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

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 501–600 of 666

Anti-termination by SIV Tat Requires Flexibility of the Nascent TAR Structure
Sommer, P., Vartanian, J., Wachsmuth, M., Henry, M., Guétard, D., & Wain–Hobson, S. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.09.042 · Cited by 8
Quantification of the HIV transcriptional activator complex in live cells by image‐based protein–protein interaction analysis
Asamitsu, K., Omagari, K., Okuda, T., Hibi, Y., & Okamoto, T. (2016) · Genes to Cells · doi:10.1111/gtc.12375 · Cited by 8
Cyclin-dependent kinase inhibition and its intersection with immunotherapy in breast cancer: more than CDK4/6 inhibition
Guo, X., Chen, H., Zhou, Y., Shen, L., Wu, S., & Chen, Y. (2022) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2022.2097067 · Cited by 7
Glucose deprivation mediates interaction between CTDK‐I and Snf1 in Saccharomyces cerevisiae
Driessche, B. V., Coddens, S., Mullem, V. V., & Vandenhaute, J. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.08.057 · Cited by 8
Activation and function of murine Cyclin T2A and Cyclin T2B during skeletal muscle differentiation
Marchesi, I., Nieddu, V., Caracciolo, V., Maioli, M., Gaspa, L., Giordano, A., & Bagella, L. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24414 · Cited by 8
Assays for Investigating Transcription by RNA Polymerase IIin Vitro
Reines, D., Dvir, A., Conaway, J. W., & Conaway, R. C. (1997) · Methods · doi:10.1006/meth.1997.0471 · Cited by 8
Deregulated expression of the keratin 18 gene in human colon carcinoma cells.
Fossar, N., Chaouche, M., Prochasson, P., Rousset, M., & Brison, O. (1999) · Somatic Cell and Molecular Genetics · doi:10.1023/a:1019231926567 · Cited by 8
Phosphorylation of OGFOD1 by Cell Cycle-Dependent Kinase 7/9 Enhances the Transcriptional Activity of RNA Polymerase II in Breast Cancer Cells
Lee, H., Lee, I.-H., Kim, J. H., Lee, S., Kwak, S., Suh, M. Y., Hwang, I., Kang, B.-G., Cha, S., Lee, B. I., et al. (2021) · Cancers · doi:10.3390/cancers13143418 · Cited by 7
HIV-2 inhibits HIV-1 gene expression via two independent mechanisms during cellular co-infection
Yapo, V., Majumder, K., Tedbury, P. R., Wen, X. R., Ong, Y. T., Johnson, M. C., & Sarafianos, S. G. (2023) · Journal of Virology · doi:10.1128/jvi.01870-22 · Cited by 7
Transcriptionally active chromatin loops contain both ‘active’ and ‘inactive’ histone modifications that exhibit exclusivity at the level of nucleosome clusters
Koestler, S. A., Ball, M. L., Mureşan, L., Dinakaran, V., & White, R. A. (2024) · Epigenetics & Chromatin · doi:10.1186/s13072-024-00535-9 · Cited by 7
Cocaine-Induced DNA-Dependent Protein Kinase Relieves RNAP II Pausing by Promoting TRIM28 Phosphorylation and RNAP II Hyperphosphorylation to Enhance HIV Transcription
Sharma, A. L., Tyagi, P., Khumallambam, M., & Tyagi, M. (2024) · Cells · doi:10.3390/cells13231950 · Cited by 8
Milestones in transcription and chromatin published in the Journal of Biological Chemistry
Gottesfeld, J. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.004162 · Cited by 8
MD simulation of the Tat/Cyclin T1/CDK9 complex revealing the hidden catalytic cavity within the CDK9 molecule upon Tat binding
Asamitsu, K., Hirokawa, T., & Okamoto, T. (2017) · PLoS ONE · doi:10.1371/journal.pone.0171727 · Cited by 7
Functional Interaction between HEXIM and Hedgehog Signaling during Drosophila Wing Development
Nguyen, D. K., Fayol, O., Buisine, N., Lecorre, P., & Uguen, P. (2016) · PLoS ONE · doi:10.1371/journal.pone.0155438 · Cited by 7
The repetitive C‐terminal domain of RNA polymerase II: Multiple conformational states drive the transcription cycle
Lin, P. S., Tremeau‐Bravard, A., & Dahmus, M. E. (2003) · The Chemical Record · doi:10.1002/tcr.10063 · Cited by 7
How Cells Protect Themselves against Stress?
Khlebodarova, T. M. (2002) · Russian Journal of Genetics · doi:10.1023/a:1015284032526 · Cited by 6
Targeting super enhancers for liver disease: a review
Yang, Z., Liu, Y., Cheng, Q., & Chen, T. (2023) · PeerJ · doi:10.7717/peerj.14780 · Cited by 5
Control of RNA initiation and elongation at the HIV-I promoter
Daelemans, D., Clercq, E. D., & Vandamme, A. (2000) · Aids Reviews · Cited by 6
Investigation of the cytotoxic effect of flavopiridol in canine lymphoma cell lines
Ema, Y., Igase, M., Takeda, Y., Yanase, T., Umeki, S., Hiraoka, H., Okuda, M., & Mizuno, T. (2015) · Veterinary and Comparative Oncology · doi:10.1111/vco.12130 · Cited by 6
GATA-1-mediated Transcriptional Repression Yields Persistent Transcription Factor IIB-Chromatin Complexes
Martowicz, M. L., Grass, J. A., & Bresnick, E. H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605774200 · Cited by 6
Modifications of the isonipecotic acid fragment of SNS-032: Analogs with improved permeability and lower efflux ratio
Fan, J., Fahr, B. J., Stockett, D. E., Chan, E., Cheeti, S., Serafimova, I. M., Lu, Y., Pham, P., Walker, D. H., Hoch, U., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.09.099 · Cited by 6
The Lawc protein is required for proper transcription by RNA polymerase II in Drosophila
Brandt, T., & Corces, V. (2008) · Zeitschrift für Induktive Abstammungs- und Vererbungslehre · doi:10.1007/s00438-008-0372-z · Cited by 7
Stress Induces Changes in the Phosphorylation of Trypanosoma cruzi RNA Polymerase II, Affecting Its Association with Chromatin and RNA Processing
Rocha, A. A., Moretti, N. S., & Schenkman, S. (2014) · Eukaryotic Cell · doi:10.1128/ec.00066-14 · Cited by 5
HSV-1 stimulation-related protein HSRG1 inhibits viral gene transcriptional elongation by interacting with Cyclin T2
Wu, W., Yu, X., Li, W., Guo, L., Liu, L., Wang, L., & Li, Q. (2011) · Science China Life Sciences · doi:10.1007/s11427-011-4160-3 · Cited by 5
PHF13: A new player involved in RNA polymerase II transcriptional regulation and co-transcriptional splicing
Fuchs, A., Torroba, M., & Kinkley, S. (2017) · Transcription · doi:10.1080/21541264.2016.1274813 · Cited by 5
Inhibition of class II trans-activator function by HIV-1 tat in mouse cells is independent of competition for binding to cyclin T1
Mudhasani, R., & Fontes, J. D. (2002) · Molecular Immunology · doi:10.1016/s0161-5890(01)00091-8 · Cited by 5
Spatial organization of transcript elongation and splicing kineticsPreprint
Casill, A. D., Haimowitz, A., Kosmyna, B., Query, C. C., Ye, K. Q., & Gamble, M. J. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.28.428713 · Cited by 5
Genome-wide dynamic nascent transcript profiles reveal that most paused RNA polymerases terminate
Mukherjee, R., & Guertin, M. J. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag128 · Cited by 4
The Promoter-Proximal Pause: A Decision Point Governing RNA Polymerase II Fate
Hyder, U., & Bentley, D. L. (2026) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051424-053703 · Cited by 5
Collaborators or competitors: the communication between RNA polymerase II and the nucleosome during eukaryotic transcription
Hardtke, H. A., & Zhang, Y. (2024) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2024.2306365 · Cited by 5
ATP-mediated activation of RNA polymerase II transcription complexes.
Kopytek, S., & Peterson, D. O. (1998) · Europe PMC (PubMed Central) · Cited by 4
Potential of Nanoparticles Chitosan for Delivery pcDNA3.1-tat
Unsunnidhal, L., Wasito, R., Setyawan, E. M. N., & Kusumawati, A. (2021) · BIO Web of Conferences · doi:10.1051/bioconf/20214107004 · Cited by 4
Molecular basis of the internalization of bovine immunodeficiency virus Tat protein
Deng, G., Su, Y., Mu, J., Sha, R., Geng, Y., Qiao, W., & Chen, Q. (2007) · Virus Genes · doi:10.1007/s11262-007-0137-5 · Cited by 4
Mechanistic basis of gene-specific transcription regulation by the Integrator complexPreprint
Sabath, K., Nabih, A., Arnold, C., Moussa, R., Domjan, D., Zaugg, J. B., & Jonas, S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.24.576984 · Cited by 4
Targeting the Transcriptome Through Globally Acting Components
Parrello, D., Vlasenok, M., Kranz, L. A., & Nechaev, S. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.749850 · Cited by 3
C-terminal determinants for RNA binding motif 7 protein stability and RNA recognition
Sobeh, A. M., & Eichhorn, C. D. (2022) · Biophysical Chemistry · doi:10.1016/j.bpc.2022.106928 · Cited by 3
Catalytic activity of the Bin3/MePCE methyltransferase domain is dispensable for 7SK snRNP function in Drosophila melanogaster
Palumbo, R. J., Yang, Y., Feigon, J. F., & Hanes, S. D. (2023) · Genetics · doi:10.1093/genetics/iyad203 · Cited by 3
Identification of a novel CDK9 inhibitor targeting the intramolecular hidden cavity of CDK9 induced by Tat binding
Asamitsu, K., Hirokawa, T., & Okamoto, T. (2022) · PLoS ONE · doi:10.1371/journal.pone.0277024 · Cited by 3
A tyrosine kinase protein interaction map reveals targetable EGFR network oncogenesis in lung cancerPreprint
Kaushik, S., Haderk, F., Zhao, X., Hu, H., Shah, K. N., Jang, G. Μ., Olivas, V. R., Nanjo, S., Jascur, J., Masto, V. B., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.02.185173 · Cited by 3
The effect of LARP7 on gene expression during osteogenesis
Ozisin, M. S., İmren, G., Aydın, B., Karaosmanoğlu, B., & Taşkıran, E. Z. (2025) · Molecular Biology Reports · doi:10.1007/s11033-024-10216-1 · Cited by 2
Chromatin Regulatory Targets for Anticancer Therapeutics
Barta, P. A., Carter, T. R., & Erb, M. A. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.5c00231 · Cited by 2
Reconstitution of Factor-Dependent, Promoter Proximal Pausing in Drosophila Nuclear Extracts
Li, J., & Gilmour, D. S. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2392-2_7 · Cited by 2
Protonation of the Neutral Repeats of the RNA Polymerase II CTD
Morris, D. P., Stevens, R. D., & Greenleaf, A. L. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8373 · Cited by 2
IDENTIFICATION OF POTENT BROMODOMAIN4 (BRD4) INHIBITORS BY ENERGY- PHARMACOPHORE BASED VIRTUAL SCREENING TO TARGET BRD4-NUT MIDLINE CARCINOMA
Devi, S. T., Tandon, H., & Ampasala, D. R. (2015) · International Journal of Pharmacy and Pharmaceutical Sciences · Cited by 2
Lost in Transcription: Molecular Mechanisms that Control
Taube, R., Peterlin, B. M., Segal, S., & Russell, R. L. (2013) · Cited by 2
Transcription Elongation Factors in Health and Disease
Dabas, P. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.103013 · Cited by 2
[21] Protein and RNA affinity selection techniques using HIV-1 Tat
Garber, M. E., Wei, P., Caderas, G., & Jones, K. A. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)06023-1 · Cited by 2
Discrete promoter elements affect specific properties of RNA polymerase II transcription complexes
Steinke, J. W. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.14.2726 · Cited by 2
Cocaine-induced DNA-PK relieves RNAP II pausing by promoting TRIM28 phosphorylationPreprint
Sharma, A. L., Tyagi, P., Khumallambam, M., & Tyagi, M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.19.608673 · Cited by 2
Stalling of elongating Pol II triggers Ser7 phosphorylation in trans to drive transcription recoveryPreprint
Shlamovitz, I., Bao, Y., Toteva, T., Crisp, A., Ye, S., Wingett, S., Cacioppo, R., Edmondson, A., Castiblanco, D., Boemo, M. A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.04.692291 · Cited by 2
Transcriptional pause release at enhancers mediates cell identity
Ekstrom, T. L., & Johnsen, S. A. (2025) · NAR Cancer · doi:10.1093/narcan/zcaf039 · Cited by 1
RNA-dependent SFPQ condensates coordinate multidimensional regulation of extra-long neuronal genes
Hosokawa, M., Kawakami, R., Imami, K., Kurosawa, R., Yoshizawa, T., Ishihama, Y., Imamura, T., Hagiwara, M., & Takeuchi, A. (2026) · Cell chemical biology · doi:10.1016/j.chembiol.2026.06.004 · Cited by 1
Functional Analysis of the RNA Polymerase II C-terminal Domain Kinase Ctk1 in the Yeast Saccharomyces cerevisiae
München, P. D. L.-M.-U. (2007) · Cited by 1
Identification of Novel Nucleocapsid Chimeric Proteins Inhibiting HIV-1 Replication
Kim, H.-I., Kim, G.-N., Yu, K.-L., Park, S., & You, J. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012340 · Cited by 1
Control of Gene Expression by mRNA Transport and Turnover
Bassett, C. L. (2007) · Springer eBooks · doi:10.1007/978-0-387-35640-2_6 · Cited by 1
Visualizing cellular stress: A hypothesis‐driven confocal laboratory exercise to identify compounds that activate heat shock factor binding at Hsp70 loci
Choi, A., Wang, M., Hrizo, S., & Buckley, M. S. (2018) · Biochemistry and Molecular Biology Education · doi:10.1002/bmb.21163 · Cited by 1
RNA Splicing: Basic Aspects Underlie Antitumor Targeting
Fergany, A., & Tatarskiy, V. V. (2020) · Recent Patents on Anti-Cancer Drug Discovery · doi:10.2174/1574892815666200908122402 · Cited by 1
Robotic Mouse
Bitoun, E., Oliver, P. L., & Davies, K. E. (2021) · Springer eBooks · doi:10.1007/978-3-030-23810-0_65 · Cited by 1
Regulation of heat shock factor 1 (HSF1) DNA-binding and transcription
Mercier, P. A. (2003) · University Library - University of Saskatchewan (University of Saskatchewan) · Cited by 1
Identification and characterization of novel protein-protein interactions with the basal transcription factor, TATA-binding protein
Prigge, J. R. (2006) · Montana State University ScholarWorks (Montana State University) · Cited by 1
The role of Schizosaccharomyces pombe cyclophilin Rct1 in RNA polymerase II transcription
Skrahina, T. (2009) · University of Vienna · doi:10.25365/thesis.8122 · Cited by 1
Structures of the Klebsiella Oxytoca Phage Phi KO2 and Vibrio Harveyi Myovirus-Like Protelomerase Far C-Terminal Domains
Smith, D. (2014) · ProQuest Demo Repository · doi:10.26053/0h-554n-n3g0 · Cited by 1
Guest Editor’s Introduction
Price, D. H. (2009) · Methods · doi:10.1016/j.ymeth.2009.07.003 · Cited by 1
Self-citation
Investigations into the regulation of histone H2B monoubiquitination
Shchebet, A. (2011) · doi:10.53846/goediss-507 · Cited by 1
The exon junction complex regulates the release and phosphorylation of paused RNA polymerase IIPreprint
Akhtar, J., Kreim, N., Marini, F., Mohana, G., Brüne, D., Binder, H., & Roignant, J. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/271544 · Cited by 1
The Role of ARID1A in Oncogenic Transcriptional (de)Regulation in Colorectal Cancer
Sen, M. (2019) · doi:10.53846/goediss-7561 · Cited by 1
TAR-RNA Recognition by a Novel Cyclic Aminoglycoside Analogue
Raghunathan, D. (2007) · doi:10.53846/goediss-2165 · Cited by 1
REGULATION OF THE 64-kDA SUBUNIT OF CLEAVAGE STIMULATORY FACTOR ACTIVITY IN MACROPHAGE AND B LYMPHOCYTE mRNA 3'-END PROCESSING
Shell, S. A. (2005) · D-Scholarship@Pitt (University of Pittsburgh) · Cited by 1
The Recruitment And Dynamics Of Transcription Factors At The Hsp70 Loci In Living Cells
Zobeck, K. L. (2011) · eCommons (Cornell University)
Disruption of DNA Repair by Cell Cycle and Transcriptional CDK Inhibition
Cornell, L., Johnson, N., & Shapiro, G. I. (2015) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-3-319-14151-0_17
Characterization of the Cyclin Dependent Kinase Complex Bur1-2 and its Interaction with RPA
Clausing, E. (2008) · Elektronische Hochschulschriften der LMU München (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.9613
HIV-1
Alonso, A., & Peterlin, B. M. (1999) · Elsevier eBooks · doi:10.1016/b978-012200741-5/50003-9
Etude de la surveillance des ARN d’Immunoglobulines au cours du développement lymphocytaire B
Chemin, G. (2011)
Cell Cycle Control
Matthews, D. J., & Gerritsen, M. E. (2010) · Wiley eBooks · doi:10.1002/9780470555293.ch6
Involvement of p53 in the S-phase Checkpoint during Nucleotide Deficiencies
Heyer, C. L. (2011) · VCU Scholars Compass (Virginia Commonwealth University) · doi:10.25772/4zf5-2439
Molecular Mechanism Involved in HIV-Tat Mediated inhibition of LPS-Induced IL-23 and IL-27 Production in Human Macrophages
Gajanayaka, N. (2015) · uO Research (University of Ottawa) · doi:10.20381/ruor-3938
Novel mechanisms of flavopiridol
Schmerwitz, U. K. (2010) · Elektronische Hochschulschriften der LMU München (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.11698
Polycomb protein Ezh2 controls rhabdomyosarcoma formation
Mura, E. V. (2012) · UnissResearch (Università degli Studi di Sassari)
Structure of the Mediator subunit Cyclin C and subunit interaction studies within the Mediator head module
Höppner, S. (2005) · Elektronische Hochschulschriften der LMU München (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.4693
Regulation of Cellular and HIV-1 Gene Expression by Positive Transcription Elongation Factor B: A Dissertation
O’Brien, S. (2010) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/yvpr-mx32
ANALYSIS OF TWO PLANT PROTEIN COMPLEXES ASSOCIATED WITH TRANSCRIPTION AND CELL CYCLE PROGRESSION
Fülöp, K. (2005) · OpenGrey (Institut de l'Information Scientifique et Technique)
Investigating the Roles of Tat Specific Factor 1 in Both HIV-1 and Cellular Gene Expression
Miller, H. B. (2009) · DukeSpace (Duke University)
Comparative genomics of cyclin-dependent kinases suggest co-evolution of the RNAP II C-terminal domain and CTD-directed CDKs
Guo, Z., & Stiller, J. W. (2004) · The Scholarship East Carolina University's Institutional Repository (East Carolina University) · doi:10.1109/csb.2004.56
Obtenção das quinases dependentes de ciclinas CDK9 e CDK11 humanas utilizando um sistema bacteriano de expressão (E. coli)
dos Santos, N. P. F. (2015) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.75.2015.tde-16062015-091524
ANDROGEN RECEPTOR IN TRANSCRIPTIONAL REGULATION AND CARCINOGENESIS
Kang, Z. (2006) · Työväentutkimus Vuosikirja
Transcription and Genomic Integrity
Poisson, J. M., Chen, Y., & Sánchez, Y. (2007) · Springer eBooks · doi:10.1007/978-0-387-40049-5_25
Respuesta al daño al ADN: un ejemplo de acoplamiento entre transcripción y splicing alternativo
Muñoz, M. J. (2009) · Repositorio Digital Institucional de la Universidad de Buenos Aires (Universidad de Buenos Aires)
Regulation of Core Splicing Factors by Alternative Splicing and Nonsense-mediated mRNA Decay
Saltzman, A. L. (2012) · TSpace (University of Toronto)
The role of H2B monoubiquitination in cellular differentiation
Karpiuk, O. (2013) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3898
The functions of the RNA polymerase II CTD in transcription and RNA processing
Hsin, J.-P. (2013) · doi:10.7916/d8gh9h96
Interplay of chromatin remodeling, transcriptional regulation, and nuclear organization
Steglich, B. (2015) · Figshare
Structure of the Mediator subunit Cyclin C and subunit interaction studies within the Mediator head module
München, P. D. L.-M.-U. (2005)
Epigenetic Regulation of Replication-Dependent Histone mRNA 3 End Processing
Pirngruber, J. (2010) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-354
Mutational Analysis of the HIV-1 Tat Protein and its Role in Downregulating CD127 on CD8 T Cells
Sugden, S. (2013) · uO Research (University of Ottawa) · doi:10.20381/ruor-2932
Dissertation zur Erlangung des Doktorgrades der Fakultät für Chemie und Pharmazie der Ludwig-Maximilians-Universität München
Karla, U., & Schmerwitz, I. (2010)
Using genetics to identify epigenetic and signal transduction targets in cancer
Bhadury, J. (2016) · Gothenburg University Publications Electronic Archive (Gothenburg University)
Regulation of CpG island promoters by the histone methyltransferase MLL2
Ladopoulos, V. (2013) · University of Birmingham Institutional Research Archive (University of Birmingham)
Design of peptide and small molecule inhibitors of cyclin dependent kinase 9/cyclin T1 protein-protein interaction using computational methods
Randjelović, J. (2013) · doi:10.2298/bg20131217randjelovic
HIV Tat and the Control of Transcriptional Elongation
Chen, R., & Zhou, Q. (2007) · Springer eBooks · doi:10.1007/978-0-387-40049-5_14
Interconnections between transcription and pre-mRNA splicing
Gonchar, O. (2016) · Figshare

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