메뉴 건너뛰기




Volumn 287, Issue 32, 2012, Pages 27106-27116

Multiple post-translational modifications affect heterologous protein synthesis

Author keywords

[No Author keywords available]

Indexed keywords

AMIDATION; CELL-FREE SYSTEM; COMPREHENSIVE STUDIES; DISULFIDE BOND FORMATION; HETEROLOGOUS PROTEINS; HUMAN PROTEINS; MYRISTOYLATION; PALMITOYLATION; POST-TRANSLATIONAL MODIFICATIONS; PRENYLATION; PROKARYOTIC SYSTEM; PROTEIN SYNTHESIS; SOLUBLE EXPRESSION; SOLUBLE PROTEINS; SPECIFIC EFFECTS; SUMOYLATION; UBIQUITINATION;

EID: 84864534856     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.366351     Document Type: Article
Times cited : (63)

References (68)
  • 1
    • 0037305599 scopus 로고    scopus 로고
    • Protein expression systems for structural genomics and proteomics
    • Yokoyama, S. (2003) Protein expression systems for structural genomics and proteomics. Curr. Opin. Chem. Biol. 7, 39-43
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 39-43
    • Yokoyama, S.1
  • 2
    • 49649127384 scopus 로고    scopus 로고
    • Target selection for structural genomics. An overview
    • Marsden, R. L., and Orengo, C. A. (2008) Target selection for structural genomics. An overview. Methods Mol. Biol. 426, 3-25
    • (2008) Methods Mol. Biol. , vol.426 , pp. 3-25
    • Marsden, R.L.1    Orengo, C.A.2
  • 4
    • 4644269746 scopus 로고    scopus 로고
    • High throughput cell-free systems for synthesis of functionally active proteins
    • Spirin, A. S. (2004) High throughput cell-free systems for synthesis of functionally active proteins. Trends Biotechnol. 22, 538-545
    • (2004) Trends Biotechnol. , vol.22 , pp. 538-545
    • Spirin, A.S.1
  • 5
    • 13944274948 scopus 로고    scopus 로고
    • The past, present and future of cell-free protein synthesis
    • DOI 10.1016/j.tibtech.2005.01.003, PII S0167779905000259
    • Katzen, F., Chang, G., and Kudlicki, W. (2005) The past, present, and future of cell-free protein synthesis. Trends Biotechnol. 23, 150-156 (Pubitemid 40269848)
    • (2005) Trends in Biotechnology , vol.23 , Issue.3 , pp. 150-156
    • Katzen, F.1    Chang, G.2    Kudlicki, W.3
  • 6
    • 56649123318 scopus 로고    scopus 로고
    • Cell-free protein synthesis. Applications in proteomics and biotechnology
    • He, M. (2008) Cell-free protein synthesis. Applications in proteomics and biotechnology. Nat. Biotechnol. 25, 126-132
    • (2008) Nat. Biotechnol. , vol.25 , pp. 126-132
    • He, M.1
  • 7
    • 0030272217 scopus 로고    scopus 로고
    • Quality and authenticity of heterologous proteins synthesized in yeast
    • DOI 10.1016/S0958-1669(96)80056-5
    • Eckart, M. R., and Bussineau, C. M. (1996) Quality and authenticity of heterologous proteins synthesized in yeast. Curr. Opin. Biotechnol. 7, 525-530 (Pubitemid 26381755)
    • (1996) Current Opinion in Biotechnology , vol.7 , Issue.5 , pp. 525-530
    • Eckart, M.R.1    Bussineau, C.M.2
  • 8
    • 0034681174 scopus 로고    scopus 로고
    • A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: Plants apparently contain a suicide system directed at ribosomes
    • DOI 10.1073/pnas.97.2.559
    • Madin, K., Sawasaki, T., Ogasawara, T., and Endo, Y. (2000) A highly efficient and robust cell-free protein synthesis system prepared from wheat germ embryos. Plants apparently contain a suicide system directed at ribosomes. Proc. Natl. Acad. Sci. U.S.A. 97, 559-564 (Pubitemid 30070348)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.2 , pp. 559-564
    • Madin, K.1    Sawasaki, T.2    Ogasawara, T.3    Endo, Y.4
  • 10
    • 38449110448 scopus 로고    scopus 로고
    • Use of reticulocyte lysates for mechanistic studies of eukaryotic translation initiation
    • Merrick, W. C., and Barth-Baus, D. (2007) Use of reticulocyte lysates for mechanistic studies of eukaryotic translation initiation. Methods Enzymol. 429, 1-21
    • (2007) Methods Enzymol. , vol.429 , pp. 1-21
    • Merrick, W.C.1    Barth-Baus, D.2
  • 11
    • 33645395535 scopus 로고    scopus 로고
    • An efficient mammalian cell-free translation system supplemented with translation factors
    • Mikami, S., Masutani, M., Sonenberg, N., Yokoyama, S., and Imataka, H. (2006) An efficient mammalian cell-free translation system supplemented with translation factors. Protein Expr. Purif. 46, 348-357
    • (2006) Protein Expr. Purif. , vol.46 , pp. 348-357
    • Mikami, S.1    Masutani, M.2    Sonenberg, N.3    Yokoyama, S.4    Imataka, H.5
  • 12
    • 33846204799 scopus 로고    scopus 로고
    • A hybridoma-based in vitro translation system that efficiently synthesizes glycoproteins
    • DOI 10.1016/j.jbiotec.2006.06.018, PII S0168165606005359
    • Mikami, S., Kobayashi, T., Yokoyama, S., and Imataka, H. (2006) A hybridoma- based in vitro translation system that efficiently synthesizes glycoproteins. J. Biotechnol. 127, 65-78 (Pubitemid 46107129)
    • (2006) Journal of Biotechnology , vol.127 , Issue.1 , pp. 65-78
    • Mikami, S.1    Kobayashi, T.2    Yokoyama, S.3    Imataka, H.4
  • 13
    • 9144261138 scopus 로고    scopus 로고
    • Mining the Structural Genomics Pipeline: Identification of Protein Properties that Affect High-throughput Experimental Analysis
    • DOI 10.1016/j.jmb.2003.11.053
    • Goh, C. S., Lan, N., Douglas, S. M., Wu, B., Echols, N., Smith, A., Milburn, D., Montelione, G. T., Zhao, H., and Gerstein, M. (2004) Mining the structural genomics pipeline. Identification of protein properties that effect high throughput experimental analysis. J. Mol. Biol. 336, 115-130 (Pubitemid 38102334)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.1 , pp. 115-130
    • Goh, C.-S.1    Lan, N.2    Douglas, S.M.3    Wu, B.4    Echols, N.5    Smith, A.6    Milburn, D.7    Montelione, G.T.8    Zhao, H.9    Gerstein, M.10
  • 15
    • 13244265563 scopus 로고    scopus 로고
    • Production of soluble mammalian proteins in Escherichia coli. Identification of protein features that correlate with successful expression
    • Dyson, M. R., Shadbolt, S. P., Vincent, K. J., Perera, R. L., and McCafferty, J. (2004) Production of soluble mammalian proteins in Escherichia coli. Identification of protein features that correlate with successful expression. BMC Biotechnol. 4, 32
    • (2004) BMC Biotechnol. , vol.4 , pp. 32
    • Dyson, M.R.1    Shadbolt, S.P.2    Vincent, K.J.3    Perera, R.L.4    McCafferty, J.5
  • 16
    • 14144255127 scopus 로고    scopus 로고
    • Understanding the relationship between the primary structure of proteins and its propensity to be soluble on overexpression in Escherichia coli
    • DOI 10.1110/ps.041009005
    • Idicula-Thomas, S., and Balaji, P. (2005) Understanding the relationships between the primary structure of proteins and its propensity to be soluble on overexpression in Escherichia coli. Protein Sci. 14, 582-592 (Pubitemid 40283896)
    • (2005) Protein Science , vol.14 , Issue.3 , pp. 582-592
    • Idicula-Thomas, S.1    Balaji, P.V.2
  • 17
    • 32144443802 scopus 로고    scopus 로고
    • A support vector machine-based method for predicting the propensity of a protein to be soluble or to form inclusion body on overexpression in Escherichia coli
    • DOI 10.1093/bioinformatics/bti810
    • Idicula-Thomas, S., Kulkarni, A. J., Kulkarni, B. D., Jayaraman, V. K., and Balaji, P. V. (2006)Asupport vector machine-based method for predicting the propensity of a protein to be soluble or to form inclusion body on overexpression in Escherichia coli. Bioinformatics 22, 278-284 (Pubitemid 43205372)
    • (2006) Bioinformatics , vol.22 , Issue.3 , pp. 278-284
    • Idicula-Thomas, S.1    Kulkarni, A.J.2    Kulkarni, B.D.3    Jayaraman, V.K.4    Balaji, P.V.5
  • 18
    • 77951633563 scopus 로고    scopus 로고
    • Comprehensive bioinformatics analysis of cell-free protein synthesis. Identification of multiple protein properties that correlate with successful expression
    • Kurotani, A., Takagi, T., Toyama, M., Shirouzu, M., Yokoyama, S., Fukami, Y., and Tokmakov, A. A. (2010) Comprehensive bioinformatics analysis of cell-free protein synthesis. Identification of multiple protein properties that correlate with successful expression. FASEB J. 24, 1095-1104
    • (2010) FASEB J. , vol.24 , pp. 1095-1104
    • Kurotani, A.1    Takagi, T.2    Toyama, M.3    Shirouzu, M.4    Yokoyama, S.5    Fukami, Y.6    Tokmakov, A.A.7
  • 20
    • 23844436061 scopus 로고    scopus 로고
    • Large scale structural proteomics project at RIKEN. Present and future
    • Yokoyama, S. (2005) Large scale structural proteomics project at RIKEN. Present and future. Tanpakushitsu Kakusan Koso 50, 836-845
    • (2005) Tanpakushitsu Kakusan Koso , vol.50 , pp. 836-845
    • Yokoyama, S.1
  • 22
    • 0001244666 scopus 로고    scopus 로고
    • ScanProsite. A reference implementation of a PROSITE scanning tool
    • Gattiker, A., Gasteiger, E., and Bairoch, A. (2002) ScanProsite. A reference implementation of a PROSITE scanning tool. Appl. Bioinformatics 1, 107-108
    • (2002) Appl. Bioinformatics , vol.1 , pp. 107-108
    • Gattiker, A.1    Gasteiger, E.2    Bairoch, A.3
  • 24
    • 54249148026 scopus 로고    scopus 로고
    • CSS-Palm 2.0. An updated software for palmitoylation sites prediction
    • Ren, J., Wen, L., Gao, X., Jin, C., Xue, Y., and Yao, X. (2008) CSS-Palm 2.0. An updated software for palmitoylation sites prediction. Protein Eng. Des. Sel. 21, 639-644
    • (2008) Protein Eng. Des. Sel. , vol.21 , pp. 639-644
    • Ren, J.1    Wen, L.2    Gao, X.3    Jin, C.4    Xue, Y.5    Yao, X.6
  • 25
    • 16344366696 scopus 로고    scopus 로고
    • NetAcet: Prediction of N-terminal acetylation sites
    • DOI 10.1093/bioinformatics/bti130
    • Kiemer, L., Bendtsen, J. D., and Blom, N. (2005) NetAcet. Prediction of N-terminal acetylation sites. Bioinformatics 21, 1269-1270 (Pubitemid 40467956)
    • (2005) Bioinformatics , vol.21 , Issue.7 , pp. 1269-1270
    • Kiemer, L.1    Bendtsen, J.D.2    Blom, N.3
  • 28
    • 31944444347 scopus 로고    scopus 로고
    • Large-scale prediction of disulphide bridges using kernel methods, two-dimensional recursive neural networks, and weighted graph matching
    • DOI 10.1002/prot.20787
    • Cheng, J., Saigo, H., and Baldi, P. (2006) Large scale prediction of disulfide bridges using kernel methods, two-dimensional recursive neural networks, and weighed graph matching. Proteins 62, 617-629 (Pubitemid 43191249)
    • (2006) Proteins: Structure, Function and Genetics , vol.62 , Issue.3 , pp. 617-629
    • Cheng, J.1    Saigo, H.2    Baldi, P.3
  • 30
    • 67650720512 scopus 로고    scopus 로고
    • Systematic study of protein sumoylation. Development of a site-specific predictor of SUMOsp 2.0
    • Ren, J., Gao, X., Jin, C., Zhu, M., Wang, X., Shaw, A., Wen, L., Yao, X., and Xue, Y. (2009) Systematic study of protein sumoylation. Development of a site-specific predictor of SUMOsp 2.0. Proteomics 9, 3409-3412
    • (2009) Proteomics , vol.9 , pp. 3409-3412
    • Ren, J.1    Gao, X.2    Jin, C.3    Zhu, M.4    Wang, X.5    Shaw, A.6    Wen, L.7    Yao, X.8    Xue, Y.9
  • 31
    • 8844239093 scopus 로고    scopus 로고
    • ProteoMix: An integrated and flexible system for interactively analyzing large numbers of protein sequences
    • DOI 10.1093/bioinformatics/bth276
    • Chikayama, E., Kurotani, A., Kuroda, Y., and Yokoyama, S. (2004) Proteo-Mix. An integrated and flexible system for interactively analyzing large numbers of protein sequences. Bioinformatics 20, 2836-2838 (Pubitemid 39530173)
    • (2004) Bioinformatics , vol.20 , Issue.16 , pp. 2836-2838
    • Chikayama, E.1    Kurotani, A.2    Kuroda, Y.3    Yokoyama, S.4
  • 32
    • 0028983855 scopus 로고
    • The Swiss-3DImage collection and PDB-Browser on the World-Wide Web
    • Peitsch, M. C., Wells, T. N., Stampf, D. R., and Sussman, J. L. (1995) The Swiss-3DImage collection and PDB-Browser on the World-Wide Web. Trends Biochem. Sci. 20, 82-84
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 82-84
    • Peitsch, M.C.1    Wells, T.N.2    Stampf, D.R.3    Sussman, J.L.4
  • 33
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • DOI 10.1093/nar/gkg520
    • Schwede, T., Kopp, J., Guex, N., and Peitsch, M. C. (2003) SWISS-MODEL. An automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385 (Pubitemid 37442164)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 34
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold, K., Bordoli, L., Kopp, J., and Schwede, T. (2006) The SWISS-MODEL workspace. A web-based environment for protein structure homology modeling. Bioinformatics 22, 195-201 (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 36
    • 78149415544 scopus 로고    scopus 로고
    • Categorical data analysis in experimental biology
    • Xu, B., Feng, X., and Burdine, R. D. (2010) Categorical data analysis in experimental biology. Dev. Biol. 348, 3-11
    • (2010) Dev. Biol. , vol.348 , pp. 3-11
    • Xu, B.1    Feng, X.2    Burdine, R.D.3
  • 38
    • 33749860977 scopus 로고    scopus 로고
    • Post-translational modifications in the context of therapeutic proteins
    • DOI 10.1038/nbt1252, PII NBT1252
    • Walsh, G., and Jefferis, R. (2006) Post-translational modifications in the context of therapeutic proteins. Nat. Biotechnol. 24, 1241-1252 (Pubitemid 44564769)
    • (2006) Nature Biotechnology , vol.24 , Issue.10 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 39
    • 33644830238 scopus 로고    scopus 로고
    • N-linked oligosaccharides as outfitters for glycoprotein folding, form and function
    • DOI 10.1016/j.tibs.2006.01.003, PII S0968000406000247
    • Mitra, N., Sinha, S., Ramya, T. N., and Surolia, A. (2006) N-Linked oligosaccharides as outfitters for glycoprotein folding, form, and function. Trends Biochem. Sci. 31, 156-163 (Pubitemid 43357996)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.3 , pp. 156-163
    • Mitra, N.1    Sinha, S.2    Ramya, T.N.C.3    Surolia, A.4
  • 41
    • 77958099601 scopus 로고    scopus 로고
    • Protein glycosylation in bacteria. Sweeter than ever
    • Nothaft, H., and Szymanski, C. M. (2010) Protein glycosylation in bacteria. Sweeter than ever. Nat. Rev. Microbiol. 8, 765-778
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 765-778
    • Nothaft, H.1    Szymanski, C.M.2
  • 42
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes
    • Tu, B. P., and Weissman, J. S. (2004) Oxidative protein folding in eukaryotes. J. Cell Biol. 164, 341-346
    • (2004) J. Cell Biol. , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 43
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx, F., and Mujacic, M. (2004) Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 22, 1399-1408
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 44
    • 0942286940 scopus 로고    scopus 로고
    • Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli
    • Kim, D. M., and Swartz, J. R. (2004) Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli. Biotechnol. Bioeng. 85, 122-129
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 122-129
    • Kim, D.M.1    Swartz, J.R.2
  • 46
    • 63149130741 scopus 로고    scopus 로고
    • Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins
    • Niwa, T., Ying, B. W., Saito, K., Jin, W., Takada, S., Ueda, T., and Taguchi, H. (2009) Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins. Proc. Natl. Acad. Sci. U.S.A. 106, 4201-4206
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 4201-4206
    • Niwa, T.1    Ying, B.W.2    Saito, K.3    Jin, W.4    Takada, S.5    Ueda, T.6    Taguchi, H.7
  • 48
    • 0033575274 scopus 로고    scopus 로고
    • Arginine 336 and asparagine 333 of the human cholecystokinin-A receptor-binding site interact with penultimate aspartic acid and the C-terminal amide of cholecystokinin
    • Gigoux, V., Escrieut, C., Fehrentz, J. A., Poirot, S., Maigret, B., Moroder, L., Gully, D., Martinez, J., Vaysse, N., and Fourmy, D. (1999) Arginine 336 and asparagine 333 of the human cholecystokinin-A receptor-binding site interact with penultimate aspartic acid and the C-terminal amide of cholecystokinin. J. Biol. Chem. 274, 20457-20464
    • (1999) J. Biol. Chem. , vol.274 , pp. 20457-20464
    • Gigoux, V.1    Escrieut, C.2    Fehrentz, J.A.3    Poirot, S.4    Maigret, B.5    Moroder, L.6    Gully, D.7    Martinez, J.8    Vaysse, N.9    Fourmy, D.10
  • 49
    • 0033179012 scopus 로고    scopus 로고
    • Conformational ensembles: The role of neuropeptide structures in receptor binding
    • Edison, A. S., Espinoza, E., and Zachariah, C. (1999) Conformational assemblies. The role of neuropeptide structures in receptor binding. J. Neurosci. 19, 6318-6326 (Pubitemid 29347432)
    • (1999) Journal of Neuroscience , vol.19 , Issue.15 , pp. 6318-6326
    • Edison, A.S.1    Espinoza, E.2    Zachariah, C.3
  • 51
    • 0041589205 scopus 로고    scopus 로고
    • The biology and enzymology of protein tyrosine Osulfation
    • Moore, K. L. (2003) The biology and enzymology of protein tyrosine Osulfation. J. Biol. Chem. 278, 24243-24246
    • (2003) J. Biol. Chem. , vol.278 , pp. 24243-24246
    • Moore, K.L.1
  • 52
    • 46749128220 scopus 로고    scopus 로고
    • Toward a framework for sulfoproteomics. Synthesis and characterization of sulfotyrosine-containing peptides
    • Seibert, C., and Sakmar, T. P. (2008) Toward a framework for sulfoproteomics. Synthesis and characterization of sulfotyrosine-containing peptides. Biopolymers 90, 459-477
    • (2008) Biopolymers , vol.90 , pp. 459-477
    • Seibert, C.1    Sakmar, T.P.2
  • 53
    • 0034721650 scopus 로고    scopus 로고
    • Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1
    • Somers, W. S., Tang, J., Shaw, G. D., and Camphausen, R. T. (2000) Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1. Cell 103, 467-479
    • (2000) Cell , vol.103 , pp. 467-479
    • Somers, W.S.1    Tang, J.2    Shaw, G.D.3    Camphausen, R.T.4
  • 54
    • 77953470577 scopus 로고    scopus 로고
    • CAAX-box protein, prenylation process, and carcinogenesis
    • Gao, J., Liao, J., and Yang, G. Y. (2009) CAAX-box protein, prenylation process, and carcinogenesis. Am. J. Tranls. Res. 1, 312-325
    • (2009) Am. J. Tranls. Res. , vol.1 , pp. 312-325
    • Gao, J.1    Liao, J.2    Yang, G.Y.3
  • 56
    • 0027284950 scopus 로고
    • Protein prenylation. A mediator of protein-protein interactions
    • Marshall, C. J. (1993) Protein prenylation. A mediator of protein-protein interactions. Science 259, 1865-1866
    • (1993) Science , vol.259 , pp. 1865-1866
    • Marshall, C.J.1
  • 57
    • 3042559944 scopus 로고    scopus 로고
    • Prenyl-binding domains: Potential targets for Ras inhibitors and anti-cancer drugs
    • DOI 10.1016/j.semcancer.2004.04.004, PII S1044579X04000215
    • Kloog, Y., and Cox, A. D. (2004) Prenyl-binding domains. Potential targets for Ras inhibitors and anti-cancer drugs. Semin. Cancer Biol. 14, 253-261 (Pubitemid 38824586)
    • (2004) Seminars in Cancer Biology , vol.14 , Issue.4 , pp. 253-261
    • Kloog, Y.1    Cox, A.D.2
  • 58
    • 67649696034 scopus 로고    scopus 로고
    • Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis
    • Saracco, S. A., Hansson, M., Scalf, M., Walker, J. M., Smith, L. M., and Vierstra, R. D. (2009) Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis. Plant J. 59, 344-358
    • (2009) Plant J. , vol.59 , pp. 344-358
    • Saracco, S.A.1    Hansson, M.2    Scalf, M.3    Walker, J.M.4    Smith, L.M.5    Vierstra, R.D.6
  • 59
    • 33747838835 scopus 로고    scopus 로고
    • SUMOsp: A web server for sumoylation site prediction
    • DOI 10.1093/nar/gkl207
    • Xue, Y., Zhou, F., Fu, C., Xu, Y., and Yao, X. (2006) SUMOsp.Aweb server for sumoylation site prediction. Nucleic Acids Res. 34, W254-W257 (Pubitemid 44529774)
    • (2006) Nucleic Acids Research , vol.34 , Issue.WEB. SERV. ISS.
    • Xue, Y.1    Zhou, F.2    Fu, C.3    Xu, Y.4    Yao, X.5
  • 61
    • 1942537173 scopus 로고    scopus 로고
    • An efficient system for high-level expression and easy purification of authentic recombinant proteins
    • DOI 10.1110/ps.04618904
    • Catanzariti, A. M., Soboleva, T. A., Jans, D. A., Board, P. G., and Baker, R. T. (2004) An efficient system for high level expression and easy purification of authentic recombinant proteins. Protein Sci. 13, 1331-1339 (Pubitemid 38526098)
    • (2004) Protein Science , vol.13 , Issue.5 , pp. 1331-1339
    • Catanzariti, A.-M.1    Soboleva, T.A.2    Jans, D.A.3    Board, P.G.4    Baker, R.T.5
  • 63
    • 0038339419 scopus 로고    scopus 로고
    • Genomic analysis of the eukaryotic protein kinase superfamily. A perspective
    • Hanks, S. K. (2003) Genomic analysis of the eukaryotic protein kinase superfamily. A perspective. Genome Biol. 4, 111
    • (2003) Genome Biol. , vol.4 , pp. 111
    • Hanks, S.K.1
  • 64
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • DOI 10.1126/science.1075762
    • Manning, G., Whyte, D. B., Martinez, R., Hunter, T., and Sudarsanam, S. (2002) The protein kinase complement of the human genome. Science 298, 1912-1934 (Pubitemid 35425239)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 65
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • DOI 10.1002/pmic.200300771
    • Blom, N., Sicheritz-Pontén, T., Gupta, R., Gammeltoft, S., and Brunak, S. (2004) Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4, 1633-1649 (Pubitemid 38738322)
    • (2004) Proteomics , vol.4 , Issue.6 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Ponten, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, S..5
  • 67
    • 63749113783 scopus 로고    scopus 로고
    • Tyrosine phosphorylation. Thirty years and counting
    • Hunter, T. (2009) Tyrosine phosphorylation. Thirty years and counting. Curr. Opin. Cell Biol. 21, 140-146
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 140-146
    • Hunter, T.1
  • 68
    • 80053469048 scopus 로고    scopus 로고
    • Mechanisms and principles of N-linked protein glycosylation
    • Schwarz, F., and Aebi, M. (2011) Mechanisms and principles of N-linked protein glycosylation. Curr. Opin. Struct. Biol. 21, 576-582
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 576-582
    • Schwarz, F.1    Aebi, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.