메뉴 건너뛰기




Volumn 8, Issue 9, 2013, Pages

Glycan Structures Contain Information for the Spatial Arrangement of Glycoproteins in the Plasma Membrane

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN; GLYCOPROTEIN; GLYCOSIDASE; GREEN FLUORESCENT PROTEIN; LECTIN; MANNOSE OLIGOSACCHARIDE; PROTEIN KV3.1; UNCLASSIFIED DRUG; UVOMORULIN;

EID: 84883642451     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0075013     Document Type: Article
Times cited : (18)

References (29)
  • 1
    • 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, (1999) On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta 1473: 4-8.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 2
    • 70449573717 scopus 로고    scopus 로고
    • Biological Roles of Glycans
    • In: Varki A, Cummings R, Esko J, Freeze H, Stanley P, et al., 2nd ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press. Chapter 6
    • Varki A, Lowe J (2009) Biological Roles of Glycans. In: Varki A, Cummings R, Esko J, Freeze H, Stanley P, et al., Essentials of Glycobiology. 2nd ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press. Chapter 6.
    • (2009) Essentials of Glycobiology
    • Varki, A.1    Lowe, J.2
  • 3
    • 78650401291 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation
    • Jaeken J, (2010) Congenital disorders of glycosylation. Ann N Y Acad Sci 1214: 190-198.
    • (2010) Ann N Y Acad Sci , vol.1214 , pp. 190-198
    • Jaeken, J.1
  • 4
    • 0037135585 scopus 로고    scopus 로고
    • Truncated, inactive N-acetylglucosaminyltransferase III (GlcNAc-TIII) induces neurological and other traits absent in mice that lack GlcNAc-TIII
    • Bhattacharyya R, Bhaumik M, Raju TS, Stanley P, (2002) Truncated, inactive N-acetylglucosaminyltransferase III (GlcNAc-TIII) induces neurological and other traits absent in mice that lack GlcNAc-TIII. J Biol Chem 277: 26300-26309.
    • (2002) J Biol Chem , vol.277 , pp. 26300-26309
    • Bhattacharyya, R.1    Bhaumik, M.2    Raju, T.S.3    Stanley, P.4
  • 5
    • 0028012014 scopus 로고
    • Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates
    • Ioffe E, Stanley P, (1994) Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates. Proc Natl Acad Sci U S A 91: 728-732.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 728-732
    • Ioffe, E.1    Stanley, P.2
  • 6
    • 0035714138 scopus 로고    scopus 로고
    • Modeling human congenital disorder of glycosylation type IIa in the mouse: conservation of asparagine-linked glycan-dependent functions in mammalian physiology and insights into disease pathogenesis
    • Wang Y, Tan J, Sutton-Smith M, Ditto D, Panico M, et al. (2001) Modeling human congenital disorder of glycosylation type IIa in the mouse: conservation of asparagine-linked glycan-dependent functions in mammalian physiology and insights into disease pathogenesis. Glycobiology 11: 1051-1070.
    • (2001) Glycobiology , vol.11 , pp. 1051-1070
    • Wang, Y.1    Tan, J.2    Sutton-Smith, M.3    Ditto, D.4    Panico, M.5
  • 8
    • 46449101373 scopus 로고    scopus 로고
    • N-glycosylation affects the adhesive function of E-Cadherin through modifying the composition of adherens junctions (AJs) in human breast carcinoma cell line MDA-MB-435
    • Zhao H, Liang Y, Xu Z, Wang L, Zhou F, et al. (2008) N-glycosylation affects the adhesive function of E-Cadherin through modifying the composition of adherens junctions (AJs) in human breast carcinoma cell line MDA-MB-435. J Cell Biochem 104: 162-175.
    • (2008) J Cell Biochem , vol.104 , pp. 162-175
    • Zhao, H.1    Liang, Y.2    Xu, Z.3    Wang, L.4    Zhou, F.5
  • 9
    • 33847395830 scopus 로고    scopus 로고
    • Complex oligosaccharides are N-linked to Kv3 voltage-gated K+ channels in rat brain
    • Cartwright TA, Corey MJ, Schwalbe RA, (2007) Complex oligosaccharides are N-linked to Kv3 voltage-gated K+ channels in rat brain. Biochim Biophys Acta 1770: 666-671.
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 666-671
    • Cartwright, T.A.1    Corey, M.J.2    Schwalbe, R.A.3
  • 10
    • 84862214081 scopus 로고    scopus 로고
    • Modulation of Voltage-Gated Ion Channels by Sialylation
    • Ednie AR, Bennett ES, (2012) Modulation of Voltage-Gated Ion Channels by Sialylation. Comprehensive Physiology 2: 1269-1301.
    • (2012) Comprehensive Physiology , vol.2 , pp. 1269-1301
    • Ednie, A.R.1    Bennett, E.S.2
  • 11
    • 79955611727 scopus 로고    scopus 로고
    • Importance of glycosylation on function of a potassium channel in neuroblastoma cells
    • Hall MK, Cartwright TA, Fleming CM, Schwalbe RA, (2011) Importance of glycosylation on function of a potassium channel in neuroblastoma cells. PLoS One 6: e19317.
    • (2011) PLoS One , vol.6
    • Hall, M.K.1    Cartwright, T.A.2    Fleming, C.M.3    Schwalbe, R.A.4
  • 12
    • 67649839223 scopus 로고    scopus 로고
    • N-Glycans
    • In: Varki A, Cummings R, Esko J, Freeze H, Stanley P, et al., 2nd ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press. Chapter 8
    • Stanley P, Schachter H, Taniguchi N (2009) N-Glycans. In: Varki A, Cummings R, Esko J, Freeze H, Stanley P, et al., Essentials of Glycobiology. 2nd ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press. Chapter 8.
    • (2009) Essentials of Glycobiology
    • Stanley, P.1    Schachter, H.2    Taniguchi, N.3
  • 13
    • 33751002037 scopus 로고    scopus 로고
    • Lectin-resistant CHO glycosylation mutants
    • Patnaik SK, Stanley P, (2006) Lectin-resistant CHO glycosylation mutants. Methods Enzymol 416: 159-182.
    • (2006) Methods Enzymol , vol.416 , pp. 159-182
    • Patnaik, S.K.1    Stanley, P.2
  • 14
    • 77949325755 scopus 로고    scopus 로고
    • Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity
    • North SJ, Huang HH, Sundaram S, Jang-Lee J, Etienne AT, et al. (2010) Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity. J Biol Chem 285: 5759-5775.
    • (2010) J Biol Chem , vol.285 , pp. 5759-5775
    • North, S.J.1    Huang, H.H.2    Sundaram, S.3    Jang-Lee, J.4    Etienne, A.T.5
  • 15
    • 70350005370 scopus 로고    scopus 로고
    • Atypical sialylated N-glycan structures are attached to neuronal voltage-gated potassium channels
    • Cartwright TA, Schwalbe RA, (2009) Atypical sialylated N-glycan structures are attached to neuronal voltage-gated potassium channels. Biosci Rep 29: 301-313.
    • (2009) Biosci Rep , vol.29 , pp. 301-313
    • Cartwright, T.A.1    Schwalbe, R.A.2
  • 16
    • 39049161608 scopus 로고    scopus 로고
    • Novel Kv3 glycoforms differentially expressed in adult mammalian brain contain sialylated N-glycans
    • Schwalbe RA, Corey MJ, Cartwright TA, (2008) Novel Kv3 glycoforms differentially expressed in adult mammalian brain contain sialylated N-glycans. Biochem Cell Biol 86: 21-30.
    • (2008) Biochem Cell Biol , vol.86 , pp. 21-30
    • Schwalbe, R.A.1    Corey, M.J.2    Cartwright, T.A.3
  • 17
    • 0037641234 scopus 로고    scopus 로고
    • JAM4, a junctional cell adhesion molecule interacting with a tight junction protein, MAGI-1
    • Hirabayashi S, Tajima M, Yao I, Nishimura W, Mori H, et al. (2003) JAM4, a junctional cell adhesion molecule interacting with a tight junction protein, MAGI-1. Mol Cell Biol 23: 4267-4282.
    • (2003) Mol Cell Biol , vol.23 , pp. 4267-4282
    • Hirabayashi, S.1    Tajima, M.2    Yao, I.3    Nishimura, W.4    Mori, H.5
  • 18
    • 33745622194 scopus 로고    scopus 로고
    • Characterization of N-glycosylation consensus sequences in the Kv3.1 channel
    • Brooks NL, Corey MJ, Schwalbe RA, (2006) Characterization of N-glycosylation consensus sequences in the Kv3.1 channel. Febs J 273: 3287-3300.
    • (2006) Febs J , vol.273 , pp. 3287-3300
    • Brooks, N.L.1    Corey, M.J.2    Schwalbe, R.A.3
  • 19
    • 80054078245 scopus 로고    scopus 로고
    • Biochemical engineering of the N-acyl side chain of sialic acids alters the kinetics of a glycosylated potassium channel Kv3.1
    • Hall MK, Reutter W, Lindhorst T, Schwalbe RA, (2011) Biochemical engineering of the N-acyl side chain of sialic acids alters the kinetics of a glycosylated potassium channel Kv3.1. FEBS Lett 585: 3322-3327.
    • (2011) FEBS Lett , vol.585 , pp. 3322-3327
    • Hall, M.K.1    Reutter, W.2    Lindhorst, T.3    Schwalbe, R.A.4
  • 20
    • 70350685770 scopus 로고    scopus 로고
    • Adaptive regulation at the cell surface by N-glycosylation
    • Dennis JW, Lau KS, Demetriou M, Nabi IR, (2009) Adaptive regulation at the cell surface by N-glycosylation. Traffic 10: 1569-1578.
    • (2009) Traffic , vol.10 , pp. 1569-1578
    • Dennis, J.W.1    Lau, K.S.2    Demetriou, M.3    Nabi, I.R.4
  • 21
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • Lau KS, Partridge EA, Grigorian A, Silvescu CI, Reinhold VN, et al. (2007) Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell 129: 123-134.
    • (2007) Cell , vol.129 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3    Silvescu, C.I.4    Reinhold, V.N.5
  • 22
    • 33645102970 scopus 로고    scopus 로고
    • Complex N-glycans are the major ligands for galectin-1, -3, and -8 on Chinese hamster ovary cells
    • Patnaik SK, Potvin B, Carlsson S, Sturm D, Leffler H, et al. (2006) Complex N-glycans are the major ligands for galectin-1,-3, and-8 on Chinese hamster ovary cells. Glycobiology 16: 305-317.
    • (2006) Glycobiology , vol.16 , pp. 305-317
    • Patnaik, S.K.1    Potvin, B.2    Carlsson, S.3    Sturm, D.4    Leffler, H.5
  • 23
    • 33747377812 scopus 로고    scopus 로고
    • N-glycosylation affects the molecular organization and stability of E-cadherin junctions
    • Liwosz A, Lei T, Kukuruzinska MA, (2006) N-glycosylation affects the molecular organization and stability of E-cadherin junctions. J Biol Chem 281: 23138-23149.
    • (2006) J Biol Chem , vol.281 , pp. 23138-23149
    • Liwosz, A.1    Lei, T.2    Kukuruzinska, M.A.3
  • 24
    • 0029933659 scopus 로고    scopus 로고
    • Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis
    • Yoshimura M, Ihara Y, Matsuzawa Y, Taniguchi N, (1996) Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis. J Biol Chem 271: 13811-13815.
    • (1996) J Biol Chem , vol.271 , pp. 13811-13815
    • Yoshimura, M.1    Ihara, Y.2    Matsuzawa, Y.3    Taniguchi, N.4
  • 25
    • 0034061923 scopus 로고    scopus 로고
    • Suppression of tumor growth and metastasis in Mgat5-deficient mice
    • Granovsky M, Fata J, Pawling J, Muller WJ, Khokha R, et al. (2000) Suppression of tumor growth and metastasis in Mgat5-deficient mice. Nat Med 6: 306-312.
    • (2000) Nat Med , vol.6 , pp. 306-312
    • Granovsky, M.1    Fata, J.2    Pawling, J.3    Muller, W.J.4    Khokha, R.5
  • 28
    • 79953721653 scopus 로고    scopus 로고
    • Modulation of E-cadherin function and dysfunction by N-glycosylation
    • Pinho SS, Seruca R, Gartner F, Yamaguchi Y, Gu J, et al. (2011) Modulation of E-cadherin function and dysfunction by N-glycosylation. Cell Mol Life Sci 68: 1011-1020.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 1011-1020
    • Pinho, S.S.1    Seruca, R.2    Gartner, F.3    Yamaguchi, Y.4    Gu, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.