CDK13 cooperates with CDK12 to control global RNA polymerase II processivity

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Inactivation of CDK12 Delineates a Distinct Immunogenic Class of Advanced Prostate Cancer

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The cyclin K/Cdk12 complex maintains genomic stability via regulation of expression of DNA damage response genes

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Quantitative ChIP-Seq normalization reveals global modulation of the epigenome

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

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

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Covalent targeting of remote cysteine residues to develop CDK12 and CDK13 inhibitors

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Genome-wide profiling of genetic synthetic lethality identifies CDK12 as a novel determinant of PARP1/2 inhibitor sensitivity

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CDK12 regulates DNA repair genes by suppressing intronic polyadenylation

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Pre-mRNA splicing is facilitated by an optimal RNA polymerase II elongation rate

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CDK12 loss in cancer cells affects DNA damage response genes through premature cleavage and polyadenylation

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Widespread intronic polyadenylation inactivates tumour suppressor genes in leukaemia

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Ovarian Cancer-associated Mutations Disable Catalytic Activity of CDK12, a Kinase That Promotes Homologous Recombination Repair and Resistance to Cisplatin and Poly(ADP-ribose) Polymerase Inhibitors

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UV Irradiation Induces a Non-coding RNA that Functionally Opposes the Protein Encoded by the Same Gene

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

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The structure and substrate specificity of human Cdk12/Cyclin K

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EWS/FLI confers tumor cell synthetic lethality to CDK12 inhibition in Ewing sarcoma

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CDK12 regulates alternative last exon mRNA splicing and promotes breast cancer cell invasion

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Transcriptional Control by Premature Termination: A Forgotten Mechanism

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Structural and functional analysis of the Cdk13/Cyclin K complex

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Cdk7: a kinase at the core of transcription and in the crosshairs of cancer drug discovery

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CDK9 inhibition by dinaciclib potently suppresses Mcl-1 to induce durable apoptotic responses in aggressive MYC-driven B-cell lymphoma in vivo

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The CDK9 Inhibitor Dinaciclib Exerts Potent Apoptotic and Antitumor Effects in Preclinical Models of MLL-Rearranged Acute Myeloid Leukemia

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CDK12 controls G1/S progression by regulating RNAPII processivity at core DNA replication genes

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RNA Polymerase II transcription elongation and Pol II CTD Ser2 phosphorylation

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Human CDK12 and CDK13, multi-tasking CTD kinases for the new millenium

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Therapeutic targeting of transcriptional cyclin-dependent kinases

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Frequent Amplification of CENPF, GMNN and CDK13 Genes in Hepatocellular Carcinomas

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PAT-seq: a method to study the integration of 3′-UTR dynamics with gene expression in the eukaryotic transcriptome

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The emerging roles of CDK12 in tumorigenesis

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Transcriptional elongation checkpoint control in development and diseasePreprint

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Cyclin-Dependent Kinase 12 Increases 3′ End Processing of Growth Factor-Induced c-FOS Transcripts

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Cyclin-Dependent Kinase-9 Is a Therapeutic Target in MYC-Expressing Diffuse Large B-Cell Lymphoma

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Expression, Purification, and Identification of Associated Proteins of the Full-length hCDK12/CyclinK Complex

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Intronic cleavage and polyadenylation regulates gene expression during DNA damage response through U1 snRNA

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Engineering an analog-sensitive CDK12 cell line using CRISPR/Cas

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Heterozygous mutations affecting the protein kinase domain of <i>CDK13</i> cause a syndromic form of developmental delay and intellectual disability

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Targeting the epigenetic regulation of antitumour immunity

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Context-specific regulation and function of mRNA alternative polyadenylation

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Cyclin-dependent protein kinases and cell cycle regulation in biology and disease

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CDK12 loss in cancer cells affects DNA damage response genes through premature cleavage and polyadenylation

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Causes and consequences of RNA polymerase II stalling during transcript elongation

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RNA polymerase II speed: a key player in controlling and adapting transcriptome composition

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Targeting transcription cycles in cancer

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Discovery and resistance mechanism of a selective CDK12 degrader

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Targeting CDK9 for Anti-Cancer Therapeutics

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Nanoparticle single-cell multiomic readouts reveal that cell heterogeneity influences lipid nanoparticle-mediated messenger RNA delivery

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CDK9 keeps RNA polymerase II on track

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Discovery of a Highly Potent and Selective Dual PROTAC Degrader of CDK12 and CDK13

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CDK13 promotes lipid deposition and prostate cancer progression by stimulating NSUN5-mediated m5C modification of ACC1 mRNA

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Noncovalent CDK12/13 dual inhibitors-based PROTACs degrade CDK12-Cyclin K complex and induce synthetic lethality with PARP inhibitor

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Selective inhibition of CDK7 reveals high-confidence targets and new models for TFIIH function in transcriptionPreprint

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Relocalizing transcriptional kinases to activate apoptosis

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Oncogenic CDK13 mutations impede nuclear RNA surveillance

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Live imaging of transcription sites using an elongating RNA polymerase II–specific probe

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The Promise and Current Status of CDK12/13 Inhibition for the Treatment of Cancer

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Dual Inhibition of CDK12/CDK13 Targets Both Tumor and Immune Cells in Ovarian Cancer

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CDK7 kinase activity promotes RNA polymerase II promoter escape by facilitating initiation factor release

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Dual inhibition of CDK12 and CDK13 uncovers actionable vulnerabilities in patient-derived ovarian cancer organoids

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The CDK12 inhibitor SR-4835 functions as a molecular glue that promotes cyclin K degradation in melanoma

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Cyclin-dependent kinase inhibitors in head and neck cancer and glioblastoma—backbone or add-on in immune-oncology?

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Oncogenic dysregulation of pre‐mRNA processing by protein kinases: challenges and therapeutic opportunities

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Cyclin‐dependent kinases: Masters of the eukaryotic universe

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CDK12 loss drives prostate cancer progression, transcription-replication conflicts, and synthetic lethality with paralog CDK13

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The PAF1 complex promotes 3′ processing of pervasive transcripts

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CDK12 and Integrator-PP2A complex modulates LEO1 phosphorylation for processive transcription elongation

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CDK12/13 promote splicing of proximal introns by enhancing the interaction between RNA polymerase II and the splicing factor SF3B1

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Inhibition of pyrimidine biosynthesis targets protein translation in acute myeloid leukemia

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CDK12 controls transcription at damaged genes and prevents MYC-induced transcription-replication conflicts

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Nuclear mRNA decay: regulatory networks that control gene expression

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Chemical inhibitors of transcription-associated kinases

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Age or lifestyle-induced accumulation of genotoxicity is associated with a length-dependent decrease in gene expression

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Targeting CDKs in cancer therapy: advances in PROTACs and molecular glues

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CKAP2L Promotes Non–Small Cell Lung Cancer Progression through Regulation of Transcription Elongation

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The phosphatase PP1 sustains global transcription by promoting RNA polymerase II pause release

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Cis-acting lnc-eRNA SEELA directly binds histone H4 to promote histone recognition and leukemia progression

Fang, K., Huang, W., Sun, Y., Chen, T.-Q., Zeng, Z., Yang, Q., Pan, Q., Han, C., Sun, L.-Y., Luo, X., et al. (2020) · Genome biology · doi:10.1186/s13059-020-02186-x · Cited by 26 · see citing works

Current progress and novel strategies that target CDK12 for drug discovery

Lei, P., Zhang, J., Liao, P., Ren, C., Wang, J., & Wang, D. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114603 · Cited by 26 · see citing works

Nuclear speckleopathies: developmental disorders caused by variants in genes encoding nuclear speckle proteins

Regan, K., & Izumi, K. (2023) · Human Genetics · doi:10.1007/s00439-023-02540-6 · Cited by 26 · see citing works

Targeting pre-mRNA splicing in cancers: roles, inhibitors, and therapeutic opportunities

Araki, S., Ohori, M., & Yugami, M. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1152087 · Cited by 27 · see citing works

Development of an orally bioavailable CDK12/13 degrader and induction of synthetic lethality with AKT pathway inhibition

Chang, Y., Wang, X., Yang, J., Tien, J. C.-Y., Mannan, R., Cruz, G., Zhang, Y., Vo, J. N., Magnuson, B., Mahapatra, S., et al. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2024.101752 · Cited by 24 · see citing works

CRL3ARMC5 ubiquitin ligase and Integrator phosphatase form parallel mechanisms to control early stages of RNA Pol II transcription

Cacioppo, R., Gillis, A., Shlamovitz, I., Zeller, A., Castiblanco, D., Crisp, A., Haworth, B., Arabiotorre, A., Abyaneh, P., Bao, Y., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.11.024 · Cited by 23 · see citing works

CDK13-related disorder: Report of a series of 18 previously unpublished individuals and description of an epigenetic signature

Rouxel, F., Relator, R., Kerkhof, J., McConkey, H., Levy, M. A., Dias, P., Barat‐Houari, M., Bednarek, N., Boute, O., Chatron, N., et al. (2022) · Genetics in Medicine · doi:10.1016/j.gim.2021.12.016 · Cited by 23 · see citing works

Regulation of gene expression by alternative polyadenylation in health and disease

Tian, B., Yu, S., & Zhang, Q. (2026) · Nature Reviews Genetics · doi:10.1038/s41576-025-00928-w · Cited by 23 · see citing works

CDK13 phosphorylates the translation machinery and promotes tumorigenic protein synthesis

Wu, C., Xie, T., Guo, Y., Wang, D., Qiu, M., Han, R., Qing, G., Liang, K.-W., & Liu, H.-D. (2023) · Oncogene · doi:10.1038/s41388-023-02653-2 · Cited by 21 · see citing works

PAF1C-mediated activation of CDK12/13 kinase activity is critical for CTD phosphorylation and transcript elongation

(2025) · doi:10.1016/j.molcel.2025.04.012 · Cited by 21 · see citing works

Imaging transcription elongation dynamics by new technologies unveils the organization of initiation and elongation in transcription factories

Kimurâ, H., & Sato, Y. (2022) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2022.01.002 · Cited by 19 · see citing works

Emerging roles of cyclin-dependent kinase 7 in health and diseases

Belew, M. D., Chen, J., & Cheng, Z. (2024) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2024.09.004 · Cited by 19 · see citing works

Acute BRCAness induction and AR pathway blockage through CDK12/7/9 degradation enhances PARP inhibitor sensitivity in prostate cancer

Gui, F., Jiang, B., Jiang, J., He, Z., Tsujino, T., Takai, T., Arai, S., Pana, C., Köllermann, J. W., Bradshaw, G. A., et al. (2025) · Science Advances · doi:10.1126/sciadv.adu0847 · Cited by 20 · see citing works

SETD1A regulates transcriptional pause release of heme biosynthesis genes in leukemia

Hoshii, T., Perlee, S. C., Kikuchi, S., Rahmutulla, B., Fukuyo, M., Masuda, T., Ohtsuki, S., Soga, T., Nabet, B., & Kaneda, A. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111727 · Cited by 18 · see citing works

Coming of Age: Targeting Cyclin K in Cancers

Xiao, Y., & Dong, J. (2023) · Cells · doi:10.3390/cells12162044 · Cited by 18 · see citing works

Cooperative regulation of coupled oncoprotein synthesis and stability in triple-negative breast cancer by EGFR and CDK12/13

Ang, H. X., Sutiman, N., Deng, X. L., Liu, A., Cerda-Smith, C. G., Hutchinson, H. M., Kim, H., Bartelt, L. C., Chen, Q., Barrera, A., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2221448120 · Cited by 17 · see citing works

The reversible inhibitor SR-4835 binds Cdk12/cyclin K in a noncanonical G-loop conformation

Schmitz, M., Kaltheuner, I. H., Anand, K., Düster, R., Moecking, J., Monastyrskyi, A., Duckett, D. R., Roush, W. R., & Geyer, M. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105501 · Cited by 19 · see citing works

Transcription by RNA polymerase II and the CTD-chromatin crosstalk

Singh, N., Asalam, M., Ansari, M. O., Gerasimova, N. S., Studitsky, V. M., & Akhtar, M. S. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.02.039 · Cited by 18 · see citing works

MYC up-regulation confers vulnerability to dual inhibition of CDK12 and CDK13 in high-risk Group 3 medulloblastoma

Pitolli, C., Marini, A., Guerra, M., Pieraccioli, M., Marabitti, V., Palluzzi, F., Giacò, L., Tamburrini, G., Cecconi, F., Nazio, F., et al. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02790-2 · Cited by 16 · see citing works

HIV-1 Nef interacts with the cyclin K/CDK13 complex to antagonize SERINC5 for optimal viral infectivity

Chai, Q., Li, S., Collins, M. K., Li, R., Ahmad, I., Johnson, S. F., Frabutt, D. A., Yang, Z., Shen, X., Sun, L., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109514 · Cited by 17 · see citing works

Integrative Studies of Human Cord Blood Derived Mononuclear Cells and Umbilical Cord Derived Mesenchyme Stem Cells in Ameliorating Bronchopulmonary Dysplasia

Chen, J., Chen, Y., Du, X., Liu, G., Fei, X., Peng, J. R., Zhang, X. Y., Xiao, F., Wang, X. B., Yang, X. H., et al. (2020) · Frontiers in Cell and Developmental Biology · doi:10.2139/ssrn.3746264 · Cited by 17 · see citing works

CDK13-Mediated Cell Cycle Disorder Promotes Tumorigenesis of High HMGA2 Expression Gastric Cancer

Wu, Z., Wang, M., Li, F., Wang, F., Jia, J., Feng, Z., Huo, X., Yang, J., Wen, J., Sa, R., et al. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.707295 · Cited by 16 · see citing works

Targeting the Heterogeneous Genomic Landscape in Triple-Negative Breast Cancer through Inhibitors of the Transcriptional Machinery

van der Noord, V. E., van de Water, B., & Dévédec, S. E. L. (2022) · Cancers · doi:10.3390/cancers14184353 · Cited by 17 · see citing works

RBM22 regulates RNA polymerase II 5′ pausing, elongation rate, and termination by coordinating 7SK-P-TEFb complex and SPT5

Du, X., Qin, W., Yang, C., Dai, L., San, M., Xia, Y., Zhou, S., Wang, M., Wu, S., Zhang, S., et al. (2024) · Genome biology · doi:10.1186/s13059-024-03242-6 · Cited by 16 · see citing works

Reciprocal Links between Pre-messenger RNA 3′-End Processing and Genome Stability

Dutertre, M., Sfaxi, R., & Vagner, S. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.01.009 · Cited by 15 · see citing works

Control of non-productive RNA polymerase II transcription via its early termination in metazoans

Rouvière, J. O., Lykke‐Andersen, S., & Jensen, T. H. (2022) · Biochemical Society Transactions · doi:10.1042/bst20201140 · Cited by 15 · see citing works

CDK12/13 inactivation triggers STING-mediated antitumor immunity in preclinical models

Bao, Y., Chang, Y., Tien, J., Cruz, G., Yang, F., Mannan, R., Mahapatra, S., Paturu, R., Cao, X.-H., Su, F.-Y., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci193745 · Cited by 9 · see citing works

Research progress of anticancer drugs targeting CDK12

Yan, Z., Du, Y., Zhang, H., Zheng, Y., Lv, H., Dong, N., & He, F. (2023) · RSC Medicinal Chemistry · doi:10.1039/d3md00004d · Cited by 13 · see citing works

Poly(A) tale: From A to A; RNA polyadenylation in prokaryotes and eukaryotes

Mofayezi, A., Jadaliha, M., Zangeneh, F., & Khoddami, V. (2024) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1837 · Cited by 12 · see citing works

Discovery and design of molecular glue enhancers of CDK12–DDB1 interactions for targeted degradation of cyclin K

Ghosh, P., Schmitz, M., Pandurangan, T., Tadesse, S., Chan, S. C., Mosior, J., Sun, L., Palve, V. C., Grassie, D., Anand, K., et al. (2024) · RSC Chemical Biology · doi:10.1039/d4cb00190g · Cited by 12 · see citing works

Transcriptional and epigenetic rewiring by the NUP98::KDM5A fusion oncoprotein directly activates CDK12

Troester, S., Eder, T., Wukowits, N., Piontek, M., Fernández‐Pernas, P., Schmoellerl, J., Haladik, B., Manhart, G., Allram, M., Maurer‐Granofszky, M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59930-9 · Cited by 11 · see citing works

Oxidative stress induces Ser 2 dephosphorylation of the RNA polymerase II CTD and premature transcription termination

Yamazaki, T., Liu, L., & Manley, J. L. (2021) · Transcription · doi:10.1080/21541264.2021.2009421 · Cited by 12 · see citing works

Structural Mass Spectrometry Probes the Inhibitor-Induced Allosteric Activation of CDK12/CDK13-Cyclin K Dissociation

Bai, Y., Liu, Z., Li, Y., Zhao, H., Lai, C., Zhao, S., Chen, K., Luo, C., Yang, X., & Wang, F. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c01697 · Cited by 12 · see citing works

A CDK11-dependent RNA polymerase II pause-checkpoint precedes CDK9-mediated transition to transcriptional elongation.

Devlin, J., Martin, B., Bartonicek, N., Ting, K. E., Fan, Z., Todorovski, I., Bjelosevic, F., Verschoor, S., Ciccone, A., Trapani, J. A., et al. (2025) · Molecules and Cells · doi:10.1016/j.molcel.2025.08.001 · Cited by 10 · see citing works

A role for human senataxin in contending with pausing and backtracking during transcript elongation

Han, Z., Fu, S., Johansen, J. V., Martínez, D. L., Lou, J., Boissière, T., He, D., Blears, D., Olthof, A. M., Dirac-Svejstrup, A. B., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.10.019 · Cited by 11 · see citing works

Defining CDK12 as a tumor suppressor and therapeutic target in mouse models of tubo-ovarian high-grade serous carcinoma

Tien, J. C.-Y., Zhai, Y., WU, R. T., Zhang, Y., Chang, Y., Cheng, Y., Todd, A. J., Wheeler, C. E., Li, S., Mannan, R., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2426909122 · Cited by 11 · see citing works

Global control of RNA polymerase II

Gillis, A., & Berry, S. M. (2024) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2024.195024 · Cited by 10 · see citing works

Targeting transcriptional regulators for treatment of anaplastic thyroid cancer

Lee, W. K. (2021) · Journal of Cancer Metastasis and Treatment · doi:10.20517/2394-4722.2021.58 · Cited by 11 · see citing works

Inhibition of CDK12 elevates cancer cell dependence on P-TEFb by stimulation of RNA polymerase II pause release

Wang, Z., Himanen, S. V., Haikala, H. M., Friedel, C. C., Vihervaara, A., & Barborič, M. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad792 · Cited by 11 · see citing works

Discovery of small molecule degraders for modulating cell cycle

Wang, L., Yang, Z., Li, G., Liu, Y., Ai, C., & Rao, Y. (2023) · Frontiers of Medicine · doi:10.1007/s11684-023-1027-5 · Cited by 10 · see citing works

Physiological and pathological roles of the transcriptional kinases CDK12 and CDK13 in the central nervous system

Pitolli, C., Marini, A., Sette, C., & Pagliarini, V. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01413-3 · Cited by 10 · see citing works

HIV-1 virological synapse formation enhances infection spread by dysregulating Aurora Kinase B

Bruce, J. W., Park, E., Magnano, C. S., Horswill, M. A., Richards, A., Potts, G. K., Hebert, A. S., Islam, N., Coon, J. J., Gitter, A., et al. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011492 · Cited by 10 · see citing works

Analysis of CDK12 alterations in a pan‐cancer database

Pan, E., Cabal, A., Javier-DesLoges, J. F., Patel, D. N., Panian, J. A., Lee, S., Shaya, J. A., Nonato, T. K., Xu, X., Stewart, T. F., et al. (2021) · Cancer Medicine · doi:10.1002/cam4.4483 · Cited by 9 · see citing works

Olfactomedin 4 regulates migration and proliferation of immortalized non-transformed keratinocytes through modulation of the cell cycle machinery and actin cytoskeleton remodelling

Cárdenas‐León, C. G., Klaas, M., Mäemets‐Allas, K., Arak, T., Eller, M., & Jaks, V. (2022) · Experimental Cell Research · doi:10.1016/j.yexcr.2022.113111 · Cited by 10 · see citing works

Mapping Cophosphoregulation Networks Linked to Transcriptional Regulator Bromodomain-Containing Protein 4

Lalu, A. C., Lubaba, F., Gopalakrishnan, A. P., Mahin, A., Subair, S., Shivamurthy, P. B., Rajeev, A. C., & Raju, R. (2025) · DNA and Cell Biology · doi:10.1089/dna.2025.0088 · Cited by 9 · see citing works

Exploiting targeted degradation of cyclins and cyclin-dependent kinases for cancer therapeutics: a review

Zheng, S., Chen, Y., Zhu, Z., Li, N., He, C., Koeffler, H. P., Han, X., Wei, Q., & Xu, L. (2025) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2500021 · Cited by 9 · see citing works

CDK7–CDK11 axis in spliceosome regulation and pre-mRNA splicing

Rájecký, M., Gajdušková, P., Maník, P., Hluchý, M., Hegedűsová, E., Kryštofová, K., Potěšil, D., Martínková, P., Slabá, Z., Khirsariya, P., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1343 · Cited by 9 · see citing works

Stable CDK12 Knock-Out Ovarian Cancer Cells Do Not Show Increased Sensitivity to Cisplatin and PARP Inhibitor Treatment

Chilà, R., Chiappa, M., Guffanti, F., Panini, N., Conconi, D., Rinaldi, A., Cascione, L., Bertoni, F., Fratelli, M., & Damia, G. L. M. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.903536 · Cited by 9 · see citing works

RPRD1B's direct interaction with phosphorylated RNA polymerase II regulates polyadenylation of cell cycle genes and drives cancer progression

Moreno, R. Y., Panina, S., & Zhang, Y. (2025) · RSC Chemical Biology · doi:10.1039/d4cb00212a · Cited by 8 · see citing works

Targeting Super-Enhancer–Driven Transcriptional Dependencies Suppresses Aberrant Hedgehog Pathway Activation and Overcomes Smoothened Inhibitor Resistance

Sui, Y., Wang, T., Mei, Y., Zhu, Y., Jiang, W., Shen, J., Yan, S., Lu, W., Zhao, K., Mo, J., et al. (2024) · Cancer Research · doi:10.1158/0008-5472.can-23-3306 · Cited by 9 · see citing works

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 · see citing works

Cdk12 Maintains the Axon Initial Segment Through Actin Remodeling

Townsend, L., Lucas-Clarke, H. J., Maddison, D. C., Jones, K., Amadio, L., Jefferson, A., Chughtai, U., Bis‐Brewer, D. M., Zuchner, S. L., Allen, N. D., et al. (2022) · Cell Death Discovery · doi:10.1038/s41420-023-01642-4 · Cited by 8 · see citing works

Phosphoproteomics Meets Chemical Genetics: Approaches for Global Mapping and Deciphering the Phosphoproteome

Jurcik, J., Siváková, B., Čipáková, I., Selicky, T., Stupenova, E., Jurcik, M., Osadská, M., Baráth, P., & Čipák, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207637 · Cited by 8 · see citing works

Roles of CDK12 mutations in PCa development and treatment

Jiang, C., Hong, Z., Liu, S., Hong, Z., & Dai, B. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189247 · Cited by 7 · see citing works

AR-A014418 regulates intronic polyadenylation and transcription of PD-L1 through inhibiting CDK12 and CDK13 in tumor cells

Zhang, G., Lan, B., Zhang, X., Lin, M., Liu, Y., Chen, J. S., & Guo, F. (2023) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2022-006483 · Cited by 7 · see citing works

Targeting CDK12 disrupts estrogen-receptor chromatin recruitment and ER-MED1 transcription in advanced ER+ breast cancer

Ottaviani, D., Ola, M., Allotta, A., Chaibi, Y. M., Hickey, S., Jagušt, P., Cosgrove, N. S., Cocchiglia, S., Bane, F. T., Fallon, R., et al. (2025) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djaf295 · Cited by 6 · see citing works

Therapeutic Discovery for Chromatin Complexes: Where Do We Stand?

Owens, D. D. G., Maitland, M. E. R., Arrowsmith, C. H., & Baršytė-Lovejoy, D. (2024) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-062822-110356 · Cited by 7 · see citing works

Chemical genetics reveals Leishmania KKT2 and CRK9 kinase activity is required for cell cycle progression

Carnielli, J. B. T., Brannigan, J. A., Jones, N. G., Ramos, P. Z., Couñago, R. M., Sjö, P., Lima, A. P. C. A., Wilkinson, A. J., & Mottram, J. C. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1014194 · Cited by 6 · see citing works

CDK12 /13 dual inhibitors are potential therapeutics for acute myeloid leukemia

Savoy, L., Long, N., Lee, H., Chen, R., Allen, B., Lin, H., Tognon, C. E., Malhotra, S. V., Tyner, J. W., & Zhang, H. (2023) · British Journal of Haematology · doi:10.1111/bjh.18843 · Cited by 6 · see citing works

Phosphorylation of SF3B1 by CDK11 orchestrates spliceosome activation via SNIP1-dependent RES complex recruitment

Gajdušková, P., Mozos, I. R. D. L., Hluchý, M., Myšková, A., Zábrady, K., Maník, P., Dragišić, N., Hanáková, K., Potěšil, D., Bologna, S., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-71119-2 · Cited by 5 · see citing works

Trans-Regulation of Alternative PD-L1 mRNA Processing by CDK12 in Non-Small-Cell Lung Cancer Cells

Larsen, T. V., Maansson, C. T., Daugaard, T. F., Andresen, B. S., Sørensen, B. S., & Nielsen, A. L. (2023) · Cells · doi:10.3390/cells12242844 · Cited by 5 · see citing works

CDK12 is a promising therapeutic target for the transcription cycle and DNA damage response in metastatic osteosarcoma

Li, Z., Li, X., Seebacher, N. A., Liu, X., Wu, W., Yu, S., Hornicek, F. J., Huang, C., & Duan, Z. (2024) · Carcinogenesis · doi:10.1093/carcin/bgae051 · Cited by 5 · see citing works

CDK12 and CDK13 cooperatively regulate RNA polymerase II elongation and alternative polyadenylation of mRNA

Fan, Z. (2020) · Minerva Access (University of Melbourne)

CDK12 globally stimulates RNA polymerase II transcription elongation and carboxyl-terminal domain phosphorylation

Tellier, M., Zaborowska, J., Caizzi, L., Mohammad, E., Velychko, T., Schwalb, B., Vicens, I. F., Blears, D., Nojima, T., Cramer, P., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa514 · Cited by 101 · see citing works

Article of Significant Interest Selected from This Issue by the Editors

(2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00099-15

CDK11 activates CDK12 to trigger the elongation of RNA Polymerase IIPreprint

Liu, H., Li, L., Gao, J., Leach, S. M., Wei, P., Zhang, Q., Huang, H., Houlès, T., Roux, P. P., & Zhang, G. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.27.678947 · Cited by 1 · see citing works

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

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