Control of RNA Polymerase II Elongation Potential by a Novel Carboxyl-terminal Domain Kinase

Transcriptional control by protein phosphorylation: signal transmission from the cell surface to the nucleus

Karin, M., & Hunter, T. R. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00151-5 · Cited by 752 · see citing works

HIV-1 Tat protein increases transcriptional initiation and stabilizes elongation

Laspia, M. F., Rice, A. P., & Mathews, M. B. (1989) · Cell · doi:10.1016/0092-8674(89)90290-0 · Cited by 571 · see citing works

Purification of P-TEFb, a Transcription Factor Required for the Transition into Productive Elongation

Marshall, N. F., & Price, D. H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.21.12335 · Cited by 564 · see citing works

The MO15 cell cycle kinase is associated with the TFIIH transcription-DNA repair factor

Roy, R., Adamczewski, J. P., Seroz, T., Vermeulen, W., Tassan, J., Schaeffer, L., Nigg, E. A., Hoeijmakers, J. H. J., & Egly, J. (1994) · Cell · doi:10.1016/0092-8674(94)90039-6 · Cited by 439 · see citing works

Cdk-activating kinase complex is a component of human transcription factor TFIIH

Shiekhattar, R., Mermelstein, F. H., Fisher, R. P., Drapkin, R., Dynlacht, B. D., Wessling, H. C., Morgan, D. O., & Reinberg, D. (1995) · Nature · doi:10.1038/374283a0 · Cited by 431 · see citing works

Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK

Feaver, W. J., Svejstrup, J. Q., Henry, N. L., & Kornberg, R. D. (1994) · Cell · doi:10.1016/0092-8674(94)90040-x · Cited by 427 · see citing works

A kinase–cyclin pair in the RNA polymerase II holoenzyme

Liao, S.-M., Zhang, J., Jeffery, D., Koleske, A. J., Thompson, C. M., Chao, D. M., Viljoen‐Bloom, M., Vuuren, H. J. J. V., & Young, R. A. (1995) · Nature · doi:10.1038/374193a0 · Cited by 419 · see citing works

Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II

Lu, H., Zawel, L. S., Fisher, L., Egly, J., & Reinberg, D. (1992) · Nature · doi:10.1038/358641a0 · Cited by 402 · see citing works

Ku autoantigen is the regulatory component of a template-associated protein kinase that phosphorylates RNA polymerase II.

Dvir, A., Peterson, S., Knuth, M. W., Lu, H., & Dynan, W. S. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.11920 · Cited by 371 · see citing works

Association of Cdk-activating kinase subunits with transcription factor TFIIH

Serizawa, H., Mäkelä, T. P., Conaway, J. W., Conaway, R. C., Weinberg, R. A., & Young, R. A. (1995) · Nature · doi:10.1038/374280a0 · Cited by 367 · see citing works

Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: candidate for a Tat cofactor

Herrmann, C. H., & Rice, A. P. (1995) · Journal of Virology · doi:10.1128/jvi.69.3.1612-1620.1995 · Cited by 335 · see citing works

Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation

O’Brien, T., Hardin, S. E., Greenleaf, A. L., & Lis, J. T. (1994) · Nature · doi:10.1038/370075a0 · Cited by 324 · see citing works

Functional redundancy and structural polymorphism in the large subunit of RNA polymerase II

Nonet, M. L., Sweetser, D., & Young, R. A. (1987) · Cell · doi:10.1016/0092-8674(87)90517-4 · Cited by 306 · see citing works

Control of formation of two distinct classes of RNA polymerase II elongation complexes.

Marshall, N. F., & Price, D. H. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.5.2078 · Cited by 298 · see citing works

The RNA polymerase II holoenzyme and its implications for gene regulation.

Koleske, A., & Young, R. (1995) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/s0968-0004(00)88977-x · Cited by 297 · see citing works

Messenger RNA synthesis in mammalian cells is catalyzed by the phosphorylated form of RNA polymerase II.

Cadena, D. L., & Dahmus, M. E. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45229-5 · Cited by 293 · see citing works

Casein kinase type II is involved in the inhibition by 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole of specific RNA polymerase II transcription.

Zandomeni, R. O., Zandomeni, M. C., Shugar, D., & Weinmann, R. S. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35799-x · Cited by 293 · see citing works

HIV‐1 Tat protein promotes formation of more‐processive elongation complexes.

Marciniak, R. A., & Sharp, P. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb04997.x · Cited by 290 · see citing works

Differential Expression of c- myb mRNA in Murine B Lymphomas by a Block to Transcription Elongation

Bender, T. P., Thompson, C. B., & Kuehl, W. M. (1987) · Science · doi:10.1126/science.3498214 · Cited by 274 · see citing works

Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2

Cisek, L. J., & Corden, J. L. (1989) · Nature · doi:10.1038/339679a0 · Cited by 272 · see citing works

The block to transcriptional elongation within the human c-myc gene is determined in the promoter-proximal region.Preprint

Krumm, A., Meulia, T., Brunvand, M. W., & Groudine, M. T. (1992) · Genes & Development · doi:10.1101/gad.6.11.2201 · Cited by 263 · see citing works

Transcriptional elongation by RNA polymerase II is stimulated by transactivators

Yankulov, K., Blau, J., Purton, T. J., Roberts, S., & Bentley, D. L. (1994) · Cell · doi:10.1016/0092-8674(94)90058-2 · Cited by 243 · see citing works

The C-terminal domain of the largest subunit of RNA polymerase II of Saccharomyces cerevisiae, Drosophila melanogaster, and mammals: a conserved structure with an essential function.

Allison, L. A., Wong, J. K., Fitzpatrick, V. D., Moyle, M., & Ingles, C. J. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.1.321 · Cited by 240 · see citing works

Transcription elongation and eukaryotic gene regulation.

Spencer, C. A., & Groudine, M. T. (1990) · PubMed · Cited by 224 · see citing works

Inhibition of in Vivo and in Vitro Transcription by Monoclonal Antibodies Prepared against Wheat Germ RNA Polymerase II That React with the Heptapeptide Repeat of Eukaryotic RNA Polymerase II

Thompson, N. E., Steinberg, T. H., Aronson, D. B., & Burgess, R. R. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60493-4 · Cited by 221 · see citing works

Genetic Analysis of the Repetitive Carboxyl-Terminal Domain of the Largest Subunit of Mouse RNA Polymerase II

Bartolomei, M. S., Halden, N. F., Cullen, C. R., & Corden, J. L. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.1.330 · Cited by 217 · see citing works

Tyrosine phosphorylation of mammalian RNA polymerase II carboxyl-terminal domain.

Baskaran, R., Dahmus, M. E., & Wang, J. Y. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11167 · Cited by 213 · see citing works

KIN28 Encodes a C-Terminal Domain Kinase That Controls mRNA Transcription in Saccharomyces cerevisiae but Lacks Cyclin-Dependent Kinase-Activating Kinase (CAK) Activity

Cismowski, M. J., Laff, G. M., Solomon, M. J., & Reed, S. I. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.6.2983 · Cited by 209 · see citing works

The C-terminal repeat domain of RNA polymerase II largest subunit is essential in vivo but is not required for accurate transcription initiation in vitro.

Zehring, W. A., Lee, J. M., Weeks, J. R., Jokerst, R. S., & Greenleaf, A. L. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.3698 · Cited by 192 · see citing works

The Transcriptional Elongation Inhibitor 5,6-Dichloro-1-β-D-ribofuranosylbenzimidazole Inhibits Transcription Factor IIH-associated Protein Kinase

Yankulov, K., Yamashita, K., Roy, R., Egly, J., & Bentley, D. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.23922 · Cited by 192 · see citing works

CTD kinase associated with yeast RNA polymerase II initiation factor b

Feaver, W. J., Gileadi, O., Li, Y., & Kornberg, R. D. (1991) · Cell · doi:10.1016/0092-8674(91)90298-d · Cited by 191 · see citing works

Requirement for TFIIH kinase activity in transcription by RNA polymerase II

Akoulitchev, S., Mäkelä, T. P., Weinberg, R. A., & Reinberg, D. (1995) · Nature · doi:10.1038/377557a0 · Cited by 189 · see citing works

TheKIN28Gene is Required both for RNA Polymerase II Mediated Transcription and Phosphorylation of the Rpb1p CTD

Valay, J.-G., Simon, M., Dubois, M., Bensaude, O., Facca, C., & Faye, G. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0316 · Cited by 186 · see citing works

Hold back of RNA polymerase II at the transcription start site mediates down‐regulation of c‐myc in vivo.

Strobl, L. J., & Eick, D. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05409.x · Cited by 184 · see citing works

Postinitiation Transcriptional Control in Drosophila melanogaster

Rougvie, A. E., & Lis, J. T. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.11.6041-6045.1990 · Cited by 172 · see citing works

Phosphorylation of the C-terminal domain of RNA polymerase II

Dahmus, M. E. (1995) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(94)00233-s · Cited by 135 · see citing works

DNA binding provides a signal for phosphorylation of the RNA polymerase II heptapeptide repeats.Preprint

Peterson, S., Dvir, A., Anderson, C. W., & Dynan, W. S. (1992) · Genes & Development · doi:10.1101/gad.6.3.426 · Cited by 133 · see citing works

RNA polymerase: regulation of transcript elongation and termination

Kerppola, T. K., & Kane, C. M. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.13.1916107 · Cited by 127 · see citing works

Novel mechanism and factor for regulation by HIV‐1 Tat.

Zhou, Q., & Sharp, P. A. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07006.x · Cited by 127 · see citing works

Inhibitors of transcription such as 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole and isoquinoline sulfonamide derivatives (H-8 and H-7) promote dephosphorylation of the carboxyl-terminal domain of RNA polymerase II largest subunit.

Dubois, M., Nguyen, V. T., Bellier, S., & Bensaude, O. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36837-0 · Cited by 122 · see citing works

A protein kinase that phosphorylates the C-terminal repeat domain of the largest subunit of RNA polymerase II.

Lee, J. M., & Greenleaf, A. L. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.10.3624 · Cited by 122 · see citing works

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

Chambers, R., Wang, B. Q., Burton, Z. F., & Dahmus, M. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.25.14962 · Cited by 122 · see citing works

A carboxyl-terminal-domain kinase associated with RNA polymerase II transcription factor delta from rat liver.

Serizawa, H., Conaway, R. C., & Conaway, J. W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7476 · Cited by 121 · see citing works

Regulation of transcriptional elongation by RNA polymerase II

Bentley, D. L. (1995) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(95)80010-7 · Cited by 111 · see citing works

c-fos gene transcription in murine macrophages is modulated by a calcium-dependent block to elongation in intron 1.

Collart, M. A., Tourkine, N., Belin, D., VASSALLI, P., Jeanteur, P., & Blanchard, J. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.5.2826 · Cited by 102 · see citing works

The Role of Multisite Phosphorylation in the Regulation of RNA Polymerase II Activity

Dahmus, M. E. (1994) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60855-7 · Cited by 98 · see citing works

Fractionation of transcription factors for RNA polymerase II from Drosophila Kc cell nuclear extracts.

Price, D. H., Sluder, A. E., & Greenleaf, A. L. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61497-8 · Cited by 98 · see citing works

Expression of mRNA encoding the macrophage colony-stimulating factor receptor (c-fms) is controlled by a constitutive promoter and tissue-specific transcription elongation.

Yue, X., Favot, P., Dunn, T. L., Cassady, A. I., & Hume, D. A. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.6.3191 · Cited by 86 · see citing works

The Major Late Promoter of Adenovirus-2 Is Accurately Transcribed by RNA Polymerases IIO, IIA, and IIB

Kim, W. Y., & Dahmus, M. E. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94046-9 · Cited by 84 · see citing works

RNA polymerases IIA and IIO have distinct roles during transcription from the TATA-less murine dihydrofolate reductase promoter.

Kang, M. E., & Dahmus, M. E. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74568-2 · Cited by 80 · see citing works

Partial purification and characterization of two distinct protein kinases that differentially phosphorylate the carboxyl-terminal domain of RNA polymerase subunit IIa.

Payne, J., & Dahmus, M. E. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54117-x · Cited by 76 · see citing works

Short Transcripts of the Ternary Complex Provide Insight into RNA Polymerase II Elongational Pausing

Rasmussen, E. B., & Lis, J. T. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0517 · Cited by 76 · see citing works

Adenosine Deaminase Gene Expression

Chinsky, J. M., Maa, M. C., Ramamurthy, V., & Kellems, R. E. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71715-8 · Cited by 67 · see citing works

Stability of Drosophila RNA polymerase II elongation complexes in vitro.

Kephart, D. D., Marshall, N. F., & Price, D. H. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.5.2067-2077.1992 · Cited by 67 · see citing works

Interplay of positive and negative effectors in function of the C-terminal repeat domain of RNA polymerase II.

Li, Y., & Kornberg, R. D. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.6.2362 · Cited by 64 · see citing works

Purification of an RNA Polymerase II Transcript Release Factor from Drosophila

Zhi, X., & Price, D. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.19.11043 · Cited by 52 · see citing works

Regulation of eukaryotic gene expression by transcriptional attenuation.

Wright, S. C. (1993) · Molecular Biology of the Cell · doi:10.1091/mbc.4.7.661 · Cited by 44 · see citing works

Phosphorylation State of the RNA Polymerase II C‐Terminal Domain (CTD) in Heat‐Shocked Cells

VENETIANER, A., Dubois, M., Nguyen, V. T., Bellier, S., Seo, S., & Bensaude, O. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.083_1.x · Cited by 43 · see citing works

Elements modulating the block of transcription elongation at the adenovirus 2 attenuation site

Kessler, M. A., Ben‐Asher, E., & Aloni, Y. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81727-6 · Cited by 39 · see citing works

Sequence Requirements for Transcriptional Arrest in Exon 1 of the Human Adenosine Deaminase Gene

Chen, Z., Innis, J. W., Sun, M., Wright, D. A., & Kellems, R. E. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.12.6248 · Cited by 31 · see citing works

Phosphorylation dependence of the initiation of productive transcription of Balbiani ring 2 genes in living cells

Egyh�zi, E., Ossoinak, A., Pigon, A., Holmgren, C., Lee, J. M., & Greenleaf, A. L. (1996) · Chromosoma · doi:10.1007/bf00352266 · Cited by 28 · see citing works

Protein kinases from Aspergillus nidulans that phosphorylate the carboxyl-terminal domain of the largest subunit of RNA polymerase II.

Stone, N., & Reinberg, D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42702-0 · Cited by 26 · see citing works

Distinct Properties of c- myc Transcriptional Elongation Are Revealed in Xenopus Oocytes and Mammalian Cells and by Template Titration, 5,6-Dichloro-1-β-D-Ribofuranosylbenzimidazole (DRB), and Promoter Mutagenesis

Meulia, T., Krumm, A., & Groudine, M. T. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.9.5647-5658.1993 · Cited by 26 · see citing works

Purification of the Drosophila RNA polymerase II general transcription factors.

Austin, R. J., & Biggin, M. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.5788 · Cited by 26 · see citing works

Premature Termination of Transcription Can Be Induced on an Injected α-Tubulin Gene in Xenopus Oocytes

Middleton, K. M., & Morgan, G. T. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.2.727-735.1990 · Cited by 23 · see citing works

The Block to Transcription Elongation at the Minute Virus of Mice Attenuator Is Regulated by Cellular Elongation Factors

Krauskopf, A., Bengal, E., & Aloni, Y. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.7.3515-3521.1991 · Cited by 18 · see citing works

Functional studies of the carboxy-terminal repeat domain of Drosophila RNA polymerase II in vivo.

Brickey, W. J., & Greenleaf, A. L. (1995) · Genetics · doi:10.1093/genetics/140.2.599 · Cited by 16 · see citing works

Premature termination of tubulin gene transcription in Xenopus oocytes is due to promoter-dependent disruption of elongation.

Hair, A., & Morgan, G. T. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7925 · Cited by 12 · see citing works

A 21-base pair DNA fragment directs transcription attenuation within the simian virus 40 late leader

Kessler, M. A., Ben‐Asher, E., Resenkov, O., Hatini, V., Bengal, E., & Aloni, Y. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98797-1 · Cited by 7 · see citing works

Selective inhibition of BET bromodomains

Filippakopoulos, P., Qi, J., Picaud, S., Shen, Y., Smith, W. B., Fedorov, O., Morse, E. M., Keates, T., Hickman, T. T., Felletar, I., et al. (2010) · Nature · doi:10.1038/nature09504 · Cited by 4,262 · see citing works

Cofactor Dynamics and Sufficiency in Estrogen Receptor–Regulated Transcription

Shang, Y., Hu, X., DiRenzo, J., Lazar, M. A., & Brown, M. A. (2000) · Cell · doi:10.1016/s0092-8674(00)00188-4 · Cited by 1,647 · see citing works

Suppression of inflammation by a synthetic histone mimic

Nicodeme, E., Jeffrey, K. L., Schaefer, U., Beinke, S., Dewell, S., Chung, C.-W., Chandwani, R., Marazzi, I., Wilson, P., Coste, H., et al. (2010) · Nature · doi:10.1038/nature09589 · Cited by 1,563 · see citing works

c-Myc Regulates Transcriptional Pause Release

Rahl, P. B., Lin, C. Y., Seila, A. C., Flynn, R. A., McCuine, S., Burge, C. B., Sharp, P. A., & Young, R. A. (2010) · Cell · doi:10.1016/j.cell.2010.03.030 · Cited by 1,279 · see citing works

A Novel CDK9-Associated C-Type Cyclin Interacts Directly with HIV-1 Tat and Mediates Its High-Affinity, Loop-Specific Binding to TAR RNA

Wei, P., Garber, M. E., Fang, S.-M., Fischer, W. H., & Jones, K. A. (1998) · Cell · doi:10.1016/s0092-8674(00)80939-3 · Cited by 1,251 · see citing works

Molecular regulation of stem cell quiescence

Cheung, T. H., & Rando, T. A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3591 · Cited by 1,148 · see citing works

Controlling the elongation phase of transcription with P-TEFb

Peterlin, B. M., & Price, D. H. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.014 · Cited by 1,144 · see citing works

NELF, a Multisubunit Complex Containing RD, Cooperates with DSIF to Repress RNA Polymerase II Elongation

Yamaguchi, Y., Takagi, T., Wada, T., Yano, K., Furuya, A., Sugimoto, S., Hasegawa, J., & Handa, H. (1999) · Cell · doi:10.1016/s0092-8674(00)80713-8 · Cited by 841 · see citing works

Regulation of H SF 1 Function in the Heat Stress Response: Implications in Aging and Disease

Anckar, J., & Sistonen, L. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060809-095203 · Cited by 779 · see citing works

Phosphorylation and functions of the RNA polymerase II CTDPreprint

Phatnani, H. P., & Greenleaf, A. L. (2006) · Genes & Development · doi:10.1101/gad.1477006 · Cited by 752 · see citing works

DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs

Wada, T., Takagi, T., Yamaguchi, Y., Ferdous, A., Imai, T., Hirose, S., Sugimoto, S., Yano, K., Hartzog, G. A., Winston, F., et al. (1998) · Genes & Development · doi:10.1101/gad.12.3.343 · Cited by 750 · see citing works

BET domain co-regulators in obesity, inflammation and cancer

Belkina, A. C., & Denis, G. V. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3256 · Cited by 727 · see citing works

Widespread intron retention in mammals functionally tunes transcriptomes

Braunschweig, U., Barbosa-Morais, N. L., Pan, Q., Nachman, E. N., Alipanahi, B., Gonatopoulos-Pournatzis, T., Frey, B., Irimia, M., & Blencowe, B. J. (2014) · Genome Research · doi:10.1101/gr.177790.114 · Cited by 664 · see citing works

Elongation by RNA polymerase II: the short and long of itPreprint

Sims, R. J., Belotserkovskaya, R., & Reinberg, D. (2004) · Genes & Development · doi:10.1101/gad.1235904 · Cited by 709 · see citing works

Transcription elongation factor P-TEFb is required for HIV-1 Tat transactivation in vitroPreprint

Zhu, Y., Peery, T., Peng, J., Ramanathan, Y., Marshall, N. F., Marshall, T. K., Amendt, B. A., Mathews, M. B., & Price, D. H. (1997) · Genes & Development · doi:10.1101/gad.11.20.2622 · Cited by 700 · see citing works

The RNA polymerase II CTD coordinates transcription and RNA processingPreprint

Hsin, J.-P., & Manley, J. L. (2012) · Genes & Development · doi:10.1101/gad.200303.112 · Cited by 696 · see citing works

p38 and Extracellular Signal-regulated Kinase Mitogen-activated Protein Kinase Pathways Are Required for Nuclear Factor-κB p65 Transactivation Mediated by Tumor Necrosis Factor

Berghe, W. V., Plaisance, S., Boone, E., Bosscher, K. D., Schmitz, M. L., Fiers, W., & Haegeman, G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3285 · Cited by 679 · see citing works

P-TEFb, a Cyclin-Dependent Kinase Controlling Elongation by RNA Polymerase II

Price, D. H. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.8.2629-2634.2000 · Cited by 678 · see citing works

Remodeling of the enhancer landscape during macrophage activation is coupled to enhancer transcription

Kaikkonen, M. U., Spann, N. J., Heinz, S., Romanoski, C. E., Allison, K. A., Stender, J. D., Chun, H. B., Tough, D. F., Prinjha, R. K., Benner, C., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.07.010 · Cited by 672 · see citing works

Inhibiting eukaryotic transcription: which compound to choose? How to evaluate its activity

Bensaude, O. (2011) · Transcription · doi:10.4161/trns.2.3.16172 · Cited by 574 · see citing works

Genome-wide dynamics of Pol II elongation and its interplay with promoter proximal pausing, chromatin, and exons

Jonkers, I., Kwak, H., & Lis, J. T. (2014) · eLife · doi:10.7554/elife.02407 · Cited by 581 · see citing works

RNA Polymerase II Elongation Control

Zhou, Q., Li, T., & Price, D. H. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052610-095910 · Cited by 568 · see citing works

Molecular Genetics of the RNA Polymerase II General Transcriptional Machinery

Hampsey, M. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.2.465-503.1998 · Cited by 561 · see citing works

P-TEFb kinase is required for HIV Tat transcriptional activation in vivo and in vitroPreprint

Mancebo, H. S. Y., Lee, G., Flygare, J. A., Tomassini, J. E., Luu, P., Zhu, Y., Peng, J., Blau, C., Hazuda, D. J., Price, D. H., et al. (1997) · Genes & Development · doi:10.1101/gad.11.20.2633 · Cited by 546 · see citing works

Identification of multiple cyclin subunits of human P-TEFb.Preprint

Peng, J.-M., Zhu, Y., Milton, J. T., & Price, D. (1998) · Genes & Development · doi:10.1101/gad.12.5.755 · Cited by 531 · see citing works

The RNA Polymerase II Carboxy-Terminal Domain (CTD) Code

Eick, D., & Geyer, M. (2013) · Chemical Reviews · doi:10.1021/cr400071f · Cited by 470 · see citing works

Flavopiridol Inhibits P-TEFb and Blocks HIV-1 Replication

Chao, S., Fujinaga, K., Marion, J. E., Taube, R., Sausville, E. A., Senderowicz, A. M., Peterlin, B. M., & Price, D. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000446200 · Cited by 456 · see citing works

Structure of activated transcription complex Pol II–DSIF–PAF–SPT6

Vos, S. M., Farnung, L., Boehning, M., Wigge, C., Linden, A., Urlaub, H., & Cramer, P. (2018) · Nature · doi:10.1038/s41586-018-0440-4 · Cited by 432 · see citing works

Born to run: control of transcription elongation by RNA polymerase II

Chen, F. X., Smith, E. R., & Shilatifard, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0010-5 · Cited by 447 · see citing works

Enhancer RNA Facilitates NELF Release from Immediate Early Genes

Schaukowitch, K., Joo, J., Liu, X., Watts, J. K., Martinez, C., & Kim, T.-K. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.08.023 · Cited by 445 · see citing works

Transcriptional and Posttranscriptional Regulation of HIV-1 Gene Expression

Karn, J., & Stoltzfus, C. M. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006916 · Cited by 437 · see citing works

BASIC MECHANISMS OF TRANSCRIPT ELONGATION AND ITS REGULATION

Uptain, S. M., Kane, C. M., & Chamberlin, M. J. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.117 · Cited by 445 · see citing works

NF-κB Binds P-TEFb to Stimulate Transcriptional Elongation by RNA Polymerase II

Barborič, M., Nissen, R. M., Kanazawa, S., Jabrane‐Ferrat, N., & Peterlin, B. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00314-8 · Cited by 434 · see citing works

The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 proteinPreprint

Garber, M. E., Wei, P., KewalRamani, V. N., Mayall, T. P., Herrmann, C. H., Rice, A. P., Littman, D. R., & Jones, K. A. (1998) · Genes & Development · doi:10.1101/gad.12.22.3512 · Cited by 430 · see citing works

Brd4 and JMJD6-Associated Anti-Pause Enhancers in Regulation of Transcriptional Pause Release

Liu, W., Ma, Q., Wong, K., Li, W., Ohgi, K., Zhang, J., Aggarwal, A. K., & Rosenfeld, M. G. (2013) · Cell · doi:10.1016/j.cell.2013.10.056 · Cited by 403 · see citing works

Direct Coupling of Transcription and mRNA Processing through the Thermogenic Coactivator PGC-1

Monsalve, M., Wu, Z., Adelmant, G., Puigserver, P., Fan, M., & Spiegelman, B. M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00031-9 · Cited by 395 · see citing works

Tackling tat

Karn, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3060 · Cited by 387 · see citing works

Activation-Induced Cytidine Deaminase Targets DNA at Sites of RNA Polymerase II Stalling by Interaction with Spt5

Pavri, R., Gazumyan, A., Janković, M., Virgilio, M. D., Klein, I. A., Ansarah-Sobrinho, C., Resch, W., Yamane, A., Reina‐San‐Martin, B., Barreto, V. M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.09.017 · Cited by 378 · see citing works

Structure of paused transcription complex Pol II–DSIF–NELF

Vos, S. M., Farnung, L., Urlaub, H., & Cramer, P. (2018) · Nature · doi:10.1038/s41586-018-0442-2 · Cited by 378 · see citing works

CDK8 is a positive regulator of transcriptional elongation within the serum response network

Donner, A. J., Ebmeier, C. C., Taatjes, D. J., & Espinosa, J. M. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1752 · Cited by 368 · see citing works

Myeloid cell factor–1 is a critical survival factor for multiple myeloma

Zhang, B., Gojo, I., & Fenton, R. G. (2002) · Blood · doi:10.1182/blood.v99.6.1885 · Cited by 368 · see citing works

A structural perspective of CTD functionPreprint

Meinhart, A., Kamenski, T., Hoeppner, S., Baumli, S., & Cramer, P. (2005) · Genes & Development · doi:10.1101/gad.1318105 · Cited by 359 · see citing works

The structure of P‐TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation

Baumli, S., Lolli, G., Lowe, E. D., Troiani, S., Rusconi, L., Bullock, A. N., Debreczeni, J. E., Knapp, S., & Johnson, L. N. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.121 · Cited by 357 · see citing works

Evidence that P‐TEFb alleviates the negative effect of DSIF on RNA polymerase II‐dependent transcription in vitro

Wada, T., Takagi, T., Yamaguchi, Y., Watanabe, D., & Handa, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7395 · Cited by 355 · see citing works

TFIIH-Associated Cdk7 Kinase Functions in Phosphorylation of C-Terminal Domain Ser7 Residues, Promoter-Proximal Pausing, and Termination by RNA Polymerase II

Glover-Cutter, K. M., Larochelle, S., Erickson, B., Zhang, C., Shokat, K. M., Fisher, R. P., & Bentley, D. L. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00637-09 · Cited by 353 · see citing works

Human Mediator Subunit MED26 Functions as a Docking Site for Transcription Elongation Factors

Takahashi, H., Parmely, T. J., Sato, S., Tomomori‐Sato, C., Banks, C. A. S., Kong, S. E., Szutorisz, H., Swanson, S. K., Martin‐Brown, S., Washburn, M. P., et al. (2011) · Cell · doi:10.1016/j.cell.2011.06.005 · Cited by 346 · see citing works

Crystal structure of HIV-1 Tat complexed with human P-TEFb

Tahirov, T. H., Babayeva, N. D., Varzavand, K., Cooper, J. J., Sedore, S. C., & Price, D. H. (2010) · Nature · doi:10.1038/nature09131 · Cited by 314 · see citing works

P-TEFb kinase recruitment and function at heat shock lociPreprint

Lis, J. T., Mason, P., Peng, J., Price, D. H., & Werner, J. K. (2000) · Genes & Development · doi:10.1101/gad.14.7.792 · Cited by 314 · see citing works

The mixed-lineage leukemia fusion partner AF4 stimulates RNA polymerase II transcriptional elongation and mediates coordinated chromatin remodeling

Bitoun, E., Oliver, P. L., & Davies, K. E. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl444 · Cited by 311 · see citing works

Binding of the 7SK snRNA turns the HEXIM1 protein into a P‐TEFb (CDK9/cyclin T) inhibitor

Michels, A. A., Fraldi, A., Li, Q., Adamson, T. E., Bonnet, F., Nguyen, V. T., Sedore, S. C., Price, J. P., Price, D. H., Lania, L., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600275 · Cited by 305 · see citing works

HSF1 at a glance

Vihervaara, A., & Sistonen, L. (2014) · Journal of Cell Science · doi:10.1242/jcs.132605 · Cited by 305 · see citing works

Association between active genes occurs at nuclear speckles and is modulated by chromatin environment

Brown, J. M., Green, J., das Neves, R. P., Wallace, H. A. C., Smith, A. J. H., Hughes, J. R., Gray, N., Taylor, S., Wood, W. G., Higgs, D. R., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200803174 · Cited by 279 · see citing works

Osmotic stress–induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p

Bonangelino, C. J., Nau, J. J., Duex, J. E., Brinkman, M., Wurmser, A. E., Gary, J. D., Emr, S. D., & Weisman, L. S. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200201002 · Cited by 271 · see citing works

The 19S Regulatory Particle of the Proteasome Is Required for Efficient Transcription Elongation by RNA Polymerase II

Ferdous, A., Gonzàlez, F., Sun, L. L., Kodadek, T. J., & Johnston, S. A. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00250-7 · Cited by 268 · see citing works

Gene-specific requirement for P-TEFb activity and RNA polymerase II phosphorylation within the p53 transcriptional programPreprint

Gomes, N. P., Bjerke, G. A., Llorente, B., Szostek, S. A., Emerson, B. M., & Espinosa, J. M. (2006) · Genes & Development · doi:10.1101/gad.1398206 · Cited by 266 · see citing works

Myc Recruits P-TEFb to Mediate the Final Step in the Transcriptional Activation of the cad Promoter

Eberhardy, S. R., & Farnham, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207441200 · Cited by 259 · see citing works

Transcription inhibition by flavopiridol: mechanism of chronic lymphocytic leukemia cell death

Chen, R., Keating, M. J., Gandhi, V. V., & Plunkett, W. K. (2005) · Blood · doi:10.1182/blood-2005-04-1678 · Cited by 261 · see citing works

Tat Modifies the Activity of CDK9 To Phosphorylate Serine 5 of the RNA Polymerase II Carboxyl-Terminal Domain during Human Immunodeficiency Virus Type 1 Transcription

Zhou, M., Halanski, M. A., Radonovich, M. F., Kashanchi, F., Peng, J., Price, D. H., & Brady, J. N. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.14.5077-5086.2000 · Cited by 261 · see citing works

PAF1, a Molecular Regulator of Promoter-Proximal Pausing by RNA Polymerase II

Chen, F., Woodfin, A. R., Gardini, A., Rickels, R. A., Marshall, S. A., Smith, E. R., Shiekhattar, R., & Shilatifard, A. (2015) · Cell · doi:10.1016/j.cell.2015.07.042 · Cited by 253 · see citing works

The RNA Polymerase II Elongation Complex

Shilatifard, A., Conaway, R. C., & Conaway, J. W. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161551 · Cited by 253 · see citing works

Acetylation on histone H3 lysine 9 mediates a switch from transcription initiation to elongation

Gates, L. A., Shi, J., Rohira, A. D., Feng, Q. F., Zhu, B., Bedford, M. T., Sagum, C. A., Jung, S. Y., Qin, J., Tsai, M., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.802074 · Cited by 247 · see citing works

The cyclin-dependent kinase inhibitor flavopiridol induces apoptosis in multiple myeloma cells through transcriptional repression and down-regulation of Mcl-1.

Gojo, I., Zhang, B., & Fenton, R. G. (2002) · PubMed · Cited by 246 · see citing works

LARP7 is a stable component of the 7SK snRNP while P-TEFb, HEXIM1 and hnRNP A1 are reversibly associated

Krueger, B. J., Jerónimo, C., Roy, B. B., Bouchard, A., Barrandon, C., Byers, S. A., Searcey, C. E., Cooper, J. J., Bensaude, O., Cohen, É. A., et al. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn061 · Cited by 245 · see citing works

Coordination of Transcription, RNA Processing, and Surveillance by P-TEFb Kinase on Heat Shock Genes

Ni, Z., Schwartz, B. E., Werner, J. K., Suárez, J.-R., & Lis, J. T. (2004) · Molecular Cell · doi:10.1016/s1097-2765(03)00526-4 · Cited by 240 · see citing works

RNA Polymerase II Elongation ControlPreprint

Peng, J., Liu, M., Marion, J. E., Zhu, Y., & Price, D. H. (1998) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1998.63.365 · Cited by 238 · see citing works

Global impact of RNA polymerase II elongation inhibition on alternative splicing regulationPreprint

Ip, J. Y. Y., Schmidt, D., Pan, Q., Ramani, A. K., Fraser, A. G., Odom, D. T., & Blencowe, B. J. (2010) · Genome Research · doi:10.1101/gr.111070.110 · Cited by 237 · see citing works

Cyclin-dependent kinase 9: a key transcriptional regulator and potential drug target in oncology, virology and cardiology

Wang, S., & Fischer, P. M. (2008) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2008.03.003 · Cited by 236 · see citing works

A La-Related Protein Modulates 7SK snRNP Integrity to Suppress P-TEFb-Dependent Transcriptional Elongation and Tumorigenesis

He, N., Jahchan, N. S., Hong, E. M., Li, Q., Bayfield, M. A., Maraia, R. J., Luo, K., & Zhou, Q. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.01.003 · Cited by 236 · see citing works

Actin and hnRNP U cooperate for productive transcription by RNA polymerase II

Kukalev, A., Nord, Y., Palmberg, C., Bergman, T., & Percipalle, P. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb904 · Cited by 232 · see citing works

Transcription factories are nuclear subcompartments that remain in the absence of transcriptionPreprint

Mitchell, J. A., & Fraser, P. (2008) · Genes & Development · doi:10.1101/gad.454008 · Cited by 225 · see citing works

Cyclin K Functions as a CDK9 Regulatory Subunit and Participates in RNA Polymerase II Transcription

Fu, T.-J., Peng, J., Lee, G., Price, D. H., & Flores, O. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.49.34527 · Cited by 224 · see citing works

Growth-related Changes in Phosphorylation of Yeast RNA Polymerase II

Patturajan, M., Schulte, R. J., Sefton, B. M., Berezney, R., Vincent, M., Bensaude, O., Warren, S. L., & Corden, J. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.8.4689 · Cited by 223 · see citing works

Domains in the SPT5 Protein That Modulate Its Transcriptional Regulatory Properties

Ivanov, D., Kwak, Y. T., Guo, J. Q., & Gaynor, R. B. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.9.2970-2983.2000 · Cited by 222 · see citing works

The glucocorticoid receptor blocks P-TEFb recruitment by NFκB to effect promoter-specific transcriptional repressionPreprint

Luecke, H. F., & Yamamoto, K. R. (2005) · Genes & Development · doi:10.1101/gad.1297105 · Cited by 217 · see citing works

Analysis of the Large Inactive P-TEFb Complex Indicates That It Contains One 7SK Molecule, a Dimer of HEXIM1 or HEXIM2, and Two P-TEFb Molecules Containing Cdk9 Phosphorylated at Threonine 186

Li, Q., Price, J. P., Byers, S. A., Cheng, D., Peng, J., & Price, D. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502712200 · Cited by 215 · see citing works

BET and HDAC inhibitors induce similar genes and biological effects and synergize to kill in Myc-induced murine lymphoma

Bhadury, J., Nilsson, L. M., Muralidharan, S. V., Green, L. C., Li, Z., Gesner, E. M., Hansen, H. C., Keller, U. B., McLure, K. G., & Nilsson, J. A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1406722111 · Cited by 215 · see citing works

c-Myc Mediates Activation of the cad Promoter via a Post-RNA Polymerase II Recruitment Mechanism

Eberhardy, S. R., & Farnham, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m109014200 · Cited by 215 · see citing works

CDK8

Galbraith, M. D., Donner, A. J., & Espinosa, J. M. (2010) · Transcription · doi:10.4161/trns.1.1.12373 · Cited by 214 · see citing works

Transcription Factor and Polymerase Recruitment, Modification, and Movement on dhsp70 In Vivo in the Minutes following Heat Shock

Boehm, A. K., Saunders, A., Werner, J. K., & Lis, J. T. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.21.7628-7637.2003 · Cited by 212 · see citing works

Transcription elongation factor hSPT5 stimulates mRNA cappingPreprint

Wen, Y., & Shatkin, A. J. (1999) · Genes & Development · doi:10.1101/gad.13.14.1774 · Cited by 210 · see citing works

MYC: a multipurpose oncogene with prognostic and therapeutic implications in blood malignancies

Ahmadi, S. E., Rahimi, S., Zarandi, B., Chegeni, R., & Safa, M. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01111-4 · Cited by 211 · see citing works

Positive Transcription Elongation Factor b Phosphorylates hSPT5 and RNA Polymerase II Carboxyl-terminal Domain Independently of Cyclin-dependent Kinase-activating Kinase

Kim, J. B., & Sharp, P. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010908200 · Cited by 208 · see citing works

Transcription elongation factor P‐TEFb mediates Tat activation of HIV‐1 transcription at multiple stages

Zhou, Q., Chen, D., Pierstorff, E. D., & Luo, K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.13.3681 · Cited by 206 · see citing works

DSIF and NELF Interact with RNA Polymerase II Elongation Complex and HIV-1 Tat Stimulates P-TEFb-mediated Phosphorylation of RNA Polymerase II and DSIF during Transcription Elongation

Ping, Y., & Rana, T. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006130200 · Cited by 206 · see citing works

Control of elongation by RNA polymerase II

Conaway, J. W., Shilatifard, A., Dvir, A., & Conaway, R. C. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01615-7 · Cited by 206 · see citing works

Taking a new TAK on Tat transactivationPreprint

Jones, K. A. (1997) · Genes & Development · doi:10.1101/gad.11.20.2593 · Cited by 203 · see citing works

Transcript cleavage factors GreA and GreB act as transient catalytic components of RNA polymerase

Laptenko, O., Lee, J., Lomakin, I. B., & Borukhov, S. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg610 · Cited by 200 · see citing works

Characterization of Human Cyclin-Dependent Kinase 12 (CDK12) and CDK13 Complexes in C-Terminal Domain Phosphorylation, Gene Transcription, and RNA Processing

Liang, K., Gao, X., Gilmore, J. M., Florens, L. A., Washburn, M. P., Smith, E. R., & Shilatifard, A. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.01426-14 · Cited by 194 · see citing works

A Highly Purified RNA Polymerase II Elongation Control System

Renner, D. B., Yamaguchi, Y., Wada, T., Handa, H., & Price, D. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104967200 · Cited by 193 · see citing works

Role of CDK/cyclin complexes in transcription and RNA splicing

Loyer, P., Trembley, J. H., Katona, R. L., Kidd, V. J., & Lahti, J. M. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2005.02.005 · Cited by 188 · see citing works

Regulation of transcription elongation by phosphorylation

Kobor, M. S., & Greenblatt, J. (2002) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(02)00457-8 · Cited by 187 · see citing works

7SK snRNA: a noncoding RNA that plays a major role in regulating eukaryotic transcription

Peterlin, B. M., Brogie, J. E., & Price, D. H. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.106 · Cited by 181 · see citing works

Heat Shock Factor 1 as a Coordinator of Stress and Developmental Pathways

Anckar, J., & Sistonen, L. (2007) · Springer eBooks · doi:10.1007/978-0-387-39975-1_8 · Cited by 181 · see citing works

Mechanisms tailoring the expression of heat shock proteins to proteostasis challenges

Boopathy, L. R. A., Jacob‐Tomas, S., Alecki, C., & Vera, M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101796 · Cited by 178 · see citing works

Histone Marks in the ‘Driver’s Seat’: Functional Roles in Steering the Transcription Cycle

Gates, L. A., Foulds, C. E., & O’Malley, B. W. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.10.004 · Cited by 169 · see citing works

Identification of a Cyclin Subunit Required for the Function ofDrosophila P-TEFb

Peng, J., Marshall, N. F., & Price, D. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13855 · Cited by 178 · see citing works

Requirement for a Kinase-specific Chaperone Pathway in the Production of a Cdk9/Cyclin T1 Heterodimer Responsible for P-TEFb-mediated Tat Stimulation of HIV-1 Transcription

O'Keeffe, B. A., Fong, Y. W., Chen, D., Zhou, S., & Zhou, Q. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.279 · Cited by 177 · see citing works

Transcription elongation factors DSIF and NELF: Promoter-proximal pausing and beyond

Yamaguchi, Y., Shibata, H., & Handa, H. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.11.007 · Cited by 176 · see citing works

Mechanisms and Control of Embryonic Genome Activation in Mammalian Embryos

Latham, K. E. (1999) · International review of cytology · doi:10.1016/s0074-7696(08)61779-9 · Cited by 175 · see citing works

RNA Polymerase II C-Terminal Domain: Tethering Transcription to Transcript and Template

Corden, J. L. (2013) · Chemical Reviews · doi:10.1021/cr400158h · Cited by 184 · see citing works

P-TEFb Is Critical for the Maturation of RNA Polymerase II into Productive Elongation In Vivo

Ni, Z., Saunders, A., Fuda, N. J., Yao, J., Suárez, J.-R., Webb, W. W., & Lis, J. T. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01859-07 · Cited by 157 · see citing works

Properties of RNA Polymerase II Elongation Complexes Before and After the P-TEFb-mediated Transition into Productive Elongation

Cheng, B. W., & Price, D. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702936200 · Cited by 165 · see citing works

Control of RNA polymerase II activity by dedicated CTD kinases and phosphatases

Majello, B. (2001) · Frontiers in bioscience · doi:10.2741/a685 · Cited by 43 · see citing works

P-TEFb, a Cyclin-Dependent Kinase Controlling Elongation by RNA Polymerase II

Price, D. H. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.8.2629-2634.2000 · Cited by 678 · see citing works

Control of formation of two distinct classes of RNA polymerase II elongation complexes.

Marshall, N. F., & Price, D. H. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.5.2078 · Cited by 298 · see citing works