메뉴 건너뛰기




Volumn 12, Issue 4, 2012, Pages 408-413

Beyond the genome and proteome: Targeting protein modifications in cancer

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLGLUCOSAMINIDASE; BIOLOGICAL MARKER; BORTEZOMIB; MEMBRANE RECEPTOR; N ACETYLGALACTOSAMINE; N ACETYLGLUCOSAMINE; N ACETYLGLUCOSAMINYLTRANSFERASE; PALMITIC ACID; PROTEOME;

EID: 84864969137     PISSN: 14714892     EISSN: 14714973     Source Type: Journal    
DOI: 10.1016/j.coph.2012.04.003     Document Type: Review
Times cited : (21)

References (47)
  • 1
    • 79251489778 scopus 로고    scopus 로고
    • Glycomics hits the big time
    • G.W. Hart, and R.J. Copeland Glycomics hits the big time Cell 143 2010 672 676
    • (2010) Cell , vol.143 , pp. 672-676
    • Hart, G.W.1    Copeland, R.J.2
  • 2
    • 70249135667 scopus 로고    scopus 로고
    • Glycosylation diseases: Quo vadis?
    • H. Schachter, and H.H. Freeze Glycosylation diseases: quo vadis? Biochim Biophys Acta 1792 2009 925 930
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 925-930
    • Schachter, H.1    Freeze, H.H.2
  • 3
    • 77951072143 scopus 로고    scopus 로고
    • The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression
    • Y. Song, J.A. Aglipay, J.D. Bernstein, S. Goswami, and P. Stanley The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression Cancer Res 70 2010 3361 3371
    • (2010) Cancer Res , vol.70 , pp. 3361-3371
    • Song, Y.1    Aglipay, J.A.2    Bernstein, J.D.3    Goswami, S.4    Stanley, P.5
  • 4
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • R. Apweiler, H. Hermjakob, and N. Sharon On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database Biochim Biophys Acta 1473 1999 4 8
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 5
    • 0027519943 scopus 로고
    • Protein glycosylation. Structural and functional aspects
    • H. Lis, and N. Sharon Protein glycosylation. Structural and functional aspects Eur J Biochem 218 1993 1 27
    • (1993) Eur J Biochem , vol.218 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 6
    • 0025369545 scopus 로고
    • Effect of the carbohydrate moiety on the secondary structure of beta 2-glycoprotein. I. Implications for the biosynthesis and folding of glycoproteins
    • M.T. Walsh, H. Watzlawick, F.W. Putnam, K. Schmid, and R. Brossmer Effect of the carbohydrate moiety on the secondary structure of beta 2-glycoprotein. I. Implications for the biosynthesis and folding of glycoproteins Biochemistry 29 1990 6250 6257
    • (1990) Biochemistry , vol.29 , pp. 6250-6257
    • Walsh, M.T.1    Watzlawick, H.2    Putnam, F.W.3    Schmid, K.4    Brossmer, R.5
  • 7
    • 0026445723 scopus 로고
    • Selectins: Interpreters of cell-specific carbohydrate information during inflammation
    • L.A. Lasky Selectins: interpreters of cell-specific carbohydrate information during inflammation Science 258 1992 964 969
    • (1992) Science , vol.258 , pp. 964-969
    • Lasky, L.A.1
  • 8
    • 0023661004 scopus 로고
    • Solution conformations of N-linked oligosaccharides
    • S.W. Homans, R.A. Dwek, and T.W. Rademacher Solution conformations of N-linked oligosaccharides Biochemistry 26 1987 6571 6578
    • (1987) Biochemistry , vol.26 , pp. 6571-6578
    • Homans, S.W.1    Dwek, R.A.2    Rademacher, T.W.3
  • 9
    • 0037137482 scopus 로고    scopus 로고
    • Modulation of receptor signaling by glycosylation: Fringe is an O-fucose-beta1,3-N-acetylglucosaminyltransferase
    • R.S. Haltiwanger, and P. Stanley Modulation of receptor signaling by glycosylation: fringe is an O-fucose-beta1,3-N-acetylglucosaminyltransferase Biochim Biophys Acta 1573 2002 328 335
    • (2002) Biochim Biophys Acta , vol.1573 , pp. 328-335
    • Haltiwanger, R.S.1    Stanley, P.2
  • 10
    • 33744799438 scopus 로고    scopus 로고
    • Mucin-type O-glycans in human colon and breast cancer: Glycodynamics and functions
    • I. Brockhausen Mucin-type O-glycans in human colon and breast cancer: glycodynamics and functions EMBO Rep 7 2006 599 604
    • (2006) EMBO Rep , vol.7 , pp. 599-604
    • Brockhausen, I.1
  • 11
    • 84862840416 scopus 로고    scopus 로고
    • Glycans as cancer biomarkers
    • 10.1016/j.bbagen.2011.12.001
    • B. Adamczyk, T. Tharmalingam, and P.M. Rudd Glycans as cancer biomarkers Biochim Biophys Acta 1820 2012 1347 1353 10.1016/j.bbagen.2011.12.001
    • (2012) Biochim Biophys Acta , vol.1820 , pp. 1347-1353
    • Adamczyk, B.1    Tharmalingam, T.2    Rudd, P.M.3
  • 12
    • 84862835063 scopus 로고    scopus 로고
    • Development of an antibody-lectin enzyme immunoassay for fucosylated α-fetoprotein
    • 10.1016/j.bbagen.2011.12.015
    • H. Korekane, T. Hasegawa, A. Matsumoto, N. Kinoshita, E. Miyoshi, and N. Taniguchi Development of an antibody-lectin enzyme immunoassay for fucosylated α-fetoprotein Biochim Biophys Acta 1820 2012 1405 1411 10.1016/j.bbagen.2011.12.015
    • (2012) Biochim Biophys Acta , vol.1820 , pp. 1405-1411
    • Korekane, H.1    Hasegawa, T.2    Matsumoto, A.3    Kinoshita, N.4    Miyoshi, E.5    Taniguchi, N.6
  • 13
    • 79957879496 scopus 로고    scopus 로고
    • Cell surface glycan-lectin interactions in tumor metastasis
    • N.D. Rambaruth, and M.V. Dwek Cell surface glycan-lectin interactions in tumor metastasis Acta Histochem 113 2011 591 600
    • (2011) Acta Histochem , vol.113 , pp. 591-600
    • Rambaruth, N.D.1    Dwek, M.V.2
  • 15
    • 77953703296 scopus 로고    scopus 로고
    • Molecular imaging of N-linked glycosylation suggests glycan biosynthesis is a novel target for cancer therapy
    • J.N. Contessa, M.S. Bhojani, H.H. Freeze, B.D. Ross, A. Rehemtulla, and T.S. Lawrence Molecular imaging of N-linked glycosylation suggests glycan biosynthesis is a novel target for cancer therapy Clin Cancer Res 16 2010 3205 3214
    • (2010) Clin Cancer Res , vol.16 , pp. 3205-3214
    • Contessa, J.N.1    Bhojani, M.S.2    Freeze, H.H.3    Ross, B.D.4    Rehemtulla, A.5    Lawrence, T.S.6
  • 16
    • 84857445346 scopus 로고    scopus 로고
    • Control of mucin-type O-glycosylation - A classification of the polypeptide GalNAc-transferase gene family
    • Epub ahead of print
    • Bennett EP, Mandel U, Clausen H, Gerken TA, Fritz TA, Tabak LA: Control of mucin-type O-glycosylation - a classification of the polypeptide GalNAc-transferase gene family. Glycobiology [Epub ahead of print].
    • Glycobiology
    • Bennett, E.P.1    Mandel, U.2    Clausen, H.3    Gerken, T.A.4    Fritz, T.A.5    Tabak, L.A.6
  • 18
    • 0033977912 scopus 로고    scopus 로고
    • The involvement of Helix pomatia lectin (HPA) binding N-acetylgalactosamine glycans in cancer progression
    • S.A. Brooks The involvement of Helix pomatia lectin (HPA) binding N-acetylgalactosamine glycans in cancer progression Histol Histopathol 15 2000 143 158
    • (2000) Histol Histopathol , vol.15 , pp. 143-158
    • Brooks, S.A.1
  • 20
    • 70450247207 scopus 로고    scopus 로고
    • Mucins in cancer: Function, prognosis and therapy
    • D.W. Kufe Mucins in cancer: function, prognosis and therapy Nat Rev Cancer 9 2009 874 885
    • (2009) Nat Rev Cancer , vol.9 , pp. 874-885
    • Kufe, D.W.1
  • 21
    • 57349187712 scopus 로고    scopus 로고
    • A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin
    • C. Slawson, T. Lakshmanan, S. Knapp, and G.W. Hart A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin Mol Biol Cell 19 2008 4130 4140
    • (2008) Mol Biol Cell , vol.19 , pp. 4130-4140
    • Slawson, C.1    Lakshmanan, T.2    Knapp, S.3    Hart, G.W.4
  • 22
    • 50349093142 scopus 로고    scopus 로고
    • Cross-talk between GlcNAcylation and phosphorylation: Roles in insulin resistance and glucose toxicity
    • R.J. Copeland, J.W. Bullen, and G.W. Hart Cross-talk between GlcNAcylation and phosphorylation: roles in insulin resistance and glucose toxicity Am J Physiol Endocrinol Metab 295 2008 E17 E28
    • (2008) Am J Physiol Endocrinol Metab , vol.295
    • Copeland, R.J.1    Bullen, J.W.2    Hart, G.W.3
  • 24
    • 70349270677 scopus 로고    scopus 로고
    • O-GlcNAc cycling: Implications for neurodegenerative disorders
    • B.D. Lazarus, D.C. Love, and J.A. Hanover O-GlcNAc cycling: implications for neurodegenerative disorders Int J Biochem Cell Biol 41 2009 2134 2146
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 2134-2146
    • Lazarus, B.D.1    Love, D.C.2    Hanover, J.A.3
  • 25
    • 80052068559 scopus 로고    scopus 로고
    • O-GlcNAc signalling: Implications for cancer cell biology
    • C. Slawson, and G.W. Hart O-GlcNAc signalling: implications for cancer cell biology Nat Rev Cancer 11 2011 678 684
    • (2011) Nat Rev Cancer , vol.11 , pp. 678-684
    • Slawson, C.1    Hart, G.W.2
  • 26
    • 84860382308 scopus 로고    scopus 로고
    • The lectin Helix pomatia agglutinin recognises O-GlcNAc containing glycoproteins in human breast cancer
    • N.D.S. Rambaruth, P. Greenwell, and M.V. Dwek The lectin Helix pomatia agglutinin recognises O-GlcNAc containing glycoproteins in human breast cancer Glycobiology 22 2012 839 848
    • (2012) Glycobiology , vol.22 , pp. 839-848
    • Rambaruth, N.D.S.1    Greenwell, P.2    Dwek, M.V.3
  • 27
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • M.B. Lazarus, Y. Nam, J. Jiang, P. Sliz, and S. Walker Structure of human O-GlcNAc transferase and its complex with a peptide substrate Nature 469 2011 564 567
    • (2011) Nature , vol.469 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5
  • 29
    • 0032488979 scopus 로고    scopus 로고
    • Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N- acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate
    • R.S. Haltiwanger, K. Grove, and G.A. Philipsberg Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy- d-glucopyranosylidene)amino-N-phenylcarbamate J Biol Chem 273 1998 3611 3617
    • (1998) J Biol Chem , vol.273 , pp. 3611-3617
    • Haltiwanger, R.S.1    Grove, K.2    Philipsberg, G.A.3
  • 31
    • 78649711427 scopus 로고    scopus 로고
    • The control of the metabolic switch in cancer by oncogenes and tumor suppressor genes
    • A.J. Levine, and A.M. Puzio-Kuter The control of the metabolic switch in cancer by oncogenes and tumor suppressor genes Science 330 2010 1340 1344
    • (2010) Science , vol.330 , pp. 1340-1344
    • Levine, A.J.1    Puzio-Kuter, A.M.2
  • 33
    • 0024592297 scopus 로고
    • Effects of the tumour promoter okadaic acid on intracellular protein phosphorylation and metabolism
    • T.A.J. Haystead, A.T.R. Sim, D. Carling, C. Honnor, Y. Tsukitani, P. Cohen, and D.G. Hardie Effects of the tumour promoter okadaic acid on intracellular protein phosphorylation and metabolism Nature 337 1989 78 81
    • (1989) Nature , vol.337 , pp. 78-81
    • Haystead, T.A.J.1    Sim, A.T.R.2    Carling, D.3    Honnor, C.4    Tsukitani, Y.5    Cohen, P.6    Hardie, D.G.7
  • 35
    • 78649878892 scopus 로고    scopus 로고
    • Protein lysine acetylation in cellular function and its role in cancer manifestation
    • M. Arif, P. Senapati, J. Shandilya, and T.K. Kundu Protein lysine acetylation in cellular function and its role in cancer manifestation Biochim Biophys Acta 1799 2011 702 716
    • (2011) Biochim Biophys Acta , vol.1799 , pp. 702-716
    • Arif, M.1    Senapati, P.2    Shandilya, J.3    Kundu, T.K.4
  • 36
    • 79952262759 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitors in recent clinical trials for cancer therapy
    • J.M. Wagner, B. Hacknson, M. Lubbert, and M. Jung Histone deacetylase (HDAC) inhibitors in recent clinical trials for cancer therapy Clin Epigenet 1 2010 117 136
    • (2010) Clin Epigenet , vol.1 , pp. 117-136
    • Wagner, J.M.1    Hacknson, B.2    Lubbert, M.3    Jung, M.4
  • 37
    • 79952109209 scopus 로고    scopus 로고
    • Errors in erasure: Links between histone lysine methylation removal and disease
    • E.M. Duncan, and C.D. Allis Errors in erasure: links between histone lysine methylation removal and disease Prog Drug Res 67 2011 69 90
    • (2011) Prog Drug Res , vol.67 , pp. 69-90
    • Duncan, E.M.1    Allis, C.D.2
  • 38
    • 77950948813 scopus 로고    scopus 로고
    • Evading tumor evasion: Current concepts and perspectives of anti-angiogenic cancer therapy
    • A. Abdollahi, and J. Folkman Evading tumor evasion: current concepts and perspectives of anti-angiogenic cancer therapy Drug Resist Updat 13 2010 16 28
    • (2010) Drug Resist Updat , vol.13 , pp. 16-28
    • Abdollahi, A.1    Folkman, J.2
  • 39
    • 64749100828 scopus 로고    scopus 로고
    • Protein tyrosine nitration - An update
    • H. Ischiropoulos Protein tyrosine nitration - an update Arch Biochem Biophys 484 2009 117 121
    • (2009) Arch Biochem Biophys , vol.484 , pp. 117-121
    • Ischiropoulos, H.1
  • 41
    • 70649085074 scopus 로고    scopus 로고
    • HIF prolyl 4-hydroxylases and their potential as drug targets
    • J. Myllyhrju HIF prolyl 4-hydroxylases and their potential as drug targets Curr Pharm Des 15 2009 3878 3885
    • (2009) Curr Pharm des , vol.15 , pp. 3878-3885
    • Myllyhrju, J.1
  • 42
    • 78650718836 scopus 로고    scopus 로고
    • The intracellular dynamic of protein palmitoylation
    • C. Slaun, J. Greaves, and L.H. Chamberlain The intracellular dynamic of protein palmitoylation J Cell Biol 191 2010 1229 1238
    • (2010) J Cell Biol , vol.191 , pp. 1229-1238
    • Slaun, C.1    Greaves, J.2    Chamberlain, L.H.3
  • 43
    • 77951729960 scopus 로고    scopus 로고
    • Palmitoylation of oncogenic NRAS is essential for leukemogenesis
    • B. Cuiffo, and R. Ren Palmitoylation of oncogenic NRAS is essential for leukemogenesis Blood 115 2010 3598 3605
    • (2010) Blood , vol.115 , pp. 3598-3605
    • Cuiffo, B.1    Ren, R.2
  • 44
    • 0034595239 scopus 로고    scopus 로고
    • Ubiquitin-like proteins: New wines in new bottle
    • E.T.H. Yeh, L. Gong, and T. Kamitani Ubiquitin-like proteins: new wines in new bottle Gene 248 2000 1 14
    • (2000) Gene , vol.248 , pp. 1-14
    • Yeh, E.T.H.1    Gong, L.2    Kamitani, T.3
  • 47
    • 78650824534 scopus 로고    scopus 로고
    • Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets
    • L. Bedford, J. Lowe, L.R. Dick, R.J. Mayer, and J.E. Brownell Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets Nat Rev Drug Discov 10 2011 29 46
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 29-46
    • Bedford, L.1    Lowe, J.2    Dick, L.R.3    Mayer, R.J.4    Brownell, J.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.