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Delineating the role of cooperativity in the design of potent PROTACs for BTK

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Quantitative Live-Cell Kinetic Degradation and Mechanistic Profiling of PROTAC Mode of Action

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Degradation of the BAF Complex Factor BRD9 by Heterobifunctional Ligands

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Discovery of QCA570 as an Exceptionally Potent and Efficacious Proteolysis Targeting Chimera (PROTAC) Degrader of the Bromodomain and Extra-Terminal (BET) Proteins Capable of Inducing Complete and Durable Tumor Regression

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Chemically Induced Degradation of Sirtuin 2 (Sirt2) by a Proteolysis Targeting Chimera (PROTAC) Based on Sirtuin Rearranging Ligands (SirReals)

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Identification and Characterization of Von Hippel-Lindau-Recruiting Proteolysis Targeting Chimeras (PROTACs) of TANK-Binding Kinase 1

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BRD7, a Novel PBAF-specific SWI/SNF Subunit, Is Required for Target Gene Activation and Repression in Embryonic Stem Cells

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BRD7 is a candidate tumour suppressor gene required for p53 function

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Modulating PCAF/GCN5 Immune Cell Function through a PROTAC Approach

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Gain at chromosomal region 5p15.33, containing TERT, is the most frequent genetic event in early stages of non-small cell lung cancer

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Translation termination factor GSPT1 is a phenotypically relevant off-target of heterobifunctional phthalimide degraders

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LP99: Discovery and Synthesis of the First Selective BRD7/9 Bromodomain Inhibitor

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Homo-PROTACs for the Chemical Knockdown of Cereblon

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Target Engagement in Lead Generation

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Jostling for Position: Optimizing Linker Location in the Design of Estrogen Receptor‐Targeting PROTACs

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BRD7, a Tumor Suppressor, Interacts with p85α and Regulates PI3K Activity

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BRD7 Regulates XBP1s’ Activity and Glucose Homeostasis through Its Interaction with the Regulatory Subunits of PI3K

Park, S. W., Herrema, H., Salazar, M., Çakır, I., Cabi, S., Sahin, F. B., Chiu, Y., Cantley, L. C., & Özcan, U. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.006 · Cited by 76 · see citing works

Evidence for a Stereoelectronic Effect in Human Oxygen Sensing

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Design and synthesis of potent and selective inhibitors of BRD7 and BRD9 bromodomains

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BRD7: a novel tumor suppressor gene in different cancers.

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Inhibition of bromodomain-containing protein 9 for the prevention of epigenetically-defined drug resistance

Crawford, T. D., Vartanian, S., Côté, A., Bellon, S. F., Duplessis, M., Flynn, E. M., Hewitt, M. C., Huang, H.-R., Kiefer, J. R., Murray, J. M., et al. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.05.063 · Cited by 43 · see citing works

Degradation of the BAF Complex Factor BRD9 by Heterobifunctional Ligands

Remillard, D., Buckley, D. L., Paulk, J., Brien, G. L., Sonnett, M., Seo, H., Dastjerdi, S., Wühr, M., Dhe‐Paganon, S., Armstrong, S. A., et al. (2017) · Angewandte Chemie · doi:10.1002/ange.201611281 · Cited by 23 · see citing works

Deconjugation of α,β-unsaturated esters and an intramolecular Michael reaction of bis-α,β-unsaturated esters with trialkylsilyl trifluoromethanesulfonate in the presence of tertiary amine: synthesis of (±)-ricciocarpin A

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Preparation of Polyfunctional Naphthyridines by Cobalt-Catalyzed Cross-Couplings of Halogenated Naphthyridines with Magnesium and Zinc Organometallics

Greiner, R., Ziegler, D., Cibu, D., et al. (2017) · Organic Letters · doi:10.1021/acs.orglett.7b03242 · Cited by 22 · see citing works

Synthesis of a Library of Propargylated and PEGylated α-Hydroxy Acids Toward “Clickable” Polylactides via Hydrolysis of Cyanohydrin Derivatives

Zhang, Q., Ren, H., & Baker, G. L. (2014) · The Journal of Organic Chemistry · doi:10.1021/jo5016135 · Cited by 16 · 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

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

Development of targeted protein degradation therapeutics

Chamberlain, P. P., & Hamann, L. G. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0362-y · Cited by 489 · 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 &amp; Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2019.04.030 · Cited by 422 · 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

SPR-measured dissociation kinetics of PROTAC ternary complexes influence target degradation rate

Roy, M. J., Winkler, S., Hughes, S. J., Whitworth, C., Galant, M., Farnaby, W., Rumpel, K., & Ciulli, A. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00092 · Cited by 386 · 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

PROTACs: great opportunities for academia and industry (an update from 2020 to 2021)

He, M., Cao, C., Ni, Z., Liu, Y., Song, P., Hao, S., He, Y., Sun, X., & Rao, Y. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00999-9 · Cited by 283 · 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

Trivalent PROTACs enhance protein degradation via combined avidity and cooperativity

Imaide, S., Riching, K. M., Makukhin, N., Vetma, V., Whitworth, C., Hughes, S. J., Trainor, N., Mahan, S. D., Murphy, N., Cowan, A. D., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00878-4 · Cited by 251 · see citing works

Targeted protein degradation via intramolecular bivalent glues

Hsia, O., Hinterndorfer, M., Cowan, A. D., Iso, K., Ishida, T., Sundaramoorthy, R., Nakasone, M. A., Imrichova, H., Schätz, C., Rukavina, A., et al. (2024) · Nature · doi:10.1038/s41586-024-07089-6 · Cited by 222 · see citing works

Extended pharmacodynamic responses observed upon PROTAC-mediated degradation of RIPK2

Mares, A., Miah, A. H., Smith, I. E. D., Rackham, M., Thawani, A. R., Cryan, J., Haile, P. A., Votta, B. J., Beal, A. M., Capriotti, C., et al. (2020) · Communications Biology · doi:10.1038/s42003-020-0868-6 · Cited by 232 · see citing works

Recent Developments in PROTAC‐Mediated Protein Degradation: From Bench to Clinic

Hu, Z., & Crews, C. M. (2022) · ChemBioChem · doi:10.1002/cbic.202100270 · Cited by 231 · see citing works

PROTAC-DB: an online database of PROTACs

Weng, G., Shen, C., Cao, D., Gao, J., Dong, X., He, Q., Yang, B., Li, D., Wu, J., & Hou, T. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa807 · Cited by 219 · see citing works

RNA‐PROTACs: Degraders of RNA‐Binding Proteins

Ghidini, A., Cléry, A., Halloy, F., Allain, F. H. T., & Hall, J. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202012330 · Cited by 197 · 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

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

Rationalizing PROTAC-Mediated Ternary Complex Formation Using Rosetta

Bai, N., Miller, S. A., Andrianov, G. V., Yates, M., Kirubakaran, P., & Karanicolas, J. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c01451 · Cited by 157 · see citing works

Amide-to-Ester Substitution as a Strategy for Optimizing PROTAC Permeability and Cellular Activity

Klein, V. G., Bond, A. G., Craigon, C., Lokey, R. S., & Ciulli, A. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01496 · Cited by 152 · see citing works

Systematic exploration of different E3 ubiquitin ligases: an approach towards potent and selective CDK6 degraders

Steinebach, C., Ng, Y. L. D., Sosič, I., Lee, C.-S., Chen, S., Lindner, S., Vu, L. P., Bricelj, A., Haschemi, R., Monschke, M., et al. (2020) · Chemical Science · doi:10.1039/d0sc00167h · Cited by 148 · 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

Discovery of PROTAC BCL-XL degraders as potent anticancer agents with low on-target platelet toxicity

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

Proteolysis Targeting Chimeras for the Selective Degradation of Mcl-1/Bcl-2 Derived from Nonselective Target Binding Ligands

Wang, 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

Snapshots and ensembles of BTK and cIAP1 protein degrader ternary complexes

Schiemer, J., Horst, R., Meng, Y., Montgomery, J. I., Xu, Y., Feng, X., Borzilleri, K., Uccello, D. P., Leverett, C., Brown, S., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-020-00686-2 · Cited by 113 · see citing works

Bifunctional chemical probes inducing protein–protein interactions

Maniaci, C., & Ciulli, A. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.07.003 · Cited by 100 · 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

In vitro and in vivo degradation of programmed cell death ligand 1 (PD-L1) by a proteolysis targeting chimera (PROTAC)

Wang, Y., Zhou, Y., Cao, S., Sun, Y., Dong, Z., Li, C., Wang, H., Yao, Y., Yu, H., Song, X., et al. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104833 · Cited by 96 · see citing works

Utilizing PROTAC technology to address the on-target platelet toxicity associated with inhibition of BCL-X _L

Zhang, X., Thummuri, D., He, Y., Liu, X., Zhang, P., Zhou, D., & Zheng, G. (2019) · Chemical Communications · doi:10.1039/c9cc07217a · Cited by 86 · see citing works

Development of selective small molecule MDM2 degraders based on nutlin

Wang, B., Wu, S., Liu, J., Yang, K., Xie, H., & Tang, W. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.05.046 · Cited by 77 · see citing works

Discovery of a Novel BCL-X_L PROTAC Degrader with Enhanced BCL-2 Inhibition

Pal, P., Thummuri, D., Lv, D., Liu, X., Zhang, P., Hu, W., Poddar, S. K., Hua, N., Khan, S., Yuan, Y., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00517 · Cited by 60 · see citing works

Structural Characterization of Degrader-Induced Ternary Complexes Using Hydrogen–Deuterium Exchange Mass Spectrometry and Computational Modeling: Implications for Structure-Based Design

Eron, S. J., Huang, H., Agafonov, R. V., Fitzgerald, M. E., Patel, J., Michael, R. E., Lee, T. D., Hart, A. A., Shaulsky, J., Nasveschuk, C. G., et al. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00376 · Cited by 57 · see citing works

Design and linkage optimization of ursane-thalidomide-based PROTACs and identification of their targeted-degradation properties to MDM2 protein

Qi, Z., Yang, G., Deng, T., Wang, J., Zhou, H., Popov, S. A., Shults, E. E., & Wang, C. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104901 · Cited by 39 · see citing works

Proteasomal and lysosomal degradation for specific and durable suppression of immunotherapeutic targets

Wang, Y., Deng, S., & Xu, J. (2020) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2020.0066 · Cited by 10 · see citing works

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БАЗАРБАЕВА, Ә. А., Майгельдиева, Ш. М., & ЖҮНДІБАЕВА, Т. Н. (2023) · Pedagogy and Psychology · doi:10.51889/2077-6861.2023.1.30.016

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Кaмирдиновa, Н., & Кaлиевa, Ш. С. (2018) · DOAJ (DOAJ: Directory of Open Access Journals)

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Mustafa, N. H., Kelesbayev, D., & Alibekova, Z. D. (2018) · The Journal of Economic Research & Business Administration · doi:10.26577/be-2018-2-2141

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Fujii, M., & Nakamoto, R. (2002) · Scientiae mathematicae Japonicae · Cited by 15 · see citing works