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Volumn 12, Issue 12, 2013, Pages 3474-3488

N- and O-Glycosylation in the murine synaptosome

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPEPTIDE; LECTIN; OLIGOSACCHARIDE; TYROSINE; WHEAT GERM AGGLUTININ;

EID: 84887406672     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M113.030007     Document Type: Article
Times cited : (143)

References (66)
  • 2
    • 84857217705 scopus 로고    scopus 로고
    • Mass spectrometric tools for systematic analysis of protein phosphorylation
    • St-Denis, N., and Gingras, A. C. (2012) Mass spectrometric tools for systematic analysis of protein phosphorylation. Prog. Mol. Biol. Transl. Sci. 106, 3-32
    • (2012) Prog. Mol. Biol. Transl. Sci. , vol.106 , pp. 3-32
    • St-Denis, N.1    Gingras, A.C.2
  • 3
    • 66149128841 scopus 로고    scopus 로고
    • Detecting the "o-GlcNAc-ome"; Detection, purification, and analysis of O-GlcNAc modified proteins
    • Zachara, N. E. (2009) Detecting the "O-GlcNAc-ome"; detection, purification, and analysis of O-GlcNAc modified proteins. Methods Mol. Biol. 534, 251-279
    • (2009) Methods Mol. Biol. , vol.534 , pp. 251-279
    • Zachara, N.E.1
  • 4
    • 84870724100 scopus 로고    scopus 로고
    • Characterizing ubiquitination sites by peptide-based immunoaffinity enrichment
    • Bustos, D., Bakalarski, C. E., Yang, Y., Peng, J., and Kirkpatrick, D. S. (2012) Characterizing Ubiquitination Sites by Peptide-based Immunoaffinity Enrichment. Mol. Cell Proteomics 11, 1529-1540
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 1529-1540
    • Bustos, D.1    Bakalarski, C.E.2    Yang, Y.3    Peng, J.4    Kirkpatrick, D.S.5
  • 5
    • 84867595774 scopus 로고    scopus 로고
    • Discovery of lysine post-translational modifications through mass spectrometric detection
    • Zee, B. M., and Garcia, B. A. (2012) Discovery of lysine post-translational modifications through mass spectrometric detection. Essays Biochem. 52, 147-163
    • (2012) Essays Biochem. , vol.52 , pp. 147-163
    • Zee, B.M.1    Garcia, B.A.2
  • 6
    • 84862728161 scopus 로고    scopus 로고
    • Vertebrate protein glycosylation: Diversity, synthesis and function
    • Moremen, K. W., Tiemeyer, M., and Nairn, A. V. (2012) Vertebrate protein glycosylation: diversity, synthesis and function. Nat. Rev. Mol. Cell Biol. 13, 448-462
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 448-462
    • Moremen, K.W.1    Tiemeyer, M.2    Nairn, A.V.3
  • 7
    • 70449732650 scopus 로고    scopus 로고
    • Pharmacological significance of glycosylation in therapeutic proteins
    • Li, H., and d'Anjou, M. (2009) Pharmacological significance of glycosylation in therapeutic proteins. Curr. Opin. Biotechnol. 20, 678-684
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 678-684
    • Li, H.1    D'Anjou, M.2
  • 8
    • 50449083310 scopus 로고    scopus 로고
    • Evaluation of the serum N-linked glycome for the diagnosis of cancer and chronic inflammation
    • Arnold, J. N., Saldova, R., Hamid, U. M., and Rudd, P. M. (2008) Evaluation of the serum N-linked glycome for the diagnosis of cancer and chronic inflammation. Proteomics 8, 3284-3293
    • (2008) Proteomics , vol.8 , pp. 3284-3293
    • Arnold, J.N.1    Saldova, R.2    Hamid, U.M.3    Rudd, P.M.4
  • 10
    • 75749084864 scopus 로고    scopus 로고
    • Regulation of intracellular signaling by extracellular glycan remodeling
    • Parker, R. B., and Kohler, J. J. (2010) Regulation of intracellular signaling by extracellular glycan remodeling. ACS Chem. Biol. 5, 35-46
    • (2010) ACS Chem. Biol. , vol.5 , pp. 35-46
    • Parker, R.B.1    Kohler, J.J.2
  • 12
    • 78449258533 scopus 로고    scopus 로고
    • O-glycosylation modulates proprotein convertase activation of angiopoietin-like protein 3: Possible role of polypeptide GalNAc-transferase-2 in regulation of concentrations of plasma lipids
    • Schjoldager, K. T., Vester-Christensen, M. B., Bennett, E. P., Levery, S. B., Schwientek, T., Yin, W., Blixt, O., and Clausen, H. (2010) O-glycosylation modulates proprotein convertase activation of angiopoietin-like protein 3: possible role of polypeptide GalNAc-transferase-2 in regulation of concentrations of plasma lipids. J. Biol. Chem. 285, 36293-36303
    • (2010) J. Biol. Chem. , vol.285 , pp. 36293-36303
    • Schjoldager, K.T.1    Vester-Christensen, M.B.2    Bennett, E.P.3    Levery, S.B.4    Schwientek, T.5    Yin, W.6    Blixt, O.7    Clausen, H.8
  • 13
    • 53549093906 scopus 로고    scopus 로고
    • Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry
    • Picariello, G., Ferranti, P., Mamone, G., Roepstorff, P., and Addeo, F. (2008) Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics 8, 3833-3847
    • (2008) Proteomics , vol.8 , pp. 3833-3847
    • Picariello, G.1    Ferranti, P.2    Mamone, G.3    Roepstorff, P.4    Addeo, F.5
  • 14
    • 80054030914 scopus 로고    scopus 로고
    • Detection, evaluation and minimization of nonenzymatic deamidation in proteomic sample preparation
    • Hao, P., Ren, Y., Alpert, A. J., and Sze, S. K. (2011) Detection, evaluation and minimization of nonenzymatic deamidation in proteomic sample preparation. Mol. Cell Proteomics 10, O111.009381
    • (2011) Mol. Cell Proteomics , vol.10
    • Hao, P.1    Ren, Y.2    Alpert, A.J.3    Sze, S.K.4
  • 15
    • 78649961364 scopus 로고    scopus 로고
    • Selective enrichment of sialic acidcontaining glycopeptides using titanium dioxide chromatography with analysis by HILIC and mass spectrometry
    • Palmisano, G., Lendal, S. E., Engholm-Keller, K., Leth-Larsen, R., Parker, B. L., and Larsen, M. R. (2010) Selective enrichment of sialic acidcontaining glycopeptides using titanium dioxide chromatography with analysis by HILIC and mass spectrometry. Nat. Protoc. 5, 1974-1982
    • (2010) Nat. Protoc. , vol.5 , pp. 1974-1982
    • Palmisano, G.1    Lendal, S.E.2    Engholm-Keller, K.3    Leth-Larsen, R.4    Parker, B.L.5    Larsen, M.R.6
  • 17
    • 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., and Aebersold, R. (2003) Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol. 21, 660-666
    • (2003) Nat. Biotechnol. , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 19
    • 84857873715 scopus 로고    scopus 로고
    • Chemical deamidation: A common pitfall in largescale N-linked glycoproteomic mass spectrometry-based analyses
    • Palmisano, G., Melo-Braga, M. N., Engholm-Keller, K., Parker, B. L., and Larsen, M. R. (2012) Chemical deamidation: a common pitfall in largescale N-linked glycoproteomic mass spectrometry-based analyses. J. Proteome Res. 11, 1949-1957
    • (2012) J. Proteome Res. , vol.11 , pp. 1949-1957
    • Palmisano, G.1    Melo-Braga, M.N.2    Engholm-Keller, K.3    Parker, B.L.4    Larsen, M.R.5
  • 20
    • 30544433136 scopus 로고    scopus 로고
    • Methods in enzymology: O-glycosylation of proteins
    • Peter-Katalinić, J. (2005) Methods in enzymology: O-glycosylation of proteins. Methods Enzymol. 405, 139-171
    • (2005) Methods Enzymol , vol.405 , pp. 139-171
    • Peter-Katalinić, J.1
  • 23
    • 72149102185 scopus 로고    scopus 로고
    • Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum
    • Darula, Z., and Medzihradszky, K. F. (2009) Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum. Mol Cell Proteomics 8, 2515-2526
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2515-2526
    • Darula, Z.1    Medzihradszky, K.F.2
  • 24
    • 84863789621 scopus 로고    scopus 로고
    • How to dig deeper? Improved enrichment methods for mucin core-1 type glycopeptides
    • Darula, Z., Sherman, J., and Medzihradszky, K. F. (2012) How to dig deeper? Improved enrichment methods for mucin core-1 type glycopeptides. Mol. Cell Proteomics 11, O111.016774
    • (2012) Mol. Cell Proteomics , vol.11
    • Darula, Z.1    Sherman, J.2    Medzihradszky, K.F.3
  • 26
    • 84859862380 scopus 로고    scopus 로고
    • Human urinary glycoproteomics; Attachment site specific analysis of N- and O-linked glycosylations by CID and ECD
    • Halim, A., Nilsson, J., Rüetschi, U., Hesse, C., and Larson, G. (2012) Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD. Mol Cell Proteomics 11, M111.013649
    • (2012) Mol Cell Proteomics , vol.11
    • Halim, A.1    Nilsson, J.2    Rüetschi, U.3    Hesse, C.4    Larson, G.5
  • 27
    • 30544454698 scopus 로고    scopus 로고
    • Characterization of protein N-glycosylation
    • Medzihradszky, K. F. (2005) Characterization of protein N-glycosylation. Methods Enzymol. 405, 116-138
    • (2005) Methods Enzymol , vol.405 , pp. 116-138
    • Medzihradszky, K.F.1
  • 31
    • 33847234661 scopus 로고    scopus 로고
    • Lookup peaks: A hybrid of de novo sequencing and database search for protein identification by tandem mass spectrometry
    • Bern, M., Cai, Y., and Goldberg, D. (2007) Lookup peaks: a hybrid of de novo sequencing and database search for protein identification by tandem mass spectrometry. Anal. Chem. 79, 1393-1400
    • (2007) Anal. Chem. , vol.79 , pp. 1393-1400
    • Bern, M.1    Cai, Y.2    Goldberg, D.3
  • 33
    • 61849088987 scopus 로고    scopus 로고
    • Elucidation of O-glycosylation structures of the beta-amyloid precursor protein by liquid chromatography-mass spectrometry using electron transfer dissociation and collision induced dissociation
    • Perdivara, I., Petrovich, R., Allinquant, B., Deterding, L. J., Tomer, K. B., and Przybylski, M. (2009) Elucidation of O-glycosylation structures of the beta-amyloid precursor protein by liquid chromatography-mass spectrometry using electron transfer dissociation and collision induced dissociation. J. Proteome Res. 8, 631-642
    • (2009) J. Proteome Res. , vol.8 , pp. 631-642
    • Perdivara, I.1    Petrovich, R.2    Allinquant, B.3    Deterding, L.J.4    Tomer, K.B.5    Przybylski, M.6
  • 35
    • 83055163797 scopus 로고    scopus 로고
    • A data processing pipeline for mammalian proteome dynamics studies using stable isotope metabolic labeling
    • Guan, S., Price, J. C., Prusiner, S. B., Ghaemmaghami, S., and Burlingame, A. L. (2011) A data processing pipeline for mammalian proteome dynamics studies using stable isotope metabolic labeling. Mol. Cell Proteomics 10, M111.010728
    • (2011) Mol Cell Proteomics , vol.10
    • Guan, S.1    Price, J.C.2    Prusiner, S.B.3    Ghaemmaghami, S.4    Burlingame, A.L.5
  • 36
    • 79960181605 scopus 로고    scopus 로고
    • Modification site localization scoring integrated into a search engine
    • Baker, P. R., Trinidad, J. C., and Chalkley, R. J. (2011) Modification site localization scoring integrated into a search engine. Mol. Cell Proteomics 10, M111.008078
    • (2011) Mol. Cell Proteomics , vol.10
    • Baker, P.R.1    Trinidad, J.C.2    Chalkley, R.J.3
  • 37
    • 67049158217 scopus 로고    scopus 로고
    • Identification of protein O-GlcNAcylation sites using electron transfer dissociation mass spectrometry on native peptides
    • Chalkley, R. J., Thalhammer, A., Schoepfer, R., and Burlingame, A. L. (2009) Identification of protein O-GlcNAcylation sites using electron transfer dissociation mass spectrometry on native peptides. Proc. Natl. Acad. Sci. U.S.A. 106, 8894-8899
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 8894-8899
    • Chalkley, R.J.1    Thalhammer, A.2    Schoepfer, R.3    Burlingame, A.L.4
  • 38
    • 0023665250 scopus 로고
    • Presence of an O-glycosidically linked hexasaccharide in fetuin
    • Edge, A. S., and Spiro, R. G. (1987) Presence of an O-glycosidically linked hexasaccharide in fetuin. J. Biol. Chem. 262, 16135-16141
    • (1987) J. Biol. Chem. , vol.262 , pp. 16135-16141
    • Edge, A.S.1    Spiro, R.G.2
  • 39
    • 84868028000 scopus 로고    scopus 로고
    • O-Mannose and O-N-acetyl galactosamine glycosylation of mammalian alpha-dystroglycan is conserved in a region-specific manner
    • Gomez Toledo, A., Raducu, M., Cruces, J., Nilsson, J., Halim, A., Larson, G., Rüetschi, U., and Grahn, A. (2012) O-Mannose and O-N-acetyl galactosamine glycosylation of mammalian alpha-dystroglycan is conserved in a region-specific manner. Glycobiology 22, 1413-1423
    • (2012) Glycobiology , vol.22 , pp. 1413-1423
    • Gomez Toledo, A.1    Raducu, M.2    Cruces, J.3    Nilsson, J.4    Halim, A.5    Larson, G.6    Rüetschi, U.7    Grahn, A.8
  • 40
    • 0022378217 scopus 로고
    • Identification of two binding sites for wheat-germ agglutinin on polylactosamine-type oligosaccharides
    • Gallagher, J. T., Morris, A., and Dexter, T. M. (1985) Identification of two binding sites for wheat-germ agglutinin on polylactosamine-type oligosaccharides. Biochem. J. 231, 115-122
    • (1985) Biochem. J. , vol.231 , pp. 115-122
    • Gallagher, J.T.1    Morris, A.2    Dexter, T.M.3
  • 42
    • 79958838943 scopus 로고    scopus 로고
    • Rapid characterization of sugar-binding specificity by in-solution proximity binding with photosensitizers
    • Chang, C. F., Pan, J. F., Lin, C. N., Wu, I. L., Wong, C. H., and Lin, C. H. (2011) Rapid characterization of sugar-binding specificity by in-solution proximity binding with photosensitizers. Glycobiology 21, 895-902
    • (2011) Glycobiology , vol.21 , pp. 895-902
    • Chang, C.F.1    Pan, J.F.2    Lin, C.N.3    Wu, I.L.4    Wong, C.H.5    Lin, C.H.6
  • 43
    • 0032007314 scopus 로고    scopus 로고
    • Neutral N-glycans in adult rat brain tissue-complete characterization reveals fucosylated hybrid and complex structures
    • Chen, Y. J., Wing, D. R., Guile, G. R., Dwek, R. A., Harvey, D. J., and Zamze, S. (1998) Neutral N-glycans in adult rat brain tissue-complete characterization reveals fucosylated hybrid and complex structures. Eur. J. Biochem. 251, 691-703
    • (1998) Eur. J. Biochem. , vol.251 , pp. 691-703
    • Chen, Y.J.1    Wing, D.R.2    Guile, G.R.3    Dwek, R.A.4    Harvey, D.J.5    Zamze, S.6
  • 44
    • 0032533383 scopus 로고    scopus 로고
    • Sialylated N-Glycans in adult rat brain tissue-A widespread distribution of disialylated antennae in complex and hybrid structures
    • Zamze, S., Harvey, D. J., Chen, Y. J., Guile, G. R., Dwek, R. A., and Wing, D. R. (1998) Sialylated N-glycans in adult rat brain tissue-a widespread distribution of disialylated antennae in complex and hybrid structures. Eur. J. Biochem. 258, 243-270
    • (1998) Eur. J. Biochem. , vol.258 , pp. 243-270
    • Zamze, S.1    Harvey, D.J.2    Chen, Y.J.3    Guile, G.R.4    Dwek, R.A.5    Wing, D.R.6
  • 45
    • 0031745290 scopus 로고    scopus 로고
    • Identification of lectin-purified neural glycoproteins, GPs 180, 116, and 110, with NMDA and AMPA receptor subunits: Conservation of glycosylation at the synapse
    • Clark, R. A., Gurd, J. W., Bissoon, N., Tricaud, N., Molnar, E., Zamze, S. E., Dwek, R. A., McIlhinney, R. A., and Wing, D. R. (1998) Identification of lectin-purified neural glycoproteins, GPs 180, 116, and 110, with NMDA and AMPA receptor subunits: conservation of glycosylation at the synapse. J. Neurochem. 70, 2594-2605
    • (1998) J. Neurochem. , vol.70 , pp. 2594-2605
    • Clark, R.A.1    Gurd, J.W.2    Bissoon, N.3    Tricaud, N.4    Molnar, E.5    Zamze, S.E.6    Dwek, R.A.7    McIlhinney, R.A.8    Wing, D.R.9
  • 46
    • 77950498615 scopus 로고    scopus 로고
    • Glycan analysis of the chicken synaptic plasma membrane glycoproteins-A major synaptic N-glycan carries the LewisX determinant
    • Koles, K., McDowell, W., Mileusnic, R., and Rose, S. P. (2005) Glycan analysis of the chicken synaptic plasma membrane glycoproteins-a major synaptic N-glycan carries the LewisX determinant. Int. J. Biol. Sci. 1, 126-134
    • (2005) Int. J. Biol. Sci. , vol.1 , pp. 126-134
    • Koles, K.1    McDowell, W.2    Mileusnic, R.3    Rose, S.P.4
  • 47
    • 77951830268 scopus 로고    scopus 로고
    • Challenges of determining O-glycopeptide heterogeneity: A fungal glucanase model system
    • Christiansen, M. N., Kolarich, D., Nevalainen, H., Packer, N. H., and Jensen, P. H. (2010) Challenges of determining O-glycopeptide heterogeneity: a fungal glucanase model system. Anal. Chem. 82, 3500-3509
    • (2010) Anal. Chem. , vol.82 , pp. 3500-3509
    • Christiansen, M.N.1    Kolarich, D.2    Nevalainen, H.3    Packer, N.H.4    Jensen, P.H.5
  • 48
    • 0033551196 scopus 로고    scopus 로고
    • Site-specific characterization of the N-linked glycans of murine prion protein by highperformance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions
    • Stimson, E., Hope, J., Chong, A., and Burlingame, A. L. (1999) Site-specific characterization of the N-linked glycans of murine prion protein by highperformance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions. Biochemistry 38, 4885-4895
    • (1999) Biochemistry , vol.38 , pp. 4885-4895
    • Stimson, E.1    Hope, J.2    Chong, A.3    Burlingame, A.L.4
  • 49
    • 77956545752 scopus 로고    scopus 로고
    • Improving software performance for peptide electron transfer dissociation data analysis by implementation of charge state- and sequence-dependent scoring
    • Baker, P. R., Medzihradszky, K. F., and Chalkley, R. J. (2010) Improving software performance for peptide electron transfer dissociation data analysis by implementation of charge state- and sequence-dependent scoring. Mol. Cell Proteomics 9, 1795-1803
    • (2010) Mol. Cell Proteomics , vol.9 , pp. 1795-1803
    • Baker, P.R.1    Medzihradszky, K.F.2    Chalkley, R.J.3
  • 50
    • 0035854496 scopus 로고    scopus 로고
    • Glycoprotein synthesis at the synapse: Fractionation of polypeptides synthesized within isolated dendritic fragments by concanavalin A affinity chromatography
    • Villanueva, S., and Steward, O. (2001) Glycoprotein synthesis at the synapse: fractionation of polypeptides synthesized within isolated dendritic fragments by concanavalin A affinity chromatography. Brain Res. Mol. Brain Res. 91, 137-147
    • (2001) Brain Res. Mol. Brain Res. , vol.91 , pp. 137-147
    • Villanueva, S.1    Steward, O.2
  • 51
    • 79956324370 scopus 로고    scopus 로고
    • Synapsin 1 is an oligomannosecarrying glycoprotein, acts as an oligomannose-binding lectin, and promotes neurite outgrowth and neuronal survival when released via gliaderived exosomes
    • Wang, S., Cesca, F., Loers, G., Schweizer, M., Buck, F., Benfenati, F., Schachner, M., and Kleene, R. (2011) Synapsin 1 is an oligomannosecarrying glycoprotein, acts as an oligomannose-binding lectin, and promotes neurite outgrowth and neuronal survival when released via gliaderived exosomes. J. Neurosci. 31, 7275-7290
    • (2011) J. Neurosci. , vol.31 , pp. 7275-7290
    • Wang, S.1    Cesca, F.2    Loers, G.3    Schweizer, M.4    Buck, F.5    Benfenati, F.6    Schachner, M.7    Kleene, R.8
  • 52
    • 33747890974 scopus 로고    scopus 로고
    • Inhibition of hybrid- and complex-type glycosylation reveals the presence of the GlcNAc transferase 1-independent fucosylation pathway
    • Crispin, M., Harvey, D. J., Chang, V. T., Yu, C., Aricescu, A. R., Jones, E. Y., Davis, S. J., Dwek, R. A., and Rudd, P. M. (2006) Inhibition of hybrid- and complex-type glycosylation reveals the presence of the GlcNAc transferase 1-independent fucosylation pathway. Glycobiology 16, 748-756
    • (2006) Glycobiology , vol.16 , pp. 748-756
    • Crispin, M.1    Harvey, D.J.2    Chang, V.T.3    Yu, C.4    Aricescu, A.R.5    Jones, E.Y.6    Davis, S.J.7    Dwek, R.A.8    Rudd, P.M.9
  • 53
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D. F., Gnad, F., Wiś niewski, J. R., and Mann, M. (2010) Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141, 897-907
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wiśniewski, J.R.3    Mann, M.4
  • 54
    • 77952378813 scopus 로고    scopus 로고
    • Glutamine-linked and nonconsensus asparagine-linked oligosaccharides present in human recombinant antibodies define novel protein glycosylation motifs
    • Valliere-Douglass, J. F., Eakin, C. M., Wallace, A., Ketchem, R. R., Wang, W., Treuheit, M. J., and Balland, A. (2010) Glutamine-linked and nonconsensus asparagine-linked oligosaccharides present in human recombinant antibodies define novel protein glycosylation motifs. J. Biol. Chem. 285, 16012-16022
    • (2010) J. Biol. Chem. , vol.285 , pp. 16012-16022
    • Valliere-Douglass, J.F.1    Eakin, C.M.2    Wallace, A.3    Ketchem, R.R.4    Wang, W.5    Treuheit, M.J.6    Balland, A.7
  • 55
    • 0242287992 scopus 로고    scopus 로고
    • Glycosidase inhibitors: Update and perspectives on practical use
    • Asano, N. (2003) Glycosidase inhibitors: update and perspectives on practical use. Glycobiology 13, 93R-104R
    • (2003) Glycobiology , vol.13
    • Asano, N.1
  • 56
    • 77952034762 scopus 로고    scopus 로고
    • Enrichment of O-GlcNAc modified proteins by the periodate oxidation-hydrazide resin capture approach
    • Klement, E., Lipinszki, Z., Kupihár, Z., Udvardy, A., and Medzihradszky, K. F. (2010) Enrichment of O-GlcNAc modified proteins by the periodate oxidation-hydrazide resin capture approach. J. Proteome Res. 9, 2200-2206
    • (2010) J. Proteome Res. , vol.9 , pp. 2200-2206
    • Klement, E.1    Lipinszki, Z.2    Kupihár, Z.3    Udvardy, A.4    Medzihradszky, K.F.5
  • 58
    • 0022578323 scopus 로고
    • Requirements of cleavage of high mannose oligosaccharides in glycoproteins by peptide N-glycosidase F
    • Chu, F. K. (1986) Requirements of cleavage of high mannose oligosaccharides in glycoproteins by peptide N-glycosidase F. J. Biol. Chem. 261, 172-177
    • (1986) J. Biol. Chem. , vol.261 , pp. 172-177
    • Chu, F.K.1
  • 59
    • 60149111900 scopus 로고    scopus 로고
    • Characterization of glycopeptides by combining collision-induced dissociation and electrontransfer dissociation mass spectrometry data
    • Alley, W. R., Jr., Mechref, Y., and Novotny, M. V. (2009) Characterization of glycopeptides by combining collision-induced dissociation and electrontransfer dissociation mass spectrometry data. Rapid Commun. Mass Spectrom 23, 161-170
    • (2009) Rapid Commun. Mass Spectrom , vol.23 , pp. 161-170
    • Alley, Jr.W.R.1    Mechref, Y.2    Novotny, M.V.3
  • 60
    • 0027205366 scopus 로고
    • O-linked fucose and other posttranslational modifications unique to EGF modules
    • Harris, R. J., and Spellman, M. W. (1993) O-linked fucose and other posttranslational modifications unique to EGF modules. Glycobiology 3, 219-224
    • (1993) Glycobiology , vol.3 , pp. 219-224
    • Harris, R.J.1    Spellman, M.W.2
  • 61
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin
    • Chiba, A., Matsumura, K., Yamada, H., Inazu, T., Shimizu, T., Kusunoki, S., Kanazawa, I., Kobata, A., and Endo, T. (1997) Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin. J. Biol. Chem. 272, 2156-2162
    • (1997) J. Biol. Chem. , vol.272 , pp. 2156-2162
    • Chiba, A.1    Matsumura, K.2    Yamada, H.3    Inazu, T.4    Shimizu, T.5    Kusunoki, S.6    Kanazawa, I.7    Kobata, A.8    Endo, T.9
  • 62
    • 0033179169 scopus 로고    scopus 로고
    • High prevalence of 2-mono- and 2,6-di-substituted manol-terminating sequences among O-glycans released from brain glycopeptides by reductive alkaline hydrolysis
    • Chai, W., Yuen, C. T., Kogelberg, H., Carruthers, R. A., Margolis, R. U., Feizi, T., and Lawson, A. M. (1999) High prevalence of 2-mono- and 2,6-di-substituted manol-terminating sequences among O-glycans released from brain glycopeptides by reductive alkaline hydrolysis. Eur. J. Biochem. 263, 879-888
    • (1999) Eur. J. Biochem. , vol.263 , pp. 879-888
    • Chai, W.1    Yuen, C.T.2    Kogelberg, H.3    Carruthers, R.A.4    Margolis, R.U.5    Feizi, T.6    Lawson, A.M.7
  • 65
    • 57749114758 scopus 로고    scopus 로고
    • Receptor tyrosine phosphatase beta (RPTPbeta) activity and signaling are attenuated by glycosylation and subsequent cell surface galectin-1 binding
    • Abbott, K. L., Matthews, R. T., and Pierce, M. (2008) Receptor tyrosine phosphatase beta (RPTPbeta) activity and signaling are attenuated by glycosylation and subsequent cell surface galectin-1 binding. J. Biol. Chem. 283, 33026-33035
    • (2008) J. Biol. Chem. , vol.283 , pp. 33026-33035
    • Abbott, K.L.1    Matthews, R.T.2    Pierce, M.3
  • 66
    • 62649083636 scopus 로고    scopus 로고
    • Densin-180: Revised membrane topology, domain structure and phosphorylation status
    • Thalhammer, A., Trinidad, J. C., Burlingame, A. L., and Schoepfer, R. (2009) Densin-180: revised membrane topology, domain structure and phosphorylation status. J. Neurochem. 109, 297-302
    • (2009) J. Neurochem. , vol.109 , pp. 297-302
    • Thalhammer, A.1    Trinidad, J.C.2    Burlingame, A.L.3    Schoepfer, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.