Selective Small Molecule Induced Degradation of the BET Bromodomain Protein BRD4

Selective inhibition of BET bromodomains

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BET Bromodomain Inhibition as a Therapeutic Strategy to Target c-Myc

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

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RNAi screen identifies Brd4 as a therapeutic target in acute myeloid leukaemia

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Suppression of inflammation by a synthetic histone mimic

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Targeting bromodomains: epigenetic readers of lysine acetylation

Filippakopoulos, P., & Knapp, S. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4286 · Cited by 1,274 · see citing works

Targeting MYC dependence in cancer by inhibiting BET bromodomains

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The many roles of FAS receptor signaling in the immune system

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The Mechanisms behind the Therapeutic Activity of BET Bromodomain Inhibition

Shi, J., & Vakoc, C. R. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.05.016 · Cited by 881 · see citing works

Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL

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Myc and cell cycle control

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BET domain co-regulators in obesity, inflammation and cancer

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Myc suppression of the p21Cip1 Cdk inhibitor influences the outcome of the p53 response to DNA damage

Seoane, J., Le, H.-V., & Massagué, J. (2002) · Nature · doi:10.1038/nature01119 · Cited by 683 · see citing works

Chemical Genetic Control of Protein Levels: Selective in Vivo Targeted Degradation

Schneekloth, J. S., Fonseca, F. N., Koldobskiy, M. A., Mandal, A., Deshaies, R. J., Sakamoto, K. M., & Crews, C. M. (2004) · Journal of the American Chemical Society · doi:10.1021/ja039025z · Cited by 502 · see citing works

Development of Protacs to Target Cancer-promoting Proteins for Ubiquitination and Degradation

Sakamoto, K. M., Kim, K. B., Verma, R., Ransick, A., Stein, B., Crews, C. M., & Deshaies, R. J. (2003) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t300009-mcp200 · Cited by 425 · see citing works

Structure-Guided Design and Optimization of Small Molecules Targeting the Protein–Protein Interaction between the von Hippel–Lindau (VHL) E3 Ubiquitin Ligase and the Hypoxia Inducible Factor (HIF) Alpha Subunit with in Vitro Nanomolar Affinities

Galdeano, C., Gadd, M. S., Soares, P., Scaffidi, S., Molle, I. V., Birced, I., Hewitt, S. H., Dias, D. M. G., & Ciulli, A. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5011258 · Cited by 424 · see citing works

The bromodomain interaction module

Filippakopoulos, P., & Knapp, S. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.04.045 · Cited by 384 · see citing works

Discovery and Characterization of Small Molecule Inhibitors of the BET Family Bromodomains

Chung, C., Coste, H., White, J. H. M., Mirguet, O., Wilde, J. I., Gosmini, R. L., Delves, C. J., Magny, S. D., Woodward, R., Hughes, S. A., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200108t · Cited by 334 · see citing works

Inhibition of BET Bromodomain Targets Genetically Diverse Glioblastoma

Cheng, Z., Gong, Y., Ma, Y., Lu, K., Lu, X., Pierce, L. A., Thompson, R. C., Müller, S., Knapp, S., & Wang, J. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-3066 · Cited by 302 · see citing works

The BET Bromodomain Inhibitor OTX015 Affects Pathogenetic Pathways in Preclinical B-cell Tumor Models and Synergizes with Targeted Drugs

Boi, M., Gaudio, E., Bonetti, P., Kwee, I., Bernasconi, E., Tarantelli, C., Rinaldi, A., Testoni, M., Cascione, L., Ponzoni, M., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-1561 · Cited by 290 · see citing works

RVX-208, an Inducer of ApoA-I in Humans, Is a BET Bromodomain Antagonist

McLure, K. G., Gesner, E. M., Tsujikawa, L. M., Kharenko, O. A., Attwell, S., Campeau, E., Wasiak, S., Stein, A. J., White, A., Fontano, E., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0083190 · Cited by 199 · see citing works

Place your BETs: the therapeutic potential of bromodomains

Prinjha, R. K., Witherington, J., & Lee, K. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.12.002 · Cited by 197 · see citing works

The Discovery of I-BET726 (GSK1324726A), a Potent Tetrahydroquinoline ApoA1 Up-Regulator and Selective BET Bromodomain Inhibitor

Gosmini, R. L., Nguyen, V. L., Toum, J., Simon, C., Brusq, J.-M. G., Krysa, G., Mirguet, O., Riou, A. M., Boursier, E. V., Trottet, L., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5010539 · Cited by 188 · see citing works

Small Molecule Inhibitors of Bromodomain–Acetyl-lysine Interactions

Brand, M. J. D., Measures, A. M., Wilson, B. G., Cortopassi, W. A., Alexander, R. P., Höss, M., Hewings, D. S., Rooney, T. P. C., Paton, R. S., & Conway, S. J. (2014) · ACS Chemical Biology · doi:10.1021/cb500996u · Cited by 177 · see citing works

Genome-wide localization of small molecules

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“Minimalist” Cyclopropene-Containing Photo-Cross-Linkers Suitable for Live-Cell Imaging and Affinity-Based Protein Labeling

Li, Z., Wang, D., Li, L., et al. (2014) · Journal of the American Chemical Society · doi:10.1021/ja502780z · Cited by 174 · see citing works

Design and Applications of Bifunctional Small Molecules: Why Two Heads Are Better Than One

Corson, T. W., Aberle, N. S., & Crews, C. M. (2008) · ACS Chemical Biology · doi:10.1021/cb8001792 · Cited by 166 · see citing works

An in-tumor genetic screen reveals that the BET bromodomain protein, BRD4, is a potential therapeutic target in ovarian carcinoma

Baratta, M. G., Schinzel, A. C., Zwang, Y., Bandopadhayay, P., Bowman-Colin, C., Kutt, J., Curtis, J. D., Piao, H., Wong, L. C., Kung, A. L., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422165112 · Cited by 166 · see citing works

Selective inhibition of BET bromodomain epigenetic signalling interferes with the bone-associated tumour vicious cycle

Lamoureux, F., Baud’huin, M., Calleja, L. R., Jacques, C., Berreur, M., Rédiní, F., Lecanda, F., Bradner, J. E., Heymann, D., & Ory, B. (2014) · Nature Communications · doi:10.1038/ncomms4511 · Cited by 148 · see citing works

A bump-and-hole approach to engineer controlled selectivity of BET bromodomain chemical probes

Baud, M. G. J., Lin-Shiao, E., Cardote, T. A. F., Tallant, C., Pschibul, A., Chan, K.-H., Zengerle, M., Garcia, J. R., Kwan, T. T.-L., Ferguson, F. M., et al. (2014) · Science · doi:10.1126/science.1249830 · Cited by 142 · see citing works

Bromodomains and Their Pharmacological Inhibitors

Gallenkamp, D., Gelato, K. A., Haendler, B., & Weinmann, H. (2014) · ChemMedChem · doi:10.1002/cmdc.201300434 · Cited by 126 · see citing works

From ApoA1 upregulation to BET family bromodomain inhibition: Discovery of I-BET151

Mirguet, O., Lamotte, Y., Donche, F., et al. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.01.125 · Cited by 116 · see citing works

Brd4 Is Essential for IL-1β-Induced Inflammation in Human Airway Epithelial Cells

Khan, Y. M., Kirkham, P., Barnes, P. J., & Adcock, I. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095051 · Cited by 106 · see citing works

Targeted Degradation of the Aryl Hydrocarbon Receptor by the PROTAC Approach: A Useful Chemical Genetic Tool

Lee, H., Puppala, D., Choi, E., Swanson, H. I., & Kim, K. (2007) · ChemBioChem · doi:10.1002/cbic.200700438 · Cited by 96 · see citing works

Chemical Inducers of Targeted Protein Degradation

Raina, K., & Crews, C. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.078105 · Cited by 64 · see citing works

The C-terminal domain of Brd2 is important for chromatin interaction and regulation of transcription and alternative splicing

Hnilicová, J., Hozeifi, S., Stejskalová, E., Dušková, E., Poser, I., Humpolíčková, J., Hof, M., & Staněk, D. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-06-0303 · Cited by 60 · see citing works

Two‐Headed PROTAC: An Effective New Tool for Targeted Protein Degradation

Cyrus, K., Wehenkel, M., Choi, E., Swanson, H. I., & Kim, K. (2010) · ChemBioChem · doi:10.1002/cbic.201000222 · Cited by 59 · see citing works

PROTAC targeted protein degraders: the past is prologue

Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395 · see citing works

Induced protein degradation: an emerging drug discovery paradigm

Lai, A. C., & Crews, C. M. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.211 · Cited by 1,486 · see citing works

Structural basis of PROTAC cooperative recognition for selective protein degradation

Gadd, M. S., Testa, A., Lucas, X., Chan, K.-H., Chen, W., Lamont, D. J., Zengerle, M., & Ciulli, A. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2329 · Cited by 1,242 · 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

Lessons in PROTAC Design from Selective Degradation with a Promiscuous Warhead

Bondeson, D. P., Smith, B. E., Burslem, G. M., Buhimschi, A. D., Hines, J., Jaime-Figueroa, S., Wang, J., Hamman, B. D., Ishchenko, A., & Crews, C. M. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.09.010 · Cited by 923 · see citing works

PROTAC-induced BET protein degradation as a therapy for castration-resistant prostate cancer

Raina, K., Lu, J., Qian, Y., Altieri, M., Gordon, D., Rossi, A. M. K., Wang, J., Chen, X., Dong, H., Siu, K., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1521738113 · Cited by 852 · see citing works

A selective BCL-XL PROTAC degrader achieves safe and potent antitumor activity

Khan, S., Zhang, X., Lv, D., Zhang, Q., He, Y., Zhang, P., Liu, X., Thummuri, D., Yuan, Y., Wiegand, J. S., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0668-z · Cited by 688 · see citing works

The Advantages of Targeted Protein Degradation Over Inhibition: An RTK Case Study

Burslem, G. M., Smith, B. E., Lai, A. C., Jaime-Figueroa, S., McQuaid, D. C., Bondeson, D. P., Toure, M., Dong, H., Qian, Y., Wang, J., et al. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.09.009 · Cited by 686 · 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

A Potent and Selective Small-Molecule Degrader of STAT3 Achieves Complete Tumor Regression In Vivo

Bai, L., Zhou, H., Xu, R., Zhao, Y., Chinnaswamy, K., McEachern, D., Chen, J., Yang, C.-Y., Liu, Z., Wang, M., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.10.002 · Cited by 652 · see citing works

Protein degraders enter the clinic — a new approach to cancer therapy

Chirnomas, D., Hornberger, K. R., & Crews, C. M. (2023) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-023-00736-3 · Cited by 658 · see citing works

Modular PROTAC design for the degradation of oncogenic BCR-ABL

Lai, A. C., Toure, M., Hellerschmied, D., Salami, J., Jaime‐Figueroa, S., Ko, E., Hines, J., & Crews, C. M. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201507634 · Cited by 618 · see citing works

Plasticity in binding confers selectivity in ligand-induced protein degradation

Nowak, R. P., DeAngelo, S. L., Buckley, D., He, Z., Donovan, K. A., An, J., Safaee, N., Jedrychowski, M. P., Ponthier, C. M., Ishoey, M., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0055-y · Cited by 615 · see citing works

Targeted protein degradation by PROTACs

Neklesa, T. K., Winkler, J. D., & Crews, C. M. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.02.027 · Cited by 599 · 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

Differential PROTAC substrate specificity dictated by orientation of recruited E3 ligase

Smith, B. E., Wang, S. L., Jaime-Figueroa, S., Harbin, A., Wang, J., Hamman, B. D., & Crews, C. M. (2019) · Nature Communications · doi:10.1038/s41467-018-08027-7 · Cited by 517 · see citing works

BET Proteins as Targets for Anticancer Treatment

Stathis, A., & Bertoni, F. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-17-0605 · Cited by 463 · see citing works

Protac-Induced Protein Degradation in Drug Discovery: Breaking the Rules or Just Making New Ones?

Churcher, I. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01272 · Cited by 491 · see citing works

BET Bromodomain Proteins Function as Master Transcription Elongation Factors Independent of CDK9 Recruitment

Winter, G. E., Mayer, A., Buckley, D. L., Erb, M. A., Roderick, J. E., Vittori, S., Reyes, J. M., di Iulio, J., Souza, A., Ott, C. J., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.004 · Cited by 465 · see citing works

E3 ubiquitin ligases: styles, structures and functions

Yang, Q., Zhao, J., Chen, D., & Wang, Y. (2021) · Molecular Biomedicine · doi:10.1186/s43556-021-00043-2 · Cited by 435 · see citing works

Drugging the undruggables: exploring the ubiquitin system for drug development

Huang, X., & Dixit, V. M. (2016) · Cell Research · doi:10.1038/cr.2016.31 · Cited by 427 · see citing works

A Chemoproteomic Approach to Query the Degradable Kinome Using a Multi-kinase Degrader

Huang, H.-T., Dobrovolsky, D., Paulk, J., Yang, G., Weisberg, E. L., Doctor, Z. M., Buckley, D. L., Cho, J.-H., Ko, E., Jang, J., et al. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.10.005 · Cited by 437 · see citing works

Harnessing the anti-cancer natural product nimbolide for targeted protein degradation

Spradlin, J. N., Hu, X., Ward, C. C., Brittain, S. M., Jones, M. D., Ou, L., To, M., Proudfoot, A., Ornelas, E., Woldegiorgis, M., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0304-8 · Cited by 432 · see citing works

Protein Degradation by In-Cell Self-Assembly of Proteolysis Targeting Chimeras

Lebraud, H., Wright, D. J., Johnson, C. N., & Heightman, T. D. (2016) · ACS Central Science · doi:10.1021/acscentsci.6b00280 · Cited by 413 · see citing works

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

Zorba, A., Nguyen, C., Xu, Y., Starr, J., Borzilleri, K., Smith, J., Zhu, H., Farley, K. A., Ding, W., Schiemer, J., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1803662115 · Cited by 419 · see citing works

Selective degradation of splicing factor CAPERα by anticancer sulfonamides

Uehara, T., Minoshima, Y., Sagane, K., Sugi, N. H., Mitsuhashi, K. O., Yamamoto, N., Kamiyama, H., Takahashi, K., Kotake, Y., Uesugi, M., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2363 · Cited by 396 · see citing works

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

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

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

Light-Induced Protein Degradation with Photocaged PROTACs

Xue, G., Wang, K., Zhou, D., Zhong, H., & Pan, Z. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b06422 · Cited by 377 · see citing works

Rational discovery of molecular glue degraders via scalable chemical profiling

Mayor-Ruiz, C., Bauer, S., Brand, M., Kozicka, Z., Siklos, M., Imrichova, H., Kaltheuner, I. H., Hahn, E., Seiler, K., Koren, A., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0594-x · Cited by 369 · 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

Small-molecule PROTACs: An emerging and promising approach for the development of targeted therapy drugs

An, S., & Fu, L. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.09.005 · Cited by 363 · see citing works

Mapping the Degradable Kinome Provides a Resource for Expedited Degrader Development

Donovan, K. A., Ferguson, F. M., Bushman, J. W., Eleuteri, N. A., Bhunia, D., Ryu, S., Tan, L., Shi, K., Yue, H., Liu, X., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.038 · Cited by 359 · see citing works

Antibody–PROTAC Conjugates Enable HER2-Dependent Targeted Protein Degradation of BRD4

Maneiro, M., Forte, N., Shchepinova, M. M., Kounde, C. S., Chudasama, V., Baker, J. R., & Tate, E. W. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00285 · Cited by 350 · see citing works

Covalent Ligand Screening Uncovers a RNF4 E3 Ligase Recruiter for Targeted Protein Degradation Applications

Ward, C. C., Kleinman, J. I., Brittain, S. M., Lee, P. S., Chung, C. Y. S., Kim, K., Petri, Y., Thomas, J. R., Tallarico, J. A., McKenna, J. M., et al. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.8b01083 · Cited by 336 · see citing works

Degradation of proteins by PROTACs and other strategies

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

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

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

Chemistries of bifunctional PROTAC degraders

Cao, C., He, M., Wang, L., He, Y., & Rao, Y. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00220e · Cited by 313 · see citing works

Discovery of a Keap1-dependent peptide PROTAC to knockdown Tau by ubiquitination-proteasome degradation pathway

Lu, M., Liu, T., Jiao, Q., Ji, J., Tao, M., Liu, Y., You, Q., & Jiang, Z. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.01.063 · Cited by 310 · see citing works

Discovery of MD-224 as a First-in-Class, Highly Potent, and Efficacious Proteolysis Targeting Chimera Murine Double Minute 2 Degrader Capable of Achieving Complete and Durable Tumor Regression

Li, Y., Yang, J., Aguilar, A., McEachern, D., Przybranowski, S., Liu, L., Yang, C.-Y., Wang, M., Han, X., & Wang, S. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00909 · Cited by 312 · see citing works

Addressing Kinase-Independent Functions of Fak via PROTAC-Mediated Degradation

Cromm, P. M., Samarasinghe, K. T. G., Hines, J., & Crews, C. M. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b08008 · Cited by 293 · see citing works

Exploring Targeted Degradation Strategy for Oncogenic KRASG12C

Zeng, M., Xiong, Y., Safaee, N., Nowak, R. P., Donovan, K. A., Yuan, C. J., Nabet, B., Gero, T. W., Feru, F., Li, L., et al. (2020) · Cell Chemical Biology · doi:10.1016/j.chembiol.2019.12.006 · Cited by 275 · see citing works

Using proteolysis-targeting chimera technology to reduce navitoclax platelet toxicity and improve its senolytic activity

He, Y., Zhang, X., Chang, J., Kim, H.-N., Zhang, P., Wang, Y., Khan, S., Liu, X., Zhang, X., Lv, D., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15838-0 · Cited by 280 · see citing works

Waste disposal—An attractive strategy for cancer therapy

Salami, J., & Crews, C. M. (2017) · Science · doi:10.1126/science.aam7340 · Cited by 279 · see citing works

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

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The PROTACtable genome

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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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Homolog-Selective Degradation as a Strategy to Probe the Function of CDK6 in AML

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Specific Knockdown of Endogenous Tau Protein by Peptide-Directed Ubiquitin-Proteasome Degradation

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PROteolysis TArgeting Chimeras (PROTACs) as emerging anticancer therapeutics

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Homo-PROTACs: bivalent small-molecule dimerizers of the VHL E3 ubiquitin ligase to induce self-degradation

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Molecular recognition of ternary complexes: a new dimension in the structure-guided design of chemical degraders

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Trivalent PROTACs enhance protein degradation via combined avidity and cooperativity

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PROTACs: An Emerging Targeting Technique for Protein Degradation in Drug Discovery

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Proteolysis‐targeting chimeras in drug development: A safety perspective

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Targeted protein degradation via intramolecular bivalent glues

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Functional TRIM24 degrader via conjugation of ineffectual bromodomain and VHL ligands

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Efficient targeted degradation via reversible and irreversible covalent PROTACs

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Targeted Protein Degradation by Small Molecules

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Antibody Conjugation of a Chimeric BET Degrader Enables <i>in vivo</i> Activity

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

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Chasing molecular glue degraders: screening approaches

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Simple Structural Modifications Converting a Bona fide MDM2 PROTAC Degrader into a Molecular Glue Molecule: A Cautionary Tale in the Design of PROTAC Degraders

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PROTACs: A novel strategy for cancer therapy

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Harnessing the Power of Proteolysis for Targeted Protein Inactivation

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Development of the first small molecule histone deacetylase 6 (HDAC6) degraders

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Enhancing Antiproliferative Activity and Selectivity of a FLT-3 Inhibitor by Proteolysis Targeting Chimera Conversion

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Antibody-Mediated Delivery of Chimeric BRD4 Degraders. Part 2: Improvement of In Vitro Antiproliferation Activity and In Vivo Antitumor Efficacy

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

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Improved Accuracy for Modeling PROTAC-Mediated Ternary Complex Formation and Targeted Protein Degradation <i>via</i> New <i>In Silico</i> Methodologies

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Discovery of SHP2-D26 as a First, Potent, and Effective PROTAC Degrader of SHP2 Protein

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Rationalizing PROTAC-Mediated Ternary Complex Formation Using Rosetta

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Antibody-Mediated Delivery of Chimeric BRD4 Degraders. Part 1: Exploration of Antibody Linker, Payload Loading, and Payload Molecular Properties

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

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DT2216—a Bcl-xL-specific degrader is highly active against Bcl-xL-dependent T cell lymphomas

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Highly Selective PTK2 Proteolysis Targeting Chimeras to Probe Focal Adhesion Kinase Scaffolding Functions

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Ligandability of E3 Ligases for Targeted Protein Degradation Applications

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The drug efflux pump MDR1 promotes intrinsic and acquired resistance to PROTACs in cancer cells

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Discovery of SIAIS178 as an Effective BCR-ABL Degrader by Recruiting Von Hippel–Lindau (VHL) E3 Ubiquitin Ligase

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Functional E3 ligase hotspots and resistance mechanisms to small-molecule degraders

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Targeted protein degradation and the enzymology of degraders

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Genome-wide screen identifies cullin-RING ligase machinery required for lenalidomide-dependent CRL4CRBN activity

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

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Integrative Modeling of PROTAC-Mediated Ternary Complexes

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PROTAC-mediated degradation of class I histone deacetylase enzymes in corepressor complexes

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Plasticity of the Cullin-RING Ligase Repertoire Shapes Sensitivity to Ligand-Induced Protein Degradation

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Functional Genomics Identify Distinct and Overlapping Genes Mediating Resistance to Different Classes of Heterobifunctional Degraders of Oncoproteins

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

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A Nimbolide-Based Kinase Degrader Preferentially Degrades Oncogenic BCR-ABL

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Bifunctional chemical probes inducing protein–protein interactions

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From Inhibition to Degradation: Targeting the Antiapoptotic Protein Myeloid Cell Leukemia 1 (MCL1)

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

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Novel immunomodulatory drugs and neo-substrates

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Advances in targeted degradation of endogenous proteins

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An affinity-directed protein missile system for targeted proteolysis

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Assessing the Cell Permeability of Bivalent Chemical Degraders Using the Chloroalkane Penetration Assay

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Discovery of thalidomide-based PROTAC small molecules as the highly efficient SHP2 degraders

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UBE2G1 governs the destruction of cereblon neomorphic substrates

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Targeting endogenous proteins for degradation through the affinity-directed protein missile system

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Therapeutic targeting of p300/CBP HAT domain for the treatment of NUT midline carcinoma

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Combined Targeting of the BRD4–NUT–p300 Axis in NUT Midline Carcinoma by Dual Selective Bromodomain Inhibitor, NEO2734

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CG13250, a novel bromodomain inhibitor, suppresses proliferation of multiple myeloma cells in an orthotopic mouse model

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PFI-1, a Highly Selective Protein Interaction Inhibitor, Targeting BET Bromodomains

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Data from Combined Targeting of the BRD4–NUT–p300 Axis in NUT Midline Carcinoma by Dual Selective Bromodomain Inhibitor, NEO2734

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