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Volumn 13, Issue 11, 2012, Pages 5653-5657

PpGalNac T1 as a potential novel marker for human bladder cancer

Author keywords

Bladder carcinoma; Glycosylation; Glycosyltransferase; ppGalNAc T1; RNAi

Indexed keywords


EID: 84874064743     PISSN: 15137368     EISSN: 2476762X     Source Type: Journal    
DOI: 10.7314/APJCP.2012.13.11.5653     Document Type: Article
Times cited : (20)

References (13)
  • 1
    • 80052390731 scopus 로고    scopus 로고
    • The effect of glycosylation on the folding kinetics of erythropoietin
    • Banks DD (2011). The effect of glycosylation on the folding kinetics of erythropoietin. J Mol Biol, 412, 536-50.
    • (2011) J Mol Biol , vol.412 , pp. 536-550
    • Banks, D.D.1
  • 2
    • 79960720473 scopus 로고    scopus 로고
    • Glycosylation, galectins and cellular signaling
    • Boscher C, Dennis JW, Nabi IR (2011). Glycosylation, galectins and cellular signaling. Curr Opin Cell Biol, 23, 383-92.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 383-392
    • Boscher, C.1    Dennis, J.W.2    Nabi, I.R.3
  • 3
    • 34250769529 scopus 로고    scopus 로고
    • Immunolocalisation of members of the polypeptide N-acetylgalactosaminyl transferase (ppGalNAc-T) family is consistent with biologically relevant altered cell surface glycosylation in breast cancer
    • Brooks SA, Carter TM, Bennett EP, et al (2007). Immunolocalisation of members of the polypeptide N-acetylgalactosaminyl transferase (ppGalNAc-T) family is consistent with biologically relevant altered cell surface glycosylation in breast cancer. Acta Histochem, 109, 273-84.
    • (2007) Acta Histochem , vol.109 , pp. 273-284
    • Brooks, S.A.1    Carter, T.M.2    Bennett, E.P.3
  • 4
    • 77950474660 scopus 로고    scopus 로고
    • Phase II study of sunitinib in patients with metastatic urothelial cancer
    • Gallagher DJ, Milowsky MI, Gerst SR, et al (2010). Phase II study of sunitinib in patients with metastatic urothelial cancer. J Clin Oncol, 28, 1373-79.
    • (2010) J Clin Oncol , vol.28 , pp. 1373-1379
    • Gallagher, D.J.1    Milowsky, M.I.2    Gerst, S.R.3
  • 5
    • 85027919117 scopus 로고    scopus 로고
    • PpGalNacT2 participating in vanadium-induced HL-60 cell differentiation
    • Gao Y, Tu YB, Guo Y, et al (2011). PpGalNacT2 participating in vanadium-induced HL-60 cell differentiation. Mol Biol Rep, 38, 1483-9.
    • (2011) Mol Biol Rep , vol.38 , pp. 1483-1489
    • Gao, Y.1    Tu, Y.B.2    Guo, Y.3
  • 6
    • 79954612783 scopus 로고    scopus 로고
    • Emerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferases
    • Gerken TA, Jamison O, Perrine CL, et al (2011). Emerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferases. J Biol Chem, 286, 14493-507.
    • (2011) J Biol Chem , vol.286 , pp. 14493-14507
    • Gerken, T.A.1    Jamison, O.2    Perrine, C.L.3
  • 7
    • 77949270759 scopus 로고    scopus 로고
    • Loss of UDPGalNAc: polypeptide N-acetylgalactosaminyltransferase 3 and reduced O-glycosylation in colon carcinoma cells selected for hepatic metastasis
    • Kato K, Takeuchi H, Kanoh A, et al (2010). Loss of UDPGalNAc: polypeptide N-acetylgalactosaminyltransferase 3 and reduced O-glycosylation in colon carcinoma cells selected for hepatic metastasis. Glycoconj J, 27, 267-76.
    • (2010) Glycoconj J , vol.27 , pp. 267-276
    • Kato, K.1    Takeuchi, H.2    Kanoh, A.3
  • 8
    • 83455179090 scopus 로고    scopus 로고
    • An anti-human ppGalNAcT-2 monoclonal antibody
    • Liu C, Lin D, Xu L, et al (2011). An anti-human ppGalNAcT-2 monoclonal antibody. Hybridoma (Larchmt), 30, 549-54.
    • (2011) Hybridoma (Larchmt) , vol.30 , pp. 549-554
    • Liu, C.1    Lin, D.2    Xu, L.3
  • 9
    • 67749133871 scopus 로고    scopus 로고
    • Glycopeptidepreferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2
    • Perrine CL, Ganguli A, Wu P, et al (2009). Glycopeptidepreferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2. J Biol Chem, 284, 20387-97.
    • (2009) J Biol Chem , vol.284 , pp. 20387-20397
    • Perrine, C.L.1    Ganguli, A.2    Wu, P.3
  • 10
    • 70349667473 scopus 로고    scopus 로고
    • Spectrum of phosphatidylinositol 3-kinase pathway gene alterations in bladder cancer
    • Platt FM, Hurst CD, Taylor CF, et al(2009). Spectrum of phosphatidylinositol 3-kinase pathway gene alterations in bladder cancer. Clin Cancer Res, 15, 6008-17.
    • (2009) Clin Cancer Res , vol.15 , pp. 6008-6017
    • Platt, F.M.1    Hurst, C.D.2    Taylor, C.F.3
  • 11
    • 19444369442 scopus 로고    scopus 로고
    • Absence of intraepidermal glycosyltransferase ppGalNac-T3 expression in familial tumoral calcinosis
    • Topaz O, Bergman R, Mandel U, et al(2005). Absence of intraepidermal glycosyltransferase ppGalNac-T3 expression in familial tumoral calcinosis. Am J Dermatopathol, 27, 211-5.
    • (2005) Am J Dermatopathol , vol.27 , pp. 211-215
    • Topaz, O.1    Bergman, R.2    Mandel, U.3
  • 12
    • 84862292485 scopus 로고    scopus 로고
    • Glycosylation of a-dystroglycan: O-mannosylation influences the subsequent addition of GalNAc by UDP-GalNAc polypeptide N-acetylgalactosaminyltransferases
    • Tran DT, Lim JM, Liu M, et al (2012). Glycosylation of a-dystroglycan: O-mannosylation influences the subsequent addition of GalNAc by UDP-GalNAc polypeptide N-acetylgalactosaminyltransferases. J Biol Chem, 287, 20967-74.
    • (2012) J Biol Chem , vol.287 , pp. 20967-20974
    • Tran, D.T.1    Lim, J.M.2    Liu, M.3
  • 13
    • 79959378642 scopus 로고    scopus 로고
    • Catalytic and glycan-binding abilities of ppGalNAc-T2 are regulated by acetylation
    • Zlocowski N, Sendra VG, Lorenz V, et al (2011). Catalytic and glycan-binding abilities of ppGalNAc-T2 are regulated by acetylation. Biochem Biophys Res Commun, 410, 140-5.
    • (2011) Biochem Biophys Res Commun , vol.410 , pp. 140-145
    • Zlocowski, N.1    Sendra, V.G.2    Lorenz, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.