Year |
Citation |
Score |
2010 |
Rogler CE, Dahmus ME. Gibberellic Acid-induced Phase Change in Hedera helix as Studied by Deoxyribonucleic Acid-Ribonucleic Acid Hybridization. Plant Physiology. 54: 88-94. PMID 16658844 DOI: 10.1104/pp.54.1.88 |
0.412 |
|
2004 |
Tremeau-Bravard A, Riedl T, Egly JM, Dahmus ME. Fate of RNA polymerase II stalled at a cisplatin lesion. The Journal of Biological Chemistry. 279: 7751-9. PMID 14672951 DOI: 10.1074/Jbc.M309853200 |
0.617 |
|
2004 |
Palancade B, Marshall NF, Tremeau-Bravard A, Bensaude O, Dahmus ME, Dubois MF. Dephosphorylation of RNA polymerase II by CTD-phosphatase FCP1 is inhibited by phospho-CTD associating proteins. Journal of Molecular Biology. 335: 415-24. PMID 14672652 DOI: 10.1016/J.Jmb.2003.10.036 |
0.736 |
|
2003 |
Lin PS, Dahmus ME. Dephosphorylation of the carboxyl-terminal domain of RNA polymerase II. Methods in Enzymology. 370: 155-65. PMID 14712641 DOI: 10.1016/S0076-6879(03)70013-5 |
0.789 |
|
2003 |
Lin PS, Tremeau-Bravard A, Dahmus ME. The repetitive C-terminal domain of RNA polymerase II: multiple conformational states drive the transcription cycle. Chemical Record (New York, N.Y.). 3: 235-45. PMID 14595832 DOI: 10.1002/Tcr.10063 |
0.777 |
|
2003 |
Yeo M, Lin PS, Dahmus ME, Gill GN. A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5. The Journal of Biological Chemistry. 278: 26078-85. PMID 12721286 DOI: 10.1074/Jbc.M301791200 |
0.782 |
|
2003 |
Liu YV, Clark DJ, Tchernajenko V, Dahmus ME, Studitsky VM. Role of C-terminal domain phosphorylation in RNA polymerase II transcription through the nucleosome. Biopolymers. 68: 528-38. PMID 12666177 DOI: 10.1002/Bip.10302 |
0.688 |
|
2002 |
Lin PS, Dubois MF, Dahmus ME. TFIIF-associating carboxyl-terminal domain phosphatase dephosphorylates phosphoserines 2 and 5 of RNA polymerase II. The Journal of Biological Chemistry. 277: 45949-56. PMID 12351650 DOI: 10.1074/Jbc.M208588200 |
0.782 |
|
2002 |
Lin PS, Marshall NF, Dahmus ME. CTD phosphatase: role in RNA polymerase II cycling and the regulation of transcript elongation. Progress in Nucleic Acid Research and Molecular Biology. 72: 333-65. PMID 12206456 DOI: 10.1016/S0079-6603(02)72074-6 |
0.789 |
|
2002 |
Hawkes NA, Otero G, Winkler GS, Marshall N, Dahmus ME, Krappmann D, Scheidereit C, Thomas CL, Schiavo G, Erdjument-Bromage H, Tempst P, Svejstrup JQ. Purification and characterization of the human elongator complex. The Journal of Biological Chemistry. 277: 3047-52. PMID 11714725 DOI: 10.1074/Jbc.M110445200 |
0.365 |
|
2001 |
Palancade B, Dubois MF, Dahmus ME, Bensaude O. Transcription-independent RNA polymerase II dephosphorylation by the FCP1 carboxy-terminal domain phosphatase in Xenopus laevis early embryos. Molecular and Cellular Biology. 21: 6359-68. PMID 11533226 DOI: 10.1128/Mcb.21.19.6359-6368.2001 |
0.719 |
|
2000 |
Marshall NF, Dahmus ME. C-terminal domain phosphatase sensitivity of RNA polymerase II in early elongation complexes on the HIV-1 and adenovirus 2 major late templates. The Journal of Biological Chemistry. 275: 32430-7. PMID 10938286 DOI: 10.1074/Jbc.M005898200 |
0.563 |
|
2000 |
Ling R, Colón E, Dahmus ME, Callis J. Histidine-tagged ubiquitin substitutes for wild-type ubiquitin in Saccharomyces cerevisiae and facilitates isolation and identification of in vivo substrates of the ubiquitin pathway Analytical Biochemistry. 282: 54-64. PMID 10860499 DOI: 10.1006/Abio.2000.4586 |
0.38 |
|
2000 |
Lehman AL, Dahmus ME. The sensitivity of RNA polymerase II in elongation complexes to C-terminal domain phosphatase. The Journal of Biological Chemistry. 275: 14923-32. PMID 10809737 DOI: 10.1074/Jbc.275.20.14923 |
0.635 |
|
1999 |
Dubois MF, Marshall NF, Nguyen VT, Dahmus GK, Bonnet F, Dahmus ME, Bensaude O. Heat shock of HeLa cells inactivates a nuclear protein phosphatase specific for dephosphorylation of the C-terminal domain of RNA polymerase II. Nucleic Acids Research. 27: 1338-44. PMID 9973623 DOI: 10.1093/Nar/27.5.1338 |
0.539 |
|
1999 |
Cmarko D, Verschure PJ, Martin TE, Dahmus ME, Krause S, Fu XD, van Driel R, Fakan S. Ultrastructural analysis of transcription and splicing in the cell nucleus after bromo-UTP microinjection. Molecular Biology of the Cell. 10: 211-23. PMID 9880337 DOI: 10.1091/MBC.10.1.211 |
0.595 |
|
1998 |
Marshall NF, Dahmus GK, Dahmus ME. Regulation of carboxyl-terminal domain phosphatase by HIV-1 tat protein. The Journal of Biological Chemistry. 273: 31726-30. PMID 9822634 DOI: 10.1074/Jbc.273.48.31726 |
0.603 |
|
1998 |
Archambault J, Pan G, Dahmus GK, Cartier M, Marshall N, Zhang S, Dahmus ME, Greenblatt J. FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO Journal of Biological Chemistry. 273: 27593-27601. PMID 9765293 DOI: 10.1074/Jbc.273.42.27593 |
0.586 |
|
1997 |
Spencer CA, Dahmus ME, Rice SA. Repression of host RNA polymerase II transcription by herpes simplex virus type 1. Journal of Virology. 71: 2031-40. PMID 9032335 DOI: 10.1128/Jvi.71.3.2031-2040.1997 |
0.524 |
|
1996 |
Dahmus ME. Phosphorylation of mammalian RNA polymerase II. Methods in Enzymology. 273: 185-93. PMID 8791612 DOI: 10.1016/S0076-6879(96)73019-7 |
0.672 |
|
1996 |
Dahmus ME. Reversible phosphorylation of the C-terminal domain of RNA polymerase II. The Journal of Biological Chemistry. 271: 19009-12. PMID 8759772 DOI: 10.1074/Jbc.271.32.19009 |
0.687 |
|
1996 |
Kang ME, Dahmus ME. The unique C-terminal domain of RNA polymerase II and its role in transcription. Advances in Enzymology and Related Areas of Molecular Biology. 71: 41-77. PMID 8644491 DOI: 10.1002/9780470123171.Ch2 |
0.683 |
|
1995 |
Chambers RS, Bo Qing Wang, Burton ZF, Dahmus ME. The activity of COOH-terminal domain phosphatase is regulated by a docking site on RNA polymerase II and by the general transcription factors IIF and IIB Journal of Biological Chemistry. 270: 14962-14969. PMID 7797476 DOI: 10.1074/Jbc.270.25.14962 |
0.729 |
|
1995 |
Dahmus ME. Phosphorylation of the C-terminal domain of RNA polymerase II. Biochimica Et Biophysica Acta. 1261: 171-82. PMID 7711060 DOI: 10.1016/0167-4781(94)00233-S |
0.717 |
|
1995 |
Kang ME, Dahmus ME. The photoactivated cross-linking of recombinant C-terminal domain to proteins in a HeLa cell transcription extract that comigrate with transcription factors IIE and IIF. The Journal of Biological Chemistry. 270: 23390-7. PMID 7559497 DOI: 10.1074/Jbc.270.40.23390 |
0.631 |
|
1994 |
Dahmus ME. The role of multisite phosphorylation in the regulation of RNA polymerase II activity. Progress in Nucleic Acid Research and Molecular Biology. 48: 143-79. PMID 7938548 DOI: 10.1016/S0079-6603(08)60855-7 |
0.755 |
|
1994 |
Dubois M, Nguyen V, Dahmus M, Pagès G, Pouysségur J, Bensaude O. Enhanced phosphorylation of the C-terminal domain of RNA polymerase II upon serum stimulation of quiescent cells: possible involvement of MAP kinases. The Embo Journal. 13: 4787-4797. DOI: 10.1002/J.1460-2075.1994.Tb06804.X |
0.533 |
|
1993 |
Tyree CM, George CP, Lira-DeVito LM, Wampler SL, Dahmus ME, Zawel L, Kadonaga JT. Identification of a minimal set of proteins that is sufficient for accurate initiation of transcription by RNA polymerase II. Genes & Development. 7: 1254-65. PMID 8319911 DOI: 10.1101/Gad.7.7A.1254 |
0.638 |
|
1993 |
Baskaran R, Dahmus ME, Wang JY. Tyrosine phosphorylation of mammalian RNA polymerase II carboxyl-terminal domain. Proceedings of the National Academy of Sciences of the United States of America. 90: 11167-71. PMID 7504297 DOI: 10.1073/pnas.90.23.11167 |
0.633 |
|
1989 |
Dahmus ME, Laybourn P, Borrebaeck CA. Production of monoclonal antibody against electrophoretically purified RNA polymerase II subunits using in vitro immunization. Molecular Immunology. 25: 997-1003. PMID 3216873 DOI: 10.1016/0161-5890(88)90006-5 |
0.469 |
|
1988 |
Roberge M, Dahmus ME, Bradbury EM. Chromosomal loop/nuclear matrix organization of transcriptionally active and inactive RNA polymerases in HeLa nuclei Journal of Molecular Biology. 201: 545-555. PMID 3418709 DOI: 10.1016/0022-2836(88)90636-5 |
0.582 |
|
1987 |
Rangel LM, Fernandez-Tomas C, Dahmus ME, Gariglio P. Modification of RNA polymerase IIO subspecies after poliovirus infection. Journal of Virology. 61: 1002-6. PMID 3029396 DOI: 10.1128/jvi.61.4.1002-1006.1987 |
0.498 |
|
1987 |
Garcia-Carranca A, Miguel F, Dahmus ME, Gariglio P. Structure of monkey kidney cell RNA polymerase II: characterization of RNA polymerase associated with SV40 late transcriptional complexes. Archives of Biochemistry and Biophysics. 251: 232-8. PMID 3024573 DOI: 10.1016/0003-9861(86)90070-6 |
0.642 |
|
1985 |
Corden JL, Cadena DL, Ahearn JM, Dahmus ME. A unique structure at the carboxyl terminus of the largest subunit of eukaryotic RNA polymerase II. Proceedings of the National Academy of Sciences of the United States of America. 82: 7934-8. PMID 2999785 DOI: 10.1073/Pnas.82.23.7934 |
0.505 |
|
1979 |
Revie D, Dahmus ME. Purification and partial characterization of a stimulatory factor for lamb thymus RNA polymerase II. Biochemistry. 18: 1813-20. PMID 435487 DOI: 10.1021/bi00576a028 |
0.532 |
|
1977 |
Daubert S, Peters D, Dahmus ME. Selective transcription of ribosomal sequences in vitro by RNA polymerase I. Archives of Biochemistry and Biophysics. 178: 381-6. PMID 319759 DOI: 10.1016/0003-9861(77)90207-7 |
0.546 |
|
1977 |
Dahmus ME, Natzle J. Purification and characterization of Novikoff ascites tumor protein kinase. Biochemistry. 16: 1901-8. PMID 192279 DOI: 10.1021/bi00628a022 |
0.401 |
|
1976 |
Dahmus ME. Stimulation of ascites tumor RNA polymerase II by protein kinase. Biochemistry. 15: 1821-9. PMID 178356 DOI: 10.1021/bi00654a006 |
0.45 |
|
1976 |
Dahmus ME. Multiple forms of a eukaryotic RNA polymerase II stimulation factor. Febs Letters. 61: 227-30. PMID 174948 DOI: 10.1016/0014-5793(76)81043-5 |
0.597 |
|
1976 |
Daubert S, Dahmus ME. Synthesis and characterization of a DNA probe complementary to rat liver 28S ribosomal RNA. Biochemical and Biophysical Research Communications. 68: 1037-44. PMID 57777 DOI: 10.1016/0006-291X(76)90300-4 |
0.442 |
|
1973 |
Lee SC, Dahmus ME. Stimulation of eukaryotic DNA-dependent RNA polymerase by protein factors. Proceedings of the National Academy of Sciences of the United States of America. 70: 1383-7. PMID 4351175 DOI: 10.1073/pnas.70.5.1383 |
0.368 |
|
1966 |
Dahmus ME, Bonner J. Increased template activity of liver chromatin, a result of hydrocortisone administration. Proceedings of the National Academy of Sciences of the United States of America. 54: 1370-5. PMID 4379587 DOI: 10.1073/Pnas.54.5.1370 |
0.321 |
|
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