Cited by 666Genomics and Chromatin DynamicsRNA Research and SplicingNuclear Structure and Function

The DOI matches its Crossref record; 69 of the 69 references it cites were found in a registry or an index.

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

Open access

Marshall, Nick F., Peng, Junmin, Xie, Zhi, Price, David H.·1996·Journal of Biological Chemistry

Open this paper in CoChat — free account Open PDF

Abstract

The entry of RNA polymerase II into a productive mode of elongation is controlled, in part, by the postinitiation activity of positive transcription elongation factor b (P-TEFb) (Marshall, N. F., and Price, D. H. (1995) J. Biol. Chem. 270, 12335-12338). We report here that removal of the carboxyl-terminal domain (CTD) of the large subunit of RNA polymerase II abolishes productive elongation. Correspondingly, we found that P-TEFb can phosphorylate the CTD of pure RNA polymerase II. Furthermore, P-TEFb can phosphorylate the CTD of RNA polymerase II when the polymerase is in an early elongation complex. Both the function and kinase activity of P-TEFb are blocked by the drugs 5, 6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB) and H-8. P-TEFb is distinct from transcription factor IIH (TFIIH) because the two factors have no subunits in common, P-TEFb is more sensitive to DRB than is TFIIH, and most importantly, TFIIH cannot substitute functionally for P-TEFb. We propose that phosphorylation of the CTD by P-TEFb controls the transition from abortive into productive elongation mode.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1074/jbc.271.43.27176

Cites

69 of 69 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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 747
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
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
Self-citation
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
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
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
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
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
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
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

Flagged first, then by citations

Show all 69 references

Research works printed but not linked: 14

Spencer, 1990, Oncogene, 5, 777
Meulia, 1993, Mol. Cell. Biol., 13, 5647
Collart, 1991, Mol. Cell. Biol., 11, 2826
Yue, 1993, Mol. Cell. Biol., 13, 3191
Ramamurthy, 1990, Mol. Cell. Biol., 10, 1484
Middleton, 1990, Mol. Cell Biol., 10, 727
Hair, 1993, Mol. Cell. Biol., 13, 7925
Krauskopf, 1991, Mol. Cell. Biol., 11, 3515
Rougvie, 1990, Mol. Cell. Biol., 10, 6041
Kephart, 1992, Mol. Cell. Biol., 12, 2067
Marshall, 1992, Mol. Cell. Biol., 12, 2078
Bartolomei, 1988, Mol. Cell. Biol., 8, 330
Allison, 1988, Mol. Cell. Biol., 8, 321
Lee, 1992, Gene Exp., 1, 149

Sorted by citations

Items 101–200 of 666

Biochemical and Functional Interactions between HIV-1 Tat Protein and TAR RNA
Rana, T. M., & Jeang, K.-T. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1206 · Cited by 175
Cellular control of gene expression by T-type cyclin/CDK9 complexes
Garriga, J., & Graña, X. (2004) · Gene · doi:10.1016/j.gene.2004.05.007 · Cited by 173
Phosphorylation of the Pol II CTD by KIN28 Enhances BUR1/BUR2 Recruitment and Ser2 CTD Phosphorylation Near Promoters
Qiu, H., Hu, C., & Hinnebusch, A. G. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.018 · Cited by 173
TAK, an HIV Tat-associated kinase, is a member of the cyclin-dependent family of protein kinases and is induced by activation of peripheral blood lymphocytes and differentiation of promonocytic cell lines
Yang, X., Gold, M. O., Tang, D. N., Lewis, D. E., Aguilar-Córdova, E., Rice, A. P., & Herrmann, C. H. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12331 · Cited by 171
THZ1 Reveals Roles for Cdk7 in Co-transcriptional Capping and Pausing
Nilson, K. A., Guo, J., Turek, M. E., Brogie, J. E., Delaney, E., Luse, D. S., & Price, D. H. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.032 · Cited by 170
Self-citation
Transcriptional Elongation by RNA Polymerase II and Histone Methylation
Gerber, M., & Shilatifard, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.r300014200 · Cited by 171
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
Self-citation
Development of a Selective CDK7 Covalent Inhibitor Reveals Predominant Cell-Cycle Phenotype
Olson, C. M., Liang, Y., Leggett, A. L., Park, W. D., Li, L., Mills, C. E., Elsarrag, S. Z., Ficarro, S. B., Zhang, T., Düster, R., et al. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.02.012 · Cited by 169
Structure of complete Pol II–DSIF–PAF–SPT6 transcription complex reveals RTF1 allosteric activation
Vos, S. M., Farnung, L., Linden, A., Urlaub, H., & Cramer, P. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0437-1 · Cited by 160
How eukaryotic genes are transcribed
Venters, B. J., & Pugh, B. F. (2009) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230902858785 · Cited by 176
Control of transcriptional elongation and cotranscriptional histone modification by the yeast BUR kinase substrate Spt5
Zhou, K., Kuo, W. H. W., Fillingham, J., & Greenblatt, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806302106 · Cited by 162
Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription
Chao, S.-H. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.3.767 · Cited by 161
Complexities in the development of cyclin-dependent kinase inhibitor drugs
Sausville, E. A. (2002) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(02)02308-0 · Cited by 159
BRCA2 Regulates Transcription Elongation by RNA Polymerase II to Prevent R-Loop Accumulation
Shivji, M. K. K., Renaudin, X., Williams, Ç. H., & Venkitaraman, A. R. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.12.086 · Cited by 162
A CTD function linking transcription to splicing
Corden, J. L., & Patturajan, M. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01125-0 · Cited by 157
Bur1 Kinase Is Required for Efficient Transcription Elongation by RNA Polymerase II
Keogh, M., Podolny, V., & Buratowski, S. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.19.7005-7018.2003 · Cited by 157
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
AID Targeting in Antibody Diversity
Pavri, R., & Nussenzweig, M. C. (2011) · Advances in immunology · doi:10.1016/b978-0-12-387663-8.00005-3 · Cited by 156
Evolutionarily Conserved Interaction between CstF-64 and PC4 Links Transcription, Polyadenylation, and Termination
Calvo, O., & Manley, J. L. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00236-2 · Cited by 154
Ready, pause, go: regulation of RNA polymerase II pausing and release by cellular signaling pathways
Liu, X., Kraus, W. L., & Bai, X. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.07.003 · Cited by 163
Modifications of RNA polymerase II are pivotal in regulating gene expression states
Brookes, E., & Pombo, A. (2009) · EMBO Reports · doi:10.1038/embor.2009.221 · Cited by 154
CDK9: A Comprehensive Review of Its Biology, and Its Role as a Potential Target for Anti-Cancer Agents
Anshabo, A. T., Milne, R. W., Wang, S., & Albrecht, H. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.678559 · Cited by 155
CDK9 Autophosphorylation Regulates High-Affinity Binding of the Human Immunodeficiency Virus Type 1 Tat–P-TEFb Complex to TAR RNA
Garber, M. E., Mayall, T. P., Suess, E. M., Meisenhelder, J., Thompson, N. E., & Jones, K. A. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6958-6969.2000 · Cited by 151
Functional Coupling of Capping and Transcription of mRNA
Moteki, S. A., & Price, D. H. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00660-3 · Cited by 150
Self-citation
FCP1, the RAP74-Interacting Subunit of a Human Protein Phosphatase That Dephosphorylates the Carboxyl-terminal Domain of RNA Polymerase IIO
Archambault, J., Pan, G., Dahmus, G. K., Cartier, M., Marshall, N. F., Zhang, S., Dahmus, M. E., & Greenblatt, J. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.42.27593 · Cited by 149
Self-citation
Three RNA Polymerase II Carboxyl-terminal Domain Kinases Display Distinct Substrate Preferences
Ramanathan, Y., Rajpara, S. M., Reza, S. M., Lees, E. M., Shuman, S., Mathews, M. B., & Pe’ery, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010975200 · Cited by 148
Regulation of RNA polymerase II activity by CTD phosphorylation and cell cycle control
Oelgeschläger, T. (2002) · Journal of Cellular Physiology · doi:10.1002/jcp.10058 · Cited by 147
An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae
Archambault, J., Chambers, R., Kobor, M. S., Ho, Y., Cartier, M., Bolotin, D., Andrews, B., Kane, C. M., & Greenblatt, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14300 · Cited by 145
Mechanisms of developmental control of transcription in the murine α- and β-globin lociPreprint
Trimborn, T., Gribnau, J. H., Grosveld, F. G., & Fraser, P. (1999) · Genes & Development · doi:10.1101/gad.13.1.112 · Cited by 145
Tat-Associated Kinase, TAK, Activity Is Regulated by Distinct Mechanisms in Peripheral Blood Lymphocytes and Promonocytic Cell Lines
Herrmann, C. H., Carroll, R. G., Wei, P., Jones, K. A., & Rice, A. P. (1998) · Journal of Virology · doi:10.1128/jvi.72.12.9881-9888.1998 · Cited by 144
CDK9 inhibition by dinaciclib potently suppresses Mcl-1 to induce durable apoptotic responses in aggressive MYC-driven B-cell lymphoma in vivo
Gregory, G. P., Hogg, S. J., Kats, L. M., Vidacs, E., Baker, A. J., Gilan, O., Lefebure, M., Martin, B. P., Dawson, M. A., Johnstone, R. W., et al. (2014) · Leukemia · doi:10.1038/leu.2015.10 · Cited by 143
Structure and Function of the Human Transcription Elongation Factor DSIF
Yamaguchi, Y., Wada, T., Watanabe, D., Takagi, T., Hasegawa, J., & Handa, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.8085 · Cited by 143
P-TEFb regulation of transcription termination factor Xrn2 revealed by a chemical genetic screen for Cdk9 substratesPreprint
Sansó, M., Levin, R. S., Lipp, J., Wang, V. Y., Greifenberg, A. K., Quezada, E. M., Ali, A., Ghosh, A., Larochelle, S., Rana, T. M., et al. (2016) · Genes & Development · doi:10.1101/gad.269589.115 · Cited by 137
The Mediator complex and transcription elongation
Conaway, R., & Conaway, J. W. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.08.017 · Cited by 146
Action of Boron at the Molecular Level Effects on Transcription and Translation in an Acellular System
Dzondo‐Gadet, M., Nzietchueng, R., Hess, K., Nabet, P., Belleville, F., & Dousset, B. (2002) · Biological Trace Element Research · doi:10.1385/bter:85:1:23 · Cited by 135
CDK9 Regulates AR Promoter Selectivity and Cell Growth through Serine 81 Phosphorylation
Gordon, V. L., Bhadel, S., Wunderlich, W., Zhang, J., Ficarro, S. B., Mollah, S., Shabanowitz, J., Hunt, D. F., Xénarios, I., Hahn, W. C., et al. (2010) · Molecular Endocrinology · doi:10.1210/me.2010-0238 · Cited by 134
Transcriptional Activation of the Integrated Chromatin-Associated Human Immunodeficiency Virus Type 1 Promoter
Kharroubi, A. E., Piras, G., Zensen, R., & Martin, M. A. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.5.2535 · Cited by 134
Novel binding partners of Ldb1 are required for haematopoietic development
Meier, N. T., Krpic, S., Rodriguez, P., Strouboulis, J., Monti, M., Krijgsveld, J., Gering, M., Patient, R. K., Hostert, A., & Grosveld, F. G. (2006) · Development · doi:10.1242/dev.02656 · Cited by 133
Set1/COMPASS and Mediator are repurposed to promote epigenetic transcriptional memory
D’Urso, A., Takahashi, Y.-H., Xiong, B., Marone, J., Coukos, R., Randise-Hinchliff, C., Wang, J.-P., Shilatifard, A., & Brickner, J. H. (2016) · eLife · doi:10.7554/elife.16691 · Cited by 142
Recruitment Timing and Dynamics of Transcription Factors at the Hsp70 Loci in Living Cells
Zobeck, K. L., Buckley, M. S., Zipfel, W. R., & Lis, J. T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.022 · Cited by 131
Direct evidence that HIV-1 tat stimulates RNA polymerase II carboxyl-terminal domain hyperphosphorylation during transcriptional elongation
Isel, C., & Karn, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2933 · Cited by 131
In vivo live imaging of RNA polymerase II transcription factories in primary cellsPreprint
Ghamari, A., van de Corput, M. P. C., Thongjuea, S., van Cappellen, W. A., van IJcken, W. F. J., van Haren, J., Soler, É., Eick, D., Lenhard, B., & Grosveld, F. G. (2013) · Genes & Development · doi:10.1101/gad.216200.113 · Cited by 131
Hyperphosphorylation of the C-terminal Repeat Domain of RNA Polymerase II Facilitates Dissociation of Its Complex with Mediator*
Max, T., Søgaard, M., & Svejstrup, J. Q. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701345200 · Cited by 150
Poised Polymerases: On Your Mark…Get Set…Go!
Price, D. H. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.001 · Cited by 128
Self-citation
Characterization of the Residues Phosphorylated in Vitro by Different C-terminal Domain Kinases
Trigon, S., Serizawa, H., Conaway, J. W., Conaway, R. C., Jackson, S. P., & Morange, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.6769 · Cited by 128
RNA Polymerase II Carboxy-Terminal Domain Kinases: Emerging Clues to Their Function
Prelich, G. (2002) · Eukaryotic Cell · doi:10.1128/ec.1.2.153-162.2002 · Cited by 128
ELL2, a new member of an ELL family of RNA polymerase II elongation factors
Shilatifard, A., Duan, D. R., Haque, D., Florence, C., Schubach, W. H., Conaway, J. W., & Conaway, R. C. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3639 · Cited by 126
Kinetic Competition between Elongation Rate and Binding of NELF Controls Promoter-Proximal Pausing
Li, J., Liu, Y., Rhee, H. S., Ghosh, S., Bai, L., Pugh, B. F., & Gilmour, D. S. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.05.016 · Cited by 124
The Cdk9 and cyclin T subunits of TAK/P-TEFb localize to splicing factor-rich nuclear speckle regions
Herrmann, C. H., & Mancini, M. A. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.8.1491 · Cited by 124
Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T
Fujinaga, K., Taube, R., Wimmer, J., Cujec, T. P., & Peterlin, B. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.4.1285 · Cited by 124
Selective CDK9 inhibition overcomes TRAIL resistance by concomitant suppression of cFlip and Mcl-1
Lemke, J., von Karstedt, S., Hay, M. Y. A. E., Conti, A., Vargas, F. A., Montinaro, A., Papenfuss, K., El-Bahrawy, M. A., & Walczak, H. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.179 · Cited by 123
Cyclin C/CDK8 and cyclin H/CDK7/p36 are biochemically distinct CTD kinases
Rickert, P., Corden, J. L., & Lees, E. M. (1999) · Oncogene · doi:10.1038/sj.onc.1202399 · Cited by 122
Inhibition of HIV-1 replication by P-TEFb inhibitors DRB, seliciclib and flavopiridol correlates with release of free P-TEFb from the large, inactive form of the complex
Biglione, S., Byers, S. A., Price, J. P., Nguyen, V. T., Bensaude, O., Price, D. H., & Maury, W. J. (2007) · Retrovirology · doi:10.1186/1742-4690-4-47 · Cited by 121
Self-citation
The regulation of HIV-1 transcription: Molecular targets for chemotherapeutic intervention
Stevens, M., Clercq, E. D., & Balzarini, J. M. (2006) · Medicinal Research Reviews · doi:10.1002/med.20081 · Cited by 123
Mitotic Transcriptional Activation: Clearance of Actively Engaged Pol II via Transcriptional Elongation Control in Mitosis
Liang, K., Woodfin, A. R., Slaughter, B. D., Unruh, J. R., Box, A., Rickels, R. A., Gao, X., Haug, J. S., Jaspersen, S. L., & Shilatifard, A. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.021 · Cited by 118
RNA Polymerase II Transcription Elongation Control
Guo, J., & Price, D. H. (2013) · Chemical Reviews · doi:10.1021/cr400105n · Cited by 119
Self-citation
A model of repression: CTD analogs and PIE-1 inhibit transcriptional elongation by P-TEFbPreprint
Zhang, F., Barborič, M., Blackwell, T. K., & Peterlin, B. M. (2003) · Genes & Development · doi:10.1101/gad.1068203 · Cited by 117
Acetylation of RNA Polymerase II Regulates Growth-Factor-Induced Gene Transcription in Mammalian Cells
Schröder, S., Herker, E., Itzen, F., He, D. X., Thomas, S., Gilchrist, D. A., Kaehlcke, K., Cho, S., Pollard, K. S., Capra, J. A., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.10.009 · Cited by 115
Leukemia Fusion Target AF9 Is an Intrinsically Disordered Transcriptional Regulator that Recruits Multiple Partners via Coupled Folding and Binding
Leach, B. I., Kuntimaddi, A., Schmidt, C., Cierpicki, T., Johnson, S. A., & Bushweller, J. H. (2012) · Structure · doi:10.1016/j.str.2012.11.011 · Cited by 114
The Writers, Readers, and Functions of the RNA Polymerase II C-Terminal Domain Code
Jerónimo, C., Bataille, A. R., & Robert, F. (2013) · Chemical Reviews · doi:10.1021/cr4001397 · Cited by 120
Phosphorylation of histone H3 at Ser10 facilitates RNA polymerase II release from promoter-proximal pausing in DrosophilaPreprint
Ivaldi, M. S., Karam, C. S., & Corces, V. G. (2007) · Genes & Development · doi:10.1101/gad.1604007 · Cited by 114
The Mechanism of Release of P-TEFb and HEXIM1 from the 7SK snRNP by Viral and Cellular Activators Includes a Conformational Change in 7SK
Krueger, B. J., Varzavand, K., Cooper, J. J., & Price, D. H. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012335 · Cited by 111
Self-citation
HEXIM2, a HEXIM1-related Protein, Regulates Positive Transcription Elongation Factor b through Association with 7SK
Byers, S. A., Price, J. P., Cooper, J. J., Li, Q., & Price, D. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500424200 · Cited by 112
Self-citation
Cyclin-dependent kinases (cdks) and the DNA damage response: rationale for cdk inhibitor–chemotherapy combinations as an anticancer strategy for solid tumors
Johnson, N., & Shapiro, G. I. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2010.525221 · Cited by 113
Nuclear pre-mRNA Compartmentalization: Trafficking of Released Transcripts to Splicing Factor Reservoirs
Melčák, I., Cermanová, Š., Jirsová, K., Koberna, K., Malínský, J., & Raška, I. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.2.497 · Cited by 111
FACT Relieves DSIF/NELF-Mediated Inhibition of Transcriptional Elongation and Reveals Functional Differences between P-TEFb and TFIIH
Wada, T., Orphanides, G., Hasegawa, J., Kim, D.-K., Shima, D., Yamaguchi, Y., Fukuda, A., Hisatake, K., Oh, S., Reinberg, D., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80272-5 · Cited by 111
CDK9: From Basal Transcription to Cancer and AIDS
Falco, G. D., & Giordano, A. (2002) · Cancer Biology & Therapy · doi:10.4161/cbt.1.4.6113 · Cited by 110
A nucleolar TAR decoy inhibitor of HIV-1 replication
Michienzi, A., Li, S. X., Zaia, J. A., & Rossi, J. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212229599 · Cited by 110
Noncoding transcription within the Igh distal V H region at PAIR elements affects the 3D structure of the Igh locus in pro-B cells
Verma‐Gaur, J., Torkamani, A., Schaffer, L., Head, S. R., Schork, N. J., & Feeney, A. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208398109 · Cited by 108
RNA Polymerase II transcription elongation and Pol II CTD Ser2 phosphorylation
Bowman, E. A., & Kelly, W. G. (2014) · Nucleus · doi:10.4161/nucl.29347 · Cited by 116
Activation of MyoD-dependent transcription by cdk9/cyclin T2
Simone, C., Stiegler, P., Bagella, L., Pucci, B., Bellan, C., Falco, G. D., Luca, A. D., Guanti, G., Puri, P., & Giordano, A. (2002) · Oncogene · doi:10.1038/sj.onc.1205493 · Cited by 108
Identification of a novel isoform of Cdk9
Shore, S. M., Byers, S. A., Maury, W. J., & Price, D. H. (2003) · Gene · doi:10.1016/s0378-1119(03)00466-9 · Cited by 108
Self-citation
Triptolide (TPL) Inhibits Global Transcription by Inducing Proteasome-Dependent Degradation of RNA Polymerase II (Pol II)
Wang, Y., Lu, J., He, L., & Yu, Q. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023993 · Cited by 104
The Cyclin-Dependent Kinase Inhibitor Roscovitine Inhibits RNA Synthesis and Triggers Nuclear Accumulation of p53 That Is Unmodified at Ser15 and Lys382
Ljungman, M. E., & Paulsen, M. T. (2001) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)12306-1 · Cited by 107
Nuclear translocation and carboxyl‐terminal domain phosphorylation of RNA polymerase II delineate the two phases of zygotic gene activation in mammalian embryos
Bellier, S., Chastant‐Maillard, S., Adenot, P. G., Vincent, M., Renard, J. P. J. P., & Bensaude, O. (1997) · The EMBO Journal · doi:10.1093/emboj/16.20.6250 · Cited by 106
Factors regulating the transcriptional elongation activity of RNA polymerase II
Shilatifard, A. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.14.1437 · Cited by 104
Control of HIV Latency by Epigenetic and Non-Epigenetic Mechanisms
Karn, J., & Mbonye, U. R. (2011) · Current HIV Research · doi:10.2174/157016211798998736 · Cited by 102
Transcriptome-wide modulation of splicing by the Exon Junction Complex
Wang, Z., Murigneux, V., & Hir, H. L. (2014) · Genome biology · doi:10.1186/preaccept-1827287072145398 · Cited by 97
Loss of Sfpq Causes Long-Gene Transcriptopathy in the Brain
Takeuchi, A., Iida, K., Tsubota, T., Hosokawa, M., Denawa, M., Brown, J. B., Ninomiya, K., Ito, M., Kimurâ, H., Abe, T., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.141 · Cited by 107
Phosphorylation of the RNA Polymerase II Carboxy-Terminal Domain by the Bur1 Cyclin-Dependent Kinase
Murray, S., Udupa, R., Yao, S., Hartzog, G. A., & Prelich, G. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.13.4089-4096.2001 · Cited by 101
Ubiquitination of RNA polymerase II large subunit signaled by phosphorylation of carboxyl-terminal domain
Mitsui, A., & Sharp, P. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6054 · Cited by 101
Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks
Csermely, P., & VÃgh, L. (2007) · Springer eBooks · doi:10.1007/978-0-387-39975-1 · Cited by 100
An Early Function during Transcription for the Yeast mRNA Export Factor Dbp5p/Rat8p Suggested by Its Genetic and Physical Interactions with Transcription Factor IIH Components
Estruch, F., & Cole, C. N. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-09-0602 · Cited by 99
Modulation of RNA Polymerase II Elongation Efficiency by C-terminal Heptapeptide Repeat Domain Kinase I
Lee, J. M., & Greenleaf, A. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.10990 · Cited by 99
Formation of a Carboxy-Terminal Domain Phosphatase (Fcp1)/TFIIF/RNA Polymerase II (pol II) Complex in Schizosaccharomyces pombe Involves Direct Interaction between Fcp1 and the Rpb4 Subunit of pol II
Kimura, M., Suzuki, H., & Ishihama, A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.5.1577-1588.2002 · Cited by 99
RNA polymerase II holoenzyme and transcriptional regulation
Greenblatt, J. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80002-6 · Cited by 99
Transcription Elongation and Human Disease
Conaway, J. W., & Conaway, R. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.301 · Cited by 99
Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II
Carty, S. M., Goldstrohm, A. C., Suñé, C., García-Blanco, M. A., & Greenleaf, A. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.160266597 · Cited by 96
TIP30 has an intrinsic kinase activity required for up‐regulation of a subset of apoptotic genes
Xiao, H., Palhan, V. B., Yang, Y., & Roeder, R. G. (2000) · The EMBO Journal · doi:10.1093/emboj/19.5.956 · Cited by 96
BET Inhibition Overcomes Receptor Tyrosine Kinase–Mediated Cetuximab Resistance in HNSCC
Leonard, B. C., Brand, T. M., O’Keefe, R. A., Lee, E. D., Zeng, Y., Kemmer, J. D., Li, H., Grandis, J. R., & Bhola, N. E. (2018) · Cancer Research · doi:10.1158/0008-5472.can-18-0459 · Cited by 99
Chromatin interaction mechanism of transcriptional control in vivo
Gribnau, J. H., de Boer, E., Trimborn, T., Wijgerde, M., Milot, É., Grosveld, F. G., & Fraser, P. (1998) · The EMBO Journal · doi:10.1093/emboj/17.20.6020 · Cited by 94
Efficient RNA polymerase II pause release requires U2 snRNP function
Caizzi, L., Monteiro-Martins, S., Schwalb, B., Lysakovskaia, K., Schmitzová, J., Sawicka, A., Chen, Y., Lidschreiber, M., & Cramer, P. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.02.016 · Cited by 103
A Nuclear Matrix Protein Interacts with the Phosphorylated C-Terminal Domain of RNA Polymerase II
Patturajan, M., Wei, X., Berezney, R., & Corden, J. L. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.4.2406 · Cited by 93
Interaction between Cyclin T1 and SCF SKP2 Targets CDK9 for Ubiquitination and Degradation by the Proteasome
Kiernan, R. E., Emiliani, S., Nakayama, K., Castro, A., Labbé, J. C., Lorca, T., Nakayama, K., & Benkirane, M. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.23.7956-7970.2001 · Cited by 93
Stress from Nucleotide Depletion Activates the Transcriptional Regulator HEXIM1 to Suppress Melanoma
Tan, J. L., Fogley, R. D., Flynn, R. A., Ablain, J., Yang, S. P., Saint‐André, V., Fan, Z. P., Do, B. T., Laga, A. C., Fujinaga, K., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.013 · Cited by 92
Self-citation
PITSLRE p110 Protein Kinases Associate with Transcription Complexes and Affect Their Activity
Trembley, J. H., Hu, D., Hsu, L.-C., Yeung, C. Y., Slaughter, C. A., Lahti, J. M., & Kidd, V. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109755200 · Cited by 92
Genetic Interactions of Spt4-Spt5 and TFIIS With the RNA Polymerase II CTD and CTD Modifying Enzymes in Saccharomyces cerevisiae
Lindstrom, D. L., & Hartzog, G. A. (2001) · Genetics · doi:10.1093/genetics/159.2.487 · Cited by 90
Tat-associated Kinase (P-TEFb): a Component of Transcription Preinitiation and Elongation Complexes
Ping, Y., & Rana, T. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.11.7399 · Cited by 90
The histone demethylase Jmjd3 sequentially associates with the transcription factors Tbx3 and Eomes to drive endoderm differentiation
Kartikasari, A. E. R., Zhou, J. X., Kanji, M. S., Chan, D. N., Sinha, A., Grapin‐Botton, A., Magnuson, M. A., Lowry, W. E., & Bhushan, A. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.78 · Cited by 90
Role of the human and murine cyclin T proteins in regulating HIV-1 tat-activation
Kwak, Y. T., Ivanov, D., Guo, J. Q., Nee, E., & Gaynor, R. B. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2664 · Cited by 89

Authors: Marshall, N. F., Peng, J., Xie, Z., & Price, D. H.
Affiliations: University of Iowa (US)
Corresponding author: Price, David H.
ORCID: Peng, Junmin
Price, David H.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1996-10
Volume: 271
Issue: 43
Pages: 27176-27183
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.271.43.27176
OpenAlex: W2020329201
Cited by: 662
References: 69
Citations by year: 2026: 11 · 2025: 7 · 2024: 16 · 2023: 20 · 2022: 11 · 2021: 15 · 2020: 20 · 2019: 19 · 2018: 13 · 2017: 13 · 2016: 18 · 2015: 27 · 2014: 20 · 2013: 30 · 2012: 27
FWCI: 11.86
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 8801 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: Yale University
National Institute of General Medical Sciences (R01GM035500, GM-35500)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: RNA polymerase II, transcription elongation, C-terminal domain, P-TEFb, CTD phosphorylation, DRB, H-8, TFIIH, kinase activity
MeSH terms: Hydrolysis, Phosphorylation, Protein Kinases, RNA Polymerase II, Transcription Factors, Transcription Factors, TFII, Transcription Factor TFIIH

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks