메뉴 건너뛰기




Volumn 207, Issue 2, 2011, Pages 91-96

Hypoxia upregulates the expression of the O-linked N-acetylglucosamine containing epitope H in human ependymal cells

Author keywords

Ependymal cells; Epitope H; Hypoxia; O GlcNAc

Indexed keywords

EPITOPE; EPITOPE H; N ACETYLGLUCOSAMINE; O LINKED N ACETYLGLUCOSAMINE; UNCLASSIFIED DRUG;

EID: 79551575002     PISSN: 03440338     EISSN: 16180631     Source Type: Journal    
DOI: 10.1016/j.prp.2010.10.008     Document Type: Article
Times cited : (8)

References (57)
  • 1
    • 33846488647 scopus 로고    scopus 로고
    • Elevation of the post-translational modification of proteins by O-linked N-acetylglucosamine leads to deterioration of the glucose-stimulated insulin secretion in the pancreas of diabetic Goto-Kakizaki rats
    • Akimoto Y., Hart G.W., Wells L., Vosseller K., Yamamoto K., Munetomo E., Ohara-Imaizumi M., Nishiwaki C., Nagamatsu S., Hirano H., et al. Elevation of the post-translational modification of proteins by O-linked N-acetylglucosamine leads to deterioration of the glucose-stimulated insulin secretion in the pancreas of diabetic Goto-Kakizaki rats. Glycobiology 2007, 17:127-140.
    • (2007) Glycobiology , vol.17 , pp. 127-140
    • Akimoto, Y.1    Hart, G.W.2    Wells, L.3    Vosseller, K.4    Yamamoto, K.5    Munetomo, E.6    Ohara-Imaizumi, M.7    Nishiwaki, C.8    Nagamatsu, S.9    Hirano, H.10
  • 3
    • 0035033440 scopus 로고    scopus 로고
    • Reactive astrocytes upregulate one or more gene products that are recognized by monoclonal antibody H
    • Arvanitis D.L., Stavridou A.I., Mori de Moro G., Szuchet S. Reactive astrocytes upregulate one or more gene products that are recognized by monoclonal antibody H. Cell Tissue Res. 2001, 304:11-19.
    • (2001) Cell Tissue Res. , vol.304 , pp. 11-19
    • Arvanitis, D.L.1    Stavridou, A.I.2    Mori de Moro, G.3    Szuchet, S.4
  • 4
    • 27144483390 scopus 로고    scopus 로고
    • The expression of the epitope H recognized by the monoclonal antibody H is higher in astrocytomas compared to anaplastic astrocytomas and glioblastomas
    • Arvanitis D.L., Arvanitis L.D., Panourias I.G., Kitsoulis P., Kanavaros P. The expression of the epitope H recognized by the monoclonal antibody H is higher in astrocytomas compared to anaplastic astrocytomas and glioblastomas. Histol. Histopathol. 2005, 20:1057-1063.
    • (2005) Histol. Histopathol. , vol.20 , pp. 1057-1063
    • Arvanitis, D.L.1    Arvanitis, L.D.2    Panourias, I.G.3    Kitsoulis, P.4    Kanavaros, P.5
  • 5
    • 18744374462 scopus 로고    scopus 로고
    • Mitochondria-rich normal, metaplastic and neoplastic cells show overexpression of the epitope H recognized by the monoclonal antibody H
    • Arvanitis D.L., Arvanitis L.D., Panourias I.G., Kitsoulis P., Kanavaros P. Mitochondria-rich normal, metaplastic and neoplastic cells show overexpression of the epitope H recognized by the monoclonal antibody H. Pathol. Res. Pract. 2005, 201:319-324.
    • (2005) Pathol. Res. Pract. , vol.201 , pp. 319-324
    • Arvanitis, D.L.1    Arvanitis, L.D.2    Panourias, I.G.3    Kitsoulis, P.4    Kanavaros, P.5
  • 6
    • 70349326052 scopus 로고    scopus 로고
    • The expression of the O-linked N-acetylglucosamine containing epitope H in the gemistocytic, pilocytic and subependymal giant cell astrocytomas
    • Arvanitis L.D., Koukoulis G.K., Kanavaros P. The expression of the O-linked N-acetylglucosamine containing epitope H in the gemistocytic, pilocytic and subependymal giant cell astrocytomas. Oncol. Rep. 2009, 22:521-524.
    • (2009) Oncol. Rep. , vol.22 , pp. 521-524
    • Arvanitis, L.D.1    Koukoulis, G.K.2    Kanavaros, P.3
  • 9
    • 77949769388 scopus 로고    scopus 로고
    • O-linked beta-N-acetylglucosamine (O-GlcNAc): extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress
    • Butkinaree C., Park K., Hart G.W. O-linked beta-N-acetylglucosamine (O-GlcNAc): extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochim. Biophys. Acta 2010, 1800:96-106.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 96-106
    • Butkinaree, C.1    Park, K.2    Hart, G.W.3
  • 10
    • 33846317766 scopus 로고    scopus 로고
    • Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein-associated O-GlcNAc
    • Champattanachai V., Marchase R.B., Chatham J.C. Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein-associated O-GlcNAc. Am. J. Physiol. Cell Physiol. 2007, 292:178-187.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292 , pp. 178-187
    • Champattanachai, V.1    Marchase, R.B.2    Chatham, J.C.3
  • 11
    • 40949083086 scopus 로고    scopus 로고
    • Hexosamine biosynthesis and protein O-glycosylation: the first line of defense against stress, ischemia, and trauma
    • Chatham J.C., Nöt L.G., Fülöp N., Marchase R.B. Hexosamine biosynthesis and protein O-glycosylation: the first line of defense against stress, ischemia, and trauma. Shock 2008, 29:431-440.
    • (2008) Shock , vol.29 , pp. 431-440
    • Chatham, J.C.1    Nöt, L.G.2    Fülöp, N.3    Marchase, R.B.4
  • 12
    • 0034718570 scopus 로고    scopus 로고
    • Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor beta
    • Cheng X., Cole R.N., Zaia J., Hart G.W. Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor beta. Biochemistry 2000, 39:11609-11620.
    • (2000) Biochemistry , vol.39 , pp. 11609-11620
    • Cheng, X.1    Cole, R.N.2    Zaia, J.3    Hart, G.W.4
  • 13
    • 0035971067 scopus 로고    scopus 로고
    • Alternative O-glycosylation/O-phosphorylation of serine-16 in murine estrogen receptor beta: post-translational regulation of turnover and transactivation activity
    • Cheng X., Hart G.W. Alternative O-glycosylation/O-phosphorylation of serine-16 in murine estrogen receptor beta: post-translational regulation of turnover and transactivation activity. J. Biol. Chem. 2001, 276:10570-10575.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10570-10575
    • Cheng, X.1    Hart, G.W.2
  • 14
    • 0026662974 scopus 로고
    • Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18
    • Chou C.F., Smith A.J., Omary B.M. Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18. J. Biol. Chem. 1992, 267:3901-3906.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3901-3906
    • Chou, C.F.1    Smith, A.J.2    Omary, B.M.3
  • 15
    • 0034962777 scopus 로고    scopus 로고
    • O-linked N-acetylglycosamine and cancer: messages from the glycosylation of c-myc
    • Chou T.Y., Hart G.W. O-linked N-acetylglycosamine and cancer: messages from the glycosylation of c-myc. Adv. Exp. Med. Biol. 2001, 491:413-418.
    • (2001) Adv. Exp. Med. Biol. , vol.491 , pp. 413-418
    • Chou, T.Y.1    Hart, G.W.2
  • 16
    • 0242582455 scopus 로고    scopus 로고
    • Diabetes and the accompanying hyperglycemia impairs cardiomyocyte cycling through increased nuclear O-GlcNAcylation
    • Clark R.J., McDonough P.M., Swanson E., Trost S.U., Suzuki M., Fukuda M., Dillmann W.H. Diabetes and the accompanying hyperglycemia impairs cardiomyocyte cycling through increased nuclear O-GlcNAcylation. J. Biol. Chem. 2003, 278:44230-44237.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44230-44237
    • Clark, R.J.1    McDonough, P.M.2    Swanson, E.3    Trost, S.U.4    Suzuki, M.5    Fukuda, M.6    Dillmann, W.H.7
  • 18
    • 0035180299 scopus 로고    scopus 로고
    • Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site
    • Du X.L., Edelstein D., Dimmeler S., Ju Q., Sui C., Brownlee M. Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site. J. Clin. Invest. 2001, 108:1341-1348.
    • (2001) J. Clin. Invest. , vol.108 , pp. 1341-1348
    • Du, X.L.1    Edelstein, D.2    Dimmeler, S.3    Ju, Q.4    Sui, C.5    Brownlee, M.6
  • 19
    • 0035864384 scopus 로고    scopus 로고
    • Use of galactosyltransferase to assess the biological function of O-linked N-acetyl-d-glycosamine A potential role for O-GlcNAc during cell division
    • Fang B., Miller M.W. Use of galactosyltransferase to assess the biological function of O-linked N-acetyl-d-glycosamine A potential role for O-GlcNAc during cell division. Exp. Cell Res. 2001, 263:243-253.
    • (2001) Exp. Cell Res. , vol.263 , pp. 243-253
    • Fang, B.1    Miller, M.W.2
  • 20
    • 0030787345 scopus 로고    scopus 로고
    • Increased flux through the hexosamine biosynthesis pathway inhibits glucose transport acutely by activation of protein kinase C
    • Filippis A., Clark S., Proietto J. Increased flux through the hexosamine biosynthesis pathway inhibits glucose transport acutely by activation of protein kinase C. Biochem. J. 1997, 324:981-985.
    • (1997) Biochem. J. , vol.324 , pp. 981-985
    • Filippis, A.1    Clark, S.2    Proietto, J.3
  • 22
    • 0037709390 scopus 로고    scopus 로고
    • The transcription factor PDX-1 is post-translationally modified by O-linked N-acetylglucosamine and this modification is correlated with its DNA binding activity and insulin secretion in min6 beta-cells
    • Gao Y., Miyazaki J., Hart G.W. The transcription factor PDX-1 is post-translationally modified by O-linked N-acetylglucosamine and this modification is correlated with its DNA binding activity and insulin secretion in min6 beta-cells. Arch. Biochem. Biophys. 2003, 415:155-163.
    • (2003) Arch. Biochem. Biophys. , vol.415 , pp. 155-163
    • Gao, Y.1    Miyazaki, J.2    Hart, G.W.3
  • 24
    • 0031566266 scopus 로고    scopus 로고
    • O-glycosylation of nuclear and cytoplasmic proteins: regulation analogous to phosphorylation?
    • Haltiwagner R.S, Busby S., Grove K. O-glycosylation of nuclear and cytoplasmic proteins: regulation analogous to phosphorylation?. Biochem. Biophys. Res. Commun. 1997, 231:237-242.
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 237-242
    • Haltiwagner, R.S.1    Busby, S.2    Grove, K.3
  • 25
    • 77949295164 scopus 로고    scopus 로고
    • The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine
    • Hanover J.A., Krause M.W., Love D.C. The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine. Biochim. Biophys. Acta 2010, 1800:80-95.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 80-95
    • Hanover, J.A.1    Krause, M.W.2    Love, D.C.3
  • 26
    • 0030943923 scopus 로고    scopus 로고
    • Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
    • Hart G.W. Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu. Rev. Biochem. 1997, 66:315-335.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 315-335
    • Hart, G.W.1
  • 28
    • 0036231781 scopus 로고    scopus 로고
    • Flux through the hexosamine pathway is a determinant of nuclear factor kappaB-dependent promoter activation
    • James L.R., Tang D., Ingram A., Ly H., Thai K., Cai L., Scholey J.W. Flux through the hexosamine pathway is a determinant of nuclear factor kappaB-dependent promoter activation. Diabetes 2002, 51:1146-1156.
    • (2002) Diabetes , vol.51 , pp. 1146-1156
    • James, L.R.1    Tang, D.2    Ingram, A.3    Ly, H.4    Thai, K.5    Cai, L.6    Scholey, J.W.7
  • 29
    • 4444337997 scopus 로고    scopus 로고
    • Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain
    • Khidekel N., Ficarro S.B., Peters E.C., Hsieh-Wilson L.C. Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:13132-13137.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13132-13137
    • Khidekel, N.1    Ficarro, S.B.2    Peters, E.C.3    Hsieh-Wilson, L.C.4
  • 30
    • 0014198738 scopus 로고
    • Studies on l-glutamine d-fructose 6-phosphate amidotransferase I. Feedback inhibition by uridine diphosphate-N-acetylglucosamine
    • Kornfeld R. Studies on l-glutamine d-fructose 6-phosphate amidotransferase I. Feedback inhibition by uridine diphosphate-N-acetylglucosamine. J. Biol. Chem. 1967, 242:3135-3141.
    • (1967) J. Biol. Chem. , vol.242 , pp. 3135-3141
    • Kornfeld, R.1
  • 31
    • 33746904776 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine suppresses thermal aggregation of Sp1
    • Lim K.H., Chang H.I. O-linked N-acetylglucosamine suppresses thermal aggregation of Sp1. FEBS Lett. 2006, 580:4645-4652.
    • (2006) FEBS Lett. , vol.580 , pp. 4645-4652
    • Lim, K.H.1    Chang, H.I.2
  • 32
    • 31444452075 scopus 로고    scopus 로고
    • Increased hexosamine biosynthesis and protein O-GlcNAc levels associated with myocardial protection against calcium paradox and ischemia
    • Liu J., Pang Y., Chang T., Bounelis P., Chatham J.C., Marchase R.B. Increased hexosamine biosynthesis and protein O-GlcNAc levels associated with myocardial protection against calcium paradox and ischemia. J. Mol. Cell Cardiol. 2006, 40:303-312.
    • (2006) J. Mol. Cell Cardiol. , vol.40 , pp. 303-312
    • Liu, J.1    Pang, Y.2    Chang, T.3    Bounelis, P.4    Chatham, J.C.5    Marchase, R.B.6
  • 33
    • 33644874204 scopus 로고    scopus 로고
    • The hexosamine signaling pathway: deciphering the " O-GlcNAc code"
    • Love D.C., Hanover J.A. The hexosamine signaling pathway: deciphering the " O-GlcNAc code" Sci. STKE 2005, 312:re13.
    • (2005) Sci. STKE , vol.312
    • Love, D.C.1    Hanover, J.A.2
  • 34
    • 9444252281 scopus 로고    scopus 로고
    • Insulin stimulates and diabetes inhibits O-linked N-acetylglucosamine transferase and O-glycosylation of Sp1
    • Majumdar G., Wright J., Markowitz P., Martinez-Hernandez A., Raghow R., Solomon S.S. Insulin stimulates and diabetes inhibits O-linked N-acetylglucosamine transferase and O-glycosylation of Sp1. Diabetes 2004, 53:3184-3192.
    • (2004) Diabetes , vol.53 , pp. 3184-3192
    • Majumdar, G.1    Wright, J.2    Markowitz, P.3    Martinez-Hernandez, A.4    Raghow, R.5    Solomon, S.S.6
  • 37
    • 0344298921 scopus 로고    scopus 로고
    • Activation of the hexosamine pathway by glucosamine in vivo induces insulin resistance of early postreceptor insulin signaling events in skeletal muscle
    • Patti M.E., Virkamaki A., Landaker E.J., Kahn C.R., Yki-Jarvinen H. Activation of the hexosamine pathway by glucosamine in vivo induces insulin resistance of early postreceptor insulin signaling events in skeletal muscle. Diabetes 1999, 48:1562-1571.
    • (1999) Diabetes , vol.48 , pp. 1562-1571
    • Patti, M.E.1    Virkamaki, A.2    Landaker, E.J.3    Kahn, C.R.4    Yki-Jarvinen, H.5
  • 41
    • 0029670515 scopus 로고    scopus 로고
    • Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin
    • Roquemore E.P., Chevrier M.R., Cotter R.J., Hart G.W. Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin. Biochemistry 1996, 35:3578-3586.
    • (1996) Biochemistry , vol.35 , pp. 3578-3586
    • Roquemore, E.P.1    Chevrier, M.R.2    Cotter, R.J.3    Hart, G.W.4
  • 43
    • 0030071548 scopus 로고    scopus 로고
    • Regulation of specific DNA binding by p53: evidence for a role for O-glycosylation and charged residues at the carboxy-terminus
    • Shaw P., Freeman J., Bovey R., Iggo R. Regulation of specific DNA binding by p53: evidence for a role for O-glycosylation and charged residues at the carboxy-terminus. Oncogene 1996, 12:921-930.
    • (1996) Oncogene , vol.12 , pp. 921-930
    • Shaw, P.1    Freeman, J.2    Bovey, R.3    Iggo, R.4
  • 44
    • 0036087478 scopus 로고    scopus 로고
    • Preconditioning prevents alterations in cardiac SR gene expression due to ischemia-reperfusion
    • Temsah R.M., Kawabata K., Chapman D., Dhalla N.S. Preconditioning prevents alterations in cardiac SR gene expression due to ischemia-reperfusion. Am. J. Physiol. Heart Circ. Physiol. 2002, 282:1461-1466.
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.282 , pp. 1461-1466
    • Temsah, R.M.1    Kawabata, K.2    Chapman, D.3    Dhalla, N.S.4
  • 46
    • 34548438595 scopus 로고    scopus 로고
    • Dynamic interplay between O-GlcNAcylation and GSK-3-dependent phosphorylation
    • Wang Z., Pandey A., Hart G.W. Dynamic interplay between O-GlcNAcylation and GSK-3-dependent phosphorylation. Mol. Cell Proteomics 2007, 6:1365-1379.
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 1365-1379
    • Wang, Z.1    Pandey, A.2    Hart, G.W.3
  • 47
    • 52949123249 scopus 로고    scopus 로고
    • Cross-talk between GlcNAcylation and phosphorylation: site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc
    • Wang Z., Gucek M., Hart G.W. Cross-talk between GlcNAcylation and phosphorylation: site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:13793-137938.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 13793-137938
    • Wang, Z.1    Gucek, M.2    Hart, G.W.3
  • 48
    • 0037127198 scopus 로고    scopus 로고
    • Dynamic O- glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic β-N-acetylglycosaminidase, O-GlcNAcase
    • Wells L., Gao Y., Mahoney K., Vosseler C., Chen A., Rosen A., Hart G.W. Dynamic O- glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic β-N-acetylglycosaminidase, O-GlcNAcase. J. Biol. Chem. 2002, 277:1755-1761.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1755-1761
    • Wells, L.1    Gao, Y.2    Mahoney, K.3    Vosseler, C.4    Chen, A.5    Rosen, A.6    Hart, G.W.7
  • 49
    • 0037436818 scopus 로고    scopus 로고
    • O-GlcNAc: a regulatory post-translational modification
    • Wells L., Whelan S.A., Hart G.W. O-GlcNAc: a regulatory post-translational modification. Biochem. Biophys. Res. Com. 2003, 302:435-441.
    • (2003) Biochem. Biophys. Res. Com. , vol.302 , pp. 435-441
    • Wells, L.1    Whelan, S.A.2    Hart, G.W.3
  • 50
    • 0344011957 scopus 로고    scopus 로고
    • Proteomic approaches to analyze the dynamic relationships between nucleocytoplasmic protein glycosylation and phosphorylation
    • Whelan S.A., Hart G.W. Proteomic approaches to analyze the dynamic relationships between nucleocytoplasmic protein glycosylation and phosphorylation. Circ. Res. 2003, 93:1047-1058.
    • (2003) Circ. Res. , vol.93 , pp. 1047-1058
    • Whelan, S.A.1    Hart, G.W.2
  • 51
    • 0036462599 scopus 로고    scopus 로고
    • The emerging significance of O-GlcNAc in cellular regulation
    • Zachara N.E., Hart G.W. The emerging significance of O-GlcNAc in cellular regulation. Chem. Rev. 2002, 102:431-438.
    • (2002) Chem. Rev. , vol.102 , pp. 431-438
    • Zachara, N.E.1    Hart, G.W.2
  • 52
    • 3042613480 scopus 로고    scopus 로고
    • O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress
    • Zachara N.E., Hart G.W. O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress. Biochem. Biophys. Acta 2004, 1673:13-28.
    • (2004) Biochem. Biophys. Acta , vol.1673 , pp. 13-28
    • Zachara, N.E.1    Hart, G.W.2
  • 53
    • 3042534011 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress A survival response of mammalian cells
    • Zachara N.E., O'Donnell N., Cheung W.D., Mercer J.J., Marth J.D., Hart G.W. Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress A survival response of mammalian cells. J. Biol. Chem. 2004, 279:30133-30142.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30133-30142
    • Zachara, N.E.1    O'Donnell, N.2    Cheung, W.D.3    Mercer, J.J.4    Marth, J.D.5    Hart, G.W.6
  • 54
    • 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 2006, 1761:599-617.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 599-617
    • Zachara, N.E.1    Hart, G.W.2
  • 55
    • 72449187655 scopus 로고    scopus 로고
    • The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways
    • Zeidan Q., Hart G.W. The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways. J. Cell Sci. 2010, 123:13-22.
    • (2010) J. Cell Sci. , vol.123 , pp. 13-22
    • Zeidan, Q.1    Hart, G.W.2
  • 56
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang F., Su K., Yang X., Bowe D.B., Paterson A.J., Kudlow J.E. O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell 2003, 115:715-725.
    • (2003) Cell , vol.115 , pp. 715-725
    • Zhang, F.1    Su, K.2    Yang, X.3    Bowe, D.B.4    Paterson, A.J.5    Kudlow, J.E.6
  • 57
    • 61949134041 scopus 로고    scopus 로고
    • The protective effect of glucosamine on cardiac function following trauma hemorrhage: downregulation of cardiac NF-[kappa]B signaling
    • Zou L.Y., Yang S., Chaudry I.H., Marchase R.B., Chatham J.C. The protective effect of glucosamine on cardiac function following trauma hemorrhage: downregulation of cardiac NF-[kappa]B signaling. Am. J. Physiol. Heart Circ. Physiol. 2009, 296:515-523.
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.296 , pp. 515-523
    • Zou, L.Y.1    Yang, S.2    Chaudry, I.H.3    Marchase, R.B.4    Chatham, J.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.