Targeted protein acetylation in cells using heterobifunctional molecules
Open accessPublished version of a preprint
Abstract
Protein acetylation is a central event in orchestrating diverse cellular processes. However, current strategies to investigate protein acetylation in cells are often nonspecific or lack temporal and magnitude control. Here, we developed an acetylation tagging system, AceTAG, to induce acetylation of targeted proteins. The AceTAG system utilizes bifunctional molecules to direct the lysine acetyltransferase p300/CBP to proteins fused with the small protein tag FKBP12 F36V, resulting in their induced acetylation. Using AceTAG, we induced targeted acetylation of a diverse array of proteins in cells, specifically histone H3.3, the NF-κB subunit p65/RelA, and the tumor suppressor p53. We demonstrate that targeted acetylation with the AceTAG system is rapid, selective, reversible and can be controlled in a dose-dependent fashion. AceTAG represents a useful strategy to modulate protein acetylation and should enable the exploration of targeted acetylation in basic biological and therapeutic contexts.
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
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
This strategy can induce time- and dose-dependent, rapid, selective acetylation of a variety of target proteins.
“This strategy can induce the time- and dose-dependent, rapid, selective acetylation of a variety of target proteins [38].”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [38]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Pérez-Riverol, Y., Csordas, A., Bai, J.-W., Bernal-Llinares, M., Hewapathirana, S., Kundu, D. J., Inuganti, A., Griss, J., Mayer, G., Eisenacher, M., et al. (2018) · Nucleic Acids Res. · doi:10.1093/nar/gky1106 · Cited by 6,216 · see citing works
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040 · see citing works
Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559 · see citing works
HaloTag: A Novel Protein Labeling Technology for Cell Imaging and Protein Analysis
Los, G. V., Encell, L. P., McDougall, M. G., Hartzell, D., Karassina, N., Zimprich, C., Wood, M. G., Learish, R., Ohana, R. F., Urh, M., et al. (2008) · ACS Chemical Biology · doi:10.1021/cb800025k · Cited by 2,527 · see citing works
Erasers of Histone Acetylation: The Histone Deacetylase EnzymesPreprint
Seto, E., & Yoshida, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018713 · Cited by 2,019 · see citing works
Phthalimide conjugation as a strategy for in vivo target protein degradation
Winter, G. E., Buckley, D. L., Paulk, J., Roberts, J. M., Souza, A., Dhe-Paganon, S., & Bradner, J. E. (2015) · Science · doi:10.1126/science.aab1433 · Cited by 1,760 · see citing works
Functions and mechanisms of non-histone protein acetylation
Narita, T., Weinert, B. T., & Choudhary, C. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0081-3 · Cited by 1,232 · see citing works
Duration of Nuclear NF-κB Action Regulated by Reversible Acetylation
Chen, L., Fischle, W., Verdin, E. M., & Greene, W. C. (2001) · Science · doi:10.1126/science.1062374 · Cited by 1,231 · see citing works
Self-citationDNA damage activates p53 through a phosphorylation–acetylation cascade
Sakaguchi, K., Herrera, J. E., Saito, S., Miki, T., Bustin, M., Vassilev, A., Anderson, C. W., & Appella, E. (1998) · Genes & Development · doi:10.1101/gad.12.18.2831 · Cited by 1,204 · see citing works
The dTAG system for immediate and target-specific protein degradation
Nabet, B., Roberts, J. M., Buckley, D. L., Paulk, J., Dastjerdi, S., Yang, A., Leggett, A. L., Erb, M. A., Lawlor, M. A., Souza, A., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0021-8 · Cited by 1,118 · see citing works
Proteolysis-Targeting Chimeras as Therapeutics and Tools for Biological Discovery
Burslem, G. M., & Crews, C. M. (2020) · Cell · doi:10.1016/j.cell.2019.11.031 · Cited by 1,079 · see citing works
The role of histone deacetylases (HDACs) in human cancer
Ropero, S., & Esteller, M. (2007) · Molecular Oncology · doi:10.1016/j.molonc.2007.01.001 · Cited by 1,007 · see citing works
Proteome-wide covalent ligand discovery in native biological systems
Backus, K. M., Correia, B. E., Lum, K. M., Forli, S., Horning, B. D., González-Páez, G. E., Chatterjee, S., Lanning, B. R., Teijaro, J. R., Olson, A. J., et al. (2016) · Nature · doi:10.1038/nature18002 · Cited by 940 · see citing works
Discovery of a selective catalytic p300/CBP inhibitor that targets lineage-specific tumours
Lasko, L. M., Jakob, C. G., Edalji, R. P., Qiu, W., Montgomery, D., Digiammarino, E. L., Hansen, T. M., Risi, R. M., Frey, R., Manaves, V., et al. (2017) · Nature · doi:10.1038/nature24028 · Cited by 858 · see citing works
p53 Sites Acetylated In Vitro by PCAF and p300 Are Acetylated In Vivo in Response to DNA Damage
Liu, L., Scolnick, D. M., Trievel, R. C., Zhang, H. B., Marmorstein, R., Halazonetis, T. D., & Berger, S. L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1202 · Cited by 776 · see citing works
DNA-encoded chemistry: enabling the deeper sampling of chemical space
Goodnow, R. A., Dumelin, C. E., & Keefe, A. D. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.213 · Cited by 621 · see citing works
Protein Lysine Acetylation by p300/CBP
Rabbitts, B. M., & Cole, P. A. (2015) · Chemical Reviews · doi:10.1021/cr500452k · Cited by 620 · see citing works
Time-Resolved Analysis Reveals Rapid Dynamics and Broad Scope of the CBP/p300 Acetylome
Weinert, B. T., Narita, T., Satpathy, S., Srinivasan, B., Hansen, B. K., Scholz, C. W., Hamilton, W. B., Zucconi, B. E., Wang, W., Liu, W. R., et al. (2018) · Cell · doi:10.1016/j.cell.2018.04.033 · Cited by 514 · see citing works
Self-citationChemically induced proximity in biology and medicine
Stanton, B. Z., Chory, E. J., & Crabtree, G. R. (2018) · Science · doi:10.1126/science.aao5902 · Cited by 475 · see citing works
Morris, M., Knudsen, G. M., Maeda, S., Trinidad, J. C., Ioanoviciu, A., Burlingame, A. L., & Mucke, L. (2015) · Nature Neuroscience · doi:10.1038/nn.4067 · Cited by 472 · see citing works
A Comprehensive Mathematical Model for Three-Body Binding Equilibria
Douglass, E. F., Miller, C. J., Sparer, G., Shapiro, H., & Spiegel, D. A. (2013) · Journal of the American Chemical Society · doi:10.1021/ja311795d · Cited by 472 · see citing works
HATs and HDACs in neurodegeneration: a tale of disconcerted acetylation homeostasis
Saha, R. N., & Pahan, K. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401769 · Cited by 439 · see citing works
Ligand and Target Discovery by Fragment-Based Screening in Human Cells
Parker, C. G., Galmozzi, A., Wang, Y., Correia, B. E., Sasaki, K., Joslyn, C. M., Kim, A. S., Cavallaro, C. L., Lawrence, R. M., Johnson, S. R., et al. (2017) · Cell · doi:10.1016/j.cell.2016.12.029 · Cited by 439 · see citing works
Self-citationNF-κB RelA Phosphorylation Regulates RelA Acetylation
Chen, L.-F., Williams, S. A., Mu, Y., Nakano, H., Duerr, J. M., Buckbinder, L., & Greene, W. C. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.18.7966-7975.2005 · Cited by 438 · see citing works
Self-citationLysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics
Ali, I., Conrad, R. J., Verdin, E. M., & Ott, M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00181 · Cited by 366 · see citing works
Regulation of intermediary metabolism by protein acetylation
Guan, K., & Xiong, Y. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.09.003 · Cited by 353 · see citing works
p53 Acetylation: Regulation and Consequences
Reed, S. M., & Quelle, D. E. (2014) · Cancers · doi:10.3390/cancers7010030 · Cited by 330 · see citing works
The emerging role of epigenetics in human autoimmune disorders
Mazzone, R., Zwergel, C., Artico, M., Taurone, S., Ralli, M., Greco, A., & Mai, A. (2019) · Clinical Epigenetics · doi:10.1186/s13148-019-0632-2 · Cited by 318 · see citing works
Nonhistone protein acetylation as cancer therapy targets
Singh, B. N., Zhang, G., Hwa, Y. L., Li, J., Dowdy, S. C., & Jiang, S. (2010) · Expert Review of Anticancer Therapy · doi:10.1586/era.10.62 · Cited by 302 · see citing works
Discovery and Optimization of Small-Molecule Ligands for the CBP/p300 Bromodomains
Hay, D. A., Fedorov, O., Martin, S., Singleton, D. C., Tallant, C., Wells, C. D., Picaud, S., Philpott, M., Monteiro, O., Rogers, C. M., et al. (2014) · Journal of the American Chemical Society · doi:10.1021/ja412434f · Cited by 287 · see citing works
Tracy, T. E., Sohn, P. D., Minami, S. S., Wang, C., Min, S.-W., Li, Y., Zhou, Y., Le, D., Lo, I., Ponnusamy, R., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.005 · Cited by 277 · see citing works
Tropberger, P., Pott, S., Keller, C., Kamieniarz-Gdula, K., Caron, M. J., Richter, F. M., Li, G., Mittler, G., Liu, E. T., Bühler, M., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.032 · Cited by 272 · see citing works
Unraveling the Role of Linker Design in Proteolysis Targeting Chimeras
Bemis, T. A., Clair, J. J. L., & Burkart, M. D. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00482 · Cited by 244 · see citing works
Hughes, S. J., & Ciulli, A. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170041 · Cited by 240 · see citing works
Faiola, F., Liu, X., Lo, S.-Y., Pan, S., Zhang, K., Lymar, E. S., Farina, A. N., & Martinez, E. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.23.10220-10234.2005 · Cited by 218 · see citing works
Regulation of STAT signaling by acetylation
Zhuang, S. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.05.007 · Cited by 199 · see citing works
Unifying principles of bifunctional, proximity-inducing small molecules
Gerry, C. J., & Schreiber, S. L. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0469-1 · Cited by 199 · see citing works
Phosphorylation-Inducing Chimeric Small Molecules
Siriwardena, S. U., Godage, D. N. P. M., Shoba, V. M., Lai, S., Shi, M., Wu, P., Chaudhary, S. K., Schreiber, S. L., & Choudhary, A. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c05537 · Cited by 196 · see citing works
Svinkina, T., Gu, H., Silva, J. C., Mertins, P., Qiao, J., Fereshetian, S., Jaffe, J. D., Kuhn, E. W., Udeshi, N. D., & Carr, S. A. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o114.047555 · Cited by 179 · see citing works
The many lives of KATs — detectors, integrators and modulators of the cellular environment
Sheikh, B. N., & Akhtar, A. (2018) · Nature Reviews Genetics · doi:10.1038/s41576-018-0072-4 · Cited by 171 · see citing works
Differences in Specificity and Selectivity Between CBP and p300 Acetylation of Histone H3 and H3/H4
Henry, R. A., Kuo, Y., & Andrews, A. J. (2013) · Biochemistry · doi:10.1021/bi400684q · Cited by 170 · see citing works
Su, H., Yang, F., Wang, Q., Shen, Q., Huang, J., Peng, C., Zhang, Y., Wan, W., Wong, C. C. L., Sun, Q., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.07.024 · Cited by 161 · see citing works
Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription
Cerbo, V. D., Mohn, F., Ryan, D., Montellier, E., Kacem, S., Tropberger, P., Kallis, E., Holzner, M., Hoerner, L., Feldmann, A., et al. (2014) · eLife · doi:10.7554/elife.01632 · Cited by 153 · see citing works
McEnaney, P. J., Parker, C. G., Zhang, A. X., & Spiegel, D. A. (2012) · ACS Chemical Biology · doi:10.1021/cb300119g · Cited by 151 · see citing works
Self-citationHeterobifunctional Molecules Induce Dephosphorylation of Kinases–A Proof of Concept Study
Yamazoe, S., Tom, J., Fu, Y., Wu, W., Zeng, L., Sun, C., Liu, Q., Lin, J. M., Lin, K., Fairbrother, W. J., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01167 · Cited by 145 · see citing works
Three-part inventions: intracellular signaling and induced proximity.
Crabtree, G., & Schreiber, S. L. (1996) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/s0968-0004(96)20027-1 · Cited by 135 · see citing works
Lysine acetylation in obesity, diabetes and metabolic disease
Iyer, A., Fairlie, D. P., & Brown, L. (2011) · Immunology and Cell Biology · doi:10.1038/icb.2011.99 · Cited by 126 · see citing works
Functional relevance of novel p300-mediated lysine 314 and 315 acetylation of RelA/p65
Buerki, C., Rothgiesser, K., Valovka, T., Owen, H. R., Rehrauer, H., Fey, M., Lane, W. S., & Hottiger, M. O. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn003 · Cited by 117 · see citing works
Mechanistic and Structural Features of PROTAC Ternary Complexes
Casement, R., Bond, A. G., Craigon, C., & Ciulli, A. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1665-9_5 · Cited by 105 · see citing works
Identification and Characterization of a Novel p300-mediated p53 Acetylation Site, Lysine 305
Wang, Y.-H., Tsay, Y.-G., Tan, B. C.-M., Lo, W.-Y., & Lee, S.-C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212574200 · Cited by 92 · see citing works
Wu, Y., Rozamus, L. W., Narula, S. S., Rollins, C. T., Yuan, R. W., Andrade, L. J., Ram, M. K., Phillips, T. B., van Schravendijk, M. R., Dalgarno, D. C., et al. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm9904396 · Cited by 90 · see citing works
Chiarella, A. M., Butler, K. V., Gryder, B. E., Lu, D., Wang, T. A., Yu, X., Pomella, S., Khan, J. I., Jin, J. J., & Hathaway, N. A. (2019) · Nature Biotechnology · doi:10.1038/s41587-019-0296-7 · Cited by 84 · see citing works
Amamoto, Y., Aoi, Y., Nagashima, N., Suto, H., Yoshidome, D., Arimura, Y., Osakabe, A., Kato, D., Kurumizaka, H., Kawashima, S. A., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b02138 · Cited by 84 · see citing works
Evaluation of fully-functionalized diazirine tags for chemical proteomic applications
Conway, L. P., Jadhav, A. M., Homan, R. A., Li, W., Rubiano, J. S., Hawkins, R., Lawrence, R. M., & Parker, C. G. (2021) · Chemical Science · doi:10.1039/d1sc01360b · Cited by 80 · see citing works
Self-citationSchreiber, S. L. (2018) · Israel Journal of Chemistry · doi:10.1002/ijch.201800113 · Cited by 76 · see citing works
Regulation of NF-κB activity by competition between RelA acetylation and ubiquitination
Li, H., Wittwer, T., Weber, A., Schneider, H., Moreno, R., Maine, G. N., Kracht, M., Schmitz, M. L., & Burstein, E. (2011) · Oncogene · doi:10.1038/onc.2011.253 · Cited by 70 · see citing works
Chemically Controlled Epigenome Editing through an Inducible dCas9 System
Chen, T., Gao, D., Zhang, R., Zeng, G., Yan, H., Lim, E., & Liang, F. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b06555 · Cited by 65 · see citing works
Small molecules as tools to study the chemical epigenetics of lysine acetylation
Schiedel, M., & Conway, S. J. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.06.015 · Cited by 44 · see citing works
Forster, N., Gallinat, S., Jabłońska, J., Weiß, S., Elsässer, H., & Lutz, W. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.11.6941 · Cited by 43 · see citing works
Biomimetic Artificial Epigenetic Code for Targeted Acetylation of Histones
Taniguchi, J., Feng, Y., Pandian, G. N., Hashiya, F., Hidaka, T., Hashiya, K., Park, S., Bando, T., Ito, S., & Sugiyama, H. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b01518 · Cited by 42 · see citing works
Live-cell epigenome manipulation by synthetic histone acetylation catalyst system
Fujiwara, Y., Yamanashi, Y., Fujimura, A., Sato, Y., Kujirai, T., Kurumizaka, H., Kimurâ, H., Yamatsugu, K., Kawashima, S. A., & Kanai, M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2019554118 · Cited by 42 · see citing works
Hamajima, W., Fujimura, A., Fujiwara, Y., Yamatsugu, K., Kawashima, S. A., & Kanai, M. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00102 · Cited by 27 · see citing works
Site-Selective Phosphoglycerate Mutase 1 Acetylation by a Small Molecule
Zhang, X., Jiang, L., Huang, K., Fang, C., Li, J., Yang, J., Li, H., Ruan, X., Wang, P., Mo, M., et al. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.9b00962 · Cited by 21 · see citing works
Antagonizing the Androgen Receptor with a Biomimetic Acyltransferase
Zhang, Y., Mantravadi, P. K., Jobbagy, S., Bao, W., & Koh, J. T. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00659 · Cited by 18 · see citing works
Mizumoto, S., Xi, S., Fujiwara, Y., Kawashima, S. A., Yamatsugu, K., & Kanai, M. (2020) · Chemistry - An Asian Journal · doi:10.1002/asia.201901737 · Cited by 15 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Targeted protein degradation: from mechanisms to clinic
Tsai, J. M., Nowak, R. P., Ebert, B. L., & Fischer, E. S. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00729-9 · Cited by 438 · see citing works
Proximity-Based Modalities for Biology and Medicine
Liu, X., & Ciulli, A. (2023) · ACS Central Science · doi:10.1021/acscentsci.3c00395 · Cited by 205 · see citing works
Chasing molecular glue degraders: screening approaches
Domostegui, A., Nieto-Barrado, L., Perez-Lopez, C., & Mayor-Ruiz, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00197g · Cited by 200 · see citing works
Targeted Biomolecule Regulation Platform: A Split-and-Mix PROTAC Approach
Yang, F., Luo, Q., Wang, Y., Liang, H., Wang, Y., Hou, Z., Wan, C., Wang, Y., Liu, Z., Ye, Y., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c12824 · Cited by 88 · see citing works
DNA-encoded library-enabled discovery of proximity-inducing small molecules
Mason, J. W., Chow, Y. T., Hudson, L., Tutter, A., Michaud, G., Westphal, M. V., Shu, W., Ma, X., Tan, Z. Y., Coley, C. W., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-023-01458-4 · Cited by 83 · see citing works
Ma, Z., & Zhou, J. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01818 · Cited by 80 · see citing works
Synthetic Gene Circuits for Regulation of Next‐Generation Cell‐Based Therapeutics
Teixeira, A. P., & Fussenegger, M. (2023) · Advanced Science · doi:10.1002/advs.202309088 · Cited by 76 · see citing works
Advancing Covalent Ligand and Drug Discovery beyond Cysteine
Kim, G., Grams, R. J., & Hsu, K. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.5c00001 · Cited by 77 · see citing works
Targeted Covalent Modification Strategies for Drugging the Undruggable Targets
Tamura, T., Kawano, M., & Hamachi, I. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00745 · Cited by 71 · see citing works
PROTAC 2.0: Expanding the frontiers of targeted protein degradation
Cornu, M., Lemaitre, T., Kieffer, C., & Voisin‐Chiret, A. S. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104376 · Cited by 68 · see citing works
Teng, M., & Gray, N. S. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.06.020 · Cited by 67 · see citing works
Targeted protein posttranslational modifications by chemically induced proximity for cancer therapy
Peng, Y., Liu, J., Inuzuka, H., & Wei, W. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104572 · Cited by 66 · see citing works
Acetylation targeting chimera enables acetylation of the tumor suppressor p53
Kabir, M., Sun, N., Hu, X., Martin, T. C., Yi, J., Zhong, Y., Xiong, Y., Kaniskan, H. Ü., Gu, W., Parsons, R., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c04640 · Cited by 65 · see citing works
Hua, L., Zhang, Q., Zhu, X., Wang, R., You, Q., & Wang, L. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00316 · Cited by 66 · see citing works
Expanding the horizons of targeted protein degradation: A non-small molecule perspective
Huang, X., Wu, F., Ye, J., Wang, L., Wang, X., Li, X., & He, G. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.01.010 · Cited by 58 · see citing works
Opportunities for Therapeutic Modulation of O-GlcNAc
Cheng, S. S., Mody, A. C., & Woo, C. M. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00417 · Cited by 61 · see citing works
Targeted Protein O-GlcNAcylation Using Bifunctional Small Molecules
Ma, B., Khan, K. S., Xu, T., Amada, J. X., Guo, Z., Huang, Y., Yan, Y., Lam, H., Cheng, A. S. L., & Ng, W. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c14380 · Cited by 56 · see citing works
Advancing Targeted Protein Degradation via Multiomics Profiling and Artificial Intelligence
Duran-Frigola, M., Cigler, M., & Winter, G. E. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c11098 · Cited by 50 · see citing works
Proximity-inducing modalities: the past, present, and future
Singh, S., Tian, W., Severance, Z. C., Chaudhary, S. K., Anokhina, V. S., Mondal, B., Pergu, R., Singh, P. R., Dhawa, U., Singha, S., et al. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00943a · Cited by 45 · see citing works
Nanoparticle‐Mediated Targeted Protein Degradation: An Emerging Therapeutics Technology
Baker, A., Ho, A. P. T., Itzhaki, L. S., & Fruk, L. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202503958 · Cited by 44 · see citing works
Kinase-targeting small-molecule inhibitors and emerging bifunctional molecules
Goebel, G. L., Qiu, X., & Wu, P. (2022) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2022.04.006 · Cited by 42 · 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
Post-translational modifications of cancer immune checkpoints: mechanisms and therapeutic strategies
Jia, H., Jiang, L., Shen, X., Ye, H., Li, X., Zhang, L., Hu, Y., Song, D., Jia, H., & Wang, Z. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02397-5 · Cited by 48 · see citing works
Wittlinger, F., Ogboo, B. C., Shevchenko, E., Damghani, T., Pham, C. D., Schaeffner, I. K., Oligny, B. T., Chitnis, S. P., Beyett, T. S., Rasch, A., et al. (2024) · Communications Chemistry · doi:10.1038/s42004-024-01108-3 · Cited by 35 · see citing works
TAC‐tics for Leveraging Proximity Biology in Drug Discovery
Nalawansha, D. A., Mangano, K., den Besten, W., & Potts, P. R. (2023) · ChemBioChem · doi:10.1002/cbic.202300712 · Cited by 36 · see citing works
Deubiquitinase-Targeting Chimeras (DUBTACs) as a Potential Paradigm-Shifting Drug Discovery Approach
Ma, Z., Zhou, M., Chen, H., Shen, Q., & Zhou, J. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02975 · Cited by 37 · see citing works
Post-translational acylation of proteins in cardiac hypertrophy
Liu, Y., Yang, Q., & He, G. (2025) · Nature Reviews Cardiology · doi:10.1038/s41569-025-01150-1 · Cited by 38 · see citing works
Protein degraders - from thalidomide to new PROTACs
Ito, T. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad113 · Cited by 33 · see citing works
Methylarginine targeting chimeras for lysosomal degradation of intracellular proteins
Seabrook, L. J., Franco, C. N., Loy, C. A., Osman, J. M., Fredlender, C., Zimak, J., Campos, M., Nguyen, S. T., Watson, R. L., Levine, S. R., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01741-y · Cited by 32 · see citing works
Current strategies for improving limitations of proteolysis targeting chimeras
Pu, C., Wang, S., Liu, L., Feng, Z., Zhang, H., Gong, Q., Sun, Y., Guo, Y., & Li, R. (2022) · Chinese Chemical Letters · doi:10.1016/j.cclet.2022.107927 · Cited by 29 · see citing works
Chemical Biology Tools for Protein Lysine Acylation
Xie, Y., Du, S., Liu, Z., Liu, M., Xu, Z., Wang, X., Kee, J. X., Yi, F., Sun, H., & Yao, S. Q. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202200303 · Cited by 29 · see citing works
Recent advances in induced proximity modalities
Ng, C. S. C., & Banik, S. M. (2022) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.102107 · Cited by 28 · see citing works
Heitel, P. (2023) · Molecules · doi:10.3390/molecules28020690 · Cited by 27 · see citing works
Roles of posttranslational modifications in lipid metabolism and cancer progression
Feng, T., Zhang, H., Zhou, Y., Zhu, Y., Shi, S., Li, K., Lin, P., & Chen, J. (2024) · Biomarker Research · doi:10.1186/s40364-024-00681-y · Cited by 23 · see citing works
Acetylation: a new target for protein degradation in cancer
Crawford, C. E. W., & Burslem, G. M. (2025) · Trends in Cancer · doi:10.1016/j.trecan.2025.01.013 · Cited by 20 · see citing works
Generative design of therapeutics that bind and modulate protein states
Chen, T., Hong, L., Yudistyra, V., Vincoff, S., & Chatterjee, P. (2023) · Current Opinion in Biomedical Engineering · doi:10.1016/j.cobme.2023.100496 · Cited by 17 · see citing works
Ma, Z., Zhang, C., Shen, Q., & Zhou, J. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01250 · Cited by 19 · see citing works
Targeted protein modification as a paradigm shift in drug discovery
Amirian, R., Azadi Badrbani, M., Izadi, Z., Samadian, H., Bahrami, G., Sarvari, S., Abdolmaleki, S., Nabavi, S. M., Derakhshankhah, H., & Jaymand, M. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115765 · Cited by 18 · see citing works
Functional investigations of p53 acetylation enabled by heterobifunctional molecules
Chen, L.-Y., Singha Roy, S. J., Jadhav, A. M., Wang, W. W., Chen, P.-H., Bishop, T., Erb, M. A., & Parker, C. G. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.4c00438 · Cited by 18 · see citing works
Self-citationProtein–Protein Interaction Prediction for Targeted Protein Degradation
Orasch, O., Weber, N., Müller, M., Amanzadi, A., Gasbarri, C., & Trummer, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137033 · Cited by 17 · see citing works
A bivalent molecular glue linking lysine acetyltransferases to oncogene-induced cell death
Nix, M. N., Gourisankar, S. P., Bowman, K., Nettles, S. A., Yang, H. H., Dwyer, B. G., Sarott, R. C., Abuzaid, H. Z., Martinez, M. M., Phillips, N. A., et al. (2026) · Cell · doi:10.1016/j.cell.2026.06.037 · Cited by 16 · see citing works
Self-citationAllosteric 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
Exploring the landscape of post-translational modification in drug discovery
Cao, Y., Yu, T., Zhu, Z., Zhang, Y., Sun, S., Li, N., Gu, C., & Yang, Y. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108749 · Cited by 15 · see citing works
Degron tagging for rapid protein degradation in mice
Hernández-Morán, B. A., Taylor, G. C. A., Lorente‐Macías, Á., & Wood, A. J. (2024) · Disease Models & Mechanisms · doi:10.1242/dmm.050613 · Cited by 15 · see citing works
Tang, G., Wang, X., Huang, H., Xu, M., Ma, X., Miao, F., Lu, X., Zhang, C., Gao, L., Zhang, Z., et al. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c07181 · Cited by 15 · see citing works
EFMC: Trends in Medicinal Chemistry and Chemical Biology
Auberson, Y. P., Arimondo, P. B., Duca, M., Essig, S., Grether, U., Rufer, A. C., Sbardella, G., Schopfer, U., Torrens, A., van der Stelt, M., et al. (2023) · ChemBioChem · doi:10.1002/cbic.202200690 · Cited by 16 · see citing works
Phosphorylation-Inducing Molecules for Regulating Dynamic Cellular Processes
Pergu, R., Sreekanth, V., Kokkonda, P., Lai, S., Tiwari, P. K., Singh, S., Kawai, J., Singha, S., Tian, W., Thimaradka, V., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c04275 · Cited by 15 · see citing works
Zou, X., Shanmugam, S. K., Kanner, S. A., Sampson, K. J., Kass, R. S., & Colecraft, H. M. (2023) · eLife · doi:10.7554/elife.83466 · Cited by 14 · see citing works
Small-molecule tools for YEATS domain proteins
Erb, M. A. (2023) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102404 · Cited by 14 · see citing works
Targeted Protein Acetylation Through Chemically Induced Proximity
Wang, W., Roy, S. J. S., & Parker, C. G. (2025) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5c00326 · Cited by 12 · see citing works
Self-citationSupramolecular Host–Guest Assemblies for Tunable and Modular Lysosome‐Targeting Protein Degradation
Chen, X., Wu, T., Chen, Y., Wu, H., Kang, W., Wang, N., You, Q., Guo, X., & Jiang, Z. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202506618 · Cited by 11 · see citing works
Ligand-Directed Self-Assembling Chimeras for Targeted Protein O-GlcNAcylation
Guo, Z., Xu, T., Khan, K. S., Scheeff, S., Qin, Y., Yu, S., Lo, R., Li, Y., Xie, Y., Ma, B., et al. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.5c00684 · Cited by 11 · see citing works
Strategies for Conditional Regulation of Proteins
Nadendla, K., Simpson, G. G., Becher, J. B., Journeaux, T., Cabeza-Cabrerizo, M., & Bernardes, G. J. L. (2023) · JACS Au · doi:10.1021/jacsau.2c00654 · Cited by 11 · see citing works
Kumar, A., Ali, S., Shen, Q., & Zhou, J. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6c02076 · Cited by 12 · see citing works
Zhao, C., Wang, H., Zhan, W., Lv, X., & Ma, X. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00079 · Cited by 9 · see citing works
Harnessing the TAF1 Acetyltransferase for Targeted Acetylation of the Tumor Suppressor p53
Kabir, M., Hu, X., Martin, T. C., Pokushalov, D., Kim, Y. J., Chen, Y., Zhong, Y., Wu, Q. D., Chipuk, J. E., Shi, Y., et al. (2024) · Advanced Science · doi:10.1002/advs.202413377 · Cited by 9 · see citing works
Opportunities in proximity modulation: Bridging academia and industry
Đikić, I., Mayor‐Ruiz, C., Winter, G. E., Koch, K., Ciulli, A., & Thomä, N. H. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.07.018 · Cited by 9 · see citing works
Molecular probes for cellular imaging of post-translational proteoforms
Suraritdechachai, S., Lakkanasirorat, B., & Uttamapinant, C. (2022) · RSC Chemical Biology · doi:10.1039/d1cb00190f · Cited by 9 · see citing works
Harmony of Protein Tags and Chimeric Molecules Empowers Targeted Protein Ubiquitination and Beyond
Lawer, A., Schulz, L. P., Sawyer, R. C., & Liu, X. (2024) · Cells · doi:10.3390/cells13050426 · Cited by 8 · see citing works
The rise of targeting chimeras (TACs): next-generation medicines that preempt cellular events
Hollingsworth, S. A., Johnson, S. A., Khakbaz, P., Meng, Y., Mouchlis, V. D., Pierce, O., Prytkova, V. D., Vik, E. S., Weiss, D. R., & Shanmugasundaram, V. (2023) · Medicinal Chemistry Research · doi:10.1007/s00044-023-03104-z · Cited by 8 · see citing works
Ke, D.-T., Zhan, Z., Zhang, W., Hu, Z., & Chen, P. (2026) · Cell chemical biology · doi:10.1016/j.chembiol.2025.12.012 · Cited by 7 · see citing works
A heterobifunctional molecule system for targeted protein acetylation in cells
Chen, L., Wang, W., Wozniak, J. M., & Parker, C. G. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.08.014 · Cited by 7 · see citing works
Self-citationRyan, E. M., Norinskiy, M. A., Bracken, A. K., Lueders, E. E., Chen, X., Fu, Q., Anderson, E. T., Zhang, S., & Abbasov, M. E. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c09073 · Cited by 7 · see citing works
Warhead Strategy for Targeted Protein S-Nitrosation
Zhang, C., Ye, H., Ji, D., Xiong, T., Yu, J., Qian, Z., Li, C., Li, H., Liang, Z., Zhang, Y., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c07409 · Cited by 6 · see citing works
Gray, J. L., Xiao, Z., Rogga, V. V., Zhang, X., & Tate, E. W. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c12299 · Cited by 4 · see citing works
Chemical Biology Tools for Protein Lysine Acylation
Xie, Y., Du, S., Liu, Z., Liu, M., Xu, Z., Wang, X., Kee, J. X., Yi, F., Sun, H., & Yao, S. Q. (2022) · Angewandte Chemie · doi:10.1002/ange.202200303 · Cited by 6 · see citing works
Methods to characterize and discover molecular degraders in cells
Lin, Z., & Woo, C. M. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00261b · Cited by 6 · see citing works
Generating Surprisingly Powerful Pharmacology from Chemically Induced Protein Interactions
Hinshaw, S. M., Banik, S. M., & Gray, N. S. (2025) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5c00225 · Cited by 5 · see citing works
Kodadek, T. J. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202316726 · Cited by 5 · see citing works
Wang, Y., He, Y., You, Q., & Wang, L. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.104194 · Cited by 5 · see citing works
Activating p53 Y220C with a Mutant-Specific Small MoleculePreprint
Zhu, X., Byun, W. S., Pieńkowska, D. E., Nguyen, K. T., Gerhartz, J., Geng, Q., Qiu, T., Zhong, J., Jiang, Z., Wang, M., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.23.619961 · Cited by 5 · see citing works
A proximity-induced chimera platform for targeted protein arginine methylation
Jian, Y., Zhou, T., Guo, C., Gao, Y., Chen, Y., Wang, Z., Jiang, X., Wang, K., Ma, J., Gao, Y., et al. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.03.049 · Cited by 4 · see citing works
Asadi, S., Taheri‐Torbati, M., Kesharwani, P., & Sahebkar, A. (2025) · Drug Development Research · doi:10.1002/ddr.70197 · Cited by 4 · see citing works
Advanced nanotechnologies for protein modulation: From Nano-PROTAC to Nano-APROM
Wang, J., Hu, X., Zhang, J., Wang, C., Dai, H., Lu(杨露), Y., Li, F., & Ling, D. (2026) · Journal of Controlled Release · doi:10.1016/j.jconrel.2026.114901 · Cited by 4 · see citing works
Sung, J., Seo, Y., & Lee, J.-Y. (2026) · Molecular Therapy · doi:10.1016/j.ymthe.2026.05.031 · Cited by 4 · see citing works
A chemical magnet: Approaches to guide precise protein localization
Kumar, S., & Nabet, B. (2024) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2024.117672 · Cited by 4 · see citing works
Nanoparticle‐Mediated Targeted Protein Degradation: An Emerging Therapeutics Technology
Baker, A., Ho, A. P. T., Itzhaki, L. S., & Fruk, L. (2025) · Angewandte Chemie · doi:10.1002/ange.202503958 · Cited by 3 · see citing works
Design and Development of DNA Damage Chemical Inducers of Proximity for Targeted Cancer Therapy
Qiu, T., Lee, Y. T., Dwyer, B. G., Tan, Y. J., Chen, T., Romero, B. A., Wang, Y., Deng, J., Zhang, T., Crabtree, G. R., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c17396 · Cited by 3 · see citing works
Fabbrizi, E., Fiorentino, F., Casano, F., Mai, A., & Rotili, D. (2025) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2025.2486146 · Cited by 3 · see citing works
Rewiring DNA repair with PARP-based chemical inducers of proximityPreprint
da Camara, B., Bilotta, E. M., Broderick, E., Premashankar, A., Barta, P. A., Carter, T. R., Hargis, L. M., Durocher, D., & Erb, M. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.26.666954 · Cited by 3 · see citing works
Chromatin Regulatory Targets for Anticancer Therapeutics
Barta, P. A., Carter, T. R., & Erb, M. A. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.5c00231 · Cited by 2 · see citing works
ProxyBind: A compendium of binding sites for proximity-induced pharmacology
Rovers, E., Liu, L., & Schapira, M. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.11.010 · Cited by 2 · see citing works
Supramolecular Host–Guest Assemblies for Tunable and Modular Lysosome‐Targeting Protein Degradation
Chen, X., Wu, T., Chen, Y., Wu, H., Kang, W., Wang, N., You, Q., Guo, X., & Jiang, Z. (2025) · Angewandte Chemie · doi:10.1002/ange.202506618 · Cited by 1 · see citing works
Sculpting Cell Fate: The Expanding Universe of Nondegradative Proximity‐Inducing Tools
Xiao, H., Wang, L., Chen, M., Zhen, T., Chen, Y., & Sun, H. (2026) · ChemMedChem · doi:10.1002/cmdc.202501088 · Cited by 1 · see citing works
Proteomics‐Driven Strategies for Proximity‐Inducing Drug Discovery
Fan, R., Ni, J., Zhou, T., Jiang, H. Q., Zhao, W., & Tan, M. (2026) · Angewandte Chemie International Edition · doi:10.1002/anie.3307512 · Cited by 1 · see citing works
TogoPhosTAC as a delivery-ready platform for targeted protein dephosphorylation
Chen, Y.-Y., Ke, D.-T., Lee, Y., Chen, H., Lin, H.-Y., Yeh, C.-L., Ko, Y.-C., Tu, M., Yu, C., Hu, Z., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-76725-8 · Cited by 1 · see citing works
Hussain, M., Tejeda, G. S., & Baillie, G. S. (2025) · FEBS Journal · doi:10.1111/febs.70205 · Cited by 1 · see citing works
Covalent Bifunctional Molecules (CBMs): Achievements and Challenges
Xin, Y., Chen, F., You, Q., Wang, L., & Zhang, Q. (2025) · Medicinal Research Reviews · doi:10.1002/med.70011 · Cited by 1 · see citing works
Targeted Protein Degradation – The Story So Far
O’Donovan, D. H., Luh, L. M., & Cromm, P. M. (2022) · doi:10.1002/9783527836208.ch1 · Cited by 1 · see citing works
Branon, T. C. (2025) · Wiley eBooks · doi:10.1002/9781394236145.ch16 · Cited by 1 · see citing works
An epigenetic bifunctional that toggles between transactivation and repressionPreprint
Sadagopan, A., Carson, M., Zamurs, E. J., Srikonda, S., Weiss, C. N., Bond, M. J., Sodhi, A., Donovan, K. A., Ryan, J. K., Fischer, E. S., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.17.712509 · Cited by 1 · see citing works
Structure-Based Survey of the Human Proteome for Opportunities in Proximity PharmacologyPreprint
Rovers, E., & Schapira, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.13.475779
The Future of Heterobifunctional Compounds: PROTACs and Beyond
Burslem, G. M. (2022) · Wiley eBooks · doi:10.1002/9783527836208.ch10
Programmable Acetylation Modification of Bacterial Proteins by a Cas12a-Guided Acetyltransferase
Liu, Y., Zhang, Z., Zuo, N., Jiang, W., & Gu, Y. (2023) · ACS Synthetic Biology · doi:10.1021/acssynbio.3c00211
Kodadek, T. J. (2023) · Angewandte Chemie · doi:10.1002/ange.202316726
New Therapeutic Chemical Modalities: Compositions, Modes-of-action, and Drug Discovery
Valeur, E. (2023) · Royal Society of Chemistry eBooks · doi:10.1039/9781788018982-00911
The next frontier in drug discovery: Unveiling the pharmacological potential of proximity inducers
Holmberg‐Douglas, N., Keenan, K. N., de Turiso, F. G.-L., Chekler, E. P., Shanmugasundaram, V., Riggs, J. R., & Zapf, C. W. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-29808-0.00018-2
Chemically Responsive Protein Switches for the Precise Control of Biological Activities
Franco, J., Drahy, N., Divoux, S., Perez, F., & Gautier, A. (2026) · ACS Chemical Biology · doi:10.1021/acschembio.6c00360
Qiu, T., Lee, Y. T., Dwyer, B. G., Tan, Y. J., Chen, T., Romero, B. A., Wang, Y., Deng, J., Zhang, T., Crabtree, G. R., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.03.686423
EMERGING MEDICINAL CHEMISTRY APPROACHES TO MODULATE TRANSCRIPTIONAL ACTIVITY BY ACETYLATION
Kutilek, V. D., Hopkins, T. D., & Biddle, M. M. (2025) · Medicinal chemistry reviews · doi:10.1021/mc-2025-vol60.ch14
- Authors
- Wang, W. W., Chen, L.-Y., Wozniak, J. M., Jadhav, A. M., Anderson, H., Malone, T. E., & Parker, C. G.
- Affiliations
- Department of Chemistry, The Scripps Research Institute, Jupiter, Florida 33458, United States
- Scripps Research Institute (US)
- Corresponding author
- Parker, Christopher G.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2021-09-30
- Volume
- 143
- Issue
- 40
- Pages
- 16700-16708
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- PMC
- PMC10793965
- OpenAlex
- W3204435125
- Cited by
- 114
- References
- 65
- Citations by year
- 2026: 25 · 2025: 32 · 2024: 18 · 2023: 24 · 2022: 15
- FWCI
- 4.47
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- Journal of the American Chemical Society (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Scripps Research Institute
- National Institutes of Health (T32 AI007244)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Physical Sciences › Chemistry › Organic Chemistry › Click Chemistry and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Keywords
- protein acetylation, heterobifunctional molecules, CBP/p300, histone acetyltransferase, histone H3.3, p53
- MeSH terms
- Acetylation, Histones, Humans, Tumor Suppressor Protein p53, p300-CBP Transcription Factors, Transcription Factor RelA
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
