Chapter
Times cited : (2)

References (85)
  • 1
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST a new generation of protein database search programs
    • ALTSCHUL S.F., MADDEN T.L., SCHAFFER A.A., ZHANG J., ZHANG Z. et al. (1997), Gapped BLAST and PSI-BLAST a new generation of protein database search programs, Nucleic Acids Res. 25,3389-3402.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 3
    • 0023856847 scopus 로고
    • Automatic classification of two-dimensional gel electrophoresis pictures by heuristic clustering analysis: a step toward machine learning
    • APPEL R., HOCHSTRASSER D., ROCH C., FUNK M., MULLER A.F., PELLEGRINI C.(1988). Automatic classification of two-dimensional gel electrophoresis pictures by heuristic clustering analysis: a step toward machine learning, Electrophoresis 9,136-142.
    • (1988) Electrophoresis , vol.9 , pp. 136-142
    • Appel, R.1    Hochstrasser, D.2    Roch, C.3    Funk, M.4    Muller, A.F.5    Pellegrini, C.6
  • 4
    • 0031445948 scopus 로고    scopus 로고
    • Melanie II - a third-generation software package for analysis of two-dimensional electrophoresis images
    • APPEL R.D., VARGAS J.R., PALAGI P.M., WALTHER, D., HOCHSTRASSER D.F. (1997), Melanie II - a third-generation software package for analysis of two-dimensional electrophoresis images, Electrophoresis 18,2735-2748.
    • (1997) Electrophoresis , vol.18 , pp. 2735-2748
    • Appel, R.D.1    Vargas, J.R.2    Palagi, P.M.3    Walther, D.4    Hochstrasser, D.F.5
  • 5
    • 0033986922 scopus 로고    scopus 로고
    • The quest to deduce protein function from sequence: the role of pattern databases
    • ATTWOOD, T.K.,(2000),The quest to deduce protein function from sequence: the role of pattern databases, Int. J. Biochem. Cell Biol. 32,139-155.
    • (2000) Int. J. Biochem. Cell Biol. , vol.32 , pp. 139-155
    • Attwood, T.K.1
  • 7
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • BACHMAIR, A., FINLEY D., VARSHAVSKY, A., (1986 ), In vivo half-life of a protein is a function of its amino-terminal residue, Science 234,179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 8
    • 0025882349 scopus 로고
    • PROSITE: A dictionary of sites and patterns in proteins
    • BAIROCH, A. (1991), PROSITE: A dictionary of sites and patterns in proteins, Nicleic Acids Res. 19,2241-2245.
    • (1991) Nicleic Acids Res. , vol.19 , pp. 2241-2245
    • Bairoch, A.1
  • 9
    • 0033957834 scopus 로고    scopus 로고
    • The SWISSPROT protein sequence database and its supplement TrEMBL in 2000
    • BAIROCH A., APWEILER R. (2000), The SWISSPROT protein sequence database and its supplement TrEMBL in 2000, Nucleic Acids Res. 28,45-48.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 45-48
    • Bairoch, A.1    Apweiler, R.2
  • 13
    • 0025618753 scopus 로고
    • Appendix 6. Mass values for amino acid residues in peptides, in: Methods in Enzymology
    • (MCCLOSKEY J.A., Ed.), San Diego, CA: Academic Press
    • BIEMANN K. (1990), Appendix 6. Mass values for amino acid residues in peptides, in: Methods in Enzymology Vol. 193 (MCCLOSKEY J.A., Ed.), pp.888. San Diego, CA: Academic Press.
    • (1990) , vol.193 , pp. 888
    • Biemann, K.1
  • 14
    • 0028050261 scopus 로고
    • OWL - a non-redundant composite protein sequence database
    • BLEASBY A.J., AKRIGG D., ATTWOOD, T.K. (1994), OWL - a non-redundant composite protein sequence database, Nucleic Acids Res. 22, 3574-3577.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3574-3577
    • Bleasby, A.J.1    Akrigg, D.2    Attwood, T.K.3
  • 15
    • 0033579464 scopus 로고    scopus 로고
    • Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites
    • BLOM N., GAMMELTOFT S., BRUNAK S., (1999), Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites, J. Mol.Biol. 294,1351-1362.
    • (1999) J. Mol.Biol. , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 16
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known 3-dimensional structure
    • BOWIE J.U., LUTHY R., EISENBERG D.,(1991), A method to identify protein sequences that fold into a known 3-dimensional structure, Science 253,164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 17
    • 0034077507 scopus 로고    scopus 로고
    • Sequencing the entire genomes of free-living organisms: the foundation of pharmacology in the new millennium
    • BRODER S., VENTER J.C. (2000), Sequencing the entire genomes of free-living organisms: the foundation of pharmacology in the new millennium,Annu. Rev. Pharmacol. Toxicol. 40,97-132.
    • (2000) Annu. Rev. Pharmacol. Toxicol. , vol.40 , pp. 97-132
    • Broder, S.1    Venter, J.C.2
  • 18
    • 0027318317 scopus 로고
    • An empirical energy function for threading a protein sequence through a folding motif
    • BRYANT S.H., LAWRENCE C.E. (1993), An empirical energy function for threading a protein sequence through a folding motif, Proteins 5,92-112.
    • (1993) Proteins , vol.5 , pp. 92-112
    • Bryant, S.H.1    Lawrence, C.E.2
  • 20
    • 0017187836 scopus 로고
    • The nature of the accessible and buried surfaces in proteins
    • CHOTHIA C. (1976),The nature of the accessible and buried surfaces in proteins, J. Mol. Biol. 105,l-14.
    • (1976) J. Mol. Biol. , vol.105 , pp. l-14
    • Chothia, C.1
  • 21
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • CHOU, P.Y., FASMAN G.D. (1974), Prediction of protein conformation, Biochemistry 13,222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 22
    • 0033957841 scopus 로고    scopus 로고
    • ProDom and ProDom-CG: tools for protein domain analysis and whole genome comparisons
    • CORPET F., SERVANT F., GOUZY J., KAHN D. (2000), ProDom and ProDom-CG: tools for protein domain analysis and whole genome comparisons, Nucleic Acids Res. 28,267-269.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 267-269
    • Corpet, F.1    Servant, F.2    Gouzy, J.3    Kahn, D.4
  • 23
    • 0020649886 scopus 로고
    • Establishing homologies in protein sequences
    • DAYHOFF M.O., BARKER W.C., HUNT L.T. (1983), Establishing homologies in protein sequences, Methods Enzymol. 91,534-545.
    • (1983) Methods Enzymol. , vol.91 , pp. 534-545
    • Dayhoff, M.O.1    Barker, W.C.2    Hunt, L.T.3
  • 24
    • 0344043346 scopus 로고    scopus 로고
    • Protein structure prediction. Implications for the biologist
    • DELEAGE G., BLANCHET C., GEOURJON C. (1997), Protein structure prediction. Implications for the biologist, Biochimie 79,681-686.
    • (1997) Biochimie , vol.79 , pp. 681-686
    • Deleage, G.1    Blanchet, C.2    Geourjon, C.3
  • 25
    • 0024058905 scopus 로고
    • ANTHEPROT: a package for protein sequence analysis using a microcomputer
    • DELEAGE, G., CLERC, F.F., ROUX, B., GAUTHERON, D.C. (1988), ANTHEPROT: a package for protein sequence analysis using a microcomputer, Comput.Appl. Biosci. 4,351-356.
    • (1988) Comput.Appl. Biosci. , vol.4 , pp. 351-356
    • Deleage, G.1    Clerc, F.F.2    Roux, B.3    Gautheron, D.C.4
  • 26
    • 0027364941 scopus 로고
    • Evolutionarily mobile modules in proteins
    • DOOLITTLE R.F., BORK, P. (1993), Evolutionarily mobile modules in proteins, Sci. Am. 269,50-56.
    • (1993) Sci. Am. , vol.269 , pp. 50-56
    • Doolittle, R.F.1    Bork, P.2
  • 28
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass-spectral data of peptides with amino-acid sequences in a protein database
    • ENG, J.K., MCCORMACK A.L., YATES J.R. (1994), An approach to correlate tandem mass-spectral data of peptides with amino-acid sequences in a protein database, J. Am. Soc. Mass Spect. 5,976-989.
    • (1994) J. Am. Soc. Mass Spect. , vol.5 , pp. 976-989
    • Eng, J.K.1    Mccormack, A.L.2    Yates, J.R.3
  • 29
    • 0022510143 scopus 로고
    • Identifying non-polar transbilayer helices in amino acid sequences of membrane proteins
    • ENGELMAN D.M., STEITZ, T.A., GOLDMAN A. (1986), Identifying non-polar 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
  • 30
    • 0029874551 scopus 로고    scopus 로고
    • Protein fold recognition using sequence-derived predictions
    • FISCHER D., EISENBERG D., (1996), Protein fold recognition using sequence-derived predictions, Protein Sci. 5,947-955.
    • (1996) Protein Sci. , vol.5 , pp. 947-955
    • Fischer, D.1    Eisenberg, D.2
  • 31
    • 0000780209 scopus 로고
    • A limiting law relating the size and shape of protein molecules to their composition
    • FISHER H.F. (1964), A limiting law relating the size and shape of protein molecules to their composition, Proc. Natl. Acad. Sci. USA 51,1285-1291.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 1285-1291
    • Fisher, H.F.1
  • 32
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implementation of simple methods for predicting the secondary structure of globular proteins
    • GARNIER J., OGUSTHORPE D.J., ROBSON B. (1978), Analysis of the accuracy and implementation of simple methods for predicting the secondary structure of globular proteins, J. Mol. Biol. 120,97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Ogusthorpe, D.J.2    Robson, B.3
  • 33
    • 0034096536 scopus 로고    scopus 로고
    • Protein identification methods in proteomics
    • GEVAERT K., VANDEKERCKHOVE J. (2000), Protein identification methods in proteomics, Electrophoresis 21,1145-1154.
    • (2000) Electrophoresis , vol.21 , pp. 1145-1154
    • Gevaert, K.1    Vandekerckhove, J.2
  • 34
    • 0034653646 scopus 로고    scopus 로고
    • Protein identification with a single accurate mass of a cysteine-containing peptide and constrained database searching
    • GOODLETT D.R., BRUCE J.E., ANDERSON G.A., RIST, B., PASA-TOLIC L. et al. (2000), Protein identification with a single accurate mass of a cysteine-containing peptide and constrained database searching, Anal. Chem. 72,1112-1118.
    • (2000) Anal. Chem. , vol.72 , pp. 1112-1118
    • Goodlett, D.R.1    Bruce, J.E.2    Anderson, G.A.3    Rist, B.4    Pasa-Tolic, L.5
  • 35
    • 0032436341 scopus 로고    scopus 로고
    • DOMO: a new database of aligned protein domains
    • GRACY J., ARGos, P. (1998), DOMO: a new database of aligned protein domains, Trends Biochem. Sci., 23,495-497.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 495-497
    • Gracy, J.1    Argos, P.2
  • 37
    • 0031809552 scopus 로고    scopus 로고
    • NetOglyc:prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility
    • HANSEN J.E., LUND O., TOLSTRUP, N., GOOLEYA, .A., WILLIAMS K.L., BRUNAK S., (1998), NetOglyc:prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility, Glycoconj. J. 15,115-130.
    • (1998) Glycoconj. J. , vol.15 , pp. 115-130
    • Hansen, J.E.1    Lund, O.2    Tolstrup, N.3    Gooleya, A.4    Williams, K.L.5    Brunak, S.6
  • 38
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • HENIKOFF S., HENIKOFF J.G. (1992), Amino acid substitution matrices from protein blocks, Proc.Natl. Acad. Sci. USA 89,10915-10919.
    • (1992) Proc.Natl. Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 39
    • 0032776495 scopus 로고    scopus 로고
    • Blocks+: a non-redundant database of protein alignment blocks derived from multiple compilations
    • HENIKOFF J.G., HENIKOFF S., PIETROKOVSKI S., (1999), Blocks+: a non-redundant database of protein alignment blocks derived from multiple compilations, Biotransformatics 15,471-479.
    • (1999) Biotransformatics , vol.15 , pp. 471-479
    • Henikoff, J.G.1    Henikoff, S.2    Pietrokovski, S.3
  • 40
    • 0024498374 scopus 로고
    • The elucidation of protein function by sequence motif analysis
    • HODGMAN T.C. (1989), The elucidation of protein function by sequence motif analysis, Comput. Applic.Biosci. 5,l-13.
    • (1989) Comput. Applic.Biosci. , vol.5 , pp. l-13
    • Hodgman, T.C.1
  • 43
    • 0030624540 scopus 로고    scopus 로고
    • Better prediction of protein cellular localization sites with the k nearest neighbor classifier
    • HORTON P., NAKAI K. (1997), Better prediction of protein cellular localization sites with the k nearest neighbor classifier, Intellig. Syst. Mol. Biol. 5,147-152.
    • (1997) Intellig. Syst. Mol. Biol. , vol.5 , pp. 147-152
    • Horton, P.1    Nakai, K.2
  • 44
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • JONES D.T. (1999), Protein secondary structure prediction based on position-specific scoring matrices, J. Mol. Biol. 292,195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 45
    • 0026690571 scopus 로고
    • A new approach to protein fold recognition
    • JONES D.T., TAYLOR W.R., THORNTON J.M. (1992), A new approach to protein fold recognition, Nature 358,86-89.
    • (1992) Nature , vol.358 , pp. 86-89
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 46
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • KYTE J., DOOLITTLE, R.F. (1982), A simple method for displaying the hydropathic 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
  • 47
    • 0015222647 scopus 로고
    • The interpretation of protein structures: estimation of static accessibility
    • LEE, B.K., RICHARDS F.M. (1971), The interpretation of protein structures: estimation of static accessibility, J. Mol. Biol. 55,379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.K.1    Richards, F.M.2
  • 48
    • 0032736946 scopus 로고    scopus 로고
    • Flicker image comparison of 2-D gel images for putative identification using the 2DWG meta-database
    • LEMKIN P.F., THORNWALL G.,(1999), Flicker image comparison of 2-D gel images for putative identification using the 2DWG meta-database, Mol.Biotechnol. 12,159-172.
    • (1999) Mol.Biotechnol. , vol.12 , pp. 159-172
    • Lemkin, P.F.1    Thornwall, G.2
  • 49
    • 0030777763 scopus 로고    scopus 로고
    • Exploring the limits of nearest neighbour secondary structure prediction
    • LEVIN J.M. (1997), Exploring the limits of nearest neighbour secondary structure prediction, Protein Eng. 10,771-776.
    • (1997) Protein Eng. , vol.10 , pp. 771-776
    • Levin, J.M.1
  • 50
    • 0023050277 scopus 로고
    • An algorithm for secondary structure determination in proteins based on sequence similarity
    • LEVIN J.M., ROBSON B., GARNER J. (1986), An algorithm for secondary structure determination in proteins based on sequence similarity, FEBS Lett.205,303-308.
    • (1986) FEBS Lett. , vol.205 , pp. 303-308
    • Levin, J.M.1    Robson, B.2    Garner, J.3
  • 51
    • 0016162558 scopus 로고
    • Algorithms for prediction of helices and beta-structural regions in globular proteins
    • LIM, V.I. (1974),Algorithms for prediction of helices and beta-structural regions in globular proteins, J. Mol. Biol. 88,873-894.
    • (1974) J. Mol. Biol. , vol.88 , pp. 873-894
    • Lim, V.I.1
  • 53
    • 0018818559 scopus 로고
    • Data-base techniques for multiple two-dimensional polyacrylamide gel electrophoresis analyses
    • LIPKIN L.E., LEMKIN P.F. (1980) Data-base techniques for multiple two-dimensional polyacrylamide gel electrophoresis analyses, Clin. Chem. 26,1403-1412.
    • (1980) Clin. Chem. , vol.26 , pp. 1403-1412
    • Lipkin, L.E.1    Lemkin, P.F.2
  • 54
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiledcoil structures
    • LUPAS A. (1996), Prediction and analysis of coiledcoil structures, Methods Enzymol. 266,513-525.
    • (1996) Methods Enzymol. , vol.266 , pp. 513-525
    • Lupas, A.1
  • 55
    • 0029086473 scopus 로고
    • Threading analysis suggests that the obese gene product may be a helical cytokine
    • MADEJ T., BOGUSKI M.S., BRYANT S.H. (1995), Threading analysis suggests that the obese gene product may be a helical cytokine, FEBS Lett. 373,13-18.
    • (1995) FEBS Lett. , vol.373 , pp. 13-18
    • Madej, T.1    Boguski, M.S.2    Bryant, S.H.3
  • 56
    • 0027608882 scopus 로고
    • Use of mass spectrometric molecular weight information to identify proteins in sequence databases
    • MANN, M., HOJRUP P., ROEPSTORFF P. (1993), Use of mass spectrometric molecular weight information to identify proteins in sequence databases, Biol.Mass Spectrom. 22,338-345.
    • (1993) Biol.Mass Spectrom. , vol.22 , pp. 338-345
    • Mann, M.1    Hojrup, P.2    Roepstorff, P.3
  • 57
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • NEEDLEMAN S.B., WUNSCH C. (1970), A general method applicable to the search for similarities in the amino acid sequence of two proteins, J. Mol.Biol. 48,443-453.
    • (1970) J. Mol.Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.2
  • 58
    • 0033044637 scopus 로고    scopus 로고
    • Machine learning approaches for the prediction of signal peptides and other protein sorting signals
    • NIELSEN H., BRUNAK S., VON HEIJNE G. (1999), Machine learning approaches for the prediction of signal peptides and other protein sorting signals,Protein Eng. 12,3-9.
    • (1999) Protein Eng. , vol.12 , pp. 3-9
    • Nielsen, H.1    Brunak, S.2    Von Heijne, G.3
  • 59
    • 0021691918 scopus 로고
    • An analysis of incorrectly folded protein models.Implications for structure predictions
    • NOVOTNY J., BRUCCOLERI R., KARPLUS M. (1984), An analysis of incorrectly folded protein models.Implications for structure predictions, J. Mol.Biol. 177,787-818.
    • (1984) J. Mol.Biol. , vol.177 , pp. 787-818
    • Novotny, J.1    Bruccoleri, R.2    Karplus, M.3
  • 60
    • 0026728019 scopus 로고
    • Construction of a dictionary of sequence motifs that characterize groups of related proteins
    • OGIWARA A., UCHIYAMA I., SETO Y., KANEHISA M. (1992), Construction of a dictionary of sequence motifs that characterize groups of related proteins, Protein Eng. 5,479-488.
    • (1992) Protein Eng. , vol.5 , pp. 479-488
    • Ogiwara, A.1    Uchiyama, I.2    Seto, Y.3    Kanehisa, M.4
  • 61
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • PAPPIN D.J.C., HOJRUP P., BLEASBY A.J. (1993). Rapid identification of proteins by peptide-mass fingerprinting. Curr. Biol. 3,327-332.
    • (1993) Curr. Biol. , vol.3 , pp. 327-332
    • Pappin, D.J.C.1    Hojrup, P.2    Bleasby, A.J.3
  • 62
    • 0033990061 scopus 로고    scopus 로고
    • Flexible sequence similarity' searching with the FASTA3 program package
    • PEARSON W.R. (2000). Flexible sequence similarity' searching with the FASTA3 program package. Methods Mol. Biol. 132,185-219.
    • (2000) Methods Mol. Biol. , vol.132 , pp. 185-219
    • Pearson, W.R.1
  • 63
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • PEARSON W.R., LIPMAN D.J. (1988), Improved tools for biological sequence comparison, Proc. Natl.Acad. Sci. USA 85,2444-2448.
    • (1988) Proc. Natl.Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 64
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • PERKINS D.N., PAPPIN D.J., CREASY D.M., COTTRELL J.S. (1999), Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20,3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 65
    • 0023803244 scopus 로고
    • Predicting the secondary structure of globular proteins using neural network models
    • QIAN, N., SEJNOWSTK T.J. (1988), Predicting the secondary structure of globular proteins using neural network models, J. Mol. Biol. 202,865-884.
    • (1988) J. Mol. Biol. , vol.202 , pp. 865-884
    • Qian, N.1    Sejnowstk, T.J.2
  • 66
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • RECHSTEINER M., ROGERS S.W. (1996). PEST sequences and regulation by proteolysis, Trends Biochem. Sci. 21,267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 67
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • RICHARDS F.M. (1977). Areas, volumes, packing and protein structure. Annu. Rev. Biophys. Bioeng. 6,151-175.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-175
    • Richards, F.M.1
  • 68
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile-based neural networks
    • ROST, B. (1996). PHD: Predicting one-dimensional protein structure by profile-based neural networks, Methods Enzymol. 266,525-539.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 69
  • 70
    • 0031577260 scopus 로고    scopus 로고
    • Protein fold recognition by prediction-based threading
    • ROST B., SCHNEIDER R., SANDER C. (1997), Protein fold recognition by prediction-based threading, J. Mol. Biol. 270,471-480.
    • (1997) J. Mol. Biol. , vol.270 , pp. 471-480
    • Rost, B.1    Schneider, R.2    Sander, C.3
  • 71
    • 0029951995 scopus 로고    scopus 로고
    • Protein fold recognition by mapping predicted secondary structures
    • RUSSEL R.B., COPELY R.R., BARTON G.J. (1996), Protein fold recognition by mapping predicted secondary structures, J. Mol. Biol. 259,349-365.
    • (1996) J. Mol. Biol. , vol.259 , pp. 349-365
    • Russel, R.B.1    Copely, R.R.2    Barton, G.J.3
  • 73
    • 0025670518 scopus 로고
    • Fragment peptide library for classification and functional prediction for proteins
    • SETO Y., IKEUCHI, Y., KANEHISA M. (1990), Fragment peptide library for classification and functional prediction for proteins, Proteins: Struct.Funct. Genet. 8,341-351.
    • (1990) Proteins: Struct.Funct. Genet. , vol.8 , pp. 341-351
    • Seto, Y.1    Ikeuchi, Y.2    Kanehisa, M.3
  • 75
    • 53249145476 scopus 로고    scopus 로고
    • Peptide sequencing by mass spectrometry for homology searches and cloning of genes
    • SHEVCHENKO A., WILM M., MANN M. (1997), Peptide sequencing by mass spectrometry for homology searches and cloning of genes, J. Protein Chem. 16,481-490.
    • (1997) J. Protein Chem. , vol.16 , pp. 481-490
    • Shevchenko, A.1    Wilm, M.2    Mann, M.3
  • 76
    • 0026704815 scopus 로고
    • Detection of nativelike models for amino acid sequences of unknown 3D structure
    • SIPPL M.J., WEITCKUS S., (1992), Detection of nativelike models for amino acid sequences of unknown 3D structure, Proteins 13,258-271.
    • (1992) Proteins , vol.13 , pp. 258-271
    • Sippl, M.J.1    Weitckus, S.2
  • 77
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • SMITH T.F., WATERMAN M.S. (1981), Identification of common molecular subsequences, J. Mol. Biol. 47,195-197.
    • (1981) J. Mol. Biol. , vol.47 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 78
    • 14744278850 scopus 로고
    • Predicting the solubility of recombinant proteins in Escherichia coli
    • WILKINSON D.L., HARRISON R.G. (1991), Predicting the solubility of recombinant proteins in Escherichia coli, Biotechnology 9,443-448.
    • (1991) Biotechnology , vol.9 , pp. 443-448
    • Wilkinson, D.L.1    Harrison, R.G.2
  • 80
    • 0033990113 scopus 로고    scopus 로고
    • PepTool and GeneTool: platform-independent tools for biological sequence analysis
    • WISHART D.S., STOTHARD P., VAN DOMSELAAR G.H. (2000), PepTool and GeneTool: platform-independent tools for biological sequence analysis, Methods Mol. Biol. 132,93-113.
    • (2000) Methods Mol. Biol. , vol.132 , pp. 93-113
    • Wishart, D.S.1    Stothard, P.2    Van Domselaar, G.H.3
  • 81
    • 0033621537 scopus 로고    scopus 로고
    • Mass spectrometry. From genomics to proteomics
    • YATES J.R. (2000), Mass spectrometry. From genomics to proteomics, Trends Genet. 16,5-8.
    • (2000) Trends Genet. , vol.16 , pp. 5-8
    • Yates, J.R.1
  • 82
    • 0030298218 scopus 로고    scopus 로고
    • Search of sequence databases with uninterpreted high-energy collision-induced dissociation spectra of peptides
    • YATES J.R., ENG, J.K., GLAUSER K.R., BULRINGAME A.L. (1996), Search of sequence databases with uninterpreted high-energy collision-induced dissociation spectra of peptides, J. Am. Soc. Mass Spect. 7,1089-1098.
    • (1996) J. Am. Soc. Mass Spect. , vol.7 , pp. 1089-1098
    • Yates, J.R.1    Eng, J.K.2    Glauser, K.R.3    Bulringame, A.L.4
  • 83
    • 0027375364 scopus 로고
    • Peptide mass maps - a highly informative approach to protein identification
    • YATES J.R., SPEICHER S., GRIFFIN P.R., HUNKAPILLER, T. (1993), Peptide mass maps - a highly informative approach to protein identification, Anal. Biochem. 214,397-408.
    • (1993) Anal. Biochem. , vol.214 , pp. 397-408
    • Yates, J.R.1    Speicher, S.2    Griffin, P.R.3    Hunkapiller, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.