Development of a Novel B-Cell Lymphoma 6 (BCL6) PROTAC To Provide Insight into Small Molecule Targeting of BCL6
Open accessAbstract
B-cell lymphoma 6 (BCL6) inhibition is a promising mechanism for treating hematological cancers but high quality chemical probes are necessary to evaluate its therapeutic potential. Here we report potent BCL6 inhibitors that demonstrate cellular target engagement and exhibit exquisite selectivity for BCL6 based on mass spectrometry analyses following chemical proteomic pull down. Importantly, a proteolysis-targeting chimera (PROTAC) was also developed and shown to significantly degrade BCL6 in a number of diffuse large B-cell lymphoma (DLBCL) cell lines, but neither BCL6 inhibition nor degradation selectively induced marked phenotypic response. To investigate, we monitored PROTAC directed BCL6 degradation in DLBCL OCI-Ly1 cells by immunofluorescence and discovered a residual BCL6 population. Analysis of subcellular fractions also showed incomplete BCL6 degradation in all fractions despite having measurable PROTAC concentrations, together providing a rationale for the weak antiproliferative response seen with both BCL6 inhibitor and degrader. In summary, we have developed potent and selective BCL6 inhibitors and a BCL6 PROTAC that effectively degraded BCL6, but both modalities failed to induce a significant phenotypic response in DLBCL despite achieving cellular concentrations.
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?
BI-3802 surpassed the efficacy of non-degrading BCL6 inhibitors such as BI-3812 or PROTAC-based BCL6 degraders, which had only shown modest pre-clinical success.
“surpassing the efficacy of non-degrading Bcl6 inhibitors such as Bi-3812 or PROtAc-based Bcl6 degraders, which had only shown modest pre-clinical success (Mccoull et al. 2018;Schlager et al. 2020).”
From From serendipity to strategy: molecular glue degraders in cancer therapeutics (2025) · cites this paper as Mccoull et al. 2018
In “Developing PROTAC Ready BCL6 Ligands” (page unavailable), McCoull et al. report weak antiproliferative effects for their BCL6 inhibitors and similarly weak effects for PROTAC 15 in lymphoma cell lines. Our copy does not establish that BI-3802 surpassed these compounds or identify BI-3812 as one of the inhibitors tested, so it supports only the limited-response portion of the claim. (LLM, conf=0.86)
Experimental — accuracy not yet measuredAnti-proliferative effects of BI-3802 in lymphoma models closely mirrored genetic BCL6 deletion.
“the anti-proliferative effects observed in lymphoma models closely mirrored genetic BCL6 deletion”
From From serendipity to strategy: molecular glue degraders in cancer therapeutics (2025) · cites this paper as Mccoull et al. 2018
The Abstract discusses BCL6 shRNA-induced lethality, while the section on antiproliferative activity reports weak, nonselective effects for the paper’s PROTAC 15. Our copy does not report BI-3802 or compare its antiproliferative effects with genetic BCL6 deletion (searched: BI-3802, genetic deletion, knockout). (LLM, conf=0.76)
Experimental — accuracy not yet measuredBCL6 is recalcitrant to hetero-bifunctional degraders, which have shown insufficient target modulation to induce growth inhibition.
“One such example is the B cell lymphoma 6 (BCL6) protein, for which hetero-bifunctional degraders have shown insufficient target modulation to induce growth inhibition5.”
From Small-molecule-induced polymerization triggers degradation of BCL6 (2020) · cites this paper as [5]
A significant subset of proteins are recalcitrant to targeted protein degradation using current approaches.
“but a significant subset of proteins are recalcitrant to targeted protein degradation using current approaches4,5.”
From Small-molecule-induced polymerization triggers degradation of BCL6 (2020) · cites this paper as [5]
BI-3802 induces rapid ubiquitination and degradation of BCL6.
“BI-3802 induces rapid ubiquitination and degradation of BCL6, resulting in profound de-repression of BCL6 target genes and anti-proliferative effects in DLBCL cell lines, comparable to a genetic knock-out21, and superior to non-degrading BCL6 inhibitors such as BI-3812 or heterobifunctional BCL6 degraders5,6.”
From Small-molecule-induced polymerization triggers degradation of BCL6 (2020) · cites this paper as [5]
The effects of BI-3802 are comparable to a genetic knock-out and superior to non-degrading BCL6 inhibitors such as BI-3812 or heterobifunctional BCL6 degraders.
“BI-3802 induces rapid ubiquitination and degradation of BCL6, resulting in profound de-repression of BCL6 target genes and anti-proliferative effects in DLBCL cell lines, comparable to a genetic knock-out21, and superior to non-degrading BCL6 inhibitors such as BI-3812 or heterobifunctional BCL6 degraders5,6.”
From Small-molecule-induced polymerization triggers degradation of BCL6 (2020) · cites this paper as [5]
BI-3802 results in profound de-repression of BCL6 target genes and anti-proliferative effects in DLBCL cell lines.
“BI-3802 induces rapid ubiquitination and degradation of BCL6, resulting in profound de-repression of BCL6 target genes and anti-proliferative effects in DLBCL cell lines, comparable to a genetic knock-out21, and superior to non-degrading BCL6 inhibitors such as BI-3812 or heterobifunctional BCL6 degraders5,6.”
From Small-molecule-induced polymerization triggers degradation of BCL6 (2020) · cites this paper as [5]
Inhibition of BCL6 or degradation by PROTACs results in insufficient inhibition of downstream targets and consequently only minor anti-proliferative effects.
“It has been previously shown that inhibition of BCL6 or degradation by PROTACs results in insufficient inhibition of downstream targets and consequently only minor anti-proliferative effects5.”
From Small-molecule-induced polymerization triggers degradation of BCL6 (2020) · cites this paper as [5]
McCoull et al. developed Bcl-6 PROTACs that could degrade Bcl-6 in a number of cells but did not improve antiproliferative activity over Bcl-6 inhibitors in DLBCL cells.
“Although the PROTAC molecules could degrade Bcl-6 in a number of cells, they did not improve antiproliferative activity over Bcl-6 inhibitors in DLBCL cells.”
From Proteolysis targeting chimeras (PROTACs) are emerging therapeutics for hematologic malignancies (2020) · cites this paper as [42]
The weak antiproliferative response of Bcl-6 PROTACs is due to incomplete Bcl-6 degradation.
“Further investigation revealed that the weak antiproliferative response is due to the incomplete Bcl-6 degradation [42].”
From Proteolysis targeting chimeras (PROTACs) are emerging therapeutics for hematologic malignancies (2020) · cites this paper as [42]
PROTACs and IMiDs are generally larger and more flexible than typical drug-like compounds, which can translate into poor membrane permeability and liability to efflux pumps.
“These molecules are generally larger and more flexible than typical drug-like compounds, which can translate into poor membrane permeability and liability to efflux pumps 39,42,43 .”
From Targeted protein degradation: expanding the toolbox (2019) · cites this paper as [43]
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
Monitoring Drug Target Engagement in Cells and Tissues Using the Cellular Thermal Shift Assay
Molina, D. M., Jafari, R., Ignatushchenko, M., Seki, T., Larsson, E. A., Dan, C., Sreekumar, L., Cao, Y., & Nordlund, P. (2013) · Science · doi:10.1126/science.1233606 · Cited by 2,261 · see citing works
Self-citationTrapping of PARP1 and PARP2 by Clinical PARP Inhibitors
Murai, J., Huang, S.-Y. N., Das, B. B., Renaud, A., Zhang, Y., Doroshow, J. H., Ji, J. J., Takeda, S., & Pommier, Y. G. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-2753 · Cited by 2,217 · 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
Hijacking the E3 Ubiquitin Ligase Cereblon to Efficiently Target BRD4
Lu, J., Qian, Y., Altieri, M., Dong, H., Wang, J., Raina, K., Hines, J., Winkler, J. D., Crew, A. P., Coleman, K., et al. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.05.009 · Cited by 1,140 · see citing works
Small molecules, big targets: drug discovery faces the protein–protein interaction challenge
Scott, D. E., Bayly, A. R., Abell, C., & Skidmore, J. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.29 · Cited by 1,137 · see citing works
Béguelin, W., Popovic, R., Teater, M. R., Jiang, Y., Bunting, K. L., Rosen, M., Shen, H., Yang, S. N., Wang, L., Ezponda, T., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.04.011 · Cited by 854 · see citing works
A selective inhibitor of EZH2 blocks H3K27 methylation and kills mutant lymphoma cells
Knutson, S. K., Wigle, T. J., Warholic, N. M., Sneeringer, C. J., Allain, C. J., Klaus, C. R., Sacks, J. D., Raimondi, A., Majer, C. R., Song, J., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1084 · Cited by 776 · see citing works
Small‐Molecule PROTACS: New Approaches to Protein Degradation
Toure, M., & Crews, C. M. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201507978 · Cited by 674 · see citing works
BCoR, a novel corepressor involved in BCL-6 repressionPreprint
Huynh, K. D., Fischle, W., Verdin, E. M., & Bardwell, V. J. (2000) · Genes & Development · doi:10.1101/gad.14.14.1810 · Cited by 475 · see citing works
Small-molecule kinase inhibitors: an analysis of FDA-approved drugs
Wu, P., Nielsen, T. E., & Clausen, M. H. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2015.07.008 · Cited by 457 · see citing works
Yoon, H., Chan, D. W., Huang, Z., Li, J., Fondell, J. D., Qin, J., & Wong, J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg120 · Cited by 444 · see citing works
Roles of BCL6 in normal and transformed germinal center B cells
Basso, K., & Dalla‐Favera, R. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01112.x · Cited by 431 · see citing works
Cattoretti, G., Pasqualucci, L., Ballon, G., Tam, W., Nandula, S. V., Shen, Q., Mo, T., Murty, V. V., & Dalla-Favera, R. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.03.037 · Cited by 383 · see citing works
Direct Repression of <i>prdm1</i> by Bcl-6 Inhibits Plasmacytic Differentiation
Tunyaplin, C., Shaffer, A. L., Angelin-Duclos, C. D., Yu, X., Staudt, L. M., & Calame, K. L. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.2.1158 · Cited by 376 · see citing works
The BCL-6 POZ domain and other POZ domains interact with the co-repressors N-CoR and SMRT
Huynh, K. D., & Bardwell, V. J. (1998) · Oncogene · doi:10.1038/sj.onc.1202197 · Cited by 311 · see citing works
FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas
Duan, S., C̆ermák, L., Pagan, J. K., Rossi, M., Martinengo, C., di Celle, P. F., Chapuy, B., Shipp, M. A., Chiarle, R., & Pagano, M. (2011) · Nature · doi:10.1038/nature10688 · Cited by 295 · see citing works
Ranuncolo, S. M., Polo, J. M., Dierov, J., Singer, M., Kuo, T., Greally, J., Green, R., Carroll, M., & Melnick, A. (2007) · Nature Immunology · doi:10.1038/ni1478 · Cited by 278 · see citing works
Chemically Induced Degradation of the Oncogenic Transcription Factor BCL6
Kerres, N., Steurer, S., Schlager, S., Bader, G., Berger, H., Caligiuri, M., Dank, C., Engen, J. R., Ettmayer, P., Fischerauer, B., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.081 · Cited by 207 · see citing works
Hatzi, K., Jiang, Y., Huang, C., Garrett-Bakelman, F. E., Gearhart, M. D., Γιαννοπούλου, Ε., Zumbo, P., Kirouac, K. N., Bhaskara, S., Polo, J. M., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.06.016 · Cited by 186 · see citing works
A peptomimetic inhibitor of BCL6 with potent antilymphoma effects in vitro and in vivo
Cerchietti, L. C. A., Yang, S. N., Shaknovich, R., Hatzi, K., Polo, J. M., Chadburn, A., Dowdy, S. F., & Melnick, A. M. (2008) · Blood · doi:10.1182/blood-2008-07-168773 · Cited by 183 · see citing works
The Expanding Role of the BCL6 Oncoprotein as a Cancer Therapeutic Target
Cárdenas, M., Oswald, E. M., Yu, W., Xue, F., MacKerell, A. D., & Melnick, A. M. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-2071 · Cited by 181 · see citing works
Rationally designed BCL6 inhibitors target activated B cell diffuse large B cell lymphoma
Cardenas, M. G., Yu, W., Beguelin, W., Teater, M. R., Geng, H., Goldstein, R. L., Oswald, E., Hatzi, K., Yang, S.-N., Cohen, J., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci85795 · Cited by 176 · see citing works
Common pitfalls in preclinical cancer target validation
Kaelin, W. G. (2017) · Nature Reviews Cancer · doi:10.1038/nrc.2017.32 · Cited by 175 · see citing works
Rapid Measurement of Intracellular Unbound Drug Concentrations
Mateus, A., Matsson, P., & Artursson, P. (2013) · Molecular Pharmaceutics · doi:10.1021/mp4000822 · Cited by 170 · see citing works
Parekh, S. S., Polo, J. M., Shaknovich, R., Juszczyński, P., Lev, P. R., Ranuncolo, S. M., Yin, Y., Klein, U., Cattoretti, G., Favera, R. D., et al. (2007) · Blood · doi:10.1182/blood-2007-01-069575 · Cited by 146 · see citing works
Polo, J. M., Juszczyński, P., Monti, S., Cerchietti, L. C. A., Ye, K. Q., Greally, J. M., Shipp, M. A., & Melnick, A. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611399104 · Cited by 135 · see citing works
Collins, I., Wang, H., Caldwell, J., & Chopra, R. (2017) · Biochemical Journal · doi:10.1042/bcj20160762 · Cited by 135 · see citing works
Prediction of intracellular exposure bridges the gap between target- and cell-based drug discovery
Mateus, A., Gordon, L. J., Wayne, G. J., Almqvist, H., Axelsson, H., Seashore-Ludlow, B. A., Treyer, A., Matsson, P., Lundbäck, T., West, A., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1701848114 · Cited by 106 · see citing works
McCoull, W., Abrams, R., Anderson, E. K., Blades, K., Barton, P., Box, M. R., Burgess, J., Byth, K. F., Cao, Q., Chuaqui, C. E., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00359 · Cited by 80 · see citing works
Self-citationKamada, Y., Sakai, N., Sogabe, S., Ida, K., Oki, H., Sakamoto, K., Lane, W., Snell, G., Iida, M., Imaeda, Y., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00313 · Cited by 57 · see citing works
A proto-oncogene BCL6 is up-regulated in the bone marrow microenvironment in multiple myeloma cells
Hideshima, T., Mitsiades, C. S., Ikeda, H., Chauhan, D., Raje, N. S., Görgün, G., Hideshima, H., Munshi, N. C., Richardson, P. G. G., Carrasco, D. R., et al. (2010) · Blood · doi:10.1182/blood-2010-02-270082 · Cited by 52 · see citing works
SnapShot: Diffuse Large B Cell Lymphoma
Pasqualucci, L., & Dalla‐Favera, R. (2014) · Cancer Cell · doi:10.1016/j.ccr.2013.12.012 · Cited by 49 · see citing works
A Versatile Method to Determine the Cellular Bioavailability of Small-Molecule Inhibitors
Teuscher, K. B., Zhang, M., & Ji, H. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00923 · Cited by 42 · see citing works
Discovery of high-affinity BCL6-binding peptide and its structure-activity relationship
Sakamoto, K., Sogabe, S., Kamada, Y., Sakai, N., Asano, K., Yoshimatsu, M., Ida, K., Imaeda, Y., & Sakamoto, J.-I. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.11.060 · Cited by 35 · see citing works
Intracellular concentrations determine the cytotoxicity of adefovir, cidofovir and tenofovir
Zhang, X., Wang, R., Piotrowski, M. A., Zhang, H., & Leach, K. L. (2014) · Toxicology in Vitro · doi:10.1016/j.tiv.2014.10.019 · Cited by 34 · see citing works
Small molecule-mediated protein knockdown as a new approach to drug discovery
Tinworth, C. P., Lithgow, H., & Churcher, I. (2016) · MedChemComm · doi:10.1039/c6md00347h · Cited by 32 · see citing works
Wappett, M., Dulak, A. M., Yang, Z. R., Al-Watban, A., Bradford, J. R., & Dry, J. R. (2016) · BMC Genomics · doi:10.1186/s12864-016-2375-1 · Cited by 22 · see citing works
Kettle, J. G., & Wilson, D. M. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.06.007 · Cited by 22 · see citing works
Self-citationAlbagli, O., Lindon, C., Lantoine, D., Quief, S., Puvion, E., Pinset, C., & Puvion-dutilleul, F. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.22.8560-8570.2000 · Cited by 20 · see citing works
DOSCHEDA: a web application for interactive chemoproteomics data analysis
Contrino, B., Miele, E., Tomlinson, R., Castaldi, M. P., & Ricchiuto, P. (2017) · PeerJ Computer Science · doi:10.7717/peerj-cs.129 · Cited by 4 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
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
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
Current strategies for the design of PROTAC linkers: a critical review
Troup, R. I., Fallan, C., & Baud, M. G. J. (2020) · Exploration of Targeted Anti-tumor Therapy · doi:10.37349/etat.2020.00018 · Cited by 424 · see citing works
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
Proteolysis-targeting chimeras (PROTACs) in cancer therapy
Li, X., Pu, W., Zheng, Q., Ai, M., Chen, S., & Peng, Y. (2022) · Molecular Cancer · doi:10.1186/s12943-021-01434-3 · Cited by 374 · 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
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
Small-molecule-induced polymerization triggers degradation of BCL6
Słabicki, M., Yoon, H., Koeppel, J., Nitsch, L., Roy Burman, S. S., Di Genua, C., Donovan, K. A., Sperling, A. S., Hunkeler, M., Tsai, J. M., et al. (2020) · Nature · doi:10.1038/s41586-020-2925-1 · Cited by 270 · 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
Han, X., Zhao, L., Xiang, W., Qin, C., Miao, B., Xu, T., Wang, M., Yang, C., Chinnaswamy, K., Stuckey, J. A., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01393 · Cited by 229 · 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
E3 ligase ligand chemistries: from building blocks to protein degraders
Sosič, I., Bricelj, A., & Steinebach, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00148a · Cited by 173 · see citing works
Discovery of SHP2-D26 as a First, Potent, and Effective PROTAC Degrader of SHP2 Protein
Wang, M., Lu, J., Wang, M., Yang, C.-Y., & Wang, S. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00471 · Cited by 172 · see citing works
Rewiring cancer drivers to activate apoptosis
Gourisankar, S. P., Krokhotin, A., Ji, W., Liu, X., Chang, C.-Y., Kim, S. H., Li, Z., Wenderski, W., Simanauskaite, J., Yang, H., et al. (2023) · Nature · doi:10.1038/s41586-023-06348-2 · Cited by 172 · see citing works
PROTACs– a game-changing technology
Konstantinidou, M., Li, J., Zhang, B., Wang, Z., Shaabani, S., ter Brake, F., Essa, K., & Dömling, A. S. S. (2019) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2019.1659242 · Cited by 167 · see citing works
Limorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 162 · 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
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
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 & Oncology · doi:10.1186/s13045-020-00924-z · Cited by 126 · see citing works
Zhang, X., Thummuri, D., Liu, X., Hu, W., Zhang, P., Khan, S., Yuan, Y., Zhou, D., & Zheng, G. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112186 · Cited by 123 · see citing works
“Despite the high molecular weight of PROTACs that are derived from PPI inhibitors, a number of PPI-targeting degraders have been successfully developed, including MCL-1 [38], BCL-2/MCL-1 [39], MDM2 [49], BCL-6 [50], and STAT3 [51,52].”
BackgroundWang, Z., He, N., Guo, Z., Niu, C., Song, T., Guo, Y., Cao, K., Wang, A., Zhu, J., Zhang, X., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00919 · Cited by 120 · 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
Development of Small Molecule Chimeras That Recruit AhR E3 Ligase to Target Proteins
Ohoka, N., Tsuji, G., Shoda, T., Fujisato, T., Kurihara, M., Demizu, Y., & Naito, M. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00704 · Cited by 117 · see citing works
Proteolysis targeting chimeras (PROTACs) in cancer therapy
Ocaña, A., & Pandiella, A. (2020) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01672-1 · Cited by 87 · see citing works
Discovery of thalidomide-based PROTAC small molecules as the highly efficient SHP2 degraders
Yang, X., Wang, Z., Pei, Y., Song, N., Xu, L., Feng, B., Wang, H., Luo, X., Hu, X., Qiu, X., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113341 · Cited by 85 · 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
Systematic Investigation of the Permeability of Androgen Receptor PROTACs
Scott, D. E., Rooney, T. P. C., Bayle, E. D., Mirza, T., Willems, H. M. G., Clarke, J. H., Andrews, S. P., & Skidmore, J. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00194 · Cited by 79 · see citing works
Relocalizing transcriptional kinases to activate apoptosis
Sarott, R. C., Gourisankar, S. P., Karim, B. A., Nettles, S. A., Yang, H., Dwyer, B. G., Simanauskaite, J., Tse, J., Abuzaid, H. Z., Krokhotin, A., et al. (2024) · Science · doi:10.1126/science.adl5361 · Cited by 80 · see citing works
Bellenie, B. R., Cheung, K.-M. J., Varela, A., Pierrat, O. A., Collie, G. W., Box, G. M., Bright, M. D., Gowan, S., Hayes, A., Rodrigues, M. J., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b02076 · Cited by 74 · see citing works
Evolution of Cereblon-Mediated Protein Degradation as a Therapeutic Modality
Chamberlain, P. P., D’Agostino, L. A., Ellis, J. M., Hansen, J. D., Matyskiela, M. E., McDonald, J. J., Riggs, J. R., & Hamann, L. G. (2019) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00425 · Cited by 69 · see citing works
Monomeric Targeted Protein Degraders
Hanan, E. J., Liang, J., Wang, X., Blake, R. A., Blaquiere, N., & Staben, S. T. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00093 · Cited by 69 · see citing works
Yang, L., Tu, W., Huang, L., Miao, B., Kaneshige, A., Jiang, W., Leng, L., Wang, M., Wen, B., Sun, D., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00953 · Cited by 69 · see citing works
Wendt, M., Bellavita, R., Gerber, A., Efrém, N., van Ramshorst, T., Pearce, N. M., Davey, P. R. J., Everard, I., Vázquez–Chantada, M., Chiarparin, E., et al. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202102082 · Cited by 66 · see citing works
Self-citationMayuri, K., Sreeraman, S., Somala, C. S., Kushwah, R. B. S., Saravanan, K. M., Sundaram, V., & Anand, T. (2023) · Future Medicinal Chemistry · doi:10.4155/fmc-2023-0072 · Cited by 63 · see citing works
General mechanism of JQ1 in inhibiting various types of cancer
Jiang, G., Deng, W., Liu, Y., & Wang, C. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.10927 · Cited by 61 · see citing works
BTB domains: A structural view of evolution, multimerization, and protein–protein interactions
Bonchuk, A. N., Balagurov, K., & Georgiev, P. G. (2022) · BioEssays · doi:10.1002/bies.202200179 · Cited by 64 · see citing works
A protein tertiary structure mimetic modulator of the Hippo signalling pathway
Adihou, H., Gopalakrishnan, R., Förster, T., Guéret, S. M., Gasper, R., Geschwindner, S., Carrillo García, C., Karatas, H., Pobbati, A. V., Vazquez‐Chantada, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19224-8 · Cited by 58 · see citing works
Self-citationHarnessing the cyclization strategy for new drug discovery
Tang, K., Wang, S., Gao, W., Song, Y., & Yu, B. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.09.022 · Cited by 58 · see citing works
Novel approaches to targeted protein degradation technologies in drug discovery
Xue, Y., Bolinger, A. A., & Zhou, J. (2023) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2187777 · Cited by 58 · see citing works
Profiling the Landscape of Drug Resistance Mutations in Neosubstrates to Molecular Glue Degraders
Gosavi, P. M., Ngan, K. C., Yeo, M. J. R., Su, C., Li, J., Lue, N. Z., Hoenig, S. M., & Liau, B. B. (2022) · ACS Central Science · doi:10.1021/acscentsci.1c01603 · Cited by 56 · see citing works
Enriching Proteolysis Targeting Chimeras with a Second Modality: When Two Are Better Than One
Salerno, A., Seghetti, F., Caciolla, J., Uliassi, E., Testi, E., Guardigni, M., Roberti, M., Milelli, A., & Bolognesi, M. L. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00302 · Cited by 55 · 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
Discovery of Proteolysis-Targeting Chimera Molecules that Selectively Degrade the IRAK3 Pseudokinase
Degorce, S. L., Tavana, O., Banks, E., Crafter, C., Gingipalli, L., Kouvchinov, D., Mao, Y., Pachl, F., Solanki, A., Valge-archer, V. E., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01125 · Cited by 55 · see citing works
Recent Advances in PROTAC-Based Antiviral Strategies
Ahmad, H., Zia, B., Husain, H., & Husain, A. (2023) · Vaccines · doi:10.3390/vaccines11020270 · Cited by 54 · see citing works
A critical evaluation of the approaches to targeted protein degradation for drug discovery
Chopra, R., Sadok, A., & Collins, I. (2019) · Drug Discovery Today: Technologies · doi:10.1016/j.ddtec.2019.02.002 · Cited by 53 · see citing works
Zhang, W., Roy Burman, S. S., Chen, J., Donovan, K. A., Cao, Y., Shu, C., Zhang, B., Zeng, Z., Gu, S., Zhang, Y., et al. (2022) · Genomics, Proteomics & Bioinformatics · doi:10.1016/j.gpb.2022.11.008 · Cited by 51 · see citing works
Aminopyrimidines: Recent synthetic procedures and anticancer activities
Filho, É. V., Pinheiro, E. M. C., Pinheiro, S., & Greco, S. J. (2021) · Tetrahedron · doi:10.1016/j.tet.2021.132256 · Cited by 48 · see citing works
Zhang, X., Liu, H., He, J., Ou, C., Donahue, T. C., Muthana, M. M., Su, L., & Wang, L. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.1c00751 · Cited by 48 · see citing works
Teng, M., Ficarro, S. B., Yoon, H., Che, J., Zhou, J., Fischer, E. S., Marto, J. A., Zhang, T., & Gray, N. S. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00111 · Cited by 48 · see citing works
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
Elhassan, R. M., Hou, X., & Fang, H. (2021) · Medicinal Research Reviews · doi:10.1002/med.21871 · Cited by 41 · see citing works
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
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
In-Cell Quantification of Drugs by Magic-Angle Spinning Dynamic Nuclear Polarization NMR
Bertarello, A., Berruyer, P., Artelsmair, M., Elmore, C. S., Heydarkhan‐Hagvall, S., Schade, M., Chiarparin, E., Schantz, S., & Emsley, L. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c12442 · Cited by 38 · see citing works
Self-citationInducible knock-out of BCL6 in lymphoma cells results in tumor stasis
Schlager, S., Salomon, C., Olt, S., Albrecht, C., Ebert, A., Bergner, O., Wachter, J., Trapani, F., Gerlach, D., Voss, T., et al. (2020) · Oncotarget · doi:10.18632/oncotarget.27506 · Cited by 36 · see citing works
Demystifying the CXCR4 conundrum in cancer biology: Beyond the surface signaling paradigm
Nengroo, M. A., Khan, M. A., Verma, A., & Datta, D. B. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188790 · Cited by 36 · see citing works
Unifying Catalysis Framework to Dissect Proteasomal Degradation Paradigms
Rodriguez-Rivera, F. P., & Levi, S. M. (2021) · ACS Central Science · doi:10.1021/acscentsci.1c00389 · Cited by 30 · see citing works
B Cell Lymphoma 6 (BCL6): A Conserved Regulator of Immunity and Beyond
Liongue, C., Almohaisen, F. L. J., & Ward, A. C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252010968 · Cited by 30 · see citing works
Progress of small molecules for targeted protein degradation: PROTACs and other technologies
Zhao, H., Xin, M., & Zhang, S. (2023) · Drug Development Research · doi:10.1002/ddr.22026 · Cited by 31 · see citing works
Mi, D., Cheng, L., Li, Y., Yao, M., Li, Y., Hong, K., Xie, C., & Chen, Y. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116789 · Cited by 29 · see citing works
Ai, Y., Hwang, L., MacKerell, A. D., Melnick, A. M., & Xue, F. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01686 · Cited by 29 · see citing works
Gu, H., He, J., Li, Y., Mi, D., Guan, T., Guo, W., Liu, B., & Chen, Y. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01433 · Cited by 29 · 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
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
Optimizing Shape Complementarity Enables the Discovery of Potent Tricyclic BCL6 Inhibitors
Davis, O. A., Cheung, K.-M. J., Brennan, A., Lloyd, M. G., Rodrigues, M. J., Pierrat, O. A., Collie, G. W., Bihan, Y. L., Huckvale, R., Harnden, A. C., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c02174 · Cited by 27 · see citing works
Breaking Bad Proteins—Discovery Approaches and the Road to Clinic for Degraders
Bouvier, C., Lawrence, R., Cavallo, F., Xolalpa, W., Jordan, A. M., Hjerpe, R., & Rodríguez, M. S. (2024) · Cells · doi:10.3390/cells13070578 · Cited by 27 · see citing works
Targeting Epigenetic protein–protein Interactions With small-molecule Inhibitors
Linhares, B. M., Grembecka, J. E., & Cierpicki, T. (2020) · Future Medicinal Chemistry · doi:10.4155/fmc-2020-0082 · Cited by 25 · see citing works
Pearce, A. C., Bamford, M. J., Barber, R. C., Bridges, A. M., Convery, M. A., Demetriou, C., Evans, S., Gobbetti, T., Hirst, D. J., Holmes, D. S., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100928 · Cited by 25 · see citing works
Targeted degradation of CD147 proteins in melanoma
Zhou, Z., Long, J., Wang, Y., Li, Y., Zhang, X., Tang, L. Y., Chang, Q., Chen, Z., Hu, G., Hu, S., et al. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104453 · Cited by 24 · see citing works
Navigating PROTACs in Cancer Therapy: Advancements, Challenges, and Future Horizons
Ibrahim, S., Khan, M. U., Khurram, I., Rehman, R., Rauf, A., Ahmad, Z., Aljohani, A. S. M., Abdulmonem, W. A., & Quradha, M. M. (2025) · Food Science & Nutrition · doi:10.1002/fsn3.70011 · Cited by 23 · see citing works
Polycomb group proteins in cancer: multifaceted functions and strategies for modulation
Wang, S. P., Ordonez‐Rubiano, S. C., Dhiman, A., Jiao, G., Strohmier, B. P., Krusemark, C. J., & Dykhuizen, E. C. (2021) · NAR Cancer · doi:10.1093/narcan/zcab039 · Cited by 23 · see citing works
An Aged/Autoimmune B-cell Program Defines the Early Transformation of Extranodal Lymphomas
Venturutti, L., Rivas, M. A., Pelzer, B. W., Flümann, R., Hansen, J., Karagiannidis, I., Xia, M., McNally, D. R., Isshiki, Y., Lytle, A. G., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-22-0561 · Cited by 23 · see citing works
The Peptide PROTAC Modality: A New Strategy for Drug Discovery
Zhu, Y., Dai, Y., & Tian, Y. (2025) · MedComm · doi:10.1002/mco2.70133 · Cited by 23 · see citing works
Synthesis, biological evaluation and clinical trials of Cereblon-based PROTACs
Vicente, A. T. S., Moura, S. P. S. P., & Salvador, J. A. R. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01598-9 · Cited by 23 · see citing works
Wolska, A., & Smolewski, P. (2022) · Cancers · doi:10.3390/cancers14153778 · Cited by 21 · see citing works
Lv, M., Hu, W., Zhang, S., He, L., Hu, C., & Yang, S. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.215716 · Cited by 19 · 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
Into Deep Water: Optimizing BCL6 Inhibitors by Growing into a Solvated Pocket
Lloyd, M. G., Huckvale, R., Cheung, K.-M. J., Rodrigues, M. J., Collie, G. W., Pierrat, O. A., Iou, M. G., Carter, M. W., Davis, O. A., McAndrew, C., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00946 · Cited by 18 · 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
Improved Binding Affinity and Pharmacokinetics Enable Sustained Degradation of BCL6 In Vivo
Huckvale, R., Harnden, A. C., Cheung, K.-M. J., Pierrat, O. A., Talbot, R., Box, G., Henley, A. T., Brandon, A. K. D. H., Hallsworth, A., Bright, M. D., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c02175 · Cited by 17 · see citing works
Proteolysis-targeting Chimeras for Targeting Protein for Degradation
Qi, J., & Zhang, G. (2019) · Future Medicinal Chemistry · doi:10.4155/fmc-2018-0557 · Cited by 15 · see citing works
Shoda, T., Ohoka, N., Tsuji, G., Fujisato, T., Inoue, H., Demizu, Y., Naito, M., & Kurihara, M. (2020) · Pharmaceuticals · doi:10.3390/ph13030034 · Cited by 15 · see citing works
Cereblon: promise and challenges for combating human diseases
Kim, H. K., Seol, J. E., Ahn, S. W., Jeon, S., Park, C., & Han, J. (2021) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-021-02624-0 · Cited by 14 · see citing works
Discovery of OICR12694: A Novel, Potent, Selective, and Orally Bioavailable BCL6 BTB Inhibitor
Mamai, A., Chau, A. M., Wilson, B. J., Watson, I. D. G., Joseph, B. B., Subramanian, P. R., Morshed, M. M., Morin, J. A., Prakesch, M. A., Lu, T., et al. (2023) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.2c00502 · Cited by 14 · see citing works
Chimera induced protein degradation: PROTACs and beyond
Yin, L., & Hu, Q. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112494 · Cited by 14 · see citing works
Wu, M., Xie, J., Xing, Y., Zhang, L., Chen, H., Tang, B., Zhou, M., Lv, S., Huang, D., Jian, S., et al. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.86303 · Cited by 13 · see citing works
Self-citationDai, M., Sridhar, R., Li, R., Tan, R., Yan, K., Fan, G., & Liu, M. (2022) · Technology in Cancer Research & Treatment · doi:10.1177/15330338221095950 · Cited by 13 · see citing works
Emerging mechanisms of targeted protein degradation by molecular glues
Frere, G. A., de Araujo, E. D., & Gunning, P. T. (2022) · Methods in cell biology · doi:10.1016/bs.mcb.2022.01.001 · Cited by 12 · see citing works
Orth, B., Sander, B., Möglich, A., Diederichs, K., Eilers, M., & Lorenz, S. (2021) · Structure · doi:10.1016/j.str.2021.06.005 · Cited by 12 · see citing works
Structural analysis of the PATZ1 BTB domain homodimer
Piepoli, S., Alt, A., Atılgan, C., Mancini, E. J., & Erman, B. (2020) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798320005355 · Cited by 11 · see citing works
Liu, J., & Zhang, H. (2024) · Biomolecules · doi:10.3390/biom14020192 · Cited by 11 · see citing works
From serendipity to strategy: molecular glue degraders in cancer therapeutics
Darling, S., Bajrami, I., & West, S. C. (2025) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2025.2564068 · Cited by 10 · see citing works
“…the efficacy of non-degrading Bcl6 inhibitors such as Bi-3812 or PROtAc-based Bcl6 degraders, which had only shown modest pre-clinical success (Mccoull et al. 2018; Schlager et al. 2020). integrated time-resolved microscopy and structural analyses revealed that Bcl6 monomers accumulated into…”
Wang, A. F., & Ayyar, V. S. (2023) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2023.10.027 · Cited by 10 · see citing works
Tsai, C.-C., Su, Y.-C., Bamodu, O. A., Chen, B., Tsai, W., Cheng, W.-H., Lee, C.-H., Hsieh, S.-M., Liu, M.-L., Fang, C.-L., et al. (2021) · Cancers · doi:10.3390/cancers13071620 · Cited by 10 · see citing works
Small molecule induced polymerization of BCL6 facilitates SIAH1 mediated degradation
Rana, S., & Natarajan, A. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00556-w · Cited by 10 · see citing works
Essential ingredients for rational drug design
Jarvis, A., & Ouvry, G. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2019.126674 · Cited by 10 · see citing works
Lipidated Stapled Peptides Targeting the Acyl Binding Protein UNC119
Cromm, P. M., Adihou, H., Kapoor, S., Vázquez–Chantada, M., Davey, P. R. J., Longmire, D., Hennes, E., Hofer, W., Küchler, P., Chiarparin, E., et al. (2019) · ChemBioChem · doi:10.1002/cbic.201900615 · Cited by 10 · see citing works
Self-citation
- Authors
- McCoull, W., Cheung, T., Anderson, E., Barton, P., Burgess, J., Byth, K., Cao, Q., Castaldi, M. P., Chen, H., Chiarparin, E., Carbajo, R. J., Code, E., Cowan, S., Davey, P. R., Ferguson, A. D., Fillery, S., Fuller, N. O., Gao, N., Hargreaves, D., Howard, M. R., Hu, J., Kawatkar, A., Kemmitt, P. D., Leo, E., Molina, D. M., O’Connell, N., Petteruti, P., Rasmusson, T., Raubo, P., Rawlins, P. B., Ricchiuto, P., Robb, G. R., Schenone, M., Waring, M. J., Zinda, M., Fawell, S., & Wilson, D. M.
- Affiliations
- AstraZeneca (United Kingdom) (GB)
- AstraZeneca (United States) (US)
- Pelago Bioscience (Sweden) (SE)
- Broad Institute (US)
- Corresponding author
- McCoull, William
- ORCID
- McCoull, William
- Byth, Kate
- Castaldi, M. Paola
- Chen, Huawei
- Chiarparin, Elisabetta
- Carbajo, Rodrigo J.
- Davey, Paul R.
- Ferguson, Andrew D.
- Fillery, Shaun
- Fuller, Nathan O.
- Gao, Ning
- Hargreaves, David
- Kawatkar, Aarti
- Kemmitt, Paul D.
- Leo, Elisabetta
- Raubo, Piotr
- Rawlins, Philip B.
- Ricchiuto, Piero
- Robb, Graeme R.
- Schenone, Monica
- Zinda, Michael
- Fawell, Stephen
- Wilson, David M.
- Venue
- ACS Chemical Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2018-10-17
- Volume
- 13
- Issue
- 11
- Pages
- 3131-3141
- ISSN
- 1554-8929 (ISSN-L)
- 1554-8937
- OpenAlex
- W2896054460
- Cited by
- 139
- References
- 40
- Citations by year
- 2026: 11 · 2025: 15 · 2024: 9 · 2023: 12 · 2022: 27 · 2021: 23 · 2020: 24 · 2019: 18
- FWCI
- 6.22
- Type
- journal article
- Language
- en
- Open access
- green
- www.osti.gov
- Locations
- ACS Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Newcastle University ePrints (Newcastle Univesity)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Health Sciences › Medicine › Pathology and Forensic Medicine › Lymphoma Diagnosis and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Keywords
- BCL6, PROTACs, BCL6 inhibitors, diffuse large B-cell lymphoma, small molecule targeting, chemical probes, cellular target engagement, chemoproteomics, subcellular localization, antiproliferative response
- MeSH terms
- Antineoplastic Agents, Humans, Ligands, Peptide Hydrolases, Protein Binding, Thalidomide, Quinolones, Lymphoma, Large B-Cell, Diffuse, Ubiquitin-Protein Ligases, Cell Line, Tumor, Adaptor Proteins, Signal Transducing, Proto-Oncogene Proteins c-bcl-6, HEK293 Cells, Proteolysis
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
