The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Elongation by RNA polymerase II: the short and long of it
Open accessAbstract
Appreciable advances into the process of transcript elongation by RNA polymerase II (RNAP II) have identified this stage as a dynamic and highly regulated step of the transcription cycle. Here, we discuss the many factors that regulate the elongation stage of transcription. Our discussion includes the classical elongation factors that modulate the activity of RNAP II, and the more recently identified factors that facilitate elongation on chromatin templates. Additionally, we discuss the factors that associate with RNAP II, but do not modulate its catalytic activity. Elongation is highlighted as a central process that coordinates multiple stages in mRNA biogenesis and maturation.
Overview
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
Cites
Statistics
Verification
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.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Weintraub, H., & Groudine, M. (1976) · Science · doi:10.1126/science.948749 · Cited by 1,809
Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution
Cramer, P., Bushnell, D. A., & Kornberg, R. D. (2001) · Science · doi:10.1126/science.1059493 · Cited by 1,247
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
Henry, K. W., Wyce, A., Lo, W.-S., Duggan, L. J., Emre, N. C. T., Kao, C.-F., Pillus, L., Shilatifard, A., Osley, M. A., & Berger, S. L. (2003) · Genes & Development · doi:10.1101/gad.1144003 · Cited by 714
Control of RNA Polymerase II Elongation Potential by a Novel Carboxyl-terminal Domain Kinase
Marshall, N. F., Peng, J., Xie, Z., & Price, D. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.27176 · Cited by 662 · cited 2×
“P-TEFb was originally shown to phosphorylate the CTD of RNAP II when RNA polymerase was in promoter clearance in vitro (Marshall et al. 1996).”
BackgroundKamura, T., Sato, S., Haque, D., Liu, L., Kaelin, W. G., Conaway, R. C., & Conaway, J. W. (1998) · Genes & Development · doi:10.1101/gad.12.24.3872 · Cited by 595
A transcription reinitiation intermediate that is stabilized by activator
Yudkovsky, N., Ranish, J. A., & Hahn, S. (2000) · Nature · doi:10.1038/35041603 · Cited by 421
Recruitment of a 19 S Proteasome Subcomplex to an Activated Promoter
Gonzalez, F., Delahodde, A., Kodadek, T., & Johnston, S. A. (2002) · Science · doi:10.1126/science.1069490 · Cited by 338 · cited 1×
“Cross-linking studies showed that specific components of the 19S particle, but not the 20S proteolytic core, are recruited to transcriptionally active genes upon induction (Gonzalez et al. 2002).”
BackgroundGiannì, M., Bauer, A., Garattini, E., Chambon, P., & Rochette‐Egly, C. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf374 · Cited by 151
Cited by
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
Transcriptional architecture and chromatin landscape of the core circadian clock in mammals
Koike, N., Yoo, S.-H., Huang, H.-C., Kumar, V., Lee, C., Kim, T.-K., & Takahashi, J. S. (2012) · Science · doi:10.1126/science.1226339 · Cited by 1,464
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
Transcriptional Regulation by P53
Beckerman, R., & Prives, C. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000935 · Cited by 569
Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation
Edmunds, J. W., Mahadevan, L. C., & Clayton, A. L. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601967 · Cited by 547
H3K4me3 breadth is linked to cell identity and transcriptional consistency
Benayoun, B. A., Pollina, E. A., Ucar, D., Mahmoudi, S., Karra, K., Wong, E. D., Devarajan, K., Daugherty, A. C., Kundaje, A. B., Mancini, E., et al. (2014) · Cell · doi:10.1016/j.cell.2014.06.027 · Cited by 536
Blazek, D., Kohoutek, J., Bartholomeeusen, K., Johansen, E., Hulinkova, P., Luo, Z., Cimermancic, P., Ule, J., & Peterlin, B. M. (2011) · Genes & Development · doi:10.1101/gad.16962311 · Cited by 522
The human SWI/SNF subunit Brm is a regulator of alternative splicing
Batsché, E., Yaniv, M., & Muchardt, C. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1030 · Cited by 471
Remote control of gene transcription
West, A. G., & Fraser, P. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi104 · Cited by 302
Crosstalk between the glucocorticoid receptor and other transcription factors: Molecular aspects
Kassel, O., & Herrlich, P. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2007.07.003 · Cited by 277
DNAPKcs-dependent arrest of RNA polymerase II transcription in the presence of DNA breaks
Pankotai, T., Bonhomme, C., Chen, D., & Soutoglou, E. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2224 · Cited by 239
Molecular components of the circadian clock in mammals
Takahashi, J. S. (2015) · Diabetes, Obesity and Metabolism · doi:10.1111/dom.12514 · Cited by 230
Chromatin domains rich in inheritance
Reinberg, D., & Vales, L. D. (2018) · Science · doi:10.1126/science.aat7871 · Cited by 151
Self-citationSpt6 enhances the elongation rate of RNA polymerase II in vivo
Ardehali, M. B., Yao, J., Adelman, K., Fuda, N. J., Petesch, S. J., Webb, W. W., & Lis, J. T. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.56 · Cited by 157
The transition from transcriptional initiation to elongation
Wade, J. T., & Struhl, K. (2008) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2007.12.008 · Cited by 117
A new paradigm in eukaryotic biology: HIV Tat and the control of transcriptional elongation
Barboric, M., & Peterlin, B. M. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030076 · Cited by 106
Genomic mapping of RNA polymerase II reveals sites of co-transcriptional regulation in human cells
Brodsky, A. S., Meyer, C. A., Swinburne, I. A., Hall, G., Keenan, B. J., Liu, X. S., Fox, E. A., & Silver, P. A. (2005) · Genome Biology · doi:10.1186/gb-2005-6-8-r64 · Cited by 94
HIV-1 Tat recruits transcription elongation factors dispersed along a flexible AFF4 scaffold
Chou, S., Upton, H., Bao, K., Schulze-Gahmen, U., Samelson, A. J., He, N., Nowak, A., Lu, H., Krogan, N. J., Zhou, Q., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216971110 · Cited by 93
Schweikhard, V., Meng, C., Murakami, K., Kaplan, C. D., Kornberg, R. D., & Block, S. M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405181111 · Cited by 92
Ccr4-Not and TFIIS Function Cooperatively To Rescue Arrested RNA Polymerase II
Dutta, A., Babbarwal, V., Fu, J., Brunke-Reese, D., Libert, D. M., Willis, J., & Reese, J. C. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00044-15 · Cited by 61
Ishibashi, T., Dangkulwanich, M., Coello, Y., Lionberger, T. A., Lubkowska, L., Ponticelli, A. S., Kashlev, M., & Bustamante, C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401611111 · Cited by 55
Adult Stem Cells Exhibit Global Suppression of RNA Polymerase II Serine-2 Phosphorylation
Freter, R., Osawa, M., & Nishikawa, S.-I. (2010) · Stem Cells · doi:10.1002/stem.476 · Cited by 43
Sub1 associates with Spt5 and influences RNA polymerase II transcription elongation rate
García, A., Collin, A., & Calvo, O. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-04-0331 · Cited by 25
Role of Ordered Proteins in the Folding-Upon-Binding of Intrinsically Disordered Proteins
Lawrence, C. W., Kumar, S., Noid, W. G., & Showalter, S. A. (2014) · The Journal of Physical Chemistry Letters · doi:10.1021/jz402729x · Cited by 25
Metadata
- Authors
- Sims, R. J., Belotserkovskaya, R., & Reinberg, D.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2004-10-15
- Volume
- 18
- Issue
- 20
- Pages
- 2437-2468
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2022936085
- Cited by
- 709
- References
- 9
- Type
- posted content
- Language
- en
- Open access
- diamond
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
