The DOI matches its Crossref record; 159 of the 159 references it cites were found in a registry or an index.
The code and beyond: transcription regulation by the RNA polymerase II carboxy-terminal domain
Abstract
The carboxy-terminal domain (CTD) extends from the largest subunit of RNA polymerase II (Pol II) as a long, repetitive and largely unstructured polypeptide chain. Throughout the transcription process, the CTD is dynamically modified by post-translational modifications, many of which facilitate or hinder the recruitment of key regulatory factors of Pol II that collectively constitute the 'CTD code'. Recent studies have revealed how the physicochemical properties of the CTD promote phase separation in the presence of other low-complexity domains. Here, we discuss the intricacies of the CTD code and how the newly characterized physicochemical properties of the CTD expand the function of the CTD beyond the code.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“CDK8 inhibition by MSC2530818 did not alter the phosphorylation profile of RBP1, suggesting that our treatment did not affect basal transcriptional programs (Sup. Figure 9B)”
From CDK8 fine-tunes IL-6 transcriptional activities by limiting STAT3 resident time at the gene loci (2020) · cites this paper as Harlen and Churchman, 2017
Citations
Cites
Liquid-Liquid Phase Separation in Biology
Hyman, A. A., Weber, C. A., & Jülicher, F. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013325 · Cited by 3,155
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927
Widespread transcription at neuronal activity-regulated enhancers
Kim, T.-K., Hemberg, M., Gray, J. M., Costa, A. M., Bear, D. M., Wu, J., Harmin, D. A., Laptewicz, M., Barbara-Haley, K., Kuersten, S., et al. (2010) · Nature · doi:10.1038/nature09033 · Cited by 2,450
The economics of ribosome biosynthesis in yeast
Warner, J. R. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01460-7 · Cited by 1,933
Promoter-proximal pausing of RNA polymerase II: emerging roles in metazoans
Adelman, K., & Lis, J. T. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3293 · Cited by 1,221
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
Ng, H., Robert, F., Young, R. A., & Struhl, K. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00092-3 · Cited by 1,131
Komarnitsky, P. B., Cho, E., & Buratowski, S. (2000) · Genes & Development · doi:10.1101/gad.824700 · Cited by 1,098
Histone exchange, chromatin structure and the regulation of transcription
Venkatesh, S., & Workman, J. L. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3941 · Cited by 997
Burke, K. A., Janke, A. M., Rhine, C. L., & Fawzi, N. L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.006 · Cited by 932
Cited by
Sorted by citations
Items 401–500 of 506
Campbell, A. E., Aljabri, A. A., Hesketh, A. R., Byrne, D. P., Bennett, H. J., Patel, S., Brownridge, P., Zacharchenko, T., Bucca, G., Eyers, P. A., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.08.592654 · Cited by 1
A phosphorylation code coordinating transcription condensate dynamics with DNA replicationPreprint
Marmolejo, C. A. O., Sanchez, C., Lee, J., Werner, M., Roberts, P. A., Hamperl, S., & Saldivar, J. C. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.10.593572 · Cited by 1
Zhu, Y., Zhang, X., Gao, M., Huang, Y., Tan, Y., Parnas, A., Wu, S., Zhan, D., Adar, S., & Hu, J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.07.602436 · Cited by 1
Co-Transcriptional Rna Processing Boosts Zygotic Gene ActivationPreprint
Xu, J., Li, X., Hao, X., Hu, X., Ma, S., Hong, Y., Zhang, J., Yan, D., Deng, H., Na, J., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.14.613088 · Cited by 1
Identification of human RNA Polymerase II interactors at early stages of transcriptionPreprint
Ozer, A., Kang, J. J., Tang, Y., Yugandhar, K., Sun, Y., DeBerardine, M., Omar, K., Lis, J. T., & Yu, H. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.08.681243 · Cited by 1
RNA polymerase loss by nuclear rupture drives LMNA cardiomyopathyPreprint
En, A., Gucwa, M. E., Rapushi, E., Barnett, C. L., Katano, W., Nduka, N., Shiraki, T., Grogan, A., Finn, A. V., Weaver, K. N., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.03.716433 · Cited by 1
Monteiro, R. S., Sell, A. C., Emdal, K. B., Lundregan, S. L., Schuh, C. M., Raineri, S., Dossin, F., Heard, É., Olsen, J. V., & Brickman, J. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.11.744124 · Cited by 1
Multi-omics analysis of transcription kinetics in human cells
Gressel, S. (2019) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-7586
TIP60 acetylation of BMAL1 links positive and negative arms of the molecular circadian clock
Petkau, N. (2019) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-7765
Identification of novel RNA Polymerase II CTD interaction sites on the mRNA Capping EnzymePreprint
Bage, M., Almohammed, R., Cowling, V. H., & Pisliakov, A. V. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.25.964700
Multiple Roles of RNA Regulatory Factors in Neuronal Development and Function in C. elegans
Andrusiak, M. G., & Jin, Y. (2020) · Oxford University Press eBooks · doi:10.1093/oxfordhb/9780190686307.013.26
Garrido-Godino, A. I., Cuevas-Bermúdez, A., Gutiérrez-Santiago, F., Mota-Trujillo, M. D. C., & Navarro, F. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.23.424112
Elevated transcriptional pausing of RNA polymerase II underlies acquired resistance to radiotherapyPreprint
Liu, H., Yu, C., Zhang, N., Meng, Y., Huang, C., Hu, C., Chen, F., Xiao, Z., Zhang, Z., Shao, H., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.11.462362
Elevated pausing of RNA Polymerase II underlies acquired resistance to ionizing radiationPreprint
Yuan, K., Liu, H., Yu, C., Zhang, N., Meng, Y., Huang, C., Hu, C., Chen, F., Hu, X., & Zhang, Z. (2021) · Research Square · doi:10.21203/rs.3.rs-1036343/v1
Transcription | RNA Polymerase II and its General Transcription Factors
Corden, J. L. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00288-7
Bähler, J. (2021) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.738090468.793585332
Bioinformatics analysis of multi-omics data elucidates U2 snRNP function in transcription
Martins, S. (2021) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8741
A Moonlighting Function of Aldh18a1 Supports Pausing RNA Polymerase II in Promoter-Proximal RegionsPreprint
Rafiee, M., Rohban, S., Davey, K., Steinhauser, S., Krijgsveld, J., Ule, J., & Luscombe, N. M. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4087712
Yeast cleavage factor Hrp1 is a novel guard protein that surveils pre-mRNA 3’ processing
Li, J. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9233
Faculty Opinions recommendation of Organizational principles of 3D genome architecture.
Goll, M. G. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734288427.793573571
Sharrocks, A. D. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.735244406.793572348
Reines, D., & Hutchinson, K. M. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.737454031.793573396
Akusjärvi, G., & Punga, T. (2017) · Wiley eBooks · doi:10.1002/9780470015902.a0000875.pub3
Reines, D. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.736374697.793578917
Ceg1 depletion reveals mechanisms governing degradation of non-capped RNAsPreprint
Zanin, O., Hebenstreit, D., & Grzechnik, P. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.24.509330
Monteverde, T., Sahoo, S., Montagna, M. L., Magee, P., Shi, L., Lee, D. C. H., Sellers, R., Baker, A. R., Leong, H. S., Fassan, M., et al. (2023) · doi:10.1158/0008-5472.c.6513016
Chen, J. J., Moy, C., Pagé, V., Monnin, C., El‐Hajj, Z. W., Avizonis, D. Z., Reyes‐Lamothe, R., & Tanny, J. C. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.24.568120
Razin, S. V. (2024) · Postępy Biochemii · doi:10.18388/pb.2021_512
The Rtf1/Prf1-dependent histone modification axis counteracts multi-drug resistance in fission yeast
Chen, J. J., Moy, C., Pagé, V., Monnin, C., El‐Hajj, Z. W., Avizonis, D. Z., Reyes‐Lamothe, R., & Tanny, J. C. (2024) · Life Science Alliance · doi:10.26508/lsa.202302494
Structural and biochemical studies on chromatin-protein complexes in transcription initiation
Garrido, J. A. (2024) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-10412
Truncating the spliceosomal ‘rope protein’ Prp45 results in Htz1 dependent phenotypes
Abrhámová, K., Groušlová, M., Valentová, A., Hao, X., Liu, B., Převorovský, M., Gahura, O., Půta, F., Sunnerhagen, P., & Folk, P. (2024) · RNA Biology · doi:10.1080/15476286.2024.2348896 · Cited by 2
Ubiquitylation of RNA Polymerase II Controls Early Stages of the Transcription CyclePreprint
Cacioppo, R., Gillis, A., Shlamovitz, I., Zeller, A., Castiblanco, D., Crisp, A., Haworth, B., Arabiotorre, A., Abyaneh, P., Bao, Y., et al. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4826625
Rtr1 is Necessary for Ctd-Ser7 Phosphorylation in VivoPreprint
Garrido-Godino, A. I., Calvo, O., & Navarro, F. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4829103
Mkhize, Z. (2023) · ResearchSpace (University of KwaZulu-Natal) · doi:10.29086/10413/23002
NMR spectroscopy of liquid-liquid phase separation related to transcription
Lushpinskaia, I. P. (2024) · doi:10.53846/goediss-10514
Clustering of RNA Polymerase II C-Terminal Domain Models upon Phosphorylation
Amith, W. D., Chen, V. T., & Dutagaci, B. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.4c04457
Klapstova, V., Šedová, K., Houser, J., & Šebesta, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.22.634233
Kang, S. W., Tran, H. T., Lee, G., Ng, J., Lim, S. B., & Kim, E. Y. (2025) · iScience · doi:10.1016/j.isci.2025.112457
Intrinsically disordered bHLH family member TCF4 drives LLPS in a DNA-dependent mannerPreprint
Sozańska, N., Klepka, B. P., Niedźwiecka-Kornaś, A., Greb‐Markiewicz, B., Ożyhar, A., & Tarczewska, A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.18.660356
mRNA Modification and Processing
Roy, S. (2025) · Springer eBooks · doi:10.1007/978-981-96-6823-6_4
Cell signaling meets gene transcription
Young, R. A. (2025) · Science · doi:10.1126/science.aec1434
Koopman, A. J., Martin, A. J., Moore, L. G., Rodriguez, M., & Chase, P. B. (2025) · Macromol—A Journal of Macromolecular Research · doi:10.3390/macromol5040056
Rtr1 and RPAP2: versatile players in transcription and more
Garrido-Godino, A. I., & Navarro, F. (2025) · Transcription · doi:10.1080/21541264.2025.2592348
Klapstova, V., Šedová, K., Houser, J., & Šebesta, M. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.111010 · Cited by 1
Quantitative modeling of P-TEFb mediated CTD phosphorylation identifies local cooperativityPreprint
Callenbach, A., Dorešić, D., Düster, R., Nakonecnij, V., Dudkin, E., Geyer, M., & Hasenauer, J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.11.29.690978
Kompocholi, S., Stamidis, N., Liu, H., Hjortø, G. M., Kafkia, E., Ruidiaz, S. F., Miller, T. C. R., Żylicz, J. J., & Gregersen, L. H. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.08.691990
Cesari, E., Ciucci, A., Pieraccioli, M., Caggiano, C., Nero, C., Bonvissuto, D., Sillano, F., Buttarelli, M., Piermattei, A., Loverro, M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26590215
Cesari, E., Ciucci, A., Pieraccioli, M., Caggiano, C., Nero, C., Bonvissuto, D., Sillano, F., Buttarelli, M., Piermattei, A., Loverro, M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26590212
Kitamura, K., Suzuki, H., Abe, R., Inohara, H., Kaneda, Y., Takahashi, H., & Nimura, K. (2022) · Figshare · doi:10.6084/m9.figshare.20097923
Bejjani, F., Evanno, E., Mahfoud, S., Tolza, C., Zibara, K., Piechaczyk, M., & Jariel‐Encontre, I. (2024) · Figshare · doi:10.6084/m9.figshare.26604916
Cesari, E., Ciucci, A., Pieraccioli, M., Caggiano, C., Nero, C., Bonvissuto, D., Sillano, F., Buttarelli, M., Piermattei, A., Loverro, M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26590209
Bejjani, F., Evanno, E., Mahfoud, S., Tolza, C., Zibara, K., Piechaczyk, M., & Jariel‐Encontre, I. (2024) · Figshare · doi:10.6084/m9.figshare.26604925
Cesari, E., Ciucci, A., Pieraccioli, M., Caggiano, C., Nero, C., Bonvissuto, D., Sillano, F., Buttarelli, M., Piermattei, A., Loverro, M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26590218
Bejjani, F., Evanno, E., Mahfoud, S., Tolza, C., Zibara, K., Piechaczyk, M., & Jariel‐Encontre, I. (2024) · Figshare · doi:10.6084/m9.figshare.26604922
Bejjani, F., Evanno, E., Mahfoud, S., Tolza, C., Zibara, K., Piechaczyk, M., & Jariel‐Encontre, I. (2024) · Figshare · doi:10.6084/m9.figshare.26604919
Bejjani, F., Evanno, E., Mahfoud, S., Tolza, C., Zibara, K., Piechaczyk, M., & Jariel‐Encontre, I. (2024) · Figshare · doi:10.6084/m9.figshare.26604931
Bejjani, F., Evanno, E., Mahfoud, S., Tolza, C., Zibara, K., Piechaczyk, M., & Jariel‐Encontre, I. (2024) · Figshare · doi:10.6084/m9.figshare.26604928
Du, X., Qin, W., Yang, C., Dai, L., San, M., Xia, Y., Zhou, S., Wang, M., Wu, S., Zhang, S., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26708906
Du, X., Qin, W., Yang, C., Dai, L., San, M., Xia, Y., Zhou, S., Wang, M., Wu, S., Zhang, S., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26708903
Du, X., Qin, W., Yang, C., Dai, L., San, M., Xia, Y., Zhou, S., Wang, M., Wu, S., Zhang, S., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26708900
Bejjani, F., Evanno, E., Mahfoud, S., Tolza, C., Zibara, K., Piechaczyk, M., & Jariel‐Encontre, I. (2024) · Figshare · doi:10.6084/m9.figshare.26604913
Oravecz, A., Tassy, O., Conic, S., Oulad‐Abdelghani, M., Molina, N., & Tora, L. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.19.695093
Liang, J., & Itkonen, H. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.27.701921
Divergent condensates tune transcriptional responses during stressPreprint
Dudley, J. N., Berends, J. E., De, C. K., He, T., Veronezi, G. M. B., Abdon, B., Sengar, A., Truttmann, M. C., Ljungman, M. E., Xiao, L., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.12.705659 · Cited by 2
Chromatin Addiction in NUT Carcinoma: Targeted Epigenetic Pharmacology Beyond BET Inhibition
Wankhade, P. P., Ghorpade, O. P., Kokane, O. S., Ganjpure, U. N., & Dhonde, P. S. (2026) · Journal of Drug Delivery and Therapeutics · doi:10.22270/jddt.v16i3.7640
Characterization of the mechanisms of transcription termination by the helicase Sen1
Han, Z. (2017) · theses.fr (ABES) · doi:10.70675/9ac97a11zb0bcz4cfczbde4z88dd45c6bb86
Hocquet, C. (2018) · theses.fr (ABES) · doi:10.70675/bfcf9f26ze4d1z4c3az86d1z0d684417d4b5
Real time imaging of transcription reveals new features of cellular and viral promoters
Kozulic-Pirher, A. (2018) · theses.fr (ABES) · doi:10.70675/0099e36bz620ez43d7z9b47z2789ed360d73
Role of general regulatory factors in the control of gene expression and transcription fidelity
Challal, D. (2019) · theses.fr (ABES) · doi:10.70675/0e32ea04zece7z4ac4z98dfz1a8e229249b7
Contrôle de l'expression génique par la RNP 7SK
Studniarek, C. (2019) · theses.fr (ABES) · doi:10.70675/4bab1779z812bz45d6zbcd4z9eea765b52e7
FragLite mapping to identify the BRD4 recruitment site of P-TEFbPreprint
Hope, I., Heath, R., Baslé, A., Martin, M. P., Waring, M. J., Endicott, J., Noble, M. E. M., & Tatum, N. J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.09.717428 · Cited by 1
RLF/ZFP292 stabilize CoREST-linked LSD1 engagement at bivalent promoters to safeguard pluripotency
Ito, T., Yoshino, M., Isobe, S.-Y., & Obuse, C. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117293
HSF2-HSP110 axis supports genome stability via RNA polymerase II transcription and DNA repair
Jin, X., Xi, C., Pandya, B., Pang, J., Fuentes, D. A. F., Eroglu, B., Moskophidis, D., & Mivechi, N. F. (2026) · The Journal of Cell Biology · doi:10.1083/jcb.202508059
Intrinsically disordered bHLH family member TCF4 drives phase separation in a DNA-dependent manner
Sozańska, N., Klepka, B. P., Niedzwiecka, A., Greb‐Markiewicz, B., Ożyhar, A., & Tarczewska, A. (2026) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2026.110829
RNA-binding proteins activate transcription through defined molecular grammarsPreprint
Wang, H., Phillips, L., Moore-Frederick, D., Webster, B. K., Xu, D., Srivastava, S., Mowry, G., Wang, E., Banka, A., Deng, C., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.29.728737
Shibuta, M. K., Komatsu, A., & Aso, T. (2026) · Plant Direct · doi:10.1002/pld3.70175
Discovery of CTX-439: A Potent and Selective CDK12 Inhibitor as a Prospective Anti-Cancer Drug
Shimokawa, K., Ono, K., Asano, M., Hirayama, T., Tokuhara, H., Tanaka, T., Banno, H., Sakauchi, N., Hirata, Y., Fujimoto, J., et al. (2026) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.6c00138
RNA polymerase II phosphorylation dynamics: from molecular mechanisms to human disease
González-Jiménez, A., Medina, I., Alfonso-Pérez, M., de Aldana, C. R. V., & Calvo, O. (2026) · RNA Biology · doi:10.1080/15476286.2026.2695549
Origin and Evolution of Transcription Elongation Complexes
Osina, E. V., Korovina, A. N., Gerasimova, N. S., Sokolova, O. S., & Stanishneva-Konovalova, T. B. (2026) · BIOPHYSICS · doi:10.1134/s0006350926700041
Madheshiya, P., Henry, S., Chen, X., Doak, N., Gierke, T. R., Tang, S., Wang, J., & Didychuk, A. L. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.29.734287
Quantitative modelling of P-TEFb mediated CTD phosphorylation identifies local cooperativity
Callenbach, A., Dorešić, D., Düster, R., Nakonecnij, V., Dudkin, E., Geyer, M., & Hasenauer, J. (2026) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1014531
Okuda, M., Yoshimura, Y., Hayashi, A., Nakayama, J., & Nishimura, Y. (2026) · Journal of Molecular Biology · doi:10.1016/j.jmb.2026.169965
Zhang, Y., & Ramsey, E. (2026) · Biochemical Society Transactions · doi:10.1042/bst20250032
Hu, R., Usher, E. T., Fraser, O. A., Chen, W., Holehouse, A. S., & Showalter, S. A. (2026) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6c03886
Transcriptional kinases drive gene expression network plasticity
Lowe, D. D., & Shilatifard, A. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.07.035
Targeting CDKs in the RNAPII transcription cycle
Fisher, R. P., & Geyer, M. (2026) · Nature Reviews Drug Discovery · doi:10.1038/s41573-026-01517-0
Fong, N., Huynh, N., Erickson, B., Sheridan, R. M., Ramachandran, S., van der Schaar, M., & Bentley, D. L. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.18.752771
A guide to transcriptional cyclin‐dependent kinases in cancer
Devlin, J. R., Kyheröinen, S., & Johnstone, R. W. (2026) · FEBS Journal · doi:10.1111/febs.70731
How do low-complexity domain interactions control transcription?
Guo, J., Han, Q., Nagashima, K., & Chong, S. (2026) · Biochemical Society Transactions · doi:10.1042/bst20250199
Protein arginine methylation rewires molecular interactions
DeAngelo, J. D., Silverstein, A. M., & Shechter, D. (2026) · Cell chemical biology · doi:10.1016/j.chembiol.2026.09.011
Metadata
- Authors
- Harlen, K. M., & Churchman, L. S.
- Affiliations
- Harvard University (US)
- Corresponding author
- Churchman, L. Stirling
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2017-03-01
- Volume
- 18
- Issue
- 4
- Pages
- 263-273
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2594707272
- Cited by
- 499
- References
- 159
- Citations by year
- 2026: 40 · 2025: 46 · 2024: 70 · 2023: 65 · 2022: 51 · 2021: 66 · 2020: 65 · 2019: 44 · 2018: 35 · 2017: 17
- FWCI
- 4.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Human Genome Research Institute (R01HG007173)
- 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, C-terminal domain, post-translational modification, transcriptional regulation, phase separation, low-complexity domains
- MeSH terms
- Protein Domains, Gene Expression Regulation, Humans, Phosphorylation, Protein Processing, Post-Translational, RNA Polymerase II, Transcription, Genetic
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