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Volumn 7, Issue 25, 2016, Pages 38796-38809

In-depth mapping of the mouse brain N-glycoproteome reveals widespread N-glycosylation of diverse brain proteins

Author keywords

Brain physiological activities; Disease biomarker; Mass spectrometry; Mouse brain; N glycoproteomics

Indexed keywords

CORTICOTROPIN RELEASING FACTOR RECEPTOR 1; GLUTAMATE RECEPTOR; GLYCOPEPTIDE; PROTEOME; BIOLOGICAL MARKER; GLYCOPROTEIN;

EID: 84978066674     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.9737     Document Type: Article
Times cited : (25)

References (41)
  • 1
    • 51649085326 scopus 로고    scopus 로고
    • Mass spectrometry and the emerging field of glycomics
    • Zaia J. Mass spectrometry and the emerging field of glycomics. Chem Biol. 2008; 15:881-892.
    • (2008) Chem Biol , vol.15 , pp. 881-892
    • Zaia, J.1
  • 2
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo K, Marth JD. Glycosylation in cellular mechanisms of health and disease. Cell. 2006; 126: 855-867.
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 4
    • 84891836688 scopus 로고    scopus 로고
    • The role of protein glycosylation in Alzheimer disease
    • Schedin-Weiss S, Winblad B, Tjernberg LO. The role of protein glycosylation in Alzheimer disease. FEBS J. 2014; 281:46-62.
    • (2014) FEBS J , vol.281 , pp. 46-62
    • Schedin-Weiss, S.1    Winblad, B.2    Tjernberg, L.O.3
  • 5
    • 84862787591 scopus 로고    scopus 로고
    • Serum profiling based on fucosylated glycoproteins for differentiating between chronic hepatitis B and hepatocellular carcinoma
    • Liao J, Zhang R, Qian H, Cao L, Zhang Y, Xu W, Li J, Wu M, Yin Z. Serum profiling based on fucosylated glycoproteins for differentiating between chronic hepatitis B and hepatocellular carcinoma. Biochem Biophys Res Commun. 2012; 420:308-314.
    • (2012) Biochem Biophys Res Commun , vol.420 , pp. 308-314
    • Liao, J.1    Zhang, R.2    Qian, H.3    Cao, L.4    Zhang, Y.5    Xu, W.6    Li, J.7    Wu, M.8    Yin, Z.9
  • 6
    • 84892660786 scopus 로고    scopus 로고
    • Glycotherapy: new advances inspire a reemergence of glycans in medicine
    • Hudak JE, Bertozzi CR. Glycotherapy: new advances inspire a reemergence of glycans in medicine. Chem Biol. 2014; 21:16-37.
    • (2014) Chem Biol , vol.21 , pp. 16-37
    • Hudak, J.E.1    Bertozzi, C.R.2
  • 7
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska DF, Gnad F, Wisniewski JR, Mann M. Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell. 2010; 141: 897-907.
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wisniewski, J.R.3    Mann, M.4
  • 8
    • 84861427459 scopus 로고    scopus 로고
    • Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery
    • Zielinska DF, Gnad F, Schropp K, Wisniewski JR, Mann M. Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell. 2012; 46:542-548.
    • (2012) Mol Cell , vol.46 , pp. 542-548
    • Zielinska, D.F.1    Gnad, F.2    Schropp, K.3    Wisniewski, J.R.4    Mann, M.5
  • 11
    • 84901918577 scopus 로고    scopus 로고
    • A Universal Chemical Enrichment Method for Mapping the Yeast N-glycoproteome by MS
    • Chen W, Smeekens JM, Wu R. A Universal Chemical Enrichment Method for Mapping the Yeast N-glycoproteome by MS. Mol Cell Proteomics. 2014; 13:1563-1572.
    • (2014) Mol Cell Proteomics , vol.13 , pp. 1563-1572
    • Chen, W.1    Smeekens, J.M.2    Wu, R.3
  • 12
    • 84896744675 scopus 로고    scopus 로고
    • Comprehensive mapping of protein N-glycosylation in human liver by combining hydrophilic interaction chromatography and hydrazide chemistry
    • Zhu J, Sun Z, Cheng K, Chen R, Ye M, Xu B, Sun D, Wang L, Liu J, Wang F, Zou H. Comprehensive mapping of protein N-glycosylation in human liver by combining hydrophilic interaction chromatography and hydrazide chemistry. J Proteome Res. 2014; 13:1713-1721.
    • (2014) J Proteome Res , vol.13 , pp. 1713-1721
    • Zhu, J.1    Sun, Z.2    Cheng, K.3    Chen, R.4    Ye, M.5    Xu, B.6    Sun, D.7    Wang, L.8    Liu, J.9    Wang, F.10    Zou, H.11
  • 13
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R, Hermjakob H, Sharon N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta. 1999; 1473:4-8.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 14
    • 84946781999 scopus 로고    scopus 로고
    • Fishing the PTM proteome with chemical approaches using functional solid phases
    • Zhang Y, Zhang C, Jiang H, Yang P, Lu H. Fishing the PTM proteome with chemical approaches using functional solid phases. Chem Soc Rev. 2015; 44:8260-8287.
    • (2015) Chem Soc Rev , vol.44 , pp. 8260-8287
    • Zhang, Y.1    Zhang, C.2    Jiang, H.3    Yang, P.4    Lu, H.5
  • 15
    • 84876125044 scopus 로고    scopus 로고
    • High-sensitivity analytical approaches for the structural characterization of glycoproteins
    • Alley WR Jr, Mann BF, Novotny MV. High-sensitivity analytical approaches for the structural characterization of glycoproteins. Chem Rev. 2013; 113:2668-2732.
    • (2013) Chem Rev , vol.113 , pp. 2668-2732
    • Alley, W.R.1    Mann, B.F.2    Novotny, M.V.3
  • 16
    • 61849164561 scopus 로고    scopus 로고
    • Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry
    • Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H. Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009; 8:651-661.
    • (2009) J Proteome Res , vol.8 , pp. 651-661
    • Chen, R.1    Jiang, X.2    Sun, D.3    Han, G.4    Wang, F.5    Ye, M.6    Wang, L.7    Zou, H.8
  • 17
    • 84879795571 scopus 로고    scopus 로고
    • Comparison and optimization of strategies for a more profound profiling of the sialylated N-glycoproteomics in human plasma using metal oxide enrichment
    • Zhao X, Ma C, Han H, Jiang J, Tian F, Wang J, Ying W, Qian X. Comparison and optimization of strategies for a more profound profiling of the sialylated N-glycoproteomics in human plasma using metal oxide enrichment. Anal Bioanal Chem. 2013; 405:5519-5529.
    • (2013) Anal Bioanal Chem , vol.405 , pp. 5519-5529
    • Zhao, X.1    Ma, C.2    Han, H.3    Jiang, J.4    Tian, F.5    Wang, J.6    Ying, W.7    Qian, X.8
  • 18
    • 84881609291 scopus 로고    scopus 로고
    • N-linked glycoproteome profiling of human serum using tandem enrichment and multiple fraction concatenation
    • Ma C, Zhao X, Han H, Tong W, Zhang Q, Qin P, Chang C, Peng B, Ying W, Qian X. N-linked glycoproteome profiling of human serum using tandem enrichment and multiple fraction concatenation. Electrophoresis. 2013; 34:2440-2450.
    • (2013) Electrophoresis , vol.34 , pp. 2440-2450
    • Ma, C.1    Zhao, X.2    Han, H.3    Tong, W.4    Zhang, Q.5    Qin, P.6    Chang, C.7    Peng, B.8    Ying, W.9    Qian, X.10
  • 19
    • 36349019291 scopus 로고    scopus 로고
    • Enhanced N-glycosylation site analysis of sialoglycopeptides by strong cation exchange prefractionation applied to platelet plasma membranes
    • Lewandrowski U, Zahedi RP, Moebius J, Walter U, Sickmann A. Enhanced N-glycosylation site analysis of sialoglycopeptides by strong cation exchange prefractionation applied to platelet plasma membranes. Mol Cell Proteomics. 2007; 6:1933-1941.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1933-1941
    • Lewandrowski, U.1    Zahedi, R.P.2    Moebius, J.3    Walter, U.4    Sickmann, A.5
  • 21
    • 84857873715 scopus 로고    scopus 로고
    • Chemical deamidation: a common pitfall in large-scale N-linked glycoproteomic mass spectrometry-based analyses
    • Palmisano G, Melo-Braga MN, Engholm-Keller K, Parker BL, Larsen MR. Chemical deamidation: a common pitfall in large-scale N-linked glycoproteomic mass spectrometry-based analyses. J Proteome Res. 2012; 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
  • 23
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da W, Sherman BT, Lempicki RA. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc. 2009; 4:44-57.
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 24
    • 5344241223 scopus 로고    scopus 로고
    • LTP and LTD: an embarrassment of riches
    • Malenka RC, Bear MF. LTP and LTD: an embarrassment of riches. Neuron. 2004; 44:5-21.
    • (2004) Neuron , vol.44 , pp. 5-21
    • Malenka, R.C.1    Bear, M.F.2
  • 25
    • 0032742810 scopus 로고    scopus 로고
    • Toward a molecular explanation for long-term potentiation
    • Sweatt JD. Toward a molecular explanation for long-term potentiation. Learn Mem. 1999; 6:399-416.
    • (1999) Learn Mem , vol.6 , pp. 399-416
    • Sweatt, J.D.1
  • 26
    • 34547956306 scopus 로고    scopus 로고
    • Posttranslational modifications and receptor-associated proteins in AMPA receptor trafficking and synaptic plasticity
    • Jiang J, Suppiramaniam V, Wooten MW. Posttranslational modifications and receptor-associated proteins in AMPA receptor trafficking and synaptic plasticity. Neurosignals. 2006; 15:266-282.
    • (2006) Neurosignals , vol.15 , pp. 266-282
    • Jiang, J.1    Suppiramaniam, V.2    Wooten, M.W.3
  • 27
    • 84940176018 scopus 로고    scopus 로고
    • Loss of alpha1, 6-fucosyltransferase decreases hippocampal long term potentiation: implictions for core fucosylation in the regulation of AMPA receptor heteromerization and cellular signaling
    • Gu W, Fukuda T, Isaji T, Hang Q, Lee HH, Sakai S, Morise J, Mitoma J, Higashi H, Taniguchi N, Yawo H, Oka S, Gu J. Loss of alpha1, 6-fucosyltransferase decreases hippocampal long term potentiation: implictions for core fucosylation in the regulation of AMPA receptor heteromerization and cellular signaling. J Biol Chem. 2015; 290:17566-17575.
    • (2015) J Biol Chem , vol.290 , pp. 17566-17575
    • Gu, W.1    Fukuda, T.2    Isaji, T.3    Hang, Q.4    Lee, H.H.5    Sakai, S.6    Morise, J.7    Mitoma, J.8    Higashi, H.9    Taniguchi, N.10    Yawo, H.11    Oka, S.12    Gu, J.13
  • 28
    • 0344457344 scopus 로고    scopus 로고
    • Glycosylation of proteins during a critical time window is necessary for the maintenance of long-term potentiation in the hippocampal CA1 region
    • Matthies HJ, Kretlow J, Matthies H, Smalla KH, Staak S, Krug M. Glycosylation of proteins during a critical time window is necessary for the maintenance of long-term potentiation in the hippocampal CA1 region. Neuroscience. 1999; 91:175-183.
    • (1999) Neuroscience , vol.91 , pp. 175-183
    • Matthies, H.J.1    Kretlow, J.2    Matthies, H.3    Smalla, K.H.4    Staak, S.5    Krug, M.6
  • 30
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimer's Disease
    • Goedert M, Spillantini MG. A century of Alzheimer's Disease. Science. 2006; 314:777-781.
    • (2006) Science , vol.314 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 31
    • 75449102536 scopus 로고    scopus 로고
    • Mechanisms Of Disease Alzheimer's Disease
    • Querfurth HW, LaFerla FM. Mechanisms Of Disease Alzheimer's Disease. New Engl J Med. 2010; 362:329-344.
    • (2010) New Engl J Med , vol.362 , pp. 329-344
    • Querfurth, H.W.1    LaFerla, F.M.2
  • 32
    • 79251552289 scopus 로고    scopus 로고
    • Lectin-affinity chromatography brain glycoproteomics and Alzheimer disease: insights into protein alterations consistent with the pathology and progression of this dementing disorder
    • Butterfield DA, Owen JB. Lectin-affinity chromatography brain glycoproteomics and Alzheimer disease: insights into protein alterations consistent with the pathology and progression of this dementing disorder. Proteomics Clin Appl. 2011; 5:50-56.
    • (2011) Proteomics Clin Appl , vol.5 , pp. 50-56
    • Butterfield, D.A.1    Owen, J.B.2
  • 34
    • 0345390947 scopus 로고    scopus 로고
    • Molecular Isoform Distribution and Glycosylation of Acetylcholinesterase Are Altered in Brain and Cerebrospinal Fluid of Patients with Alzheimer's Disease
    • Sáez-Valero J, Sberna G, McLean CA, Small DH. Molecular Isoform Distribution and Glycosylation of Acetylcholinesterase Are Altered in Brain and Cerebrospinal Fluid of Patients with Alzheimer's Disease. J Neurochem. 1999; 72:1600-1608.
    • (1999) J Neurochem , vol.72 , pp. 1600-1608
    • Sáez-Valero, J.1    Sberna, G.2    McLean, C.A.3    Small, D.H.4
  • 37
    • 84899978366 scopus 로고    scopus 로고
    • Biomarkers in Alzheimer's disease analysis by mass spectrometry-based proteomics
    • Liu Y, Qing H, Deng Y. Biomarkers in Alzheimer's disease analysis by mass spectrometry-based proteomics. Int J Mol Sci. 2014; 15:7865-7882.
    • (2014) Int J Mol Sci , vol.15 , pp. 7865-7882
    • Liu, Y.1    Qing, H.2    Deng, Y.3
  • 40
    • 84928719458 scopus 로고    scopus 로고
    • Releasing N-glycan from peptide N-terminus by N-terminal succinylation assisted enzymatic deglycosylation
    • Weng Y, Sui Z, Jiang H, Shan Y, Chen L, Zhang S, Zhang L, Zhang Y. Releasing N-glycan from peptide N-terminus by N-terminal succinylation assisted enzymatic deglycosylation. Sci Rep. 2015; 5:9770.
    • (2015) Sci Rep , vol.5 , pp. 9770
    • Weng, Y.1    Sui, Z.2    Jiang, H.3    Shan, Y.4    Chen, L.5    Zhang, S.6    Zhang, L.7    Zhang, Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.