10.1016/s0304-4165(99)00176-2
Crossref journal-article
Elsevier BV
Biochimica et Biophysica Acta (BBA) - General Subjects (78)
Bibliography

Comer, F. I., & Hart, G. W. (1999). O-GlcNAc and the control of gene expression. Biochimica et Biophysica Acta (BBA) - General Subjects, 1473(1), 161–171.

Authors 2
  1. Frank I Comer (first)
  2. Gerald W Hart (additional)
References 56 Referenced 144
  1. 10.1016/S0021-9258(17)43295-9 / J. Biol. Chem. / Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes by Torres (1984)
  2. 10.1146/annurev.biochem.66.1.315 / Annu. Rev. Biochem. / Dynamic O-glycosylation of nuclear and cytoskeletal proteins by Hart (1997)
  3. L.K. Kreppel and G.W. Hart, Functional Significance of O-GlcNAc glycoproteins in the nucleus and cytoplasm, in: M. Fukuda and O. Hindsgaul (Eds.), Molecular and Cellular Glycobiology: Frontiers in Molecular Biology. Oxford University Press, Oxford (submitted).
  4. 10.1016/S0074-7696(08)60416-7 / Int. Rev. Cytol. / Nuclear and cytoplasmic glycosylation by Snow (1998)
  5. 10.1016/S0021-9258(18)82216-5 / J. Biol. Chem. / RNA polymerase II is a glycoprotein: modification of the C-terminal domain by O-GlcNAc by Kelly (1993)
  6. 10.1006/excr.1994.1054 / Exp. Cell. Res. / Expression, glycosylation, and phosphorylation of human keratins 8 18 in insect cells by Ku (1994)
  7. 10.1074/jbc.270.32.18961 / J. Biol. Chem. / c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas by Chou (1995)
  8. 10.1016/S0021-9258(19)50380-5 / J. Biol. Chem. / Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosaminepolypeptide β-N-acetylglucosaminyltransferase by Haltiwanger (1992)
  9. {'key': '10.1016/S0304-4165(99)00176-2_BIB9', 'first-page': 'A1120', 'article-title': 'Cloning and characterization of O-GlcNAc transferase: A novel highly conserved enzyme', 'volume': '10', 'author': 'Kreppel', 'year': '1996', 'journal-title': 'FASEB J.'} / FASEB J. / Cloning and characterization of O-GlcNAc transferase: A novel highly conserved enzyme by Kreppel (1996)
  10. 10.1074/jbc.272.14.9316 / J. Biol. Chem. / O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats by Lubas (1997)
  11. 10.1016/S0021-9258(17)32170-1 / J. Biol. Chem. / Purification and characterization of an O-GlcNAc selective N-acetyl-β-D-glucosaminidase from rat spleen cytosol by Dong (1994)
  12. 10.1073/pnas.88.5.1701 / Proc. Natl. Acad. Sci. USA / Lymphocyte activation induces rapid changes in nuclear and cytoplasmic glycoproteins by Kearse (1991)
  13. 10.1016/0092-8674(89)90962-8 / Cell / Glycosylation of chromosomal proteins: localization of O-linked N-acetylglucosamine in Drosophila chromatin by Kelly (1989)
  14. W.G. Kelly and G.W. Hart, Carbohydrate modification of chromosomal proteins: Evidence for O-GlcNAc addition, J. Cell. Biol., 1988 (in press).
  15. 10.1016/S0959-437X(98)80138-X / Curr. Opin. Genet. Dev. / Covalent modifications of histones: expression from chromatin templates by Davie (1998)
  16. 10.1016/S0092-8674(00)80924-1 / Cell / Eukaryotic transcription: an interlaced network of transcription factors and chromatin-modifying machines by Kadonaga (1998)
  17. 10.1016/0092-8674(88)90015-3 / Cell / O-Glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulation by Jackson (1988)
  18. 10.1128/MCB.17.5.2550 / Mol. Cell. Biol. / Reduced O glycosylation of Sp1 is associated with increased proteasome suseptibility by Han (1997)
  19. 10.1128/MCB.17.11.6472 / Mol. Cell. Biol. / O Glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions by Roos (1997)
  20. 10.1016/S0021-9258(17)44887-3 / J. Biol. Chem. / 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 by Schaufele (1990)
  21. 10.1146/annurev.bi.61.070192.000415 / Annu. Rev. Biochem. / Structure and function of simian virus 40 large tumor antigen by Fanning (1992)
  22. 10.1016/0006-291X(79)91492-X / Biochem. Biophys. Res. Commun. / Biochemical and immunochemical characterization of two simian virus 40 (SV40)-specific glycoproteins in nuclear and surface membranes of SV40-transformed cells by Schmidt-Ullrich (1979)
  23. 10.1093/glycob/8.4.383 / Glycobiology / SV40 large T antigen is modified with O-linked N-acetylglucosamine but not with other forms of glycosylation by Medina (1998)
  24. 10.1126/science.3499668 / Science / Interaction of a liver-specific nuclear factor with the fibrinogen and α 1-antitrypsin promoters by Courtois (1987)
  25. 10.1016/0092-8674(89)90055-X / Cell / A glycosylated liver-specific transcription factor stimulates transcription of the albumin gene by Lichtsteiner (1989)
  26. 10.1126/science.8023155 / Science / p53: a glimpse at the puppet behind the shadow play by Friend (1994)
  27. {'key': '10.1016/S0304-4165(99)00176-2_BIB27', 'first-page': '921', 'article-title': 'Regulation of specific DNA binding by p53: evidence for a role for O-glycosylation and charged residues at the carboxy-terminus', 'volume': '12', 'author': 'Shaw', 'year': '1996', 'journal-title': 'Oncogene'} / Oncogene / Regulation of specific DNA binding by p53: evidence for a role for O-glycosylation and charged residues at the carboxy-terminus by Shaw (1996)
  28. 10.1073/pnas.92.10.4417 / Proc. Natl. Acad. Sci. USA / Glycosylation of the C-Myc transactivation domain by Chou (1995)
  29. 10.1038/359423a0 / Nature / Transcriptional activation by the human c-Myc oncoprotein in yeast requires interaction with Max by Amati (1992)
  30. 10.1128/MCB.15.8.4031 / Mol. Cell. Biol. / A link between increased transforming activity of lymphoma-derived MYC mutant allels, their defective regulation by p107, and altered phophorylation of the c-Myc transactivation domain by Hoang (1995)
  31. 10.1128/jvi.64.1.463-466.1990 / J. Virol. / A subpopulation of the avian erythroblastosis virus v-erbA protein, a member of the nuclear hormone receptor family, is glycosylated by Privalsky (1990)
  32. 10.1074/jbc.273.18.10926 / J. Biol. Chem. / Phosphorylation of thyroid hormone receptors by protein kinase A regulates DNA recognition by specific inhibition of receptor monomer binding by Tzagarakis-Foster (1998)
  33. 10.1016/S0021-9258(18)41871-6 / J. Biol. Chem. / Localization of O-GlcNAc modification on the serum response transcription factor by Reason (1992)
  34. 10.1016/0968-0004(92)90013-Y / Trends Biochem. Sci. / The serum response element by Treisman (1992)
  35. 10.1074/jbc.272.4.2421 / J. Biol. Chem. / A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine by Jiang (1997)
  36. 10.1016/S0968-0004(96)10031-1 / Trends Biochem. Sci. / PEST sequences and regulation by proteolysis by Rechsteiner (1996)
  37. 10.1128/MMBR.62.2.465-503.1998 / Microbiol. Mol. Biol. Rev. / Molecular genetics of the RNA polymerase II general transcriptional machinery by Hampsey (1998)
  38. 10.1016/0167-4781(94)00233-S / Biochim. Biophys. Acta / Phosphorylation of the C-terminal domain of RNA polymerase II by Dahmus (1995)
  39. 10.1016/0968-0004(90)90236-5 / Trends Biochem. Sci. / Tails of RNA polymerase II by Corden (1990)
  40. {'key': '10.1016/S0304-4165(99)00176-2_BIB40', 'first-page': '27', 'article-title': 'The RNA polymerase II general elongation complex', 'volume': '379', 'author': 'Shilatifard', 'year': '1998', 'journal-title': 'Biol. Chem.'} / Biol. Chem. / The RNA polymerase II general elongation complex by Shilatifard (1998)
  41. 10.1016/S0092-8674(00)80230-5 / Cell / Pre-mRNA processing and the CTD of RNA polymerase II: the tail that wags the dog? by Steinmetz (1997)
  42. 10.1016/S0021-9258(19)57510-X / J. Biol. Chem. / The subcellular distribution of terminal N-acetylglucosamine moieties: localization of a novel protein-saccharide linkage O-linked GlcNAc by Holt (1986)
  43. 10.1083/jcb.104.5.1157 / J. Cell. Biol. / Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine by Holt (1987)
  44. 10.1096/fasebj.6.6.1312045 / FASEB J. / The nuclear pore: at the crossroads by Hanover (1992)
  45. 10.1083/jcb.104.2.189 / J. Cell. Biol. / Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores by Finlay (1987)
  46. 10.1016/0092-8674(90)90712-N / Cell / Reconstitution of biochemically altered nuclear pores: transport can be eliminated and restored by Finlay (1990)
  47. 10.1083/jcb.107.4.1289 / J. Cell. Biol. / A monoclonal antibody against the nuclear pore complex inhibits nucleocytoplasmic transport of protein and RNA in vivo by Featherstone (1988)
  48. 10.1016/0962-8924(91)90065-H / Trends Cell Biol. / Pathways for the nuclear transport of proteins and RNA’s by Goldfarb (1991)
  49. 10.1111/j.1432-1033.1996.00747.x / Eur. J. Biochem. / Initiation of protein synthesis in eukaryotic cells by Pain (1996)
  50. {'key': '10.1016/S0304-4165(99)00176-2_BIB50', 'first-page': '239', 'article-title': 'Mammalian peptide chain initiation: thirty years of research', 'volume': '33', 'author': 'Gupta', 'year': '1996', 'journal-title': 'Int. J. Biochem. Biophys.'} / Int. J. Biochem. Biophys. / Mammalian peptide chain initiation: thirty years of research by Gupta (1996)
  51. 10.1073/pnas.85.10.3324 / Proc. Natl. Acad. Sci. USA / Roles of a 67-kDa polypeptide in reversal of protein synthesis inhibition in heme-deficient reticulocyte lysate by Datta (1988)
  52. 10.1016/S0021-9258(19)47108-1 / J. Biol. Chem. / Glycosylation of eukaryotic peptide chain initiation factor 2 (eIF-2)-associated 67-kDa polypeptide (p67) and its possible role in the inhibition of eIF-2 kinase-catalyzed phosphorylation of the eIF-2 α-subunit by Datta (1989)
  53. 10.1073/pnas.89.2.539 / Proc. Natl. Acad. Sci. USA / The eukaryotic initiation factor 2-associated 67-kDa polypeptide (p67) plays a critical role in regulation of protein synthesis initiation in animal cells by Ray (1992)
  54. 10.1021/bi00187a041 / Biochemistry / Regulation of eIF-2 α-subunit phosphorylation in reticulocyte lysate by Chakraborty (1994)
  55. 10.1073/pnas.96.1.2 / Proc. Natl. Acad. Sci. USA / Transcriptional regulation: Contending with complexity by Holstege (1999)
  56. 10.1006/abio.1996.0047 / Anal. Biochem. / Selective detection and site-analysis of O-GlcNAc-modified glycopeptides by β-elimination and tandem electrospray mass spectrometry by Greis (1996)
Dates
Type When
Created 23 years, 1 month ago (July 26, 2002, 12:30 a.m.)
Deposited 2 years, 8 months ago (Dec. 23, 2022, 1:48 p.m.)
Indexed 4 weeks, 2 days ago (Aug. 2, 2025, 12:32 a.m.)
Issued 25 years, 9 months ago (Dec. 1, 1999)
Published 25 years, 9 months ago (Dec. 1, 1999)
Published Print 25 years, 9 months ago (Dec. 1, 1999)
Funders 0

None

@article{Comer_1999, title={O-GlcNAc and the control of gene expression}, volume={1473}, ISSN={0304-4165}, url={http://dx.doi.org/10.1016/s0304-4165(99)00176-2}, DOI={10.1016/s0304-4165(99)00176-2}, number={1}, journal={Biochimica et Biophysica Acta (BBA) - General Subjects}, publisher={Elsevier BV}, author={Comer, Frank I and Hart, Gerald W}, year={1999}, month=dec, pages={161–171} }