Modulating PCAF/GCN5 Immune Cell Function through a PROTAC Approach

Protacs: Chimeric molecules that target proteins to the Skp1–Cullin–F box complex for ubiquitination and degradation

Sakamoto, K. M., Kim, K. B., Kumagai, A., Mercurio, F., Crews, C. M., & Deshaies, R. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.141230798 · Cited by 2,609 · see citing works

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 · see citing works

Catalytic in vivo protein knockdown by small-molecule PROTACs

Bondeson, D. P., Mares, A., Smith, I. E. D., Ko, E., Campos, S., Miah, A. H., Mulholland, K. E., Routly, N., Buckley, D. L., Gustafson, J. L., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1858 · Cited by 1,356 · see citing works

Bromodomain: an acetyl‐lysine binding domain

Zeng, L., & Zhou, M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(01)03309-9 · Cited by 751 · see citing works

Differential cytokine modulation and T cell activation by two distinct classes of thalidomide analogues that are potent inhibitors of TNF-alpha.

Corral, L. G., Haslett, P. A. J., Muller, G. W., Chen, R., Wong, L. M., Ocampo, C. J., Patterson, R. T., Stirling, D., & Kaplan, G. (1999) · PubMed · Cited by 729 · see citing works

Differential Cytokine Modulation and T Cell Activation by Two Distinct Classes of Thalidomide Analogues That Are Potent Inhibitors of TNF-α

Corral, L. G., Haslett, P. A. J., Muller, G. W., Chen, R., Wong, L.-M., Ocampo, C. J., Patterson, R. T., Stirling, D., & Kaplan, G. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.1.380 · Cited by 654 · see citing works

Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation

Nagy, Z., & Tora, L. (2007) · Oncogene · doi:10.1038/sj.onc.1210604 · Cited by 416 · see citing works

Drugs for Autoimmune Inflammatory Diseases: From Small Molecule Compounds to Anti-TNF Biologics

Li, P., Zheng, Y., & Chen, X. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00460 · Cited by 349 · see citing works

Histone acetyl transferases as emerging drug targets

Dekker, F. J., & Haisma, H. J. (2009) · Drug Discovery Today · doi:10.1016/j.drudis.2009.06.008 · Cited by 319 · see citing works

Enhancement of Cytokine Production and AP-1 Transcriptional Activity in T Cells by Thalidomide-Related Immunomodulatory Drugs

Schafer, P. H., Gandhi, A. K., Loveland, M. A., Chen, R. S., Man, H., Schnetkamp, P. P. M., Wolbring, G., Govinda, S., Corral, L. G., Payvandi, F., et al. (2003) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.048496 · Cited by 182 · see citing works

The Role of Histone Acetyltransferases in Normal and Malignant Hematopoiesis

Sun, X., Man, N., Tan, Y., Nimer, S. D., & Wang, L. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00108 · Cited by 140 · see citing works

Discovery of a Potent, Cell Penetrant, and Selective p300/CBP-Associated Factor (PCAF)/General Control Nonderepressible 5 (GCN5) Bromodomain Chemical Probe

Humphreys, P. G., Bamborough, P., Chung, C., Craggs, P. D., Gordon, L. J., Grandi, P., Hayhow, T. G., Hussain, J., Jones, K. L., Lindon, M. J., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01566 · Cited by 102 · see citing works

Clinical progress and pharmacology of small molecule bromodomain inhibitors

Theodoulou, N. H., Tomkinson, N. C. O., Prinjha, R. K., & Humphreys, P. G. (2016) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2016.05.028 · Cited by 75 · see citing works

Lysine Acetyltransferase PCAF Is a Key Regulator of Arteriogenesis

Bastiaansen, A. J. N. M., Ewing, M. M., de Boer, H. C., Kraan, T. C. T. M. V. D. P., de Vries, M. R., Peters, E. A. B., Welten, S. M. J., Arens, R., Moore, S. M., Faber, J. E., et al. (2013) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.113.301579 · Cited by 63 · see citing works

The epigenetic factor PCAF regulates vascular inflammation and is essential for intimal hyperplasia development

de Jong, R. C. M., Ewing, M. M., de Vries, M. R., Karper, J. C., Bastiaansen, A. J. N. M., Peters, H. A. B., Baghana, F., van den Elsen, P. J., Gongora, C., Jukema, J. W., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0185820 · Cited by 46 · see citing works

Immunotherapeutic Implication of IL-6 Blockade

Tanaka, T., & Kishimoto, T. (2011) · Immunotherapy · doi:10.2217/imt.11.147 · Cited by 38 · see citing works

Immune Disease-Associated Variants in Gene Enhancers Point to BET Epigenetic Mechanisms for Therapeutic Intervention

Tough, D. F., & Prinjha, R. K. (2016) · Epigenomics · doi:10.2217/epi-2016-0144 · Cited by 37 · see citing works

Alteration of working memory but not in anxiety or stress response in p300/CBP associated factor (PCAF) histone acetylase knockout mice bred on a C57BL/6 background

Duclot, F., Jacquet, C., Gongora, C., & Maurice, T. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.03.077 · Cited by 34 · see citing works

Epigenetic pathway targets for the treatment of disease: accelerating progress in the development of pharmacological tools: IUPHAR Review 11

Tough, D. F., Lewis, H. D., Rioja, I., Lindon, M. J., & Prinjha, R. K. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12848 · Cited by 29 · see citing works

Acetylation of cyclin A: a new cell cycle regulatory mechanism

Mateo, F., Vidal-Laliena, M., Pujol, M. J., & Bachs, O. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380083 · Cited by 21 · see citing works

Rabex-5 is a lenalidomide target molecule that negatively regulates TLR-induced type 1 IFN production

Millrine, D., Tei, M., Gemechu, Y., & Kishimoto, T. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1611751113 · Cited by 18 · see citing works

Anti-inflammatory Effects of BET Protein Inhibition Through Modulation of Gene Transcription

Tough, D. F., Rioja, I., & Prinjha, R. K. (2015) · Springer eBooks · doi:10.1007/978-3-319-18102-8_10 · Cited by 1 · see citing works

Targeted protein degradation: expanding the toolbox

Schapira, M., Calabrese, M. F., Bullock, A. N., & Crews, C. M. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0047-y · Cited by 960 · see citing works

PROteolysis TArgeting Chimeras (PROTACs) — Past, present and future

Pettersson, M., & Crews, C. M. (2019) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2019.01.002 · Cited by 818 · see citing works

PROTACs: past, present and future

Li, K., & Crews, C. M. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00193d · Cited by 869 · see citing works

PROTACs: great opportunities for academia and industry

Sun, X., Gao, H., Yang, Y., He, M., Wu, Y., Song, Y.-G., Tong, Y., & Rao, Y. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0101-6 · Cited by 651 · see citing works

Targeted protein degradation: elements of PROTAC design

Paiva, S.-L., & Crews, C. M. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.02.022 · Cited by 586 · see citing works

BAF complex vulnerabilities in cancer demonstrated via structure-based PROTAC design

Farnaby, W., Koegl, M., Roy, M. J., Whitworth, C., Diers, E., Trainor, N., Zollman, D., Steurer, S., Karolyi-Oezguer, J., Riedmueller, C., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0294-6 · Cited by 562 · see citing works

PROTACs: An Emerging Therapeutic Modality in Precision Medicine

Nalawansha, D. A., & Crews, C. M. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.07.020 · Cited by 514 · see citing works

Bromodomains: a new target class for drug development

Cochran, A. G., Conery, A. R., & Sims, R. J. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0030-7 · Cited by 438 · see citing works

Advances in Targeting ‘Undruggable’ transcription Factors With Small Molecules

Henley, M. J., & Koehler, A. N. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00199-0 · Cited by 409 · see citing works

Proteolysis targeting chimeras (PROTACs) in ‘beyond rule-of-five’ chemical space: Recent progress and future challenges

Edmondson, S. D., Yang, B., & Fallan, C. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2019.04.030 · Cited by 422 · see citing works

PROTAC Technology: Opportunities and Challenges

Gao, H., Sun, X., & Rao, Y. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00597 · Cited by 361 · see citing works

Degradation of proteins by PROTACs and other strategies

Wang, Y., Jiang, X., Feng, F., Liu, W., & Sun, H. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.08.001 · Cited by 335 · see citing works

Iterative Design and Optimization of Initially Inactive Proteolysis Targeting Chimeras (PROTACs) Identify VZ185 as a Potent, Fast, and Selective von Hippel–Lindau (VHL) Based Dual Degrader Probe of BRD9 and BRD7

Zoppi, V., Hughes, S. J., Maniaci, C., Testa, A., Gmaschitz, T., Wieshofer, C., Koegl, M., Riching, K. M., Daniels, D. L., Spallarossa, A., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01413 · Cited by 336 · see citing works

Targeted protein degradation: A promise for undruggable proteins

Samarasinghe, K. T. G., & Crews, C. M. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.011 · Cited by 291 · see citing works

The PROTACtable genome

Schneider, M., Radoux, C. J., Hercules, A., Ochoa, D., Dunham, I., Zalmas, L.-P., Hessler, G., Ruf, S., Shanmugasundaram, V., Hann, M. M., et al. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00245-x · Cited by 273 · see citing works

Proteolysis targeting chimera (PROTAC) in drug discovery paradigm: Recent progress and future challenges

Zeng, S., Huang, W., Zheng, X., Cheng, L., Zhang, Z., Wang, J., & Shen, Z. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112981 · Cited by 262 · see citing works

PROteolysis TArgeting Chimeras (PROTACs) as emerging anticancer therapeutics

Khan, S., He, Y., Zhang, X., Yuan, Y., Pu, S., Kong, Q., Zheng, G., & Zhou, D. (2020) · Oncogene · doi:10.1038/s41388-020-1336-y · Cited by 252 · see citing works

E3 Ligase Ligands in Successful PROTACs: An Overview of Syntheses and Linker Attachment Points

Bricelj, A., Steinebach, C., Kuchta, R. D., Gütschow, M., & Sosič, I. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.707317 · Cited by 226 · see citing works

<i>In Silico</i> Modeling of PROTAC-Mediated Ternary Complexes: Validation and Application

Drummond, M. L., & Williams, C. I. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.8b00872 · Cited by 199 · see citing works

Targeted protein degradation as a powerful research tool in basic biology and drug target discovery

Wu, T., Yoon, H., Xiong, Y., Dixon-Clarke, S. E., Nowak, R. P., & Fischer, E. S. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0438-0 · Cited by 188 · see citing works

PROTACs: A novel strategy for cancer therapy

Liu, J., Ma, J., Liu, Y., Xia, J., Li, Y., Wang, Z. P., & Wei, W. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.02.006 · Cited by 186 · see citing works

Harnessing the Power of Proteolysis for Targeted Protein Inactivation

Verma, R., Mohl, D., & Deshaies, R. J. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.01.010 · Cited by 185 · see citing works

Development of Multifunctional Histone Deacetylase 6 Degraders with Potent Antimyeloma Activity

Wu, H., Yang, K., Zhang, Z., Leisten, E. D., Li, Z., Xie, H., Liu, J., Smith, K. A., Novakova, Z., Barinka, C., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00516 · Cited by 180 · see citing works

Targeted degradation of the enhancer lysine acetyltransferases CBP and p300

Vannam, R., Sayilgan, J., Ojeda, S., Karakyriakou, B., Hu, E., Kreuzer, J., Morris, R., Herrera Lopez, X. I., Rai, S., Haas, W., et al. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2020.12.004 · Cited by 177 · see citing works

Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies

Limorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 162 · see citing works

Developing degraders: principles and perspectives on design and chemical space

Maple, H. J., Clayden, N., Baron, A., Stacey, C., & Felix, R. L. (2019) · MedChemComm · doi:10.1039/c9md00272c · Cited by 159 · see citing works

Cereblon versus VHL: Hijacking E3 ligases against each other using PROTACs

Girardini, M., Maniaci, C., Hughes, S. J., Testa, A., & Ciulli, A. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.02.048 · Cited by 157 · see citing works

Developments of CRBN-based PROTACs as potential therapeutic agents

Wang, C., Zhang, Y., Wu, Y., & Xing, D. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113749 · Cited by 152 · see citing works

Programming inactive RNA-binding small molecules into bioactive degraders

Tong, Y., Lee, Y., Liu, X., Childs‐Disney, J. L., Suresh, B. M., Benhamou, R. I., Yang, C., Li, W., Costales, M. G., Haniff, H. S., et al. (2023) · Nature · doi:10.1038/s41586-023-06091-8 · Cited by 151 · see citing works

Characteristic roadmap of linker governs the rational design of PROTACs

Dong, Y., Ma, T., Xu, T., Feng, Z., Li, Y., Song, L., Yao, X., Ashby, C. R., & Hao, G.-F. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.04.007 · Cited by 146 · see citing works

The state of the art of PROTAC technologies for drug discovery

Wang, C., Zheng, C., Wang, H., Zhang, L., Liu, Z., & Xu, P. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114290 · Cited by 129 · see citing works

Proteolysis targeting chimeras (PROTACs) are emerging therapeutics for hematologic malignancies

He, Y., Khan, S., Huo, Z., Lv, D., Zhang, X., Liu, X., Yuan, Y., Hromas, R., Xu, M., Zheng, G., et al. (2020) · Journal of Hematology &amp; Oncology · doi:10.1186/s13045-020-00924-z · Cited by 126 · see citing works

Bivalent Ligands for Protein Degradation in Drug Discovery

Scheepstra, M., Hekking, K. F. W., Hijfte, L. V., & Folmer, R. H. A. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.01.006 · Cited by 120 · see citing works

PROTAC degraders as chemical probes for studying target biology and target validation

Němec, V., Schwalm, M. P., Müller, S., & Knapp, S. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00478j · Cited by 98 · see citing works

Induced protein degradation of histone deacetylases 3 (HDAC3) by proteolysis targeting chimera (PROTAC)

Cao, F., de Weerd, S., Chen, D., Zwinderman, M. R. H., van der Wouden, P. E., & Dekker, F. J. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112800 · Cited by 91 · see citing works

PROTAC: A promising technology for cancer treatment

Zhou, X., Dong, R., Zhang, J., Zheng, X. X., & Sun, L. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112539 · Cited by 84 · see citing works

The GCN5: its biological functions and therapeutic potentials

Haque, M. E., Jakaria, M., Akther, M., Cho, D.-Y., Kim, I., & Choi, D. (2021) · Clinical Science · doi:10.1042/cs20200986 · Cited by 81 · see citing works

Targeting the Ubiquitin-Proteasome System for Cancer Therapeutics by Small-Molecule Inhibitors

LaPlante, G., & Zhang, W. (2021) · Cancers · doi:10.3390/cancers13123079 · Cited by 82 · see citing works

Epigenetic Regulation of Inflammatory Signaling and Inflammation-Induced Cancer

Tan, S. Y. X., Zhang, J., & Tee, W. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.931493 · Cited by 83 · see citing works

Recent Advances in PROTACs for Drug Targeted Protein Research

Yao, T., Xiao, H., Wang, H., & Xu, X. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810328 · Cited by 78 · see citing works

Targeted protein degradation in vivo with Proteolysis Targeting Chimeras: Current status and future considerations

Watt, G. F., Scott‐Stevens, P., & Gaohua, L. (2019) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2019.02.005 · Cited by 72 · see citing works

Histone lysine acetyltransferase inhibitors: an emerging class of drugs for cancer therapy

White, J., Derheimer, F. A., Jensen-Pergakes, K., O’Connell, S. M., Sharma, S., Spiegel, N., & Paul, T. A. (2024) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2024.01.010 · Cited by 67 · see citing works

Targeted protein degradation in cancers: Orthodox PROTACs and beyond

Li, J., Chen, X., Lü, A., & Liang, C. (2023) · The Innovation · doi:10.1016/j.xinn.2023.100413 · Cited by 66 · see citing works

Ubiquitin proteasome system in immune regulation and therapeutics

Bhat, S., Vasi, Z., Adhikari, R., Gudur, A., Ali, A., Jiang, L., Ferguson, R., Liang, D., & Kuchay, S. (2022) · Current opinion in pharmacology (Print) · doi:10.1016/j.coph.2022.102310 · Cited by 59 · see citing works

Proteolysis targeting chimeras (PROTACs) for epigenetics research

Vogelmann, A., Robaa, D., Sippl, W., & Jung, M. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2020.01.010 · Cited by 59 · see citing works

Pharmacological targeting of the cancer epigenome

Mabe, N. W., Perry, J. A., Malone, C. F., & Stegmaier, K. (2024) · Nature Cancer · doi:10.1038/s43018-024-00777-2 · Cited by 58 · see citing works

Small molecule PROTACs in targeted therapy: An emerging strategy to induce protein degradation

Xi, M., Chen, Y., Yang, H., Xu, H., Du, K., Wu, C., Xu, Y., Deng, L., Luo, X., Yu, L., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.04.036 · Cited by 56 · see citing works

Design, Synthesis, and Evaluation of Potent, Selective, and Bioavailable AKT Kinase Degraders

Yu, X., Xu, J., Xie, L., Wang, L., Shen, Y., Cahuzac, K. M., Chen, X., Liu, J., Parsons, R. E., & Jin, J. J. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01476 · Cited by 53 · see citing works

Advancements in the Development of non‐BET Bromodomain Chemical Probes

Clegg, M. A., Tomkinson, N. C. O., Prinjha, R. K., & Humphreys, P. G. (2019) · ChemMedChem · doi:10.1002/cmdc.201800738 · Cited by 50 · see citing works

Proteases and Their Modulators in Cancer Therapy: Challenges and Opportunities

Song, R., Qiao, W., He, J., Huang, J., Luo, Y., & Yang, T. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01640 · Cited by 45 · see citing works

Targeting key proteins involved in transcriptional regulation for cancer therapy: Current strategies and future prospective

Pei, H., Guo, W., Peng, Y., Xiong, H., & Chen, Y. (2022) · Medicinal Research Reviews · doi:10.1002/med.21886 · Cited by 45 · see citing works

Advances and perspectives of proteolysis targeting chimeras (PROTACs) in drug discovery

Xi, J., Zhang, R., Chen, K., Yao, L., Li, M., Jiang, R., Li, X., & Fan, L. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.105848 · Cited by 45 · see citing works

PROTACs: New method to degrade transcription regulating proteins

Hu, B.-C., Zhou, Y., Sun, D., Yang, Y., Liu, Y., Li, X., Li, H., & Chen, L. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112698 · Cited by 43 · see citing works

PROTACS: A technology with a gold rush-like atmosphere

Wang, Y., Lan, L., Wang, M., Zhang, J., Gao, Y., Shi, L., & Sun, L. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.115037 · Cited by 42 · see citing works

Degraders in epigenetic therapy: PROTACs and beyond

Dai, X., Ji, S., Fu, M., Liu, G.-Z., Liu, H., Wang, S., Shen, L., Wang, N., Herdewijn, P. A., Zheng, Y., et al. (2024) · Theranostics · doi:10.7150/thno.92526 · Cited by 44 · see citing works

Induced proximity-based therapeutic modalities

King, E. A., Meyers, M., & Nomura, D. K. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01316-z · Cited by 42 · see citing works

PROTACs, molecular glues and bifunctionals from bench to bedside: Unlocking the clinical potential of catalytic drugs

Maneiro, M., Vita, E. D., Conole, D., Kounde, C. S., Zhang, Q., & Tate, E. W. (2021) · Progress in medicinal chemistry · doi:10.1016/bs.pmch.2021.01.002 · Cited by 38 · see citing works

Targeting bromodomain-containing proteins: research advances of drug discovery

Pan, Z., Zhao, Y., Wang, X., Xie, X., Liu, M., Zhang, K., Wang, L., Bai, D., Foster, L. J., Shu, R., et al. (2023) · Molecular Biomedicine · doi:10.1186/s43556-023-00127-1 · Cited by 41 · see citing works

Light-Controllable PROTACs for Temporospatial Control of Protein Degradation

Liu, J., Peng, Y., & Wei, W. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.678077 · Cited by 38 · see citing works

Application of Atypical Acetyl-lysine Methyl Mimetics in the Development of Selective Inhibitors of the Bromodomain-Containing Protein 7 (BRD7)/Bromodomain-Containing Protein 9 (BRD9) Bromodomains

Clegg, M. A., Bamborough, P., Chung, C., Craggs, P. D., Gordon, L. J., Grandi, P., Leveridge, M. V., Lindon, M. J., Liwicki, G. M., Michon, A., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00075 · Cited by 37 · see citing works

PROTAC: targeted drug strategy. Principles and limitations

Koroleva, O. A., Dutikova, Y. V., Trubnikov, A. V., Zenov, F. A., Manasova, E. V., Shtil, A. A., & Kurkin, A. V. (2022) · Russian Chemical Bulletin · doi:10.1007/s11172-022-3659-z · Cited by 38 · see citing works

Small molecule targeting of chromatin writers in cancer

Conery, A. R., Rocnik, J. L., & Trojer, P. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00920-5 · Cited by 36 · see citing works

Selectively targeting individual bromodomain: Drug discovery and molecular mechanisms

Wang, Q., Shao, X., Leung, E. L., Chen, Y., & Yao, X. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105804 · Cited by 35 · see citing works

Chemically induced degradation of epigenetic targets

Kabir, M., Yu, X., Kanıskan, H. Ü., & Jin, J. J. (2023) · Chemical Society Reviews · doi:10.1039/d3cs00100h · Cited by 35 · see citing works

Targeting the SAGA and ATAC Transcriptional Coactivator Complexes in MYC-Driven Cancers

Mustachio, L. M., Roszik, J., Farria, A. T., & Dent, S. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-3652 · Cited by 34 · see citing works

The fungal‐specific histone acetyltransferase Rtt109 regulates development, DNA damage response, and virulence in Aspergillus fumigatus

Zhang, Y., Fan, J., Ye, J., & Lü, L. (2020) · Molecular Microbiology · doi:10.1111/mmi.14665 · Cited by 33 · see citing works

Recent Advances on Small-Molecule Bromodomain-Containing Histone Acetyltransferase Inhibitors

Liu, M., Zhang, K., Li, Q., Pang, H., Pan, Z., Huang, X., Wang, L., Wu, F., & He, G. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01638 · Cited by 33 · see citing works

Targeting epigenetic reader domains by chemical biology

Cipriano, A., Sbardella, G., & Ciulli, A. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2020.05.006 · Cited by 31 · see citing works

PROTACs technology for targeting non-oncoproteins: Advances and perspectives

Wang, C., Zhang, Y., Xing, D., & Zhang, R. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105109 · Cited by 31 · see citing works

Catalysis by protein acetyltransferase Gcn5

Albaugh, B. N., & Denu, J. M. (2020) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2020.194627 · Cited by 31 · see citing works

T herapeutic targeting of chromatin: status and opportunities

Siklos, M. I., & Kubicek, S. (2021) · FEBS Journal · doi:10.1111/febs.15966 · Cited by 28 · see citing works

Targeting macrophage M1 polarization suppression through PCAF inhibition alleviates autoimmune arthritis via synergistic NF-κB and H3K9Ac blockade

Li, J., Feng, Y., Xu, X., Xu, P., Wang, P., Guan, Z., Ye, G., Yu, W., Su, Z., Lin, J., et al. (2023) · Journal of Nanobiotechnology · doi:10.1186/s12951-023-02012-z · Cited by 29 · see citing works

The new direction of drug development: Degradation of undruggable targets through targeting chimera technology

Liang, X., Ren, H., Han, F., Liang, R., Zhao, J., & Liu, H. S. (2023) · Medicinal Research Reviews · doi:10.1002/med.21992 · Cited by 28 · see citing works

Protacs in cancer therapy: mechanisms, design, clinical trials, and future directions

Vikal, A., Maurya, R., Patel, B. B., Sharma, R. K., Patel, P., Patil, U. K., & Kurmi, B. D. (2024) · Drug Delivery and Translational Research · doi:10.1007/s13346-024-01754-z · Cited by 28 · see citing works

PROTAC unleashed: Unveiling the synthetic approaches and potential therapeutic applications

Pravin, N., & Jóźwiak, K. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116837 · Cited by 28 · see citing works

Emerging modes-of-action in drug discovery

Valeur, E., Narjes, F., Ottmann, C., & Plowright, A. T. (2019) · MedChemComm · doi:10.1039/c9md00263d · Cited by 27 · see citing works

Improved methods for targeting epigenetic reader domains of acetylated and methylated lysine

Engelberg, I. A., Foley, C. A., James, L. I., & Frye, S. V. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.03.002 · Cited by 27 · see citing works

Post-translational lysine ac(et)ylation in health, ageing and disease

Blasl, A., Schulze, S., Qin, C., Graf, L. G., Vogt, R., & Lammers, M. (2021) · Biological Chemistry · doi:10.1515/hsz-2021-0139 · Cited by 29 · see citing works

Technologies of targeting histone deacetylase in drug discovery: Current progress and emerging prospects

Ru, J., Wang, Y., Li, Z., Wang, J., Ren, C., & Zhang, J. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115800 · Cited by 27 · see citing works

Elucidation of genome-wide understudied proteins targeted by PROTAC-induced degradation using interpretable machine learning

Xie, L., & Xie, L. (2023) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1010974 · Cited by 26 · see citing works

Epigenetic alterations as therapeutic targets in Testicular Germ Cell Tumours : current and future application of ‘epidrugs’

Cardoso, A. R., Lobo, J., Miranda‐Gonçalves, V., Henrique, R., & Jerónimo, C. (2020) · Epigenetics · doi:10.1080/15592294.2020.1805682 · Cited by 26 · see citing works

Emerging role of GCN5 in human diseases and its therapeutic potential

Xiao, H., Jin, J., & Zheng, Z. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114835 · Cited by 26 · see citing works

Expanding Bromodomain Targeting into Neglected Parasitic Diseases

Tallant, C., Bamborough, P., Chung, C., Gamo, F., Kirkpatrick, R. B., Larminie, C., Martin, J. J., Prinjha, R. K., Rioja, I., Simola, D. F., et al. (2021) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.1c00387 · Cited by 25 · see citing works

Recent insights of PROTAC developments in inflammation-mediated and autoimmune targets: a critical review

Galla, M. S., Sharma, N., Mishra, P., & Shankaraiah, N. (2024) · RSC Medicinal Chemistry · doi:10.1039/d4md00142g · Cited by 24 · see citing works

Opportunity knocks for uncovering the new function of an understudied nucleosome remodeling complex member, the bromodomain PHD finger transcription factor, BPTF

Zahid, H., Olson, N. M., & Pomerantz, W. C. K. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.02.003 · Cited by 24 · see citing works

Developments of PROTACs technology in immune-related diseases

Wang, C., Zhang, Y., Deng, J., Liang, B., & Xing, D. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115127 · Cited by 23 · see citing works

Breakthroughs in Medicinal Chemistry: New Targets and Mechanisms, New Drugs, New Hopes–6

Eynde, J. J. V., Mangoni, A. A., Rautio, J., Leprince, J., Azuma, Y., García‐Sosa, A. T., Hulme, C., Jampílek, J., Karaman, R., Li, W., et al. (2019) · Molecules · doi:10.3390/molecules25010119 · Cited by 23 · see citing works

Advancing Design Strategy of PROTACs for Cancer Therapy

Luo, H., Tian, Y., Abdullah, R., Zhang, B., Ma, Y., & Zhang, G. (2025) · MedComm · doi:10.1002/mco2.70258 · Cited by 22 · see citing works

Optimization of Potent Ligands for the E3 Ligase DCAF15 and Evaluation of Their Use in Heterobifunctional Degraders

Lucas, S. C. C., Ahmed, A., Ashraf, S. N., Argyrou, A., Bauer, M. R., Donatis, G. M. D., Demanze, S., Eisele, F., Fusani, L., Hock, A., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c02136 · Cited by 21 · see citing works

Discovery of Pyrrolo[3,2- d ]pyrimidin-4-one Derivatives as a New Class of Potent and Cell-Active Inhibitors of P300/CBP-Associated Factor Bromodomain

Huang, L., Li, H., Li, L., Niu, L., Seupel, R., Wu, C., Cheng, W., Chen, C., Ding, B., Brennan, P. E., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00096 · Cited by 21 · see citing works

Advances and Opportunities in Epigenetic Chemical Biology

Beyer, J. N., Raniszewski, N. R., & Burslem, G. M. (2020) · ChemBioChem · doi:10.1002/cbic.202000459 · Cited by 23 · see citing works

Recent advances in epigenetic proteolysis targeting chimeras (Epi-PROTACs)

Tomaselli, D., Mautone, N., Mai, A., & Rotili, D. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112750 · Cited by 21 · see citing works

The KAT module of the SAGA complex maintains the oncogenic gene expression program in MYCN- amplified neuroblastoma

Malone, C. F., Mabe, N. W., Forman, A. B., Alexe, G., Engel, K. L., Chen, Y.-J. C., Soeung, M., Salhotra, S., Thayakumar, A., Liu, B., et al. (2024) · Science Advances · doi:10.1126/sciadv.adm9449 · Cited by 20 · see citing works

TIP60 is required for tumorigenesis in non‐small cell lung cancer

Shibahara, D., Akanuma, N., Kobayashi, I. S., Heo, E., Ando, M., Fujii, M., Jiang, F., Prin, P. N., Pan, G., Wong, K., et al. (2023) · Cancer Science · doi:10.1111/cas.15785 · Cited by 20 · see citing works

Targeting SMAD-Dependent Signaling: Considerations in Epithelial and Mesenchymal Solid Tumors

Runa, F., Ortíz-Soto, G., de Barros, N. R., & Kelber, J. A. (2024) · Pharmaceuticals · doi:10.3390/ph17030326 · Cited by 20 · see citing works

Recent advances in the molecular design and applications of proteolysis targeting chimera-based multi-specific antiviral modality

Zhou, Y., Xu, S., López‐Carrobles, N., Ding, D., Liu, X., Menéndez‐Arias, L., & Zhan, P. (2023) · Acta Materia Medica · doi:10.15212/amm-2023-0019 · Cited by 19 · see citing works

Development of Human Carbonic Anhydrase II Heterobifunctional Degraders

O’Herin, C., Moriuchi, Y. W., Bemis, T. A., Kohlbrand, A. J., Burkart, M. D., & Cohen, S. M. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01843 · Cited by 20 · see citing works

Allostery in Disease: Anticancer Drugs, Pockets, and the Tumor Heterogeneity Challenge

Nussinov, R., Yavuz, B. R., & Jang, H. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169050 · Cited by 19 · see citing works

Design and pharmaceutical applications of proteolysis-targeting chimeric molecules

Liang, Y., Nandakumar, K. S., & Cheng, K. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114211 · Cited by 16 · see citing works

Allosteric PROTACs: Expanding the Horizon of Targeted Protein Degradation

Frost, A. B., O’Connor, S., & Ciulli, A. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c14840 · Cited by 21 · see citing works

P300/CBP‐associated factor (PCAF) attenuated M1 macrophage inflammatory responses possibly through KLF2 and KLF4

Wang, X., Li, H., Chen, S., He, J., Chen, W., Ding, Y., & Huang, J. (2021) · Immunology and Cell Biology · doi:10.1111/imcb.12455 · Cited by 44 · see citing works

IL-1β–specific recruitment of GCN5 histone acetyltransferase induces the release of PAF1 from chromatin for the de-repression of inflammatory response genes

Kim, N., Sun, H.-Y., Youn, M., & Yoo, J.-Y. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt156 · Cited by 18 · see citing works

Transcriptome Analysis Revealed Unique Genes as Targets for the Anti-inflammatory Action of Activated Protein C in Human Macrophages

Pereira, C. P., Bächli, E., Schaer, D. J., & Schoedon, G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015352 · Cited by 8 · see citing works

Protocatechuic acid inhibits human dendritic cell functional activation: Role of PPARγ up-modulation

Cornò, M. D., Varano, B., Scazzocchio, B., Filesi, C., Masella, R., & Gessani, S. (2014) · Immunobiology · doi:10.1016/j.imbio.2014.01.007 · Cited by 29 · see citing works

Preventive Effects of Protocatechuic Acid on LPS-Induced Inflammatory Response in Human Gingival Fibroblasts via Activating PPAR-γ

Wang, Y., Zhou, J., Fu, S., Wang, C., & Zhou, B. (2014) · Inflammation · doi:10.1007/s10753-014-0073-1 · Cited by 41 · see citing works