메뉴 건너뛰기




Volumn 12, Issue 6, 2015, Pages 561-567

Isotope-targeted glycoproteomics (IsoTaG): A mass-independent platform for intact N- and O-glycopeptide discovery and analysis

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN; GLYCOPEPTIDE; ISOPROTEIN; GLYCOPROTEIN; PROTEOME;

EID: 84930181837     PISSN: 15487091     EISSN: 15487105     Source Type: Journal    
DOI: 10.1038/nmeth.3366     Document Type: Article
Times cited : (211)

References (51)
  • 1
    • 0035490864 scopus 로고    scopus 로고
    • Inhibition of the glycosylation and alteration in the intracellular trafficking of mucins and other glycoproteins by GalNAc-O-bn in mucosal cell lines: An effect mediated through the intracellular synthesis of complex GalNAc-O-bn oligosaccharides
    • Gouyer, V. et al. Inhibition of the glycosylation and alteration in the intracellular trafficking of mucins and other glycoproteins by GalNAc-O-bn in mucosal cell lines: an effect mediated through the intracellular synthesis of complex GalNAc-O-bn oligosaccharides. Front. Biosci. 6, D1235-D1244 (2001).
    • (2001) Front. Biosci. , vol.6 , pp. D1235-D1244
    • Gouyer, V.1
  • 2
    • 33745272509 scopus 로고    scopus 로고
    • Cell signaling, the essential role of O-GlcNAc!
    • Zachara, N. E. & Hart, G. W. Cell signaling, the essential role of O-GlcNAc!. Biochim. Biophys. Acta. 1761, 599-617 (2006).
    • (2006) Biochim. Biophys. Acta. , vol.1761 , pp. 599-617
    • Zachara, N.E.1    Hart, G.W.2
  • 3
    • 84890937257 scopus 로고    scopus 로고
    • Glycocalyx engineering reveals a Siglec-based mechanism for NK cell immunoevasion
    • Hudak, J. E., Canham, S. M. & Bertozzi, C. R. Glycocalyx engineering reveals a Siglec-based mechanism for NK cell immunoevasion. Nat. Chem. Biol. 10, 69-75 (2014).
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 69-75
    • Hudak, J.E.1    Canham, S.M.2    Bertozzi, C.R.3
  • 4
    • 84858664547 scopus 로고    scopus 로고
    • Increasing O-Glcnac slows neurodegeneration and stabilizes tau against aggregation
    • Yuzwa, S. A. et al. Increasing O-Glcnac slows neurodegeneration and stabilizes tau against aggregation. Nat. Chem. Biol. 8, 393-399 (2012).
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 393-399
    • Yuzwa, S.A.1
  • 5
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: Glycans as novel therapeutic targets
    • Fuster, M. M. & Esko, J. D. The sweet and sour of cancer: glycans as novel therapeutic targets. Nat. Rev. Cancer 5, 526-542 (2005).
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 7
    • 84907572385 scopus 로고    scopus 로고
    • Immature truncated O-glycophenotype of cancer directly induces oncogenic features
    • USA
    • Radhakrishnan, P. et al. Immature truncated O-glycophenotype of cancer directly induces oncogenic features. Proc. Natl. Acad. Sci. USA 111, E4066-E4075 (2014).
    • (2014) Proc. Natl. Acad. Sci. , vol.111 , pp. E4066-E4075
    • Radhakrishnan, P.1
  • 8
    • 77956931053 scopus 로고    scopus 로고
    • A systematic approach to protein glycosylation analysis: A path through the maze
    • Mariño, K., Bones, J., Kattla, J. J. & Rudd, P. M. A systematic approach to protein glycosylation analysis: a path through the maze. Nat. Chem. Biol. 6, 713-723 (2010).
    • (2010) Nat Chem. Biol. , vol.6 , pp. 713-723
    • Mariño, K.1    Bones, J.2    Kattla, J.J.3    Rudd, P.M.4
  • 9
    • 78651105000 scopus 로고    scopus 로고
    • Mass spectrometry based glycoproteomics-from a proteomics perspective
    • Pan, S., Chen, R., Aebersold, R. & Brentnall, T. A. Mass spectrometry based glycoproteomics-from a proteomics perspective. Mol. Cell Proteomics 10, R110 003251 (2011).
    • (2011) Mol. Cell Proteomics , vol.10 , pp. R110003251
    • Pan, S.1    Chen, R.2    Aebersold, R.3    Brentnall, T.A.4
  • 10
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou, H., Watts, J. D. & Aebersold, R. A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 19, 375-378 (2001).
    • (2001) Nat Biotechnol. , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 11
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V. et al. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648 (2006).
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1
  • 12
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary, C. et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325, 834-840 (2009).
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1
  • 13
    • 2942585313 scopus 로고    scopus 로고
    • Glycoform composition profiling of O-glycopeptides derived from human serum IgA1 by matrix-assisted laser desorption ionization-time of flight-mass spectrometry
    • Pouria, S. et al. Glycoform composition profiling of O-glycopeptides derived from human serum IgA1 by matrix-assisted laser desorption ionization-time of flight-mass spectrometry. Anal. Biochem. 330, 257-263 (2004).
    • (2004) Anal. Biochem. , vol.330 , pp. 257-263
    • Pouria, S.1
  • 14
    • 84876148755 scopus 로고    scopus 로고
    • III Protein analysis by shotgun/bottom-up proteomics
    • Zhang, Y., Fonslow, B. R., Shan, B., Baek, M. C. & Yates, J. R. III. Protein analysis by shotgun/bottom-up proteomics. Chem. Rev. 113, 2343-2394 (2013).
    • (2013) Chem. Rev. , vol.113 , pp. 2343-2394
    • Zhang, Y.1    Fonslow, B.R.2    Shan, B.3    Baek, M.C.4    Yates, J.R.5
  • 15
    • 79952747341 scopus 로고    scopus 로고
    • Metabolic cross-talk allows labeling of O-linked -N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway
    • USA
    • Boyce, M. et al. Metabolic cross-talk allows labeling of O-linked -N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway. Proc. Natl. Acad. Sci. USA 108, 3141-3146 (2011).
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , pp. 3141-3146
    • Boyce, M.1
  • 17
    • 84906879108 scopus 로고    scopus 로고
    • Changes in metabolic chemical reporter structure yield a selective probe of O-GlcNAc modification
    • Chuh, K. N., Zaro, B. W., Piller, F., Piller, V. & Pratt, M. R. Changes in metabolic chemical reporter structure yield a selective probe of O-GlcNAc modification. J. Am. Chem. Soc. 136, 12283-12295 (2014).
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 12283-12295
    • Chuh, K.N.1    Zaro, B.W.2    Piller, F.3    Piller, V.4    Pratt, M.R.5
  • 18
    • 79957694784 scopus 로고    scopus 로고
    • Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1
    • USA
    • Zaro, B. W., Yang, Y. Y., Hang, H. C. & Pratt, M. R. Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1. Proc. Natl. Acad. Sci. USA 108, 8146-8151 (2011).
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , pp. 8146-8151
    • Zaro, B.W.1    Yang, Y.Y.2    Hang, H.C.3    Pratt, M.R.4
  • 19
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang, H., Li, X. J., Martin, D. B. & Aebersold, R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol. 21, 660-666 (2003).
    • (2003) Nat. Biotechnol. , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 20
    • 70350735945 scopus 로고    scopus 로고
    • Enrichment of glycopeptides for glycan structure and attachment site identification
    • Nilsson, J. et al. Enrichment of glycopeptides for glycan structure and attachment site identification. Nat. Methods 6, 809-811 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 809-811
    • Nilsson, J.1
  • 21
    • 34249032767 scopus 로고    scopus 로고
    • Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics
    • Khidekel, N. et al. Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics. Nat. Chem. Biol. 3, 339-348 (2007).
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 339-348
    • Khidekel, N.1
  • 22
    • 33646900710 scopus 로고    scopus 로고
    • O-Linked N-Acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry
    • Vosseller, K. et al. O-Linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry. Mol. Cell. Proteomics 5, 923-934 (2006).
    • (2006) Mol Cell. Proteomics , vol.5 , pp. 923-934
    • Vosseller, K.1
  • 23
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D. F., Gnad, F., Wisniewski, J. R. & Mann, M. Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141, 897-907 (2010).
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wisniewski, J.R.3    Mann, M.4
  • 25
    • 4444269089 scopus 로고    scopus 로고
    • A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation
    • Hägglund, P., Bunkenborg, J., Elortza, F., Jensen, O. N. & Roepstorff, P. A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation. J. Proteome Res. 3, 556-566 (2004).
    • (2004) J Proteome Res , vol.3 , pp. 556-566
    • Hägglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5
  • 26
    • 80255141853 scopus 로고    scopus 로고
    • Mining the O-glycoproteome using zinc-finger nuclease-glycoengineered SimpleCell lines
    • Steentoft, C. et al. Mining the O-glycoproteome using zinc-finger nuclease-glycoengineered SimpleCell lines. Nat. Methods 8, 977-982 (2011).
    • (2011) Nat. Methods , vol.8 , pp. 977-982
    • Steentoft, C.1
  • 27
    • 84878644998 scopus 로고    scopus 로고
    • Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology
    • Steentoft, C. et al. Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology. EMBO J. 32, 1478-1488 (2013).
    • (2013) EMBO J. , vol.32 , pp. 1478-1488
    • Steentoft, C.1
  • 28
    • 80051967494 scopus 로고    scopus 로고
    • Isotopic signature transfer and mass pattern prediction (IsoStamp): An enabling technique for chemically-directed proteomics
    • Palaniappan, K. K. et al. Isotopic signature transfer and mass pattern prediction (IsoStamp): an enabling technique for chemically-directed proteomics. ACS Chem. Biol. 6, 829-836 (2011).
    • (2011) ACS Chem. Biol. , vol.6 , pp. 829-836
    • Palaniappan, K.K.1
  • 29
    • 84875140066 scopus 로고    scopus 로고
    • Strategies for coupling molecular units if subsequent decoupling is required
    • Bielski, R. & Witczak, Z. Strategies for coupling molecular units if subsequent decoupling is required. Chem. Rev. 113, 2205-2243 (2013).
    • (2013) Chem. Rev. , vol.113 , pp. 2205-2243
    • Bielski, R.1    Witczak, Z.2
  • 30
    • 78650590308 scopus 로고    scopus 로고
    • Cleavable biotin probes for labeling of biomolecules via azide-alkyne cycloaddition
    • Szychowski, J. et al. Cleavable biotin probes for labeling of biomolecules via azide-alkyne cycloaddition. J. Am. Chem. Soc. 132, 18351-18360 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 18351-18360
    • Szychowski, J.1
  • 31
    • 4344704630 scopus 로고    scopus 로고
    • Chemical remodelling of cell surfaces in living animals
    • Prescher, J. A., Dube, D. H. & Bertozzi, C. R. Chemical remodelling of cell surfaces in living animals. Nature 430, 873-877 (2004).
    • (2004) Nature , vol.430 , pp. 873-877
    • Prescher, J.A.1    Dube, D.H.2    Bertozzi, C.R.3
  • 32
    • 84930186506 scopus 로고    scopus 로고
    • 2nd edn (eds. Varki, A. et al. ) Ch. Cold Spring Harbor Laboratory Press
    • Hart, G. W. & Akimoto, Y. in Essentials of Glycobiology 2nd edn. (eds. Varki, A. et al. ) Ch. 18 (Cold Spring Harbor Laboratory Press, 2009).
    • (2009) Essentials of Glycobiology , vol.18
    • Hart, G.W.1    Akimoto, Y.2
  • 33
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • USA
    • Syka, J. E. P., Coon, J. J., Schroeder, M. J., Shabanowitz, J. & Hunt, D. F. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl. Acad. Sci. USA 101, 9528-9533 (2004).
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 9528-9533
    • Syka, J.E.P.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 34
    • 40949133707 scopus 로고    scopus 로고
    • Human tumor antigens Tn and sialyl Tn arise from mutations in Cosmc
    • Ju, T. et al. Human tumor antigens Tn and sialyl Tn arise from mutations in Cosmc. Cancer Res. 68, 1636-1646 (2008).
    • (2008) Cancer Res. , vol.68 , pp. 1636-1646
    • Ju, T.1
  • 35
    • 7444262496 scopus 로고    scopus 로고
    • The status, quality, and expansion of the NIH full-length cDNA project: The Mammalian Gene Collection (MGC)
    • Gerhard, D. S. et al. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 14, 2121-2127 (2004).
    • (2004) Genome Res. , vol.14 , pp. 2121-2127
    • Gerhard, D.S.1
  • 36
    • 33847643281 scopus 로고    scopus 로고
    • A highly conserved protein secreted by the prostate cancer cell line PC-3 is expressed in benign and malignant prostate tissue
    • Valtonen-André, C. et al. A highly conserved protein secreted by the prostate cancer cell line PC-3 is expressed in benign and malignant prostate tissue. Biol. Chem. 388, 289-295 (2007).
    • (2007) Biol Chem. , vol.388 , pp. 289-295
    • Valtonen-André, C.1
  • 37
    • 67249117049 scopus 로고    scopus 로고
    • Potential etiologic and functional implications of genome-wide association loci for human diseases and traits
    • USA
    • Hindorff, L. A. et al. Potential etiologic and functional implications of genome-wide association loci for human diseases and traits. Proc. Natl. Acad. Sci. USA 106, 9362-9367 (2009).
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 9362-9367
    • Hindorff, L.A.1
  • 38
    • 83055176451 scopus 로고    scopus 로고
    • Mapping intact protein isoforms in discovery mode using top-down proteomics
    • Tran, J. C. et al. Mapping intact protein isoforms in discovery mode using top-down proteomics. Nature 480, 254-258 (2011).
    • (2011) Nature , vol.480 , pp. 254-258
    • Tran, J.C.1
  • 39
    • 84907269780 scopus 로고    scopus 로고
    • Proteogenomic characterization of human colon and rectal cancer
    • Zhang, B. et al. Proteogenomic characterization of human colon and rectal cancer. Nature 513, 382-387 (2014).
    • (2014) Nature , vol.513 , pp. 382-387
    • Zhang, B.1
  • 40
    • 84904436467 scopus 로고    scopus 로고
    • The cancer glycocalyx mechanically primes integrin-mediated growth and survival
    • Paszek, M. J. et al. The cancer glycocalyx mechanically primes integrin-mediated growth and survival. Nature 511, 319-325 (2014).
    • (2014) Nature , vol.511 , pp. 319-325
    • Paszek, M.J.1
  • 41
    • 73849145104 scopus 로고    scopus 로고
    • A global view of protein expression in human cells, tissues, and organs
    • Pontén, F. et al. A global view of protein expression in human cells, tissues, and organs. Mol. Syst. Biol. 5, 337 (2009).
    • (2009) Mol Syst. Biol. , vol.5 , pp. 337
    • Pontén, F.1
  • 42
    • 51349166164 scopus 로고    scopus 로고
    • Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins
    • Clark, P. M. et al. Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins. J. Am. Chem. Soc. 130, 11576-11577 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11576-11577
    • Clark, P.M.1
  • 44
    • 84876009601 scopus 로고    scopus 로고
    • Glycoproteomic analysis of the secretome of human endothelial cells
    • Yin, X. et al. Glycoproteomic analysis of the secretome of human endothelial cells. Mol. Cell. Proteomics 12, 956-978 (2013).
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 956-978
    • Yin, X.1
  • 45
    • 84901776609 scopus 로고    scopus 로고
    • Novel LC-MS2 product dependent parallel data acquisition function and data analysis workflow for sequencing and identification of intact glycopeptides
    • Wu, S. W., Pu, T. H., Viner, R. & Khoo, K. H. Novel LC-MS2 product dependent parallel data acquisition function and data analysis workflow for sequencing and identification of intact glycopeptides. Anal. Chem. 86, 5478-5486 (2014).
    • (2014) Anal. Chem. , vol.86 , pp. 5478-5486
    • Wu, S.W.1    Pu, T.H.2    Viner, R.3    Khoo, K.H.4
  • 46
    • 24044513966 scopus 로고    scopus 로고
    • Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations
    • Elias, J. E., Haas, W., Faherty, B. K. & Gygi, S. P. Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations. Nat. Methods 2, 667-675 (2005).
    • (2005) Nat. Methods , vol.2 , pp. 667-675
    • Elias, J.E.1    Haas, W.2    Faherty, B.K.3    Gygi, S.P.4
  • 49
    • 80053464015 scopus 로고    scopus 로고
    • Sulfated ligands for the copper(I)-catalyzed azide-alkyne cycloaddition
    • Wang, W. et al. Sulfated ligands for the copper(I)-catalyzed azide-alkyne cycloaddition. Chem. Asian J. 6, 2796-2802 (2011).
    • (2011) Chem. Asian J. , vol.6 , pp. 2796-2802
    • Wang, W.1
  • 50
    • 0345598906 scopus 로고    scopus 로고
    • A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation
    • USA
    • Hang, H. C., Yu, C., Kato, D. L. & Bertozzi, C. R. A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation. Proc. Natl. Acad. Sci. USA 100, 14846-14851 (2003).
    • (2003) Proc Natl. Acad. Sci. , vol.100 , pp. 14846-14851
    • Hang, H.C.1    Yu, C.2    Kato, D.L.3    Bertozzi, C.R.4
  • 51
    • 4344704630 scopus 로고    scopus 로고
    • Chemical remodelling of cell surfaces in living animals
    • Prescher, J. A., Dube, D. H. & Bertozzi, C. R. Chemical remodelling of cell surfaces in living animals. Nature 430, 873-877 (2004).
    • (2004) Nature , vol.430 , pp. 873-877
    • Prescher, J.A.1    Dube, D.H.2    Bertozzi, C.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.