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Volumn 134, Issue 2-3, 2001, Pages 103-116

Review: Prediction of in vivo fates of proteins in the era of genomics and proteomics

Author keywords

in vivo fates of proteins; Posttranslational modification; Prediction; Protein degradation; Subcellular localization

Indexed keywords

AMINO ACID; LIPID; MEMBRANE PROTEIN; PROTEIN; PROTEOME;

EID: 0035782686     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2001.4378     Document Type: Review
Times cited : (41)

References (130)
  • 1
    • 0034723134 scopus 로고    scopus 로고
    • Sequence signals for generation of antigenic peptides by the proteasome: Implications for proteasomal cleavage mechanism
    • Altuvia, Y., and Margalit, H. (2000) Sequence signals for generation of antigenic peptides by the proteasome: Implications for proteasomal cleavage mechanism. J. Mol. Biol. 295, 879-890.
    • (2000) J. Mol. Biol. , vol.295 , pp. 879-890
    • Altuvia, Y.1    Margalit, H.2
  • 2
    • 0034046248 scopus 로고    scopus 로고
    • Poor correspondence between predicted and experimental binding of peptides to class I MHC molecules
    • Anderson, M. H., Tan, L., Sondergaard, I., Zeuthen, J., Elliott, T., and Haurum, J. S. (2000) Poor correspondence between predicted and experimental binding of peptides to class I MHC molecules. Tissue Antigens 55, 519-531.
    • (2000) Tissue Antigens , vol.55 , pp. 519-531
    • Anderson, M.H.1    Tan, L.2    Sondergaard, I.3    Zeuthen, J.4    Elliott, T.5    Haurum, J.S.6
  • 3
    • 0028107155 scopus 로고
    • Statistical prediction of the locus of endoproteolytic cleavage of the nascent polypeptide in glycosylphosphatidylinositol-anchored proteins
    • Antony, A. C., and Miller, M. E. (1994) Statistical prediction of the locus of endoproteolytic cleavage of the nascent polypeptide in glycosylphosphatidylinositol-anchored proteins. Biochem. J. 298, 9-16.
    • (1994) Biochem. J. , vol.298 , pp. 9-16
    • Antony, A.C.1    Miller, M.E.2
  • 6
    • 0028685490 scopus 로고
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers
    • Bailey, T. L., and Elkan, C. (1994) Fitting a mixture model by expectation maximization to discover motifs in biopolymers. ISMB 2, 28-36.
    • (1994) ISMB , vol.2 , pp. 28-36
    • Bailey, T.L.1    Elkan, C.2
  • 7
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom, N., Gammeltoft, S., and 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
  • 8
    • 0034020087 scopus 로고    scopus 로고
    • Favourable side-chain orientation of cleavage site dibasic residues of prohormone in proteolytic processing by prohormone convertase 1/3
    • Brakch, N., Rholam, M., Simonetti, M., and Cohen, P. (2000) Favourable side-chain orientation of cleavage site dibasic residues of prohormone in proteolytic processing by prohormone convertase 1/3. Eur. J. Biochem. 267, 1626-1632.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1626-1632
    • Brakch, N.1    Rholam, M.2    Simonetti, M.3    Cohen, P.4
  • 9
    • 0034308219 scopus 로고    scopus 로고
    • Chloroplast transit peptides: Structure, function and evolution
    • Bruce, B. D. (2000) Chloroplast transit peptides: Structure, function and evolution. Trends Cell Biol. 10, 440-447.
    • (2000) Trends Cell Biol. , vol.10 , pp. 440-447
    • Bruce, B.D.1
  • 10
    • 0031811850 scopus 로고    scopus 로고
    • MHCPEP, a database of MHC-binding peptides: Update 1997
    • Brusic, V., Rudy, G., and Harrison, L. C. (1998a) MHCPEP, a database of MHC-binding peptides: Update 1997. Nucleic Acids Res. 26, 368-371.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 368-371
    • Brusic, V.1    Rudy, G.2    Harrison, L.C.3
  • 11
    • 0031825709 scopus 로고    scopus 로고
    • Prediction of MHC class II-binding peptides using an evolutionary algorithm and artificial neural network
    • Brusic, V., Rudy, G., Honeyman, M., Hammer, J., and Harrison, L. (1998b) Prediction of MHC class II-binding peptides using an evolutionary algorithm and artificial neural network. Bioinformatics 14, 121-130.
    • (1998) Bioinformatics , vol.14 , pp. 121-130
    • Brusic, V.1    Rudy, G.2    Honeyman, M.3    Hammer, J.4    Harrison, L.5
  • 12
    • 0033118895 scopus 로고    scopus 로고
    • Description and prediction of peptide MHC binding: The 'human MHC project.'
    • Buus, S. (1999) Description and prediction of peptide MHC binding: The 'human MHC project.' Curr. Opin. Immunol. 11, 209-213.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 209-213
    • Buus, S.1
  • 13
    • 15444346372 scopus 로고    scopus 로고
    • In silico identification of glycosylphosphatidylinositol-anchored plasma-membrane and cell wall proteins of Saccharomyces cerevisiae
    • Caro, L. H., Tettelin, H., Vossen, J. H., Ram, A. F., van den Ende, H., and Klis, F. M. (1997) In silico identification of glycosylphosphatidylinositol-anchored plasma-membrane and cell wall proteins of Saccharomyces cerevisiae. Yeast 13, 1477-1489.
    • (1997) Yeast , vol.13 , pp. 1477-1489
    • Caro, L.H.1    Tettelin, H.2    Vossen, J.H.3    Ram, A.F.4    Van den Ende, H.5    Klis, F.M.6
  • 14
    • 0031588694 scopus 로고    scopus 로고
    • Relation between amino acid composition and cellular location of proteins
    • Cedano, J., Aloy, P., Perez-Pons, J. A., and Querol, E. (1997) Relation between amino acid composition and cellular location of proteins. J. Mol. Biol. 266, 594-600.
    • (1997) J. Mol. Biol. , vol.266 , pp. 594-600
    • Cedano, J.1    Aloy, P.2    Perez-Pons, J.A.3    Querol, E.4
  • 15
    • 0035030201 scopus 로고    scopus 로고
    • Using subsite coupling to predict signal peptides
    • Chou, K.-C. (2001) Using subsite coupling to predict signal peptides. Protein Eng. 14, 75-79.
    • (2001) Protein Eng. , vol.14 , pp. 75-79
    • Chou, K.-C.1
  • 16
    • 0032501152 scopus 로고    scopus 로고
    • Using discriminant function for prediction of subcellular location of prokaryotic proteins
    • Chou, K. C., and Elrod, D. W. (1998) Using discriminant function for prediction of subcellular location of prokaryotic proteins. Biochem. Biophys. Res. Commun. 252, 63-68.
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 63-68
    • Chou, K.C.1    Elrod, D.W.2
  • 17
    • 0032940342 scopus 로고    scopus 로고
    • Protein subcellular location prediction
    • Chou, K. C., and Elrod, D. W. (1999a) Protein subcellular location prediction. Protein Eng. 12, 107-118.
    • (1999) Protein Eng. , vol.12 , pp. 107-118
    • Chou, K.C.1    Elrod, D.W.2
  • 18
    • 0032910566 scopus 로고    scopus 로고
    • Prediction of membrane protein types and subcellular locations
    • Chou, K. C., and Elrod, D. W. (1999b) Prediction of membrane protein types and subcellular locations. Proteins 34, 137-153.
    • (1999) Proteins , vol.34 , pp. 137-153
    • Chou, K.C.1    Elrod, D.W.2
  • 19
    • 13044294041 scopus 로고    scopus 로고
    • A database analysis of potential glycosylating Asn-X-Ser/Thr consensus sequences
    • Christlet, T. H., Biswas, M., and Veluraja, K. (1999) A database analysis of potential glycosylating Asn-X-Ser/Thr consensus sequences. Acta Crystallogr. Sect. D Biol. Crystallogr. 55(Pt. 8), 1414-1420.
    • (1999) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.55 , Issue.PART 8 , pp. 1414-1420
    • Christlet, T.H.1    Biswas, M.2    Veluraja, K.3
  • 21
    • 0035170507 scopus 로고    scopus 로고
    • GlycoSuiteDB: A new curated relational database of glycoprotein glycan structures and their biological sources
    • Cooper, C. A., Harrison, M. J., Wilkins, M. R., and Packer, N. H. (2001) GlycoSuiteDB: A new curated relational database of glycoprotein glycan structures and their biological sources. Nucleic Acids Res. 29, 332-335.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 332-335
    • Cooper, C.A.1    Harrison, M.J.2    Wilkins, M.R.3    Packer, N.H.4
  • 23
    • 0031883733 scopus 로고    scopus 로고
    • Lysosomes, a meeting point of proteins, chaperones, and proteases
    • Cuervo, A. M., and Dice, J. F. (1998) Lysosomes, a meeting point of proteins, chaperones, and proteases. J. Mol. Med. 76, 6-12.
    • (1998) J. Mol. Med. , vol.76 , pp. 6-12
    • Cuervo, A.M.1    Dice, J.F.2
  • 25
    • 0026029553 scopus 로고
    • Consensus sequence for processing of peptide precursors at monobasic sites
    • Devi, L. (1991) Consensus sequence for processing of peptide precursors at monobasic sites. FEBS Lett. 280, 189-194.
    • (1991) FEBS Lett. , vol.280 , pp. 189-194
    • Devi, L.1
  • 26
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice, J. F. (1990) Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem. Sci. 15, 305-309.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 28
    • 0034714135 scopus 로고    scopus 로고
    • A Bayesian system integrating expression data with sequence patterns for localizing proteins: Comprehensive application to the yeast genome
    • Drawid, A., and Gerstein, M. (2000) A Bayesian system integrating expression data with sequence patterns for localizing proteins: Comprehensive application to the yeast genome. J. Mol. Biol. 301, 1059-1075.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1059-1075
    • Drawid, A.1    Gerstein, M.2
  • 29
    • 0034307634 scopus 로고    scopus 로고
    • Genome-wide analysis relating expression level with protein subcellular localization
    • Drawid, A., Jansen, R., and Gerstein, M. (2000) Genome-wide analysis relating expression level with protein subcellular localization. Trends Genet. 16, 426-430.
    • (2000) Trends Genet. , vol.16 , pp. 426-430
    • Drawid, A.1    Jansen, R.2    Gerstein, M.3
  • 30
    • 0031887946 scopus 로고    scopus 로고
    • Wanted: Subcellular localization of proteins based on sequence
    • Eisenhaber, F., and Bork, P. (1998) Wanted: Subcellular localization of proteins based on sequence. Trends Cell Biol. 8, 169-170.
    • (1998) Trends Cell Biol. , vol.8 , pp. 169-170
    • Eisenhaber, F.1    Bork, P.2
  • 31
    • 0032409445 scopus 로고    scopus 로고
    • Sequence properties of GPI-anchored proteins near the omega-site: Constraints for the polypeptide binding site of the putative transamidase
    • Eisenhaber, B., Bork, P., and Eisenhaber, F. (1998) Sequence properties of GPI-anchored proteins near the omega-site: constraints for the polypeptide binding site of the putative transamidase. Protein Eng. 11, 1155-1161.
    • (1998) Protein Eng. , vol.11 , pp. 1155-1161
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 32
    • 0033600935 scopus 로고    scopus 로고
    • Prediction of potential GPI-modification sites in proprotein sequences
    • Eisenhaber, B., Bork, P., and Eisenhaber, F. (1999) Prediction of potential GPI-modification sites in proprotein sequences. J. Mol. Biol. 292, 741-758.
    • (1999) J. Mol. Biol. , vol.292 , pp. 741-758
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 34
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson, O., Nielsen, H., and von Heijne, G. (1999) ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 8, 978-984.
    • (1999) Protein Sci. , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 35
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson, O., Nielsen, H., Brunak, S., and von Heijne, G. (2000) Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 300, 1005-1016.
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 36
    • 0028344533 scopus 로고
    • Structure of peptides associated with class I and class II MHC molecules
    • Engelhard, V. H. (1994) Structure of peptides associated with class I and class II MHC molecules. Annu. Rev. Immunol. 12, 181-207.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 181-207
    • Engelhard, V.H.1
  • 38
    • 0033957839 scopus 로고    scopus 로고
    • The Resid database of protein structure modifications: 2000 update
    • Garavelli, J. S. (2000) The Resid database of protein structure modifications: 2000 update. Nucleic Acids Res. 28, 209-211.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 209-211
    • Garavelli, J.S.1
  • 39
    • 0035162787 scopus 로고    scopus 로고
    • The Resid database of protein structure modifications and the NRL-3D sequence-structure database
    • Garavelli, J. S., Hou, Z., Pattabiraman, N., and Stephens, R. M. (2001) The Resid database of protein structure modifications and the NRL-3D sequence-structure database. Nucleic Acids Res. 29, 199-201.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 199-201
    • Garavelli, J.S.1    Hou, Z.2    Pattabiraman, N.3    Stephens, R.M.4
  • 40
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel, Y., and von Heijne, G. (1990) Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering. Protein Eng. 3, 433-442.
    • (1990) Protein Eng. , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 42
    • 0031576987 scopus 로고    scopus 로고
    • Two complementary methods for predicting peptidases binding major histocompatibility complex molecules
    • Gulukota, K., Sidney, J., Sette, A., and DeLisi, C. (1997) Two complementary methods for predicting peptidases binding major histocompatibility complex molecules. J. Mol. Biol. 267, 1258-1267.
    • (1997) J. Mol. Biol. , vol.267 , pp. 1258-1267
    • Gulukota, K.1    Sidney, J.2    Sette, A.3    DeLisi, C.4
  • 43
    • 0032919585 scopus 로고    scopus 로고
    • O-GLYCBASE version 4.0: A revised database of O-glycosylated proteins
    • Gupta, R., Birch, H., Rapacki, K., Brunak, S., and Hansen, J. E. (1999a) O-GLYCBASE version 4.0: A revised database of O-glycosylated proteins. Nucleic Acids Res. 27, 370-372.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 370-372
    • Gupta, R.1    Birch, H.2    Rapacki, K.3    Brunak, S.4    Hansen, J.E.5
  • 44
    • 0032828561 scopus 로고    scopus 로고
    • Scanning the available Dictyostelium discoideum proteome for O-linked GlcNAc glycosylation sites using neural networks
    • Gupta, R., Jung, E., Gooley, A. A., Williams, K. L., Brunak, S., and Hansen, J. (1999b) Scanning the available Dictyostelium discoideum proteome for O-linked GlcNAc glycosylation sites using neural networks. Glycobiology 9, 1009-1022.
    • (1999) Glycobiology , vol.9 , pp. 1009-1022
    • Gupta, R.1    Jung, E.2    Gooley, A.A.3    Williams, K.L.4    Brunak, S.5    Hansen, J.6
  • 45
    • 0031922234 scopus 로고    scopus 로고
    • Screening for glycosilphosphatidylinositol (GPI)-dependent cell wall proteins in Saccharomyces cerevisiae
    • Hamada, K., Fukuchi, S., Arisawa, M., Baba, M., and Kitada, K. (1998) Screening for glycosilphosphatidylinositol (GPI)-dependent cell wall proteins in Saccharomyces cerevisiae. Mol. Gen. Genet. 258, 53-59.
    • (1998) Mol. Gen. Genet. , vol.258 , pp. 53-59
    • Hamada, K.1    Fukuchi, S.2    Arisawa, M.3    Baba, M.4    Kitada, K.5
  • 46
    • 0029003322 scopus 로고
    • Prediction of O-glycosylation of mammalian proteins: Specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
    • Hansen, J. E., Lund, O., Engelbrecht, J., Bohr, H., Nielsen, J. O., and Hansen, J. E. (1995) Prediction of O-glycosylation of mammalian proteins: Specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. Biochem. J. 308(Pt. 3), 801-813.
    • (1995) Biochem. J. , vol.308 , Issue.PART 3 , pp. 801-813
    • Hansen, J.E.1    Lund, O.2    Engelbrecht, J.3    Bohr, H.4    Nielsen, J.O.5    Hansen, J.E.6
  • 47
    • 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., Gooley, A. A., Williams, K. L., and 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    Gooley, A.A.4    Williams, K.L.5    Brunak, S.6
  • 48
    • 0033106369 scopus 로고    scopus 로고
    • Gettin' down with ubiquitin: Turning off cell-surface receptors, transporters and channels
    • Hicke, L. (1999) Gettin' down with ubiquitin: Turning off cell-surface receptors, transporters and channels. Trends Cell Biol. 9, 107-112.
    • (1999) Trends Cell Biol. , vol.9 , pp. 107-112
    • Hicke, L.1
  • 49
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke, L., and Riezman, H. (1996) Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84, 277-287.
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 50
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • Hilt, W., and Wolf, D. H. (1996) Proteasomes: Destruction as a programme. Trends Biochem. Sci. 21, 96-102.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 51
    • 0034725918 scopus 로고    scopus 로고
    • Biochemistry. All in the ubiquitin family
    • Hochstrasser, M. (2000) Biochemistry. All in the ubiquitin family. Science 289, 563-564.
    • (2000) Science , vol.289 , pp. 563-564
    • Hochstrasser, M.1
  • 53
    • 0033529034 scopus 로고    scopus 로고
    • Protein modification: Docking sites for kinases
    • Holland, P. M., and Cooper, J. A. (1999) Protein modification: Docking sites for kinases. Curr. Biol. 9, R329-R331.
    • (1999) Curr. Biol. , vol.9
    • Holland, P.M.1    Cooper, J.A.2
  • 54
    • 0345291184 scopus 로고    scopus 로고
    • A theoretical approach towards the identification of cleavage-determining amino acid motifs of the 20 S proteasome
    • Holzhütter, H. G., Frömmel, C., and Kloetzel, P. M. (1999) A theoretical approach towards the identification of cleavage-determining amino acid motifs of the 20 S proteasome. J. Mol. Biol. 286, 1251-1265.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1251-1265
    • Holzhütter, H.G.1    Frömmel, C.2    Kloetzel, P.M.3
  • 55
    • 0032577051 scopus 로고    scopus 로고
    • The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: Its role in cell growth and disease
    • Hunter, T. (1998) The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: Its role in cell growth and disease. Philos. Trans. R. Soc. London B Biol. Sci. 353, 583-605.
    • (1998) Philos. Trans. R. Soc. London B Biol. Sci. , vol.353 , pp. 583-605
    • Hunter, T.1
  • 56
    • 0034119780 scopus 로고    scopus 로고
    • Adaptive encoding neural networks for the recognition of human signal peptide cleavage sites
    • Jagla, B., and Schuchhardt, J. (2000) Adaptive encoding neural networks for the recognition of human signal peptide cleavage sites. Bioinformatics 16, 245-250.
    • (2000) Bioinformatics , vol.16 , pp. 245-250
    • Jagla, B.1    Schuchhardt, J.2
  • 57
    • 0034041537 scopus 로고    scopus 로고
    • Nuclear targeting signal recognition: A key control point in nuclear transport?
    • Jans, D. A., Xiao, C.-Y., and Lam, M. H. C. (2000) Nuclear targeting signal recognition: A key control point in nuclear transport? BioEssays 22, 532-544.
    • (2000) BioEssays , vol.22 , pp. 532-544
    • Jans, D.A.1    Xiao, C.-Y.2    Lam, M.H.C.3
  • 58
    • 0035171080 scopus 로고    scopus 로고
    • Kabat Database and its applications: Future directions
    • Johnson, G., and Wu, T. T. (2001) Kabat Database and its applications: Future directions. Nucleic Acids Res. 29, 205-206.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 205-206
    • Johnson, G.1    Wu, T.T.2
  • 59
    • 0032560489 scopus 로고    scopus 로고
    • The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases
    • Johnson, L. N., Lowe, E. D., Noble, M., and Owen, D. J. (1998a) The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases. FEBS Lett. 430, 1-11.
    • (1998) FEBS Lett. , vol.430 , pp. 1-11
    • Johnson, L.N.1    Lowe, E.D.2    Noble, M.3    Owen, D.J.4
  • 60
    • 0032563319 scopus 로고    scopus 로고
    • Degradation signal masking by heterodimerization of MATα2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway
    • Johnson, P. R., Swanson, R., Rakhilina, L., and Hochstrasser, M. (1998b) Degradation signal masking by heterodimerization of MATα2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway. Cell 94, 217-227.
    • (1998) Cell , vol.94 , pp. 217-227
    • Johnson, P.R.1    Swanson, R.2    Rakhilina, L.3    Hochstrasser, M.4
  • 61
    • 0032522587 scopus 로고    scopus 로고
    • Rules for the addition of O-linked N-acetylglucosamine to secreted proteins in Dictyostelium discoideum: In vivo studies on glycosylation of mucin MUC1 and MUC2 repeats
    • Jung, E., Gooley, A. A., Packer, N. H., Karuso, P., and Williams, K. L. (1998) Rules for the addition of O-linked N-acetylglucosamine to secreted proteins in Dictyostelium discoideum: In vivo studies on glycosylation of mucin MUC1 and MUC2 repeats. Eur. J. Biochem. 253, 517-524.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 517-524
    • Jung, E.1    Gooley, A.A.2    Packer, N.H.3    Karuso, P.4    Williams, K.L.5
  • 62
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian, J. A., and von Heijne, G. (2000) How proteins adapt to a membrane-water interface. Trends Biochem. Sci. 25, 429-434.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 429-434
    • Killian, J.A.1    Von Heijne, G.2
  • 63
    • 0030949874 scopus 로고    scopus 로고
    • ER quality control: The cytoplasmic connection
    • Kopito, R. R. (1997) ER quality control: The cytoplasmic connection. Cell 88, 427-430.
    • (1997) Cell , vol.88 , pp. 427-430
    • Kopito, R.R.1
  • 64
    • 0032560583 scopus 로고    scopus 로고
    • Statistical analysis of protein kinase specificity determinants
    • Kreegipuu, A., Blom, N., Brunak, S., and Jarv, J. (1998) Statistical analysis of protein kinase specificity determinants. FEBS Lett. 430, 45-50.
    • (1998) FEBS Lett. , vol.430 , pp. 45-50
    • Kreegipuu, A.1    Blom, N.2    Brunak, S.3    Jarv, J.4
  • 65
    • 0032922002 scopus 로고    scopus 로고
    • PhosphoBase, a database of phosphorylation sites: Release 2.0
    • Kreegipuu, A., Blom, N., and Brunak, S. (1999) PhosphoBase, a database of phosphorylation sites: Release 2.0. Nucleic Acids Res. 27, 237-239.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 237-239
    • Kreegipuu, A.1    Blom, N.2    Brunak, S.3
  • 66
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J. Mol. Biol. 305, 567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 68
    • 0033953050 scopus 로고    scopus 로고
    • Large-scale predictions of secretory proteins from mammalian genomic and EST sequences
    • Ladunga, I. (2000) Large-scale predictions of secretory proteins from mammalian genomic and EST sequences. Curr. Opin. Biotechnol. 11, 13-18.
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 13-18
    • Ladunga, I.1
  • 69
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • Laney, J. D., and Hochstrasser, M. (1999) Substrate targeting in the ubiquitin system. Cell 97, 427-430.
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 70
    • 0035166917 scopus 로고    scopus 로고
    • IMGT, the international ImMunoGeneTics database
    • Lefranc, M.-P. (2001) IMGT, the international ImMunoGeneTics database. Nucleic Acids Res. 29, 207-209.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 207-209
    • Lefranc, M.-P.1
  • 72
    • 0030928254 scopus 로고    scopus 로고
    • An iterative algorithm for converting a class II MHC binding motif into a quantitative prediction model
    • Mallios, R. R. (1997) An iterative algorithm for converting a class II MHC binding motif into a quantitative prediction model. Comput. Appl. Biosci. 13, 211-215.
    • (1997) Comput. Appl. Biosci. , vol.13 , pp. 211-215
    • Mallios, R.R.1
  • 74
    • 0032510739 scopus 로고    scopus 로고
    • The amino acid following an Asn-X-Ser/Thr sequon is an important determinant of N-linked core glycosylation efficiency
    • Mellquist, J. L., Kasturi, L., Spitalnik, S. L., and Shakin-Eshleman, S. H. (1998) The amino acid following an Asn-X-Ser/Thr sequon is an important determinant of N-linked core glycosylation efficiency. Biochemistry 37, 6833-6837.
    • (1998) Biochemistry , vol.37 , pp. 6833-6837
    • Mellquist, J.L.1    Kasturi, L.2    Spitalnik, S.L.3    Shakin-Eshleman, S.H.4
  • 75
    • 0034495418 scopus 로고    scopus 로고
    • A collection of well characterized integral membrane proteins
    • Möller, S., Kriventseva, E. V., and Apweiler, R. (2000) A collection of well characterized integral membrane proteins. Bioinformatics 16, 1159-1160.
    • (2000) Bioinformatics , vol.16 , pp. 1159-1160
    • Möller, S.1    Kriventseva, E.V.2    Apweiler, R.3
  • 76
    • 0034710302 scopus 로고    scopus 로고
    • Protein kinases and phosphatases in the Drosophila genome
    • Morrison, D. K., Murakami, M. S., and Cleghon, V. (2000) Protein kinases and phosphatases in the Drosophila genome. J. Cell Biol. 150, F57-F62.
    • (2000) J. Cell Biol. , vol.150
    • Morrison, D.K.1    Murakami, M.S.2    Cleghon, V.3
  • 77
    • 0005946413 scopus 로고    scopus 로고
    • Intracellular transport of GPI-anchored proteins
    • Muniz, M., and Riezman, H. (2000) Intracellular transport of GPI-anchored proteins. EMBO J. 19, 10-15.
    • (2000) EMBO J. , vol.19 , pp. 10-15
    • Muniz, M.1    Riezman, H.2
  • 78
    • 0033909566 scopus 로고    scopus 로고
    • Protein sorting signals and prediction of subcellular localization
    • Nakai, K. (2000) Protein sorting signals and prediction of subcellular localization. Adv. Protein Chem. 54, 277-344.
    • (2000) Adv. Protein Chem. , vol.54 , pp. 277-344
    • Nakai, K.1
  • 79
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai, K., and Horton, P. (1999) PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 24, 34-35.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-35
    • Nakai, K.1    Horton, P.2
  • 80
    • 0024120457 scopus 로고
    • Prediction of in vivo modification sites of proteins from their primary structures
    • Nakai, K., and Kanehisa, M. (1988) Prediction of in vivo modification sites of proteins from their primary structures. J. Biochem. 104, 693-699.
    • (1988) J. Biochem. , vol.104 , pp. 693-699
    • Nakai, K.1    Kanehisa, M.2
  • 81
    • 0025933503 scopus 로고
    • Expert system for predicting protein localization sites in gram-negative bacteria
    • Nakai, K., and Kanehisa, M. (1991) Expert system for predicting protein localization sites in gram-negative bacteria. Proteins Struct. Funct. Genet. 11, 95-110.
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 95-110
    • Nakai, K.1    Kanehisa, M.2
  • 82
    • 0027105007 scopus 로고
    • A knowledge base for predicting protein localization sites in eukaryotic cells
    • Nakai, K., and Kanehisa, M. (1992) A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics 14, 897-911.
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 83
    • 0028239038 scopus 로고
    • Discrimination of intracellular and extracellular proteins using amino acid composition and residue-pair frequencies
    • Nakashima, H., and Nishikawa, K. (1994) Discrimination of intracellular and extracellular proteins using amino acid composition and residue-pair frequencies. J. Mol. Biol. 238, 54-61.
    • (1994) J. Mol. Biol. , vol.238 , pp. 54-61
    • Nakashima, H.1    Nishikawa, K.2
  • 84
    • 0033214738 scopus 로고    scopus 로고
    • Protein farnesylation in plants: A greasy tale
    • Nambara, E., and McCourt, P. (1999) Protein farnesylation in plants: A greasy tale. Curr. Opin. Plant Biol. 2, 398-392.
    • (1999) Curr. Opin. Plant Biol. , vol.2 , pp. 398-392
    • Nambara, E.1    McCourt, P.2
  • 85
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S., and von Heijne, G. (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10, 1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 86
    • 0033044637 scopus 로고    scopus 로고
    • Machine learning approaches for the prediction of signal peptides and other protein sorting signals
    • Nielsen, H., Brunak, S., and 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
  • 87
    • 0032185234 scopus 로고    scopus 로고
    • Forced transmembrane orientation of hydrophilic polypeptide segments in multispanning membrane proteins
    • Ota, K., Sakaguchi, M., von Heijne, G., Hamasaki, N., and Mihara, K. (1998) Forced transmembrane orientation of hydrophilic polypeptide segments in multispanning membrane proteins. Mol. Cell 2, 495-503.
    • (1998) Mol. Cell , vol.2 , pp. 495-503
    • Ota, K.1    Sakaguchi, M.2    Von Heijne, G.3    Hamasaki, N.4    Mihara, K.5
  • 88
    • 0034659815 scopus 로고    scopus 로고
    • Proteomics to study genes and genomes
    • Pandey, A., and Mann, M. (2000) Proteomics to study genes and genomes. Nature 405, 837-846.
    • (2000) Nature , vol.405 , pp. 837-846
    • Pandey, A.1    Mann, M.2
  • 89
    • 0028052724 scopus 로고
    • Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual peptide side-chains
    • Parker, K. C., Bednarek, M. A., and Coligan, J. E. (1994) Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual peptide side-chains. J. Immunol. 152, 163-175.
    • (1994) J. Immunol. , vol.152 , pp. 163-175
    • Parker, K.C.1    Bednarek, M.A.2    Coligan, J.E.3
  • 90
    • 0034657712 scopus 로고    scopus 로고
    • Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation
    • Parodi, A. J. (2000) Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation. Biochem. J. 348(Pt. 1), 1-13.
    • (2000) Biochem. J. , vol.348 , Issue.PART 1 , pp. 1-13
    • Parodi, A.J.1
  • 91
    • 0032249156 scopus 로고    scopus 로고
    • Cell walls: Structures and signals
    • Pennel, R. (1998) Cell walls: Structures and signals. Curr. Opin. Plant Biol. 1, 504-510.
    • (1998) Curr. Opin. Plant Biol. , vol.1 , pp. 504-510
    • Pennel, R.1
  • 92
    • 0032937844 scopus 로고    scopus 로고
    • A statistical analysis of N- and O-glycan linkage conformations from crystallographic data
    • Petrescu, A. J., Petrescu, S. M., Dwek, R. A., and Wormald, M. R. (1999) A statistical analysis of N- and O-glycan linkage conformations from crystallographic data. Glycobiology 9, 343-352.
    • (1999) Glycobiology , vol.9 , pp. 343-352
    • Petrescu, A.J.1    Petrescu, S.M.2    Dwek, R.A.3    Wormald, M.R.4
  • 93
    • 0034214123 scopus 로고    scopus 로고
    • Protein sorting: Recognizing mitochondrial presequences
    • Pfanner, N. (2000) Protein sorting: Recognizing mitochondrial presequences. Curr. Biol. 10, R412-R415.
    • (2000) Curr. Biol. , vol.10
    • Pfanner, N.1
  • 97
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M., and 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
  • 98
    • 0032077533 scopus 로고    scopus 로고
    • Using neural networks for prediction of the subcellular location of proteins
    • Reinhardt, A., and Hubbard, T. (1998) Using neural networks for prediction of the subcellular location of proteins. Nucleic Acids Res. 26, 2230-2236.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2230-2236
    • Reinhardt, A.1    Hubbard, T.2
  • 99
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh, M. D. (1999) Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451, 1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 100
    • 0028797003 scopus 로고
    • Role of amino acid sequence flanking dibasic cleavage sites in precursor proteolytic processing. The importance of the first residue C-terminal of the cleavage site
    • Rholam, M., Brakch, N., Germain, D., Thomas, D. Y., Fahy, C., Boussetta, H., Boileau, G., and Cohen, P. (1995) Role of amino acid sequence flanking dibasic cleavage sites in precursor proteolytic processing. The importance of the first residue C-terminal of the cleavage site. Eur. J. Biochem. 227, 707-714.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 707-714
    • Rholam, M.1    Brakch, N.2    Germain, D.3    Thomas, D.Y.4    Fahy, C.5    Boussetta, H.6    Boileau, G.7    Cohen, P.8
  • 101
    • 0035161548 scopus 로고    scopus 로고
    • IMGT/HLA database - A sequence database for the human major histocompatibility complex
    • Robinson, J., Waller, M. J., Parham, P., Bodmer, J. G., and Marsh, S. G. E. (2001) IMGT/HLA database - A sequence database for the human major histocompatibility complex. Nucleic Acids Res. 29, 210-213.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 210-213
    • Robinson, J.1    Waller, M.J.2    Parham, P.3    Bodmer, J.G.4    Marsh, S.G.E.5
  • 102
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • Rock, K. L., and Goldberg, A. L. (1999) Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu. Rev. Immunol. 17, 739-779.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 739-779
    • Rock, K.L.1    Goldberg, A.L.2
  • 103
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers, S., Wells, R., and Rechsteiner, M. (1986) Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis. Science 234, 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 104
    • 0033118642 scopus 로고    scopus 로고
    • Genome annotation: Which tools do we have for it?
    • Rouze, P., Pavy, N., and Rombauts, S. (1999) Genome annotation: Which tools do we have for it? Curr. Opin. Plant Biol. 2, 90-95.
    • (1999) Curr. Opin. Plant Biol. , vol.2 , pp. 90-95
    • Rouze, P.1    Pavy, N.2    Rombauts, S.3
  • 106
    • 0032817742 scopus 로고    scopus 로고
    • How many potentially secreted proteins are contained in a bacterial genome?
    • Schneider, G. (1999) How many potentially secreted proteins are contained in a bacterial genome? Gene 237, 113-121.
    • (1999) Gene , vol.237 , pp. 113-121
    • Schneider, G.1
  • 107
  • 108
    • 0034630098 scopus 로고    scopus 로고
    • Recent advances in the study of prenylated proteins
    • Sinensky, M. (2000) Recent advances in the study of prenylated proteins. Biochim. Biophys. Acta 1484, 93-106.
    • (2000) Biochim. Biophys. Acta , vol.1484 , pp. 93-106
    • Sinensky, M.1
  • 110
    • 0034650295 scopus 로고    scopus 로고
    • ADEPTs: Information necessary for subcellular distribution of eukaryotic sorting isozymes resides in domains missing from eubacterial and archaeal counterparts
    • Stanford, D. R., Martin, N. C., and Hopper, A. K. (2000) ADEPTs: Information necessary for subcellular distribution of eukaryotic sorting isozymes resides in domains missing from eubacterial and archaeal counterparts. Nucleic Acids Res. 28, 383-392.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 383-392
    • Stanford, D.R.1    Martin, N.C.2    Hopper, A.K.3
  • 111
    • 0027078415 scopus 로고
    • The new enzymology of precursor processing endopeptidases
    • Steiner, D. F., Smeekens, S. P., Ohagi, S., and Chan, S. J. (1992) The new enzymology of precursor processing endopeptidases. J. Biol. Chem. 267, 23435-23438.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23435-23438
    • Steiner, D.F.1    Smeekens, S.P.2    Ohagi, S.3    Chan, S.J.4
  • 112
    • 0033231281 scopus 로고    scopus 로고
    • Degradation signals in the lysine-asparagine sequence space
    • Suzuki, T., and Varshavsky, A. (1999) Degradation signals in the lysine-asparagine sequence space. EMBO J. 18, 6017-6026.
    • (1999) EMBO J. , vol.18 , pp. 6017-6026
    • Suzuki, T.1    Varshavsky, A.2
  • 113
    • 0031716649 scopus 로고    scopus 로고
    • The proteasome: A protein-destroying machine
    • Tanaka, K., and Chiba, T. (1998) The proteasome: A protein-destroying machine. Genes Cells 3, 499-510.
    • (1998) Genes Cells , vol.3 , pp. 499-510
    • Tanaka, K.1    Chiba, T.2
  • 114
    • 0033937939 scopus 로고    scopus 로고
    • Multiple pathways allow protein secretion across the bacterial outer membrane
    • Thanassi, D. G., and Hultgren, S. J. (2000) Multiple pathways allow protein secretion across the bacterial outer membrane. Curr. Opin. Cell Biol. 12, 420-430.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 420-430
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 115
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: Application to topology prediction
    • Tusnády, 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
    • Tusnády, G.E.1    Simon, I.2
  • 117
    • 0033118158 scopus 로고    scopus 로고
    • Specificity of the proteasome and the TAP transporter
    • Uebel, S., and Tampé, R. (1999) Specificity of the proteasome and the TAP transporter. Curr. Opin. Immunol. 11, 203-208.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 203-208
    • Uebel, S.1    Tampé, R.2
  • 119
    • 0034057802 scopus 로고    scopus 로고
    • Membrane topology and insertion of membrane proteins: Search for topogenic signals
    • van Geest, M., and Lolkema, J. S. (2000) Membrane topology and insertion of membrane proteins: Search for topogenic signals. Microbiol. Mol. Biol. Rev. 64, 13-33.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 13-33
    • Van Geest, M.1    Lolkema, J.S.2
  • 120
    • 0027111729 scopus 로고
    • 1H NMR database computer program for the analysis of the primary structure of complex carbohydrates
    • 1H NMR database computer program for the analysis of the primary structure of complex carbohydrates. Carbohydr. Res. 235, 53-68.
    • (1992) Carbohydr. Res. , vol.235 , pp. 53-68
    • Van Kuik, J.A.1    Hard, K.2    Vliegenthart, J.F.3
  • 121
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky, A. (1996) The N-end rule: Functions, mysteries, uses. Proc. Natl Acad. Sci. USA 93, 12142-12149.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 122
    • 0030632048 scopus 로고    scopus 로고
    • The N-end rule pathway of protein degradation
    • Varshavsky, A. (1997) The N-end rule pathway of protein degradation. Genes Cells 2, 13-28.
    • (1997) Genes Cells , vol.2 , pp. 13-28
    • Varshavsky, A.1
  • 123
    • 0033695299 scopus 로고    scopus 로고
    • Proteolysis in MHC class II antigen presentation: Who's in charge?
    • Villadangos, J. A., and Ploegh, H. L. (2000) Proteolysis in MHC class II antigen presentation: Who's in charge? Immunity 12, 233-239.
    • (2000) Immunity , vol.12 , pp. 233-239
    • Villadangos, J.A.1    Ploegh, H.L.2
  • 124
    • 0033956278 scopus 로고    scopus 로고
    • Calpain and caspase: Can you tell the difference?
    • Wang, K. K. W. (2000) Calpain and caspase: Can you tell the difference? Trends Neurosci. 23, 20-26.
    • (2000) Trends Neurosci. , vol.23 , pp. 20-26
    • Wang, K.K.W.1
  • 125
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner, S., Maurizi, M. R., and Gottesman, S. (1999) Posttranslational quality control: Folding, refolding, and degrading proteins. Science 286, 1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 126
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • Wilkinson, K. D. (2000) Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome. Semin. Cell Dev. Biol. 11, 141-148.
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 127
    • 0025865091 scopus 로고
    • Amino acid distributions around O-linked glycosylation sites
    • Wilson, I. B., Gavel, Y., and von Heijne, G. (1991) Amino acid distributions around O-linked glycosylation sites. Biochem. J. 275(Pt. 2), 529-534.
    • (1991) Biochem. J. , vol.275 , Issue.PART. 2 , pp. 529-534
    • Wilson, I.B.1    Gavel, Y.2    Von Heijne, G.3
  • 128
    • 0032863016 scopus 로고    scopus 로고
    • Sequence pattern for the occurrence of N-glycosylation in proteins
    • Yan, B., Zhang, W., Ding, J., and Gao, P. (1999) Sequence pattern for the occurrence of N-glycosylation in proteins. J. Protein Chem. 18, 511-521.
    • (1999) J. Protein Chem. , vol.18 , pp. 511-521
    • Yan, B.1    Zhang, W.2    Ding, J.3    Gao, P.4
  • 129
    • 0032938624 scopus 로고    scopus 로고
    • Prediction of protein subcellular locations using Markov chain models
    • Yuan, Z. (1999) Prediction of protein subcellular locations using Markov chain models. FEBS Lett. 451, 23-26.
    • (1999) FEBS Lett. , vol.451 , pp. 23-26
    • Yuan, Z.1
  • 130
    • 0033597852 scopus 로고    scopus 로고
    • Proteolytic processing in the secretory pathway
    • Zhou, A., Webb, G., Zhu, X., and Steiner, D. F. (1999) Proteolytic processing in the secretory pathway. J. Biol. Chem. 30, 20745-20748.
    • (1999) J. Biol. Chem. , vol.30 , pp. 20745-20748
    • Zhou, A.1    Webb, G.2    Zhu, X.3    Steiner, D.F.4


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