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Volumn 6, Issue 8, 2008, Pages 1316-1325

Protein sialylation by sialyltransferase involves radiation resistance

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDE ALPHA(2,6) SIALYLTRANSFERASE; BETA1 INTEGRIN; CASPASE 3; NEURAMINIDASE 2; NEURAMINIDASE 3; SIALYLTRANSFERASE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; BETA D GALACTOSIDE ALPHA 2 6 SIALYLTRANSFERASE; BETA-D-GALACTOSIDE ALPHA 2-6-SIALYLTRANSFERASE; GLYCOPROTEIN; SIALIC ACID DERIVATIVE;

EID: 52449128933     PISSN: 15417786     EISSN: None     Source Type: Journal    
DOI: 10.1158/1541-7786.MCR-07-2209     Document Type: Article
Times cited : (58)

References (65)
  • 1
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 1993;3:97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 2
    • 0034444960 scopus 로고    scopus 로고
    • Achievements and challenges of sialic acid research
    • Schauer R. Achievements and challenges of sialic acid research. Glycoconj J 2000;17:485-99.
    • (2000) Glycoconj J , vol.17 , pp. 485-499
    • Schauer, R.1
  • 3
    • 0030993576 scopus 로고    scopus 로고
    • Sialic acids as ligands in recognition phenomena
    • Varki A. Sialic acids as ligands in recognition phenomena. FASEB J 1997;11:248-55.
    • (1997) FASEB J , vol.11 , pp. 248-255
    • Varki, A.1
  • 4
    • 0030792933 scopus 로고    scopus 로고
    • Sialic acids in molecular and cellular interactions
    • Kelm S, Schauer R. Sialic acids in molecular and cellular interactions. Int Rev Cytol 1997;175:137-240.
    • (1997) Int Rev Cytol , vol.175 , pp. 137-240
    • Kelm, S.1    Schauer, R.2
  • 5
    • 0024448635 scopus 로고
    • Increased CMP-NeuAc:Gal β1,4GlcNAc-R α2,6 sialyltransferase activity in human colorectal cancer tissues
    • Dall'Olio F, Malagolini N, di Stefano G, Minni F, Marrano D, Serafini-Cessi F. Increased CMP-NeuAc:Gal β1,4GlcNAc-R α2,6 sialyltransferase activity in human colorectal cancer tissues. Int J Cancer 1989;44:434-9.
    • (1989) Int J Cancer , vol.44 , pp. 434-439
    • Dall'Olio, F.1    Malagolini, N.2    di Stefano, G.3    Minni, F.4    Marrano, D.5    Serafini-Cessi, F.6
  • 6
    • 0027723424 scopus 로고
    • Enhanced activity of CMP-neuAc: Gal β1-4GlcNAc:α2,6-sialyltransferase in metastasizing human colorectal tumor tissue and serum of tumor patients
    • Gessner P, Riedl S, Quentmaier A, Kemmner W. Enhanced activity of CMP-neuAc: Gal β1-4GlcNAc:α2,6-sialyltransferase in metastasizing human colorectal tumor tissue and serum of tumor patients. Cancer Lett 1993;75:143-9.
    • (1993) Cancer Lett , vol.75 , pp. 143-149
    • Gessner, P.1    Riedl, S.2    Quentmaier, A.3    Kemmner, W.4
  • 8
    • 2242438080 scopus 로고    scopus 로고
    • Characterization of the second type of human β-galactoside α2,6-sialyltransferase (ST6Gal II), which sialylates Galβ1,4GlcNAc structures on oligosaccharides preferentially. Genomic analysis of human sialyltransferase genes
    • Takashima S, Tsuji S, Tsujimoto M. Characterization of the second type of human β-galactoside α2,6-sialyltransferase (ST6Gal II), which sialylates Galβ1,4GlcNAc structures on oligosaccharides preferentially. Genomic analysis of human sialyltransferase genes. J Biol Chem 2002;277:45719-28.
    • (2002) J Biol Chem , vol.277 , pp. 45719-45728
    • Takashima, S.1    Tsuji, S.2    Tsujimoto, M.3
  • 9
    • 0037335932 scopus 로고    scopus 로고
    • Identification and functional expression of a second human β-galactoside α2,6- sialyltransferase, ST6Gal II
    • Krzewinski-Recchi MA, Julien S, Juliant S, et al. Identification and functional expression of a second human β-galactoside α2,6- sialyltransferase, ST6Gal II. Eur J Biochem 2003;270:950-61.
    • (2003) Eur J Biochem , vol.270 , pp. 950-961
    • Krzewinski-Recchi, M.A.1    Julien, S.2    Juliant, S.3
  • 10
    • 0028284424 scopus 로고
    • Different sialyltransferase activities in human colorectal carcinoma cells from surgical specimens detected by specific glycoprotein and glycolipid acceptors
    • Kemmner W, Kruck D, Schlag P. Different sialyltransferase activities in human colorectal carcinoma cells from surgical specimens detected by specific glycoprotein and glycolipid acceptors. Clin Exp Metastasis 1994;12:245-54.
    • (1994) Clin Exp Metastasis , vol.12 , pp. 245-254
    • Kemmner, W.1    Kruck, D.2    Schlag, P.3
  • 11
    • 0026096558 scopus 로고
    • α2,6 sialylation of N-acetyllactosaminic sequences in human colorectal cancer cell lines. Relationship with non-adherent growth
    • Dall'Olio F, Malagolini N, Di Stefano G, Ciambella M, Serafini-Cessi F. α2,6 sialylation of N-acetyllactosaminic sequences in human colorectal cancer cell lines. Relationship with non-adherent growth. Int J Cancer 1991;47:291-7.
    • (1991) Int J Cancer , vol.47 , pp. 291-297
    • Dall'Olio, F.1    Malagolini, N.2    Di Stefano, G.3    Ciambella, M.4    Serafini-Cessi, F.5
  • 12
    • 0037031849 scopus 로고    scopus 로고
    • Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation
    • Martin LT, Marth JD, Varki A, Varki NM. Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation. J Biol Chem 2002;277:32930-8.
    • (2002) J Biol Chem , vol.277 , pp. 32930-32938
    • Martin, L.T.1    Marth, J.D.2    Varki, A.3    Varki, N.M.4
  • 13
    • 0027419736 scopus 로고
    • Chromosome mapping and organization of the human β-galactoside α2,6-sialyltransferase gene. Differential and cell-type specific usage of upstream exon sequences in B-lymphoblastoid cells
    • Wang X, Vertino A, Eddy RL, et al. Chromosome mapping and organization of the human β-galactoside α2,6-sialyltransferase gene. Differential and cell-type specific usage of upstream exon sequences in B-lymphoblastoid cells. J Biol Chem 1993;268:4355-61.
    • (1993) J Biol Chem , vol.268 , pp. 4355-4361
    • Wang, X.1    Vertino, A.2    Eddy, R.L.3
  • 14
    • 0031474823 scopus 로고    scopus 로고
    • The gene encoding β-galactoside α2,6-sialyltransferase maps to mouse chromosome 16
    • Kalcheva I, Elliott RW, Dalziel M, Lau JT. The gene encoding β-galactoside α2,6-sialyltransferase maps to mouse chromosome 16. Mamm Genome 1997;8:619-20.
    • (1997) Mamm Genome , vol.8 , pp. 619-620
    • Kalcheva, I.1    Elliott, R.W.2    Dalziel, M.3    Lau, J.T.4
  • 16
    • 0024364391 scopus 로고
    • Tissue-specific expression of sialyltransferases
    • Paulson JC, Weinstein J, Schauer A. Tissue-specific expression of sialyltransferases. J Biol Chem 1989;264:10931-4.
    • (1989) J Biol Chem , vol.264 , pp. 10931-10934
    • Paulson, J.C.1    Weinstein, J.2    Schauer, A.3
  • 17
    • 0020491419 scopus 로고
    • Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal β1 to 3(4)GlcNAc α2 to 3 sialyltransferase and a Gal β1 to 4GlcNAc α2 to 6 sialyltransferase from rat liver
    • Weinstein J, de Souza-e-Silva U, Paulson JC. Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal β1 to 3(4)GlcNAc α2 to 3 sialyltransferase and a Gal β1 to 4GlcNAc α2 to 6 sialyltransferase from rat liver. J Biol Chem 1982;257:13845-53.
    • (1982) J Biol Chem , vol.257 , pp. 13845-13853
    • Weinstein, J.1    de Souza-e-Silva, U.2    Paulson, J.C.3
  • 18
    • 0034001204 scopus 로고    scopus 로고
    • Murine B cell differentiation is accompanied by programmed expression of multiple novel β-galactoside α2,6-sialyltransferase mRNA forms
    • Wuensch SA, Huang RY, Ewing J, Liang X, Lau JT. Murine B cell differentiation is accompanied by programmed expression of multiple novel β-galactoside α2,6-sialyltransferase mRNA forms. Glycobiology 2000;10:67-75.
    • (2000) Glycobiology , vol.10 , pp. 67-75
    • Wuensch, S.A.1    Huang, R.Y.2    Ewing, J.3    Liang, X.4    Lau, J.T.5
  • 20
    • 0035526267 scopus 로고    scopus 로고
    • Dall'Olio F, Chiricolo M. Sialyltransferases in cancer. Glycoconj J 2001;18:841-50.
    • Dall'Olio F, Chiricolo M. Sialyltransferases in cancer. Glycoconj J 2001;18:841-50.
  • 21
    • 0035883156 scopus 로고    scopus 로고
    • α2,6- sialylation of cell-surface N-glycans inhibits glioma formation in vivo
    • Yamamoto H, Oviedo A, Sweeley C, Saito T, Moskal JR. α2,6- sialylation of cell-surface N-glycans inhibits glioma formation in vivo. Cancer Res 2001;61:6822-9.
    • (2001) Cancer Res , vol.61 , pp. 6822-6829
    • Yamamoto, H.1    Oviedo, A.2    Sweeley, C.3    Saito, T.4    Moskal, J.R.5
  • 22
    • 0030611923 scopus 로고    scopus 로고
    • α2,6-Sialyltransferase gene transfection into a human glioma cell line (U373 MG) results in decreased invasivity
    • Yamamoto H, Kaneko Y, Rebbaa A, Bremer EG, Moskal JR. α2,6-Sialyltransferase gene transfection into a human glioma cell line (U373 MG) results in decreased invasivity. J Neurochem 1997;68:2566-76.
    • (1997) J Neurochem , vol.68 , pp. 2566-2576
    • Yamamoto, H.1    Kaneko, Y.2    Rebbaa, A.3    Bremer, E.G.4    Moskal, J.R.5
  • 23
    • 33646453766 scopus 로고    scopus 로고
    • Organ-specific gene expressions in C57BL/6 mice after exposure to low-dose radiation
    • Lee WJ, Majumder ZR, Jeoung DI, et al. Organ-specific gene expressions in C57BL/6 mice after exposure to low-dose radiation. Radiat Res 2006;165:562-9.
    • (2006) Radiat Res , vol.165 , pp. 562-569
    • Lee, W.J.1    Majumder, Z.R.2    Jeoung, D.I.3
  • 25
    • 19644364143 scopus 로고    scopus 로고
    • Hypersialylation of β1 integrins, observed in colon adenocarcinoma, may contribute to cancer progression by up-regulating cell motility
    • Seales EC, Jurado GA, Brunson BA, Wakefield JK, Frost AR, Bellis SL. Hypersialylation of β1 integrins, observed in colon adenocarcinoma, may contribute to cancer progression by up-regulating cell motility. Cancer Res 2005;65:4645-52.
    • (2005) Cancer Res , vol.65 , pp. 4645-4652
    • Seales, E.C.1    Jurado, G.A.2    Brunson, B.A.3    Wakefield, J.K.4    Frost, A.R.5    Bellis, S.L.6
  • 26
    • 0032965207 scopus 로고    scopus 로고
    • Differential expression of the hepatic transcript of β-galactoside α2,6-sialyltransferase in human colon cancer cell lines
    • Dall'Olio F, Chiricolo M, Lau JT. Differential expression of the hepatic transcript of β-galactoside α2,6-sialyltransferase in human colon cancer cell lines. Int J Cancer 1999;81:243-7.
    • (1999) Int J Cancer , vol.81 , pp. 243-247
    • Dall'Olio, F.1    Chiricolo, M.2    Lau, J.T.3
  • 27
    • 18744409082 scopus 로고    scopus 로고
    • Purification and characterization of a soluble recombinant human ST6Gal I functionally expressed in Escherichia coli
    • Hidari KI, Horie N, Murata T, et al. Purification and characterization of a soluble recombinant human ST6Gal I functionally expressed in Escherichia coli. Glycoconj J 2005;22:1-11.
    • (2005) Glycoconj J , vol.22 , pp. 1-11
    • Hidari, K.I.1    Horie, N.2    Murata, T.3
  • 28
    • 0036923878 scopus 로고    scopus 로고
    • Changes in sialic acid expression in the lung during intrauterine development of the human fetus
    • Cerna A, Janega P, Martanovic P, Lisy M, Babal P. Changes in sialic acid expression in the lung during intrauterine development of the human fetus. Acta Histochem 2002;104:339-42.
    • (2002) Acta Histochem , vol.104 , pp. 339-342
    • Cerna, A.1    Janega, P.2    Martanovic, P.3    Lisy, M.4    Babal, P.5
  • 29
    • 0034807766 scopus 로고    scopus 로고
    • Sialylation is modulated through maturation in hemocytes from Macrobrachium rosenbergii
    • Sierra C, Guevara J, Lascurain R, et al. Sialylation is modulated through maturation in hemocytes from Macrobrachium rosenbergii. Comp Biochem Physiol C Toxicol Pharmacol 2001;130:179-89.
    • (2001) Comp Biochem Physiol C Toxicol Pharmacol , vol.130 , pp. 179-189
    • Sierra, C.1    Guevara, J.2    Lascurain, R.3
  • 30
    • 0037388120 scopus 로고    scopus 로고
    • Protein glycosylation in disease: New insights into the congenital muscular dystrophies
    • Martin-Rendon E, Blake DJ. Protein glycosylation in disease: new insights into the congenital muscular dystrophies. Trends Pharmacol Sci 2003;24:178-83.
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 178-183
    • Martin-Rendon, E.1    Blake, D.J.2
  • 31
    • 0035279221 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: Genetic model systems lead the way
    • Aebi M, Hennet T. Congenital disorders of glycosylation: genetic model systems lead the way. Trends Cell Biol 2001;11:136-41.
    • (2001) Trends Cell Biol , vol.11 , pp. 136-141
    • Aebi, M.1    Hennet, T.2
  • 33
    • 0031755183 scopus 로고    scopus 로고
    • Altered glycosylation pattern of proteins in Alzheimer disease
    • Guevara J, Espinosa B, Zenteno E, et al. Altered glycosylation pattern of proteins in Alzheimer disease. J Neuropathol Exp Neurol 1998;57:905-14.
    • (1998) J Neuropathol Exp Neurol , vol.57 , pp. 905-914
    • Guevara, J.1    Espinosa, B.2    Zenteno, E.3
  • 36
    • 0037675876 scopus 로고    scopus 로고
    • Characterization of α2,6-sialyltransferase cleavage by Alzheimer's β-secretase (BACE1)
    • Kitazume S, Tachida Y, Oka R, et al. Characterization of α2,6-sialyltransferase cleavage by Alzheimer's β-secretase (BACE1). J Biol Chem 2003;278:14865-71.
    • (2003) J Biol Chem , vol.278 , pp. 14865-14871
    • Kitazume, S.1    Tachida, Y.2    Oka, R.3
  • 37
    • 36849001215 scopus 로고    scopus 로고
    • β-Galactoside α2,6-sialyltransferase I cleavage by BACE1 enhances the sialylation of soluble glycoproteins. A novel regulatory mechanism for α2,6-sialylation
    • Sugimoto I, Futakawa S, Oka R, et al. β-Galactoside α2,6-sialyltransferase I cleavage by BACE1 enhances the sialylation of soluble glycoproteins. A novel regulatory mechanism for α2,6-sialylation. J Biol Chem 2007;282:34896-903.
    • (2007) J Biol Chem , vol.282 , pp. 34896-34903
    • Sugimoto, I.1    Futakawa, S.2    Oka, R.3
  • 38
    • 0021955354 scopus 로고
    • Intracellular movement of cell surface receptors after endocytosis: Resialylation of asialo-transferrin receptor in human erythroleukemia cells
    • Snider MD, Rogers OC. Intracellular movement of cell surface receptors after endocytosis: resialylation of asialo-transferrin receptor in human erythroleukemia cells. J Cell Biol 1985;100:826-34.
    • (1985) J Cell Biol , vol.100 , pp. 826-834
    • Snider, M.D.1    Rogers, O.C.2
  • 39
    • 34249946040 scopus 로고    scopus 로고
    • Radiation-induced late effects in two affected individuals of the Lilo radiation accident
    • Scherthan H, Abend M, Muller K, et al. Radiation-induced late effects in two affected individuals of the Lilo radiation accident. Radiat Res 2007;167:615-23.
    • (2007) Radiat Res , vol.167 , pp. 615-623
    • Scherthan, H.1    Abend, M.2    Muller, K.3
  • 40
    • 0028239080 scopus 로고
    • Functional role of N-glycosylation in α5β1 integrin receptor. De-N-glycosylation induces dissociation or altered association of α5 and β1 subunits and concomitant loss of fibronectin binding activity
    • Zheng M, Fang H, Hakomori S. Functional role of N-glycosylation in α5β1 integrin receptor. De-N-glycosylation induces dissociation or altered association of α5 and β1 subunits and concomitant loss of fibronectin binding activity. J Biol Chem 1994;269:12325-31.
    • (1994) J Biol Chem , vol.269 , pp. 12325-12331
    • Zheng, M.1    Fang, H.2    Hakomori, S.3
  • 41
    • 0029021007 scopus 로고
    • Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V
    • Demetriou M, Nabi IR, Coppolino M, Dedhar S, Dennis JW. Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V. J Cell Biol 1995;130:383-92.
    • (1995) J Cell Biol , vol.130 , pp. 383-392
    • Demetriou, M.1    Nabi, I.R.2    Coppolino, M.3    Dedhar, S.4    Dennis, J.W.5
  • 42
    • 8744286641 scopus 로고    scopus 로고
    • Expression of sialyl-Tn epitopes on β1 integrin alters epithelial cell phenotype, proliferation and haptotaxis
    • Clement M, Rocher J, Loirand G, Le Pendu J. Expression of sialyl-Tn epitopes on β1 integrin alters epithelial cell phenotype, proliferation and haptotaxis. J Cell Sci 2004;117:5059-69.
    • (2004) J Cell Sci , vol.117 , pp. 5059-5069
    • Clement, M.1    Rocher, J.2    Loirand, G.3    Le Pendu, J.4
  • 44
    • 0344234442 scopus 로고    scopus 로고
    • Glycosylation profile of integrin α3β1 changes with melanoma progression
    • Pochec E, Litynska A, Amoresano A, Casbarra A. Glycosylation profile of integrin α3β1 changes with melanoma progression. Biochim Biophys Acta 2003;1643:113-23.
    • (2003) Biochim Biophys Acta , vol.1643 , pp. 113-123
    • Pochec, E.1    Litynska, A.2    Amoresano, A.3    Casbarra, A.4
  • 45
    • 0028949428 scopus 로고
    • Lewis X structure increases cell substratum adhesion in L cells
    • Sudou A, Ozawa M, Muramatsu T. Lewis X structure increases cell substratum adhesion in L cells. J Biochem (Tokyo) 1995;117:271-5.
    • (1995) J Biochem (Tokyo) , vol.117 , pp. 271-275
    • Sudou, A.1    Ozawa, M.2    Muramatsu, T.3
  • 46
    • 0035896632 scopus 로고    scopus 로고
    • Carbohydrate-carbohydrate binding of ganglioside to integrin α(5) modulates α(5)β(1) function
    • Wang X, Sun P, Al-Qamari A, Tai T, Kawashima I, Paller AS. Carbohydrate-carbohydrate binding of ganglioside to integrin α(5) modulates α(5)β(1) function. J Biol Chem 2001;276:8436-44.
    • (2001) J Biol Chem , vol.276 , pp. 8436-8444
    • Wang, X.1    Sun, P.2    Al-Qamari, A.3    Tai, T.4    Kawashima, I.5    Paller, A.S.6
  • 47
    • 0024436107 scopus 로고
    • Analysis of the role of glycosylation of the human fibronectin receptor
    • Akiyama SK, Yamada SS, Yamada KM. Analysis of the role of glycosylation of the human fibronectin receptor. J Biol Chem 1989;264:18011-8.
    • (1989) J Biol Chem , vol.264 , pp. 18011-18018
    • Akiyama, S.K.1    Yamada, S.S.2    Yamada, K.M.3
  • 48
    • 31144475414 scopus 로고    scopus 로고
    • Phenotypic changes induced by expression of β-galactoside α2,6 sialyltransferase I in the human colon cancer cell line SW948
    • Chiricolo M, Malagolini N, Bonfiglioli S, Dall'Olio F. Phenotypic changes induced by expression of β-galactoside α2,6 sialyltransferase I in the human colon cancer cell line SW948. Glycobiology 2006;16:146-54.
    • (2006) Glycobiology , vol.16 , pp. 146-154
    • Chiricolo, M.1    Malagolini, N.2    Bonfiglioli, S.3    Dall'Olio, F.4
  • 50
    • 0026583928 scopus 로고
    • The c-Ha-ras oncogene induces increased expression of β-galactoside α-2,6-sialyltransferase in rat fibroblast (FR3T3) cells
    • Le Marer N, Laudet V, Svensson EC, et al. The c-Ha-ras oncogene induces increased expression of β-galactoside α-2,6-sialyltransferase in rat fibroblast (FR3T3) cells. Glycobiology 1992;2:49-56.
    • (1992) Glycobiology , vol.2 , pp. 49-56
    • Le Marer, N.1    Laudet, V.2    Svensson, E.C.3
  • 51
    • 0035978521 scopus 로고    scopus 로고
    • Suppression of a sialyltransferase by antisense DNA reduces invasiveness of human colon cancer cells in vitro
    • Zhu Y, Srivatana U, Ullah A, Gagneja H, Berenson CS, Lance P. Suppression of a sialyltransferase by antisense DNA reduces invasiveness of human colon cancer cells in vitro. Biochim Biophys Acta 2001;1536:148-60.
    • (2001) Biochim Biophys Acta , vol.1536 , pp. 148-160
    • Zhu, Y.1    Srivatana, U.2    Ullah, A.3    Gagneja, H.4    Berenson, C.S.5    Lance, P.6
  • 52
    • 0026598841 scopus 로고
    • Enhanced CMP-NeuAc:Gal β1,4GlcNAc-R α2,6 sialyltransferase activity of human colon cancer xenografts in athymic nude mice and of xenograft-derived cell lines
    • Dall'Olio F, Malagolini N, Serafini-Cessi F. Enhanced CMP-NeuAc:Gal β1,4GlcNAc-R α2,6 sialyltransferase activity of human colon cancer xenografts in athymic nude mice and of xenograft-derived cell lines. Int J Cancer 1992;50:325-30.
    • (1992) Int J Cancer , vol.50 , pp. 325-330
    • Dall'Olio, F.1    Malagolini, N.2    Serafini-Cessi, F.3
  • 53
    • 0029863463 scopus 로고    scopus 로고
    • Enhanced sialylation of mucin-associated carbohydrate structures in human colon cancer metastasis
    • Bresalier RS, Ho SB, Schoeppner HL, et al. Enhanced sialylation of mucin-associated carbohydrate structures in human colon cancer metastasis. Gastroenterology 1996;110:1354-67.
    • (1996) Gastroenterology , vol.110 , pp. 1354-1367
    • Bresalier, R.S.1    Ho, S.B.2    Schoeppner, H.L.3
  • 54
    • 0032530423 scopus 로고    scopus 로고
    • Multiplex reverse transcription polymerase chain reaction assessment of sialyltransferase expression in human breast cancer
    • Recchi MA, Hebbar M, Hornez L, Harduin-Lepers A, Peyrat JP, Delannoy P. Multiplex reverse transcription polymerase chain reaction assessment of sialyltransferase expression in human breast cancer. Cancer Res 1998;58:4066-70.
    • (1998) Cancer Res , vol.58 , pp. 4066-4070
    • Recchi, M.A.1    Hebbar, M.2    Hornez, L.3    Harduin-Lepers, A.4    Peyrat, J.P.5    Delannoy, P.6
  • 55
    • 0034785582 scopus 로고    scopus 로고
    • Altered mRNA expression of sialyltransferase in squamous cell carcinomas of the cervix
    • Wang PH, Li YF, Juang CM, et al. Altered mRNA expression of sialyltransferase in squamous cell carcinomas of the cervix. Gynecol Oncol 2001;83:121-7.
    • (2001) Gynecol Oncol , vol.83 , pp. 121-127
    • Wang, P.H.1    Li, Y.F.2    Juang, C.M.3
  • 56
    • 0032173446 scopus 로고    scopus 로고
    • Elevation of α2→6 sialyltransferase and α1→2 fucosyltransferase activities in human choriocarcinoma
    • Fukushima K, Hara-Kuge S, Seko A, Ikehara Y, Yamashita K. Elevation of α2→6 sialyltransferase and α1→2 fucosyltransferase activities in human choriocarcinoma. Cancer Res 1998;58:4301-6.
    • (1998) Cancer Res , vol.58 , pp. 4301-4306
    • Fukushima, K.1    Hara-Kuge, S.2    Seko, A.3    Ikehara, Y.4    Yamashita, K.5
  • 57
    • 34248185926 scopus 로고    scopus 로고
    • Inhibition of TGF-β with neutralizing antibodies prevents radiation-induced acceleration of metastatic cancer progression
    • Biswas S, Guix M, Rinehart C, et al. Inhibition of TGF-β with neutralizing antibodies prevents radiation-induced acceleration of metastatic cancer progression. J Clin Invest 2007;117:1305-13.
    • (2007) J Clin Invest , vol.117 , pp. 1305-1313
    • Biswas, S.1    Guix, M.2    Rinehart, C.3
  • 58
    • 34249691352 scopus 로고    scopus 로고
    • Cause of death and neoplasia in mice continuously exposed to very lowdose rates of gamma rays
    • Tanaka IB III, Tanaka S, Ichinohe K, et al. Cause of death and neoplasia in mice continuously exposed to very lowdose rates of gamma rays. Radiat Res 2007;167:417-37.
    • (2007) Radiat Res , vol.167 , pp. 417-437
    • Tanaka III, I.B.1    Tanaka, S.2    Ichinohe, K.3
  • 59
    • 24044485916 scopus 로고    scopus 로고
    • HSP25 inhibits protein kinase Cδ-mediated cell death through direct interaction
    • Lee YJ, Lee DH, Cho CK, et al. HSP25 inhibits protein kinase Cδ-mediated cell death through direct interaction. J Biol Chem 2005;280:18108-19.
    • (2005) J Biol Chem , vol.280 , pp. 18108-18119
    • Lee, Y.J.1    Lee, D.H.2    Cho, C.K.3
  • 60
    • 0033818673 scopus 로고    scopus 로고
    • Hsp25-induced radioresistance is associated with reduction of death by apoptosis: Involvement of Bcl2 and the cell cycle
    • Park SH, Cho HN, Lee SJ, et al. Hsp25-induced radioresistance is associated with reduction of death by apoptosis: involvement of Bcl2 and the cell cycle. Radiat Res 2000;154:421-8.
    • (2000) Radiat Res , vol.154 , pp. 421-428
    • Park, S.H.1    Cho, H.N.2    Lee, S.J.3
  • 61
    • 0034053245 scopus 로고    scopus 로고
    • Inducible heat-shock protein 70 is involved in the radioadaptive response
    • Park SH, Lee SJ, Chung HY, et al. Inducible heat-shock protein 70 is involved in the radioadaptive response. Radiat Res 2000;153:318-26.
    • (2000) Radiat Res , vol.153 , pp. 318-326
    • Park, S.H.1    Lee, S.J.2    Chung, H.Y.3
  • 62
    • 34548787810 scopus 로고    scopus 로고
    • Radioprotective effect of heat shock protein 25 on submandibular glands of rats
    • Lee HJ, Lee YJ, Kwon HC, et al. Radioprotective effect of heat shock protein 25 on submandibular glands of rats. Am J Pathol 2006;169:1601-11.
    • (2006) Am J Pathol , vol.169 , pp. 1601-1611
    • Lee, H.J.1    Lee, Y.J.2    Kwon, H.C.3
  • 63
    • 0036351383 scopus 로고    scopus 로고
    • Cell surface α2,6 sialylation affects adhesion of breast carcinoma cells
    • Lin S, Kemmner W, Grigull S, Schlag PM. Cell surface α2,6 sialylation affects adhesion of breast carcinoma cells. Exp Cell Res 2002;276:101-10.
    • (2002) Exp Cell Res , vol.276 , pp. 101-110
    • Lin, S.1    Kemmner, W.2    Grigull, S.3    Schlag, P.M.4
  • 64
    • 9644287775 scopus 로고    scopus 로고
    • Lectin-based three-color flow cytometric approach for studying cell surface glycosylation changes that occur during apoptosis
    • Batisse C, Marquet J, Greffard A, Fleury-Feith J, Jaurand MC, Pilatte Y. Lectin-based three-color flow cytometric approach for studying cell surface glycosylation changes that occur during apoptosis. Cytometry A 2004;62:81-8.
    • (2004) Cytometry A , vol.62 , pp. 81-88
    • Batisse, C.1    Marquet, J.2    Greffard, A.3    Fleury-Feith, J.4    Jaurand, M.C.5    Pilatte, Y.6
  • 65
    • 33845629320 scopus 로고    scopus 로고
    • Increase in β1-6 GlcNAc branching caused by N-acetylglucosaminyltransferase V directs integrin β1 stability in human hepatocellular carcinoma cell line SMMC-7721
    • Wang L, Liang Y, Li Z, et al. Increase in β1-6 GlcNAc branching caused by N-acetylglucosaminyltransferase V directs integrin β1 stability in human hepatocellular carcinoma cell line SMMC-7721. J Cell Biochem 2007;100:230-41.
    • (2007) J Cell Biochem , vol.100 , pp. 230-241
    • Wang, L.1    Liang, Y.2    Li, Z.3


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