메뉴 건너뛰기




Volumn 73, Issue , 2003, Pages 107-136

Dynamic Interplay between O-Glycosylation and O-Phosphorylation of Nucleocytoplasmic Proteins: A New Paradigm for Metabolic Control of Signal Transduction and Transcription

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0345277743     PISSN: 00796603     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0079-6603(03)01004-3     Document Type: Article
Times cited : (108)

References (184)
  • 1
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • C-R Torres G.W Hart Topography and polypeptide distribution of terminal N -acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O -linked GlcNAc J. Biol. Chem. 259 1984 3308 3317
    • (1984) J. Biol. Chem. , vol.259 , pp. 3308-3317
    • Torres, C-R1    Hart, G.W2
  • 3
    • 0030943923 scopus 로고    scopus 로고
    • Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
    • G.W Hart Dynamic O -linked glycosylation of nuclear and cytoskeletal proteins Annu. Rev. Biochem. 66 1997 315 335
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 315-335
    • Hart, G.W1
  • 5
    • 0030959555 scopus 로고    scopus 로고
    • Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
    • L.K Kreppel M.A Blomberg G.W Hart Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O -GlcNAc transferase with multiple tetratricopeptide repeats J. Biol. Chem. 272 1997 9308 9315
    • (1997) J. Biol. Chem. , vol.272 , pp. 9308-9315
    • Kreppel, L.K1    Blomberg, M.A2    Hart, G.W3
  • 6
    • 0030944105 scopus 로고    scopus 로고
    • O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats
    • W.A Lubas D.W Frank M Krause J.A Hanover O -Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats J. Biol. Chem. 272 1997 9316 9324
    • (1997) J. Biol. Chem. , vol.272 , pp. 9316-9324
    • Lubas, W.A1    Frank, D.W2    Krause, M3    Hanover, J.A4
  • 7
    • 0035971182 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a neutral, cytosolic β-N-acetylglucosaminidase from human brain
    • Y Gao L Wells F.I Comer G.J Parker G.W Hart Dynamic O -glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a neutral, cytosolic β- N -acetylglucosaminidase from human brain J. Biol. Chem. 276 2001 9838 9845
    • (2001) J. Biol. Chem. , vol.276 , pp. 9838-9845
    • Gao, Y1    Wells, L2    Comer, F.I3    Parker, G.J4    Hart, G.W5
  • 8
    • 0029049198 scopus 로고
    • c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas
    • T-Y Chou G.W Hart C.V Dang c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas J. Biol. Chem. 270 1995 18961 18965
    • (1995) J. Biol. Chem. , vol.270 , pp. 18961-18965
    • Chou, T-Y1    Hart, G.W2    Dang, C.V3
  • 9
    • 0034718570 scopus 로고    scopus 로고
    • Alternative O-glycosylation⧸O-phosphorylation of the murine estrogen receptor β
    • X Cheng R.N Cole J Zaia G.W Hart Alternative O -glycosylation⧸ O -phosphorylation of the murine estrogen receptor β Biochemistry 39 2000 11609 11620
    • (2000) Biochemistry , vol.39 , pp. 11609-11620
    • Cheng, X1    Cole, R.N2    Zaia, J3    Hart, G.W4
  • 10
    • 0031949577 scopus 로고    scopus 로고
    • SV40 T antigen is modified with O-linked N-acetylglucosamine but not with other forms of glycosylation
    • L Medina K Grove R.S Haltiwanger SV40 T antigen is modified with O -linked N -acetylglucosamine but not with other forms of glycosylation Glycobiology 8 1998 383 391
    • (1998) Glycobiology , vol.8 , pp. 383-391
    • Medina, L1    Grove, K2    Haltiwanger, R.S3
  • 11
    • 0035180299 scopus 로고    scopus 로고
    • Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site
    • X.L Du D Edelstein S Dimmeler Q Ju C Sui M Brownlee Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site J. Clin. Invest. 108 2001 1341 1348
    • (2001) J. Clin. Invest. , vol.108 , pp. 1341-1348
    • Du, X.L1    Edelstein, D2    Dimmeler, S3    Ju, Q4    Sui, C5    Brownlee, M6
  • 12
    • 0032734974 scopus 로고    scopus 로고
    • O-GlcNAc and the control of gene expression
    • F.I Comer G.W Hart O -GlcNAc and the control of gene expression Biochim. Biophys. Acta 1473 1999 161 171
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 161-171
    • Comer, F.I1    Hart, G.W2
  • 13
    • 0034703095 scopus 로고    scopus 로고
    • O-Glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and O-phosphate
    • F.I Comer G.W Hart O -Glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O -GlcNAc and O -phosphate J. Biol. Chem. 275 2000 29179 29182
    • (2000) J. Biol. Chem. , vol.275 , pp. 29179-29182
    • Comer, F.I1    Hart, G.W2
  • 14
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc
    • L Wells K Vosseller G.W Hart Glycosylation of nucleocytoplasmic proteins: Signal transduction and O -GlcNAc Science 291 2001 2376 2378
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L1    Vosseller, K2    Hart, G.W3
  • 15
    • 0034854157 scopus 로고    scopus 로고
    • Glycan-dependent signaling: O-linked N-acetylglucosamine
    • J.A Hanover Glycan-dependent signaling: O -linked N -acetylglucosamine FASEB J. 15 2001 1865 1876
    • (2001) FASEB J. , vol.15 , pp. 1865-1876
    • Hanover, J.A1
  • 16
    • 0036462599 scopus 로고    scopus 로고
    • The emerging significance of O-GlcNAc in cellular regulation
    • N.E Zachara G.W Hart The emerging significance of O -GlcNAc in cellular regulation Chem. Rev. 102 2002 431 438
    • (2002) Chem. Rev. , vol.102 , pp. 431-438
    • Zachara, N.E1    Hart, G.W2
  • 17
    • 0032905924 scopus 로고    scopus 로고
    • c-Myc target genes involved in cell growth, apoptosis, and metabolism
    • C.V Dang c-Myc target genes involved in cell growth, apoptosis, and metabolism Mol. Cell Biol. 19 1999 1 11
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1-11
    • Dang, C.V1
  • 18
    • 0034524132 scopus 로고    scopus 로고
    • The Myc⧸Max⧸Mad network and the transcriptional control of cell behavior
    • C Grandori S.M Cowley L.P James R.N Eisenman The Myc⧸Max⧸Mad network and the transcriptional control of cell behavior Annu. Rev. Cell Dev. Biol. 16 2000 653 699
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 653-699
    • Grandori, C1    Cowley, S.M2    James, L.P3    Eisenman, R.N4
  • 19
    • 0031806044 scopus 로고    scopus 로고
    • The molecular role of Myc in growth and transformation: Recent discoveries lead to new insights
    • L.M Facchini L.Z Penn The molecular role of Myc in growth and transformation: Recent discoveries lead to new insights FASEB J. 12 1998 633 651
    • (1998) FASEB J. , vol.12 , pp. 633-651
    • Facchini, L.M1    Penn, L.Z2
  • 20
    • 0035089346 scopus 로고    scopus 로고
    • Function of the c-Myc oncoproteins in chromatin remodeling and transcription
    • B Amati S.R Frank D Donjerkovic S Taubert Function of the c-Myc oncoproteins in chromatin remodeling and transcription Biochim. Biophys. Acta 1471 2001 M135 M145
    • (2001) Biochim. Biophys. Acta , vol.1471 , pp. M135-M145
    • Amati, B1    Frank, S.R2    Donjerkovic, D3    Taubert, S4
  • 21
    • 0027383378 scopus 로고
    • Phosphorylation sites mapping in the N-terminal domain of c-myc modulates its transforming potential
    • M Henriksson A Bakardjiev G Klein B Luscher Phosphorylation sites mapping in the N-terminal domain of c- myc modulates its transforming potential Oncogene 8 1993 3199 3209
    • (1993) Oncogene , vol.8 , pp. 3199-3209
    • Henriksson, M1    Bakardjiev, A2    Klein, G3    Luscher, B4
  • 22
    • 0028115718 scopus 로고
    • Site-specific modulation of c-Myc cotransformation by residues phosphorylated in vivo
    • B.J Pulverer C Fisher K Vousden T Littlewood G Evan J.R Woodgett Site-specific modulation of c-Myc cotransformation by residues phosphorylated in vivo Oncogene 9 1994 59 70
    • (1994) Oncogene , vol.9 , pp. 59-70
    • Pulverer, B.J1    Fisher, C2    Vousden, K3    Littlewood, T4    Evan, G5    Woodgett, J.R6
  • 23
    • 0029019572 scopus 로고
    • Glycosylation of the c-Myc transactivation domain
    • T-Y Chou C.V Dang G.W Hart Glycosylation of the c-Myc transactivation domain Proc. Natl. Acad. Sci. USA 92 1995 4417 4421
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4417-4421
    • Chou, T-Y1    Dang, C.V2    Hart, G.W3
  • 24
    • 3543060464 scopus 로고    scopus 로고
    • myc boxes, which are conserved in myc family proteins, are signals for protein degradation via the proteasome
    • E.M Flinn C.M.C Busch A.P Wright myc boxes, which are conserved in myc family proteins, are signals for protein degradation via the proteasome Mol. Cell Biol. 18 1998 5961 5969
    • (1998) Mol. Cell Biol. , vol.18 , pp. 5961-5969
    • Flinn, E.M1    Busch, C.M.C2    Wright, A.P3
  • 26
    • 0033081027 scopus 로고    scopus 로고
    • Destruction of Myc by ubiquitin-mediated proteolysis: Cancer-associated and transforming mutations stabilize Myc
    • S.E Salghetti S.Y Kim W.P Tansey Destruction of Myc by ubiquitin-mediated proteolysis: Cancer-associated and transforming mutations stabilize Myc EMBO J. 18 1999 717 726
    • (1999) EMBO J. , vol.18 , pp. 717-726
    • Salghetti, S.E1    Kim, S.Y2    Tansey, W.P3
  • 27
    • 0034306997 scopus 로고    scopus 로고
    • Multiple Ras-dependent phosphorylation pathways regulate Myc protein stability
    • R Sears F Nuckolls E Haura Y Taya K Tamai J.R Nevins Multiple Ras-dependent phosphorylation pathways regulate Myc protein stability Genes Dev. 14 2000 2501 2514
    • (2000) Genes Dev. , vol.14 , pp. 2501-2514
    • Sears, R1    Nuckolls, F2    Haura, E3    Taya, Y4    Tamai, K5    Nevins, J.R6
  • 28
    • 0018928955 scopus 로고
    • Phosphorylation of the nonstructural proteins encoded by three avian acute leukemia viruses and by avian Fujinami sarcoma virus
    • K Bister W-H Lee P.H Duesberg Phosphorylation of the nonstructural proteins encoded by three avian acute leukemia viruses and by avian Fujinami sarcoma virus J. Virol. 36 1980 617 621
    • (1980) J. Virol. , vol.36 , pp. 617-621
    • Bister, K1    Lee, W-H2    Duesberg, P.H3
  • 29
    • 0020056927 scopus 로고
    • Isolation and biochemical characterization of partially transformation-defective mutants of avian myelocytomatosis virus strain MC29: Localization of the mutation to the myc domain of the 110,000-dalton gag-myc polyprotein
    • G.M Ramsay M.J Hayman Isolation and biochemical characterization of partially transformation-defective mutants of avian myelocytomatosis virus strain MC29: Localization of the mutation to the myc domain of the 110,000-dalton gag-myc polyprotein J. Virol. 41 1982 745 753
    • (1982) J. Virol. , vol.41 , pp. 745-753
    • Ramsay, G.M1    Hayman, M.J2
  • 30
    • 3142636201 scopus 로고
    • The protein encoded by the human proto-oncogene c-myc
    • G Ramsay G.I Evan J.M Bishop The protein encoded by the human proto-oncogene c- myc Proc. Natl. Acad. Sci. USA 81 1984 7742 7746
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7742-7746
    • Ramsay, G1    Evan, G.I2    Bishop, J.M3
  • 31
    • 0020616953 scopus 로고
    • Proteins encoded by v-myc and c-myc oncogenes: Identification and localization in acute leukemia virus transformants and bursal lymphoma cell lines
    • S.R Hann H.D Abrams L.R Rohrschneider R.N Eisenman Proteins encoded by v- myc and c- myc oncogenes: Identification and localization in acute leukemia virus transformants and bursal lymphoma cell lines Cell 34 1983 789 798
    • (1983) Cell , vol.34 , pp. 789-798
    • Hann, S.R1    Abrams, H.D2    Rohrschneider, L.R3    Eisenman, R.N4
  • 32
    • 0021688655 scopus 로고
    • Proteins encoded by the human c-myc oncogene: Differential expression in neoplastic cells
    • S.R Hann R.N Eisenman Proteins encoded by the human c- myc oncogene: Differential expression in neoplastic cells Mol. Cell Biol. 4 1984 2486 2497
    • (1984) Mol. Cell Biol. , vol.4 , pp. 2486-2497
    • Hann, S.R1    Eisenman, R.N2
  • 33
    • 0024446021 scopus 로고
    • Myc oncoproteins are phosphorylated by casein kinase II
    • B Luscher E.A Kuenzel E.G Krebs R.N Eisenman Myc oncoproteins are phosphorylated by casein kinase II EMBO J. 8 1989 1111 1119
    • (1989) EMBO J. , vol.8 , pp. 1111-1119
    • Luscher, B1    Kuenzel, E.A2    Krebs, E.G3    Eisenman, R.N4
  • 34
    • 0025871767 scopus 로고
    • Pro-Leu-Ser⧸Thr-Pro is a consensus primary sequence for substrate protein phosphorylation. Characterization of the phosphorylation of c-myc and c-jun proteins by an epidermal growth factor receptor theronine 669 protein kinase
    • E Alvarez I.C Northwood F.A Gonzalez D.A Latour A Seth C Abate T Curran R.J Davis Pro-Leu-Ser⧸Thr-Pro is a consensus primary sequence for substrate protein phosphorylation. Characterization of the phosphorylation of c- myc and c- jun proteins by an epidermal growth factor receptor theronine 669 protein kinase J. Biol. Chem. 266 1991 15277 15285
    • (1991) J. Biol. Chem. , vol.266 , pp. 15277-15285
    • Alvarez, E1    Northwood, I.C2    Gonzalez, F.A3    Latour, D.A4    Seth, A5    Abate, C6    Curran, T7    Davis, R.J8
  • 35
    • 0026343730 scopus 로고
    • A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression
    • 2-terminal domain of c-Myc increases transactivation of gene expression J. Biol. Chem. 266 1991 23521 23524
    • (1991) J. Biol. Chem. , vol.266 , pp. 23521-23524
    • Seth, A1    Alvarez, E2    Gupta, S3    Davis, R.J4
  • 36
    • 0026464922 scopus 로고
    • Signal transduction within the nucleus by mitogen-activated protein kinase
    • A Seth F.A Gonzalez S Gupta D.L Raden R.J Davis Signal transduction within the nucleus by mitogen-activated protein kinase J. Biol. Chem. 267 1992 24796 24804
    • (1992) J. Biol. Chem. , vol.267 , pp. 24796-24804
    • Seth, A1    Gonzalez, F.A2    Gupta, S3    Raden, D.L4    Davis, R.J5
  • 37
    • 0026657897 scopus 로고
    • Mitosis-specific phosphorylation of the nuclear oncoproteins Myc and Myb
    • B Luscher R.N Eisenman Mitosis-specific phosphorylation of the nuclear oncoproteins Myc and Myb J. Cell Biol. 118 1992 775 784
    • (1992) J. Cell Biol. , vol.118 , pp. 775-784
    • Luscher, B1    Eisenman, R.N2
  • 38
    • 0027417593 scopus 로고
    • Transactivation of gene expression by Myc is inhibited by mutation at the phosphorylation sites Thr-58 and Ser-62
    • S Gupta A Seth R.J Davis Transactivation of gene expression by Myc is inhibited by mutation at the phosphorylation sites Thr-58 and Ser-62 Proc. Natl. Acad. Sci. USA 90 1993 3216 3220
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3216-3220
    • Gupta, S1    Seth, A2    Davis, R.J3
  • 39
    • 0028023421 scopus 로고
    • Hieralchical phosphorylation at N-terminal transformation-sensitive sites in c-Myc protein is regulated by mitogens and in mitosis
    • B Lutterbuch S.R Hann Hieralchical phosphorylation at N-terminal transformation-sensitive sites in c-Myc protein is regulated by mitogens and in mitosis Mol. Cell Biol. 14 1994 5510 5522
    • (1994) Mol. Cell Biol. , vol.14 , pp. 5510-5522
    • Lutterbuch, B1    Hann, S.R2
  • 40
    • 0029001787 scopus 로고
    • A link between increased transforming activity of lymphoma-derived Myc mutant alleles, their defective regulation by p107, and altered phosphorylation of the c-Myc transactivation domain
    • A.T Hoang B Lutterbach B.C Lewis T Yano T-Y Chou J.F Barrett M Raffeld S.R Hann C.V Dang A link between increased transforming activity of lymphoma-derived Myc mutant alleles, their defective regulation by p107, and altered phosphorylation of the c-Myc transactivation domain Mol. Cell Biol. 15 1995 4031 4042
    • (1995) Mol. Cell Biol. , vol.15 , pp. 4031-4042
    • Hoang, A.T1    Lutterbach, B2    Lewis, B.C3    Yano, T4    Chou, T-Y5    Barrett, J.F6    Raffeld, M7    Hann, S.R8    Dang, C.V9
  • 41
    • 0032703216 scopus 로고    scopus 로고
    • Regulation of c-Myc through phosphorylation at Ser-62 and Ser-71 by c-Jun N-terminal kinase
    • K Noguchi C Kitanaka H Yamana A Kokubu T Mochizuki Y Kuchino Regulation of c-Myc through phosphorylation at Ser-62 and Ser-71 by c-Jun N-terminal kinase J. Biol. Chem. 274 1999 32580 32587
    • (1999) J. Biol. Chem. , vol.274 , pp. 32580-32587
    • Noguchi, K1    Kitanaka, C2    Yamana, H3    Kokubu, A4    Mochizuki, T5    Kuchino, Y6
  • 42
    • 0037166352 scopus 로고    scopus 로고
    • Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins. Alternative glycosylation⧸phosphorylation of Thr-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens
    • K Kamemura B.K Hayes F.I Comer G.W Hart Dynamic interplay between O -glycosylation and O -phosphorylation of nucleocytoplasmic proteins. Alternative glycosylation⧸phosphorylation of Thr-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens J. Biol. Chem. 277 2002 19229 19235
    • (2002) J. Biol. Chem. , vol.277 , pp. 19229-19235
    • Kamemura, K1    Hayes, B.K2    Comer, F.I3    Hart, G.W4
  • 46
    • 0034059667 scopus 로고    scopus 로고
    • c-Myc proteolysis by the ubiquitin-proteasome pathway: Stabilization of c-Myc in Burkitt's lymphoma cells
    • M.A Gregory S.R Hann c-Myc proteolysis by the ubiquitin-proteasome pathway: Stabilization of c-Myc in Burkitt's lymphoma cells Mol. Cell Biol. 20 2000 2423 2435
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2423-2435
    • Gregory, M.A1    Hann, S.R2
  • 47
    • 0034653998 scopus 로고    scopus 로고
    • c-Myc hot spot mutations in lymphomas result in inefficient ubiquitination and decreased proteasome-mediated turnover
    • F Bahram N von der Lehr C Cetinkaya L-G Larsson c-Myc hot spot mutations in lymphomas result in inefficient ubiquitination and decreased proteasome-mediated turnover Blood 95 2000 2104 2110
    • (2000) Blood , vol.95 , pp. 2104-2110
    • Bahram, F1    von der Lehr, N2    Cetinkaya, C3    Larsson, L-G4
  • 50
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • D Voges P Zwickl W Baumeister The 26S proteasome: A molecular machine designed for controlled proteolysis Annu. Rev. Biochem. 68 1999 1015 1068
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D1    Zwickl, P2    Baumeister, W3
  • 51
    • 0030907389 scopus 로고    scopus 로고
    • Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility
    • I Han J.E Kudlow Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility Mol. Cell Biol. 17 1997 2550 2558
    • (1997) Mol. Cell Biol. , vol.17 , pp. 2550-2558
    • Han, I1    Kudlow, J.E2
  • 52
    • 0035971067 scopus 로고    scopus 로고
    • Alternative O-glycosylation⧸O-phosphorylation of Serine-16 in murine estrogen receptor β. Post-translational regulation of turnover and transactivation activity
    • X Cheng G.W Hart Alternative O -glycosylation⧸ O -phosphorylation of Serine-16 in murine estrogen receptor β. Post-translational regulation of turnover and transactivation activity J. Biol. Chem. 276 2001 10570 10575
    • (2001) J. Biol. Chem. , vol.276 , pp. 10570-10575
    • Cheng, X1    Hart, G.W2
  • 54
    • 0035839844 scopus 로고    scopus 로고
    • Translocation involving c-myc and c-myc function
    • L.M Boxer C.V Dang Translocation involving c- myc and c- myc function Oncogene 20 2001 5595 5610
    • (2001) Oncogene , vol.20 , pp. 5595-5610
    • Boxer, L.M1    Dang, C.V2
  • 55
    • 0028055178 scopus 로고
    • Ongoing mutations in the N-terminal domain of c-Myc affect transactivation in Burkitt's lymphoma cell lines
    • T Albert B Urlbauer F Kohlhuber B Hammersen D Eick Ongoing mutations in the N-terminal domain of c-Myc affect transactivation in Burkitt's lymphoma cell lines Oncogene 9 1994 759 763
    • (1994) Oncogene , vol.9 , pp. 759-763
    • Albert, T1    Urlbauer, B2    Kohlhuber, F3    Hammersen, B4    Eick, D5
  • 57
    • 0030989077 scopus 로고    scopus 로고
    • Overexpression of c-Myc and cell immortalization alters c-Myc phosphorylation
    • B Lutterbach S.R Hann Overexpression of c-Myc and cell immortalization alters c-Myc phosphorylation Oncogene 14 1997 967 975
    • (1997) Oncogene , vol.14 , pp. 967-975
    • Lutterbach, B1    Hann, S.R2
  • 58
    • 0034724166 scopus 로고    scopus 로고
    • Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis
    • S.E Salghetti M Muratani H Wijnen B Futcher W.P Tansey Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis Proc. Natl. Acad. Sci. USA 97 2000 3118 3123
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3118-3123
    • Salghetti, S.E1    Muratani, M2    Wijnen, H3    Futcher, B4    Tansey, W.P5
  • 59
    • 0035979738 scopus 로고    scopus 로고
    • Regulation of transcriptional activation domain function by ubiquitin
    • S.E Salghetti A.A Caudy J.G Chenoweth W.P Tansey Regulation of transcriptional activation domain function by ubiquitin Science 293 2001 1651 1653
    • (2001) Science , vol.293 , pp. 1651-1653
    • Salghetti, S.E1    Caudy, A.A2    Chenoweth, J.G3    Tansey, W.P4
  • 60
    • 0037123605 scopus 로고    scopus 로고
    • Emerging roles of ubiquitin in transcription regulation
    • R.C Conaway C.S Brower J.W Conaway Emerging roles of ubiquitin in transcription regulation Science 296 2002 1254 1258
    • (2002) Science , vol.296 , pp. 1254-1258
    • Conaway, R.C1    Brower, C.S2    Conaway, J.W3
  • 61
    • 0033551388 scopus 로고    scopus 로고
    • New Myc-interacting proteins: A second Myc network emerges
    • D Sakamuro G.C Prendergast New Myc-interacting proteins: A second Myc network emerges Oncogene 18 1999 2942 2954
    • (1999) Oncogene , vol.18 , pp. 2942-2954
    • Sakamuro, D1    Prendergast, G.C2
  • 62
    • 0035882058 scopus 로고    scopus 로고
    • Deconstructing Myc
    • R.N Eisenman Deconstructing Myc Genes Dev. 15 2001 2023 2030
    • (2001) Genes Dev. , vol.15 , pp. 2023-2030
    • Eisenman, R.N1
  • 63
    • 0032493894 scopus 로고    scopus 로고
    • The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins
    • S.B McMahon H.A van Buskirk K.A Dugan T.D Copeland M.D Cole The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins Cell 94 1998 363 374
    • (1998) Cell , vol.94 , pp. 363-374
    • McMahon, S.B1    van Buskirk, H.A2    Dugan, K.A3    Copeland, T.D4    Cole, M.D5
  • 64
    • 0032963671 scopus 로고    scopus 로고
    • c-Myc interacts with INI1⧸hSNF5 and requires the SWI⧸SNF complex for transactivation function
    • S-W.G Cheng K.P Davies E Yung R.J Beltran J Yu G.V Kalpana c-Myc interacts with INI1⧸hSNF5 and requires the SWI⧸SNF complex for transactivation function Nat. Genet. 22 1999 102 105
    • (1999) Nat. Genet. , vol.22 , pp. 102-105
    • Cheng, S-W.G1    Davies, K.P2    Yung, E3    Beltran, R.J4    Yu, J5    Kalpana, G.V6
  • 65
    • 0033970431 scopus 로고    scopus 로고
    • The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc
    • S.B McMahon M.A Wood M.D Cole The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc Mol. Cell Biol. 20 2000 556 562
    • (2000) Mol. Cell Biol. , vol.20 , pp. 556-562
    • McMahon, S.B1    Wood, M.A2    Cole, M.D3
  • 66
    • 0036173140 scopus 로고    scopus 로고
    • BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation
    • J Park M.A Wood M.D Cole BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation Mol. Cell Biol. 22 2002 1307 1316
    • (2002) Mol. Cell Biol. , vol.22 , pp. 1307-1316
    • Park, J1    Wood, M.A2    Cole, M.D3
  • 67
    • 13144250143 scopus 로고    scopus 로고
    • Identification of a large Myc-binding protein that contains RCC1-like repeats
    • Q Guo J Xie C.V Dang E.T Liu J.M Bishop Identification of a large Myc-binding protein that contains RCC1-like repeats Proc. Natl. Acad. Sci. USA 95 1998 9172 9177
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9172-9177
    • Guo, Q1    Xie, J2    Dang, C.V3    Liu, E.T4    Bishop, J.M5
  • 68
    • 0027979267 scopus 로고
    • Intracellular association of the protein product of the c-myc oncogene with the TATA-binding protein
    • S Maheswaran H Lee G.E Sonenshein Intracellular association of the protein product of the c- myc oncogene with the TATA-binding protein Mol. Cell Biol. 14 1994 1147 1152
    • (1994) Mol. Cell Biol. , vol.14 , pp. 1147-1152
    • Maheswaran, S1    Lee, H2    Sonenshein, G.E3
  • 69
    • 0035930571 scopus 로고    scopus 로고
    • c-Myc mediates activation of the cad promoter via a post-RNA polemerase II recruitment mechanism
    • S.R Eberhardy P.J Farnham c-Myc mediates activation of the cad promoter via a post-RNA polemerase II recruitment mechanism J. Biol. Chem. 276 2001 48562 48571
    • (2001) J. Biol. Chem. , vol.276 , pp. 48562-48571
    • Eberhardy, S.R1    Farnham, P.J2
  • 70
    • 0035014553 scopus 로고    scopus 로고
    • Mechanism for the transcriptional repression by c-Myc on PDGF β-receptor
    • H Izumi C Molander L.Z Penn A Ishisaki K Kohno K Funa Mechanism for the transcriptional repression by c-Myc on PDGF β-receptor J. Cell Sci. 114 2001 1533 1544
    • (2001) J. Cell Sci. , vol.114 , pp. 1533-1544
    • Izumi, H1    Molander, C2    Penn, L.Z3    Ishisaki, A4    Kohno, K5    Funa, K6
  • 71
    • 0021088187 scopus 로고
    • Altered nucleotide sequences of a translocated c-myc gene in Burkitt lymphoma
    • T.H Rabbitts P.H Hamlyn R Baer Altered nucleotide sequences of a translocated c- myc gene in Burkitt lymphoma Nature 306 1983 760 765
    • (1983) Nature , vol.306 , pp. 760-765
    • Rabbitts, T.H1    Hamlyn, P.H2    Baer, R3
  • 72
    • 0022430244 scopus 로고
    • Sequence curiosity in v-myc oncogene
    • T.S Papas J.A Lautenberger Sequence curiosity in v- myc oncogene Nature 318 1985 237
    • (1985) Nature , vol.318 , pp. 237
    • Papas, T.S1    Lautenberger, J.A2
  • 73
    • 0021925123 scopus 로고
    • Cloning and sequencing of a c-myc oncogene in a Burkitt's lymphoma cell line that is translocated to a germ line alpha switch region
    • L.C Showe M Ballantine K Nishikura J Erikson H Kaji C.M Croce Cloning and sequencing of a c- myc oncogene in a Burkitt's lymphoma cell line that is translocated to a germ line alpha switch region Mol. Cell Biol. 5 1985 501 509
    • (1985) Mol. Cell Biol. , vol.5 , pp. 501-509
    • Showe, L.C1    Ballantine, M2    Nishikura, K3    Erikson, J4    Kaji, H5    Croce, C.M6
  • 74
    • 0027220503 scopus 로고
    • Clustered mutations in the second exon of the Myc gene in sporadic Burkitt's lymphoma
    • T Yano C.A Sander H.M Clark M.V Dolezal E.S Jaffe M Raffeld Clustered mutations in the second exon of the Myc gene in sporadic Burkitt's lymphoma Oncogene 8 1993 2741 2748
    • (1993) Oncogene , vol.8 , pp. 2741-2748
    • Yano, T1    Sander, C.A2    Clark, H.M3    Dolezal, M.V4    Jaffe, E.S5    Raffeld, M6
  • 75
    • 0027275755 scopus 로고
    • Point mutations in the c-Myc transactivation domain are common in Burkitt's lymphoma and mouse plasmacytomas
    • K Bhatia K Huppi G Spangler D Siwarski R Iyer I Magrath Point mutations in the c-Myc transactivation domain are common in Burkitt's lymphoma and mouse plasmacytomas Nat. Genet. 5 1993 56 61
    • (1993) Nat. Genet. , vol.5 , pp. 56-61
    • Bhatia, K1    Huppi, K2    Spangler, G3    Siwarski, D4    Iyer, R5    Magrath, I6
  • 76
    • 0028298840 scopus 로고
    • Mutations in the coding region of c-myc occur frequently in acquired immunodeficiency syndrome-associated lymphomas
    • K Bhatia G Spangler G Gaidano N Hamdy R Dalla-Favera I Magrath Mutations in the coding region of c- myc occur frequently in acquired immunodeficiency syndrome-associated lymphomas Blood 84 1994 883 888
    • (1994) Blood , vol.84 , pp. 883-888
    • Bhatia, K1    Spangler, G2    Gaidano, G3    Hamdy, N4    Dalla-Favera, R5    Magrath, I6
  • 77
    • 0028305664 scopus 로고
    • Mutations in the coding region of c-Myc in AIDS-associated and other aggressive lymphomas
    • H.M Clark T Yano T Otsuki E.S Jaffe D Shibata M Raffeld Mutations in the coding region of c-Myc in AIDS-associated and other aggressive lymphomas Cancer Res. 54 1994 3383 3386
    • (1994) Cancer Res. , vol.54 , pp. 3383-3386
    • Clark, H.M1    Yano, T2    Otsuki, T3    Jaffe, E.S4    Shibata, D5    Raffeld, M6
  • 78
    • 0034037132 scopus 로고    scopus 로고
    • The c-Myc transactivation domain is a direct modulator of apoptotic versus proliferative signals
    • D.W Chang G.F Claassen S.R Hann M.D Cole The c-Myc transactivation domain is a direct modulator of apoptotic versus proliferative signals Mol. Cell Biol. 20 2000 4309 4319
    • (2000) Mol. Cell Biol. , vol.20 , pp. 4309-4319
    • Chang, D.W1    Claassen, G.F2    Hann, S.R3    Cole, M.D4
  • 79
    • 0028307489 scopus 로고
    • Binding and suppression of the c-Myc transcriptional activation domain by p107
    • W Gu K Bhatia I.T Magrath C.V Dang R Dalla-Favera Binding and suppression of the c-Myc transcriptional activation domain by p107 Science 264 1994 251 254
    • (1994) Science , vol.264 , pp. 251-254
    • Gu, W1    Bhatia, K2    Magrath, I.T3    Dang, C.V4    Dalla-Favera, R5
  • 80
    • 0027956609 scopus 로고
    • Interaction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivation
    • R.L Beijersberden E.M Hijimans L Zhu R Bernards Interaction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivation EMBO J. 13 1994 4080 4086
    • (1994) EMBO J. , vol.13 , pp. 4080-4086
    • Beijersberden, R.L1    Hijimans, E.M2    Zhu, L3    Bernards, R4
  • 81
    • 0035835827 scopus 로고    scopus 로고
    • p107 and p130: Versatile proteins with interesting pockets
    • M Classon N Dyson p107 and p130: Versatile proteins with interesting pockets Exp. Cell Res. 264 2001 135 147
    • (2001) Exp. Cell Res. , vol.264 , pp. 135-147
    • Classon, M1    Dyson, N2
  • 82
    • 0030667320 scopus 로고    scopus 로고
    • E2F activity is regulated by cell cycle-dependent changes in subcellular localization
    • R Verona K Moberg S Estes M Starz J.P Vernon J.A Lees E2F activity is regulated by cell cycle-dependent changes in subcellular localization Mol. Cell Biol. 17 1997 7268 7282
    • (1997) Mol. Cell Biol. , vol.17 , pp. 7268-7282
    • Verona, R1    Moberg, K2    Estes, S3    Starz, M4    Vernon, J.P5    Lees, J.A6
  • 84
    • 0023731952 scopus 로고
    • Identification of the human c-myc protein nuclear translocation signal
    • C.V Dang W.M Lee Identification of the human c-myc protein nuclear translocation signal Mol. Cell Biol. 8 1988 4048 4054
    • (1988) Mol. Cell Biol. , vol.8 , pp. 4048-4054
    • Dang, C.V1    Lee, W.M2
  • 86
    • 0026700792 scopus 로고
    • Comparative analysis of the intracellular localization of c-Myc, c-Fos, and replicative proteins during cell cycle progression
    • S Vriz J-M Lemaitre M Leibovici N Thierry M Mechali Comparative analysis of the intracellular localization of c-Myc, c-Fos, and replicative proteins during cell cycle progression Mol. Cell Biol. 12 1992 3548 3555
    • (1992) Mol. Cell Biol. , vol.12 , pp. 3548-3555
    • Vriz, S1    Lemaitre, J-M2    Leibovici, M3    Thierry, N4    Mechali, M5
  • 87
    • 0033935653 scopus 로고    scopus 로고
    • Disruption of Myc-tubulin interaction by hyperphosphorylation of c-Myc during mitosis or by constitutive hyperphosphorylation of mutant c-Myc in Burkitt's lymphoma
    • J Niklinski G Claassen C Meyers M.A Gregory C.J Allegra F.J Kaye S.R Hann M Zajac-Kaye Disruption of Myc-tubulin interaction by hyperphosphorylation of c-Myc during mitosis or by constitutive hyperphosphorylation of mutant c-Myc in Burkitt's lymphoma Mol. Cell Biol. 20 2000 5276 5284
    • (2000) Mol. Cell Biol. , vol.20 , pp. 5276-5284
    • Niklinski, J1    Claassen, G2    Meyers, C3    Gregory, M.A4    Allegra, C.J5    Kaye, F.J6    Hann, S.R7    Zajac-Kaye, M8
  • 88
    • 0032575705 scopus 로고    scopus 로고
    • A matter of life and cell death
    • G Evan T Littlewood A matter of life and cell death Science 281 1998 1317 1322
    • (1998) Science , vol.281 , pp. 1317-1322
    • Evan, G1    Littlewood, T2
  • 89
    • 0035902115 scopus 로고    scopus 로고
    • Proliferation, cell cycle and apoptosis in cancer
    • G.I Evan K.H Vousden Proliferation, cell cycle and apoptosis in cancer Nature 411 2001 342 348
    • (2001) Nature , vol.411 , pp. 342-348
    • Evan, G.I1    Vousden, K.H2
  • 90
    • 0025937489 scopus 로고
    • Constitutive c-myc expression in an IL-3-dependent myeloid cell line suppresses cell cycle arrest and accelerates apoptosis
    • D.S Askew R.A Ashmun B.C Simmons J.L Cleveland Constitutive c- myc expression in an IL-3-dependent myeloid cell line suppresses cell cycle arrest and accelerates apoptosis Oncogene 6 1991 1915 1922
    • (1991) Oncogene , vol.6 , pp. 1915-1922
    • Askew, D.S1    Ashmun, R.A2    Simmons, B.C3    Cleveland, J.L4
  • 92
    • 0031918741 scopus 로고    scopus 로고
    • The many roles of c-Mycin apoptosis
    • E.B Thompson The many roles of c-Mycin apoptosis Annu. Rev. Physiol. 60 1998 575 600
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 575-600
    • Thompson, E.B1
  • 93
    • 0033551387 scopus 로고    scopus 로고
    • Mechanisms of apoptosis by c-Myc
    • G.C Prendergast Mechanisms of apoptosis by c-Myc Oncogene 18 1999 2967 2987
    • (1999) Oncogene , vol.18 , pp. 2967-2987
    • Prendergast, G.C1
  • 94
    • 0029741917 scopus 로고    scopus 로고
    • Bin1 is a novel Myc-interacting protein with features of a tumour suppressor
    • D Sakamuro K.J Elliott R Wechsler-Reya G.C Prendergast Bin1 is a novel Myc-interacting protein with features of a tumour suppressor Nat. Genet. 14 1996 69 77
    • (1996) Nat. Genet. , vol.14 , pp. 69-77
    • Sakamuro, D1    Elliott, K.J2    Wechsler-Reya, R3    Prendergast, G.C4
  • 95
    • 0034726959 scopus 로고    scopus 로고
    • The c-Myc-interacting adaptor protein Bin1 activates a caspase-independent cell death program
    • K Elliott K Ge W Du G Prendergast The c-Myc-interacting adaptor protein Bin1 activates a caspase-independent cell death program Oncogene 19 2000 4669 4684
    • (2000) Oncogene , vol.19 , pp. 4669-4684
    • Elliott, K1    Ge, K2    Du, W3    Prendergast, G4
  • 96
    • 0035300436 scopus 로고    scopus 로고
    • Bin1 mediates apoptosis by c-Myc in transformed primary cells
    • J.B DuHadaway D Sakamuro D.L Ewert G.C Prendergast Bin1 mediates apoptosis by c-Myc in transformed primary cells Cancer Res. 61 2001 3151 3156
    • (2001) Cancer Res. , vol.61 , pp. 3151-3156
    • DuHadaway, J.B1    Sakamuro, D2    Ewert, D.L3    Prendergast, G.C4
  • 97
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • R.M Evans The steroid and thyroid hormone receptor superfamily Science 240 1988 889 895
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M1
  • 98
    • 0035878743 scopus 로고    scopus 로고
    • Estrogen receptor interaction with estrogen responce elements
    • C.M Klinge Estrogen receptor interaction with estrogen responce elements Nucleic Acids Res. 29 2001 2905 2919
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2905-2919
    • Klinge, C.M1
  • 99
    • 0033305438 scopus 로고    scopus 로고
    • Estrogen receptor null mice: What have we learned and where will they lead us?
    • J.F Couse K.S Korach Estrogen receptor null mice: What have we learned and where will they lead us? Endocrine Rev. 20 1999 358 417
    • (1999) Endocrine Rev. , vol.20 , pp. 358-417
    • Couse, J.F1    Korach, K.S2
  • 100
    • 0036225994 scopus 로고    scopus 로고
    • Molecular forms of the estrogen receptor in breast cancer
    • G Leclercq Molecular forms of the estrogen receptor in breast cancer J. Steroid Biochem. Mol. Biol. 80 2002 259 272
    • (2002) J. Steroid Biochem. Mol. Biol. , vol.80 , pp. 259-272
    • Leclercq, G1
  • 101
    • 0035813112 scopus 로고    scopus 로고
    • The multifaceted mechanisms of estradiol and estrogen receptor signaling
    • J.M Hall J.F Couse K.S Korach The multifaceted mechanisms of estradiol and estrogen receptor signaling J. Biol. Chem. 276 2001 36869 36872
    • (2001) J. Biol. Chem. , vol.276 , pp. 36869-36872
    • Hall, J.M1    Couse, J.F2    Korach, K.S3
  • 103
    • 0028833473 scopus 로고
    • Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro
    • S.F Arnold J.D Obourn H Jaffe A.C Notides Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro Mol. Endocrinol. 9 1995 24 33
    • (1995) Mol. Endocrinol. , vol.9 , pp. 24-33
    • Arnold, S.F1    Obourn, J.D2    Jaffe, H3    Notides, A.C4
  • 104
    • 0029855010 scopus 로고    scopus 로고
    • Steroid hormone receptor and their regulation by phosphorylation
    • N.L Weigel Steroid hormone receptor and their regulation by phosphorylation Biochem. J. 319 1996 657 667
    • (1996) Biochem. J. , vol.319 , pp. 657-667
    • Weigel, N.L1
  • 105
    • 0027405070 scopus 로고
    • Modulation of transcriptional activation by ligand-dependent phosphorylation of the human oestrogen receptor A⧸B region
    • S Ali D Metzger J.M Bornert P Chambon Modulation of transcriptional activation by ligand-dependent phosphorylation of the human oestrogen receptor A⧸B region EMBO J. 12 1993 1153 1160
    • (1993) EMBO J. , vol.12 , pp. 1153-1160
    • Ali, S1    Metzger, D2    Bornert, J.M3    Chambon, P4
  • 106
    • 0028111526 scopus 로고
    • Phosphorylation of the human estrogen receptor. Identification of hormone-regulated sites and examination of their influence on transcriptional activity
    • P le Goff M.M Montano D.J Schodin B.S Katzenellenbogen Phosphorylation of the human estrogen receptor. Identification of hormone-regulated sites and examination of their influence on transcriptional activity J. Biol. Chem. 269 1994 4458 4466
    • (1994) J. Biol. Chem. , vol.269 , pp. 4458-4466
    • le Goff, P1    Montano, M.M2    Schodin, D.J3    Katzenellenbogen, B.S4
  • 107
    • 0028850007 scopus 로고
    • Phosphorylation of the human estrogen receptor by mitogen-activated protein kinase and casein kinase II: Consequence on DNA binding
    • S.F Arnold J.D Obourn H Jaffe A.C Notides Phosphorylation of the human estrogen receptor by mitogen-activated protein kinase and casein kinase II: Consequence on DNA binding J. Steroid Biochem. Mol. Biol. 55 1995 163 172
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.55 , pp. 163-172
    • Arnold, S.F1    Obourn, J.D2    Jaffe, H3    Notides, A.C4
  • 109
    • 0033120030 scopus 로고    scopus 로고
    • Ligand-independent recruitment of SRC-1 to estrogen receptor β through phosphorylation of activation function AF-1
    • A Tremblay G.B Tremblay F Labrie V Giguere Ligand-independent recruitment of SRC-1 to estrogen receptor β through phosphorylation of activation function AF-1 Mol. Cell 3 1999 513 519
    • (1999) Mol. Cell , vol.3 , pp. 513-519
    • Tremblay, A1    Tremblay, G.B2    Labrie, F3    Giguere, V4
  • 110
    • 0027978187 scopus 로고
    • Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor
    • S.F Arnold J.D Obourn H Jaffe A.C Notides Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor Mol. Endocrinol. 8 1994 1208 1214
    • (1994) Mol. Endocrinol. , vol.8 , pp. 1208-1214
    • Arnold, S.F1    Obourn, J.D2    Jaffe, H3    Notides, A.C4
  • 111
    • 0032906876 scopus 로고    scopus 로고
    • Phosphorylation of human estrogen receptor α by protein kinase A regulates dimerization
    • D Chen P.E Pace R.C Coombes S Ali Phosphorylation of human estrogen receptor α by protein kinase A regulates dimerization Mol. Cell Biol. 19 1999 1002 1015
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1002-1015
    • Chen, D1    Pace, P.E2    Coombes, R.C3    Ali, S4
  • 113
    • 0031017574 scopus 로고    scopus 로고
    • A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine
    • M-S Jiang G.W Hart A subpopulation of estrogen receptors are modified by O -linked N -acetylglucosamine J. Biol. Chem. 272 1997 2421 2428
    • (1997) J. Biol. Chem. , vol.272 , pp. 2421-2428
    • Jiang, M-S1    Hart, G.W2
  • 114
    • 0034671011 scopus 로고    scopus 로고
    • Glycosylation of the murine estrogen receptor-α
    • X Cheng G.W Hart Glycosylation of the murine estrogen receptor-α J. Steroid Biochem. Mol. Biol. 75 2000 147 158
    • (2000) J. Steroid Biochem. Mol. Biol. , vol.75 , pp. 147-158
    • Cheng, X1    Hart, G.W2
  • 115
    • 0026644374 scopus 로고
    • Estrogen receptor phosphorylation. Hormonal dependence and consequence on specific DNA binding
    • R.R Denton N.J Koszewski A.C Notides Estrogen receptor phosphorylation. Hormonal dependence and consequence on specific DNA binding J. Biol. Chem. 267 1992 7263 7268
    • (1992) J. Biol. Chem. , vol.267 , pp. 7263-7268
    • Denton, R.R1    Koszewski, N.J2    Notides, A.C3
  • 117
    • 0029877913 scopus 로고    scopus 로고
    • Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation
    • G Bunone P.A Briand R.J Miksicek D Picard Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation EMBO J. 15 1996 2174 2183
    • (1996) EMBO J. , vol.15 , pp. 2174-2183
    • Bunone, G1    Briand, P.A2    Miksicek, R.J3    Picard, D4
  • 119
    • 0030601135 scopus 로고    scopus 로고
    • Phosphorylation of purified estradiol-liganded estrogen receptor by casein kinase II increases estrogen responce element binding but does not alter ligand stability
    • D.Z Tzeng C.M Klinge Phosphorylation of purified estradiol-liganded estrogen receptor by casein kinase II increases estrogen responce element binding but does not alter ligand stability Biochem. Biophys. Res. Commun. 223 1996 554 560
    • (1996) Biochem. Biophys. Res. Commun. , vol.223 , pp. 554-560
    • Tzeng, D.Z1    Klinge, C.M2
  • 121
    • 0033060824 scopus 로고    scopus 로고
    • Implication of proteasome in estrogen receptor degradation
    • A.E Khissiin G Leclercq Implication of proteasome in estrogen receptor degradation FEBS Lett. 448 1999 160 166
    • (1999) FEBS Lett. , vol.448 , pp. 160-166
    • Khissiin, A.E1    Leclercq, G2
  • 122
    • 0029100143 scopus 로고
    • Ubiquitination of the rat uterine estrogen receptor: Dependence of estradiol
    • P.B Nirmala R.V Thampan Ubiquitination of the rat uterine estrogen receptor: Dependence of estradiol Biochem. Biophys. Res. Commun. 213 1995 24 31
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 24-31
    • Nirmala, P.B1    Thampan, R.V2
  • 123
    • 0037204724 scopus 로고    scopus 로고
    • Connections and regulation of the human estrogen receptor
    • D.P McDonnell J.D Norris Connections and regulation of the human estrogen receptor Science 296 2002 1642 1644
    • (2002) Science , vol.296 , pp. 1642-1644
    • McDonnell, D.P1    Norris, J.D2
  • 124
    • 0031462103 scopus 로고    scopus 로고
    • Transcriptional regulation by the Sp family proteins
    • L Lania B Majello P de Luca Transcriptional regulation by the Sp family proteins Int. J. Biochem. Cell Biol. 29 1997 1313 1323
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 1313-1323
    • Lania, L1    Majello, B2    de Luca, P3
  • 125
    • 0032459235 scopus 로고    scopus 로고
    • Cofactor requirements for transcriptional activation by Sp1
    • A.M Naar S Ryu R Tjian Cofactor requirements for transcriptional activation by Sp1 Cold Spring Harb. Symp. Quant. Biol. 63 1998 189 199
    • (1998) Cold Spring Harb. Symp. Quant. Biol. , vol.63 , pp. 189-199
    • Naar, A.M1    Ryu, S2    Tjian, R3
  • 126
    • 0003049247 scopus 로고    scopus 로고
    • Sp1 and its likes: Biochemical and functional predictions for a growing family of zinc finger transcription factors
    • T Cook B Gebelein R Urrutia Sp1 and its likes: Biochemical and functional predictions for a growing family of zinc finger transcription factors Ann. N.Y. Acad. Sci. 880 1999 94 102
    • (1999) Ann. N.Y. Acad. Sci. , vol.880 , pp. 94-102
    • Cook, T1    Gebelein, B2    Urrutia, R3
  • 127
    • 0024280897 scopus 로고
    • O-Glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulation
    • S.P Jackson R Tjian O -Glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulation Cell 55 1988 125 133
    • (1988) Cell , vol.55 , pp. 125-133
    • Jackson, S.P1    Tjian, R2
  • 128
    • 0030772457 scopus 로고    scopus 로고
    • O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions
    • M.D Roos K Su J.R Baker J.E Kudlow O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions Mol. Cell Biol. 17 1997 6472 6480
    • (1997) Mol. Cell Biol. , vol.17 , pp. 6472-6480
    • Roos, M.D1    Su, K2    Baker, J.R3    Kudlow, J.E4
  • 130
    • 0035811072 scopus 로고    scopus 로고
    • O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability
    • X Yang K Su M.D Roos Q Chang A.J Paterson J.E Kudlow O -linkage of N -acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability Proc. Natl. Acad. Sci. USA 98 2001 6611 6616
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6611-6616
    • Yang, X1    Su, K2    Roos, M.D3    Chang, Q4    Paterson, A.J5    Kudlow, J.E6
  • 131
    • 0025167314 scopus 로고
    • Overlapping Pit-1 and Sp1 binding sites are both essential to full rat growth hormone gene promoter activity despite mutually exclusive Pit-1 and Sp1 binding
    • F Schaufele B.L West T.L Reudelhuber Overlapping Pit-1 and Sp1 binding sites are both essential to full rat growth hormone gene promoter activity despite mutually exclusive Pit-1 and Sp1 binding J. Biol. Chem. 265 1990 17189 17196
    • (1990) J. Biol. Chem. , vol.265 , pp. 17189-17196
    • Schaufele, F1    West, B.L2    Reudelhuber, T.L3
  • 132
    • 0032488979 scopus 로고    scopus 로고
    • Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-β-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate
    • R.S Haltiwanger K Grove G.A Philipsberg Modulation of O -linked N -acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O -GlcNAc-β- 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.S1    Grove, K2    Philipsberg, G.A3
  • 133
    • 0034710891 scopus 로고    scopus 로고
    • Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation
    • X-L Du L Edelstein L Rossetti I.G Fantus H Goldberg F Ziyadeh J Wu M Brownlee Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation Proc. Natl. Acad. Sci. USA 97 2000 12222 12226
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12222-12226
    • Du, X-L1    Edelstein, L2    Rossetti, L3    Fantus, I.G4    Goldberg, H5    Ziyadeh, F6    Wu, J7    Brownlee, M8
  • 135
    • 0036141208 scopus 로고    scopus 로고
    • Hexosamines regulate leptin production in 3T3-L1 adipocytes through transcriptional mechanisms
    • P Zhang E.S Klenk M.A Lazzaro L.B Williams R.V Considine Hexosamines regulate leptin production in 3T3-L1 adipocytes through transcriptional mechanisms Endocrinology 143 2002 99 106
    • (2002) Endocrinology , vol.143 , pp. 99-106
    • Zhang, P1    Klenk, E.S2    Lazzaro, M.A3    Williams, L.B4    Considine, R.V5
  • 136
    • 0037088695 scopus 로고    scopus 로고
    • Sp1 transcriptional activity is up-regulated by phosphatase 2A in dividing T lymphocytes
    • I Lacroix C Lipcey J Imbert B Kahn-Perles Sp1 transcriptional activity is up-regulated by phosphatase 2A in dividing T lymphocytes J. Biol. Chem. 277 2002 9598 9605
    • (2002) J. Biol. Chem. , vol.277 , pp. 9598-9605
    • Lacroix, I1    Lipcey, C2    Imbert, J3    Kahn-Perles, B4
  • 137
    • 0025037502 scopus 로고
    • GC box binding induces phosphorylation of Sp1 by a DNA-dependent protein kinase
    • S.P Jackson J.J MacDonald S Lees-Miller R Tjian GC box binding induces phosphorylation of Sp1 by a DNA-dependent protein kinase Cell 63 1990 155 165
    • (1990) Cell , vol.63 , pp. 155-165
    • Jackson, S.P1    MacDonald, J.J2    Lees-Miller, S3    Tjian, R4
  • 138
    • 0030973394 scopus 로고    scopus 로고
    • Casein kinase II-mediated phosphorylation of the C terminus of Sp1 decreases its DNA binding activity
    • S.A Armstrong D.A Barry R.W Leggett C.R Mueller Casein kinase II-mediated phosphorylation of the C terminus of Sp1 decreases its DNA binding activity J. Biol. Chem. 272 1997 13489 13495
    • (1997) J. Biol. Chem. , vol.272 , pp. 13489-13495
    • Armstrong, S.A1    Barry, D.A2    Leggett, R.W3    Mueller, C.R4
  • 139
    • 0030771433 scopus 로고    scopus 로고
    • Modulation of transcription factor Sp1 by cAMP-dependent protein kinase
    • C Rohlff S Ahmad F Borellini J Lei R.I Glazer Modulation of transcription factor Sp1 by cAMP-dependent protein kinase J. Biol. Chem. 272 1997 21137 21141
    • (1997) J. Biol. Chem. , vol.272 , pp. 21137-21141
    • Rohlff, C1    Ahmad, S2    Borellini, F3    Lei, J4    Glazer, R.I5
  • 140
    • 0032500637 scopus 로고    scopus 로고
    • Activation of Sp1-mediated vascular permeability factor⧸vascular endothelial growth factor transcription requires specific interaction with protein kinase C zeta
    • S Pal K.P Claffey H.T Cohen D Mukhopadhyay Activation of Sp1-mediated vascular permeability factor⧸vascular endothelial growth factor transcription requires specific interaction with protein kinase C zeta J. Biol. Chem. 273 1998 26277 26280
    • (1998) J. Biol. Chem. , vol.273 , pp. 26277-26280
    • Pal, S1    Claffey, K.P2    Cohen, H.T3    Mukhopadhyay, D4
  • 141
    • 0033555521 scopus 로고    scopus 로고
    • Growth⧸cell cycle regulation of Sp1 phosphorylation
    • A.R Black D Jensen S-Y Lin J.C Azizkhan Growth⧸cell cycle regulation of Sp1 phosphorylation J. Biol. Chem. 274 1999 1207 1215
    • (1999) J. Biol. Chem. , vol.274 , pp. 1207-1215
    • Black, A.R1    Jensen, D2    Lin, S-Y3    Azizkhan, J.C4
  • 142
    • 0035887030 scopus 로고    scopus 로고
    • Cyclin A-CDK phosphorylates Sp1 and enhances Sp1-mediated transcription
    • P.F de Borja N.K Collins P Du J Azizkhan-Clifford M Mudryj Cyclin A-CDK phosphorylates Sp1 and enhances Sp1-mediated transcription EMBO J. 20 2001 5737 5747
    • (2001) EMBO J. , vol.20 , pp. 5737-5747
    • de Borja, P.F1    Collins, N.K2    Du, P3    Azizkhan-Clifford, J4    Mudryj, M5
  • 143
    • 0037036451 scopus 로고    scopus 로고
    • Identification of two Sp1 phosphorylation sites for p42⧸p44 mitogen-activated protein kinases
    • J Milianini-Mongiat J Pouyssegur G Pages Identification of two Sp1 phosphorylation sites for p42⧸p44 mitogen-activated protein kinases J. Biol. Chem. 277 2002 20631 20639
    • (2002) J. Biol. Chem. , vol.277 , pp. 20631-20639
    • Milianini-Mongiat, J1    Pouyssegur, J2    Pages, G3
  • 144
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin-carbohydrate recognition
    • W.I Weis K Drickamer Structural basis of lectin-carbohydrate recognition Annu. Rev. Biochem. 65 1996 441 473
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 441-473
    • Weis, W.I1    Drickamer, K2
  • 145
    • 0024290265 scopus 로고
    • Distinct regions of Sp1 modulate DNA binding and transcriptional activation
    • J.T Kadonaga A.J Courey J Ladika R Tjian Distinct regions of Sp1 modulate DNA binding and transcriptional activation Science 242 1988 1566 1570
    • (1988) Science , vol.242 , pp. 1566-1570
    • Kadonaga, J.T1    Courey, A.J2    Ladika, J3    Tjian, R4
  • 146
    • 0037067659 scopus 로고    scopus 로고
    • Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: Coupling protein O-GlcNAcylation to transcriptional repression
    • X Yang F Zhang J.E Kudlow Recruitment of O -GlcNAc transferase to promoters by corepressor mSin3A: Coupling protein O -GlcNAcylation to transcriptional repression Cell 110 2002 69 80
    • (2002) Cell , vol.110 , pp. 69-80
    • Yang, X1    Zhang, F2    Kudlow, J.E3
  • 147
    • 0034644780 scopus 로고    scopus 로고
    • Glucose regulation of gene transcription
    • S Vaulont M Vasseur-Cognet A Kahn Glucose regulation of gene transcription J. Biol. Chem. 275 2000 31555 31558
    • (2000) J. Biol. Chem. , vol.275 , pp. 31555-31558
    • Vaulont, S1    Vasseur-Cognet, M2    Kahn, A3
  • 148
    • 0030061116 scopus 로고    scopus 로고
    • Sp1 mediates glucose activation of the acetyl-CoA carboxylase promoter
    • S Daniel K-H Kim Sp1 mediates glucose activation of the acetyl-CoA carboxylase promoter J. Biol. Chem. 271 1996 1385 1392
    • (1996) J. Biol. Chem. , vol.271 , pp. 1385-1392
    • Daniel, S1    Kim, K-H2
  • 149
    • 17544379257 scopus 로고    scopus 로고
    • Glucose metabolism to glucosamine is necessary for glucose stimulation of transforming growth factor-α gene transcription
    • P.P Sayeski J.E Kudlow Glucose metabolism to glucosamine is necessary for glucose stimulation of transforming growth factor-α gene transcription J. Biol. Chem. 271 1996 15237 15243
    • (1996) J. Biol. Chem. , vol.271 , pp. 15237-15243
    • Sayeski, P.P1    Kudlow, J.E2
  • 150
    • 0032478827 scopus 로고    scopus 로고
    • Sp1 sites mediate activation of the plasminogen activator inhibitor-1 promoter by glucose in vascular smooth muscle cells
    • Y-Q Chen M Su R.R Walia Q Hao J.W Covington D.E Vaughan Sp1 sites mediate activation of the plasminogen activator inhibitor-1 promoter by glucose in vascular smooth muscle cells J. Biol. Chem. 273 1998 8225 8231
    • (1998) J. Biol. Chem. , vol.273 , pp. 8225-8231
    • Chen, Y-Q1    Su, M2    Walia, R.R3    Hao, Q4    Covington, J.W5    Vaughan, D.E6
  • 152
    • 0036231781 scopus 로고    scopus 로고
    • Flux through the hexosamine pathway is a determinant of nuclear factor κB-dependent promoter activation
    • L.R James D Tang A Ingram H Ly K Thai L Cai J.W Scholey Flux through the hexosamine pathway is a determinant of nuclear factor κB-dependent promoter activation Diabetes 51 2002 1146 1156
    • (2002) Diabetes , vol.51 , pp. 1146-1156
    • James, L.R1    Tang, D2    Ingram, A3    Ly, H4    Thai, K5    Cai, L6    Scholey, J.W7
  • 153
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • M Brownlee Biochemistry and molecular cell biology of diabetic complications Nature 414 2001 813 820
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M1
  • 154
    • 0032520153 scopus 로고    scopus 로고
    • Direct evidence for the importance of endothelium-derived nitric oxide in vascular remodeling
    • R.D Rudic E.G Shesely N Maeda O Smithies S.S Segal W.C Sessa Direct evidence for the importance of endothelium-derived nitric oxide in vascular remodeling J. Clin. Invest. 101 1998 731 736
    • (1998) J. Clin. Invest. , vol.101 , pp. 731-736
    • Rudic, R.D1    Shesely, E.G2    Maeda, N3    Smithies, O4    Segal, S.S5    Sessa, W.C6
  • 157
    • 0033542476 scopus 로고    scopus 로고
    • Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
    • S Dimmeler I Fleming B Fisslthaler C Hermann R Busse A.M Zeiher Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation Nature 399 1999 601 605
    • (1999) Nature , vol.399 , pp. 601-605
    • Dimmeler, S1    Fleming, I2    Fisslthaler, B3    Hermann, C4    Busse, R5    Zeiher, A.M6
  • 158
    • 0037162342 scopus 로고    scopus 로고
    • Insulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endothelial cells
    • M Federici R Menghini A Mauriello M.L Hribal F Ferrelli D Lauro P Sbraccia L.G Spagnoli G Sesti R Lauro Insulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endothelial cells Circulation 106 2002 466 472
    • (2002) Circulation , vol.106 , pp. 466-472
    • Federici, M1    Menghini, R2    Mauriello, A3    Hribal, M.L4    Ferrelli, F5    Lauro, D6    Sbraccia, P7    Spagnoli, L.G8    Sesti, G9    Lauro, R10
  • 159
  • 160
    • 0035797897 scopus 로고    scopus 로고
    • Adhesion signaling: How β-catenin interacts with its partners
    • C.J Gottardi B.M Gumbiner Adhesion signaling: How β-catenin interacts with its partners Curr. Biol. 11 2001 R792 R794
    • (2001) Curr. Biol. , vol.11 , pp. R792-R794
    • Gottardi, C.J1    Gumbiner, B.M2
  • 161
    • 0036270763 scopus 로고    scopus 로고
    • The subcellular destinations of APC proteins
    • M Bienz The subcellular destinations of APC proteins Nat. Rev. Mol. Cell Biol. 3 2002 328 338
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 328-338
    • Bienz, M1
  • 162
    • 0028266975 scopus 로고
    • A repeating amino acid motif shared by proteins with diverse cellular roles
    • M Peifer S Berg A.B Reynolds A repeating amino acid motif shared by proteins with diverse cellular roles Cell 76 1994 789 791
    • (1994) Cell , vol.76 , pp. 789-791
    • Peifer, M1    Berg, S2    Reynolds, A.B3
  • 163
    • 0033695362 scopus 로고    scopus 로고
    • Structure of the dimerization and β-catenin-binding region of α-catenin
    • S Pokutta W.I Weis Structure of the dimerization and β-catenin-binding region of α-catenin Mol. Cell 5 2000 533 543
    • (2000) Mol. Cell , vol.5 , pp. 533-543
    • Pokutta, S1    Weis, W.I2
  • 164
    • 0029915306 scopus 로고    scopus 로고
    • Binding to cadherins antagonizes the signaling activity of β-catenin during axis formation in Xenopus
    • F Fagotto N Funayama U Gluck B Gumbiner Binding to cadherins antagonizes the signaling activity of β-catenin during axis formation in Xenopus J. Cell Biol. 132 1996 1105 1114
    • (1996) J. Cell Biol. , vol.132 , pp. 1105-1114
    • Fagotto, F1    Funayama, N2    Gluck, U3    Gumbiner, B4
  • 165
    • 0037205007 scopus 로고    scopus 로고
    • The promise and perils of Wnt signaling through β-catenin
    • R.T Moon B Bowerman M Boutros N Perrimon The promise and perils of Wnt signaling through β-catenin Science 296 2002 1644 1646
    • (2002) Science , vol.296 , pp. 1644-1646
    • Moon, R.T1    Bowerman, B2    Boutros, M3    Perrimon, N4
  • 166
    • 0036224633 scopus 로고    scopus 로고
    • Signal transduction in development: Holding the key
    • A.J Harwood Signal transduction in development: Holding the key Dev. Cell 2 2002 384 385
    • (2002) Dev. Cell , vol.2 , pp. 384-385
    • Harwood, A.J1
  • 167
    • 0035503219 scopus 로고    scopus 로고
    • Cytoplasmic O-glycosylation prevents cell surface transport of E-cadherin during apoptosis
    • W Zhu B Leber D.W Andrews Cytoplasmic O -glycosylation prevents cell surface transport of E-cadherin during apoptosis EMBO J. 20 2001 5999 6007
    • (2001) EMBO J. , vol.20 , pp. 5999-6007
    • Zhu, W1    Leber, B2    Andrews, D.W3
  • 168
    • 0037117511 scopus 로고    scopus 로고
    • Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes
    • K Vosseller L Wells M.D Lane G.W Hart Elevated nucleocytoplasmic glycosylation by O -GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes Proc. Natl. Acad. Sci. USA 99 2002 5313 5318
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5313-5318
    • Vosseller, K1    Wells, L2    Lane, M.D3    Hart, G.W4
  • 169
    • 0011961115 scopus 로고    scopus 로고
    • A role for O-GlcNAc as a nutrient sensor and mediator of insulin resistance
    • L Wells K Vosseller G.W Hart A role for O -GlcNAc as a nutrient sensor and mediator of insulin resistance Cell. Mol. Life Sci. 60 2003 1 7
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1-7
    • Wells, L1    Vosseller, K2    Hart, G.W3
  • 170
    • 0035843148 scopus 로고    scopus 로고
    • Insulin and IGF-1 stimulate the β-catenin pathway through two signaling cascades involving GSK-3β inhibition and Ras activation
    • C Desbois-Mouthon A Cadoret M-J.B-V Eggelpoel F Bertrand G Cherqui C Perret J Capeau Insulin and IGF-1 stimulate the β-catenin pathway through two signaling cascades involving GSK-3β inhibition and Ras activation Oncogene 20 2001 252 259
    • (2001) Oncogene , vol.20 , pp. 252-259
    • Desbois-Mouthon, C1    Cadoret, A2    Eggelpoel, M-J.B-V3    Bertrand, F4    Cherqui, G5    Perret, C6    Capeau, J7
  • 171
    • 0036120562 scopus 로고    scopus 로고
    • The cadherin-catenin adhesion system in signaling and cancer
    • M Conacci-Sorrell J Zhurinsky A Ben-Ze'ev The cadherin-catenin adhesion system in signaling and cancer J. Clin. Invest. 109 2002 987 991
    • (2002) J. Clin. Invest. , vol.109 , pp. 987-991
    • Conacci-Sorrell, M1    Zhurinsky, J2    Ben-Ze'ev, A3
  • 173
    • 0034705030 scopus 로고    scopus 로고
    • The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny
    • S Shafi S.P.N Iyer L.G Ellies N O'Donnell K.W Marek D Chui G.W Hart J.D Marth The O -GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny Proc. Natl. Acad. Sci. USA 97 2000 5735 5739
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5735-5739
    • Shafi, S1    Iyer, S.P.N2    Ellies, L.G3    O'Donnell, N4    Marek, K.W5    Chui, D6    Hart, G.W7    Marth, J.D8
  • 174
    • 0036021405 scopus 로고    scopus 로고
    • Two O-linked N-acetylglucosamine transferase genes of Arabidopsis thaliana L. Heynh have overlapping functions necessary for gamete and seed development
    • L.M Hartweck C.L Scott N.E Olszewski Two O -linked N -acetylglucosamine transferase genes of Arabidopsis thaliana L. Heynh have overlapping functions necessary for gamete and seed development Genetics 161 2002 1279 1291
    • (2002) Genetics , vol.161 , pp. 1279-1291
    • Hartweck, L.M1    Scott, C.L2    Olszewski, N.E3
  • 175
    • 0033853832 scopus 로고    scopus 로고
    • Distribution of O-GlcNAc transferase in the rat pancreas
    • Y Akimoto G.W Hart H Hirano Distribution of O -GlcNAc transferase in the rat pancreas Acta Histochem. Cytochem. 33 2000 163 167
    • (2000) Acta Histochem. Cytochem. , vol.33 , pp. 163-167
    • Akimoto, Y1    Hart, G.W2    Hirano, H3
  • 176
    • 0035872340 scopus 로고    scopus 로고
    • Hyperglycemia and the O-GlcNAc transferase in rat aortic smooth muscle cells: Elevated expression and altered patterns of O-GlcNAcylation
    • Y Akimoto L.K Kreppel H Hirano G.W Hart Hyperglycemia and the O -GlcNAc transferase in rat aortic smooth muscle cells: Elevated expression and altered patterns of O -GlcNAcylation Arch. Biochem. Biophys. 389 2001 166 175
    • (2001) Arch. Biochem. Biophys. , vol.389 , pp. 166-175
    • Akimoto, Y1    Kreppel, L.K2    Hirano, H3    Hart, G.W4
  • 177
    • 0003457299 scopus 로고    scopus 로고
    • O-GlcNAc transferase
    • S.P.N Iyer G.W Hart O -GlcNAc transferase N Taniguchi K Honke M Fukuda 2000 Springer-Verlag Tokyo 158 163 Chap. 21
    • (2000) , pp. 158-163
    • Iyer, S.P.N1    Hart, G.W2
  • 178
    • 0037127198 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolc proteins. Further characterization of the nucleocytoplasmic β-N-acetylglucosaminidase, O-GlcNAcase
    • L Wells Y Gao J.A Mahoney K Vosseller C Chen A Rosen G.W Hart Dynamic O -glycosylation of nuclear and cytosolc proteins. Further characterization of the nucleocytoplasmic β- N -acetylglucosaminidase, O -GlcNAcase J. Biol. Chem. 277 2002 1755 1761
    • (2002) J. Biol. Chem. , vol.277 , pp. 1755-1761
    • Wells, L1    Gao, Y2    Mahoney, J.A3    Vosseller, K4    Chen, C5    Rosen, A6    Hart, G.W7
  • 179
    • 0041906482 scopus 로고    scopus 로고
    • Detection and analysis of proteins modified by O-linked N-acetylglucosamine
    • N.E Zachara R.N Cole G.W Hart Y Gao Detection and analysis of proteins modified by O -linked N -acetylglucosamine J.E Coligan B.M Dunn H.L Ploegh D.W Speicher P.T Wingfield “Current Protocols in Protein Science” Suppl. 25 2001 John Wiley & Sons, Inc New York 12.8.1 12.8.25
    • (2001) , pp. 12.8.1-12.8.25
    • Zachara, N.E1    Cole, R.N2    Hart, G.W3    Gao, Y4
  • 180
    • 0030025149 scopus 로고    scopus 로고
    • Selective detection and site-analysis of O-GlcNAc-modified glycopeptides by β-elimination and tandem electrospray mass spectrometry
    • K.D Greis B.K Hayes F.I Comer M Kirk S Barnes T.L Lowary G.W Hart Selective detection and site-analysis of O -GlcNAc-modified glycopeptides by β-elimination and tandem electrospray mass spectrometry Anal. Biochem. 234 1996 38 49
    • (1996) Anal. Biochem. , vol.234 , pp. 38-49
    • Greis, K.D1    Hayes, B.K2    Comer, F.I3    Kirk, M4    Barnes, S5    Lowary, T.L6    Hart, G.W7
  • 181
    • 85120218487 scopus 로고    scopus 로고
    • Haynes, P. A. and Aebersold, R. (2000) Simultaneous detection and identification of O -GlcNAc-modified glycoproteins using liquid chromatography-tandem mass spectrometry. Anal. Chem. 72, 5402–541
  • 182
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications
    • L Wells K Vosseller R.N Cole J Cross M.J Matunis G.W Hart Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications Mol. Cell. Proteomics 1 2002 791 804
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 791-804
    • Wells, L1    Vosseller, K2    Cole, R.N3    Cross, J4    Matunis, M.J5    Hart, G.W6
  • 183
    • 0034851055 scopus 로고    scopus 로고
    • Nucleocytoplasmic O-glycosylation: O-GlcNAc and functional proteomics
    • K Vosseller L Wells G.W Hart Nucleocytoplasmic O -glycosylation: O -GlcNAc and functional proteomics Biochimie 83 2001 575 581
    • (2001) Biochimie , vol.83 , pp. 575-581
    • Vosseller, K1    Wells, L2    Hart, G.W3
  • 184
    • 0035876021 scopus 로고    scopus 로고
    • Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine
    • F.I Comer K Vosseller L Wells M.A Accavitti G.W Hart Characterization of a mouse monoclonal antibody specific for O -linked N -acetylglucosamine Anal. Biochem. 293 2001 169 177
    • (2001) Anal. Biochem. , vol.293 , pp. 169-177
    • Comer, F.I1    Vosseller, K2    Wells, L3    Accavitti, M.A4    Hart, G.W5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.