Proteolysis-Targeting Chimeras as Therapeutics and Tools for Biological Discovery

The ubiquitin code

Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679 · see citing works

The druggable genome

Hopkins, A. L., & Groom, C. R. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd892 · Cited by 3,305 · see citing works

Defining a Cancer Dependency Map

Tsherniak, A., Vazquez, F., Montgomery, P. G., Weir, B. A., Kryukov, G., Cowley, G. S., Gill, S., Harrington, W. F., Pantel, S., Krill-Burger, J. M., et al. (2017) · Cell · doi:10.1016/j.cell.2017.06.010 · Cited by 3,276 · see citing works

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

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

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

Lenalidomide Causes Selective Degradation of IKZF1 and IKZF3 in Multiple Myeloma Cells

Krönke, J., Udeshi, N. D., Narla, A., Grauman, P., Hurst, S. N., McConkey, M., Svinkina, T., Heckl, D., Comer, E., Li, X., et al. (2014) · Science · doi:10.1126/science.1244851 · Cited by 1,879 · see citing works

Transcription Factors Activate Genes through the Phase-Separation Capacity of Their Activation Domains

Boija, A., Klein, I. A., Sabari, B. R., Dall’Agnese, A., Coffey, E. L., Zamudio, A. V., Li, C. H., Shrinivas, K., Manteiga, J. C., Hannett, N. M., et al. (2018) · Cell · doi:10.1016/j.cell.2018.10.042 · Cited by 1,815 · 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

The current state and future directions of RNAi-based therapeutics

Setten, R. L., Rossi, J. J., & Han, S.-P. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0017-4 · Cited by 1,443 · see citing works

Catalytic in vivo protein knockdown by small-molecule PROTACs

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

RNA Interference: Biology, Mechanism, and Applications

Agrawal, N., Dasaradhi, P. V. N., Mohmmed, A., Malhotra, P., Bhatnagar, R. K., & Mukherjee, S. K. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.4.657-685.2003 · Cited by 1,312 · 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

Structure of the DDB1–CRBN E3 ubiquitin ligase in complex with thalidomide

Fischer, E. S., Böhm, K., Lydeard, J. R., Yang, H., Stadler, M. B., Cavadini, S., Nagel, J., Serluca, F., Acker, V., Lingaraju, G. M., et al. (2014) · Nature · doi:10.1038/nature13527 · Cited by 1,141 · 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

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

The increasing complexity of the ubiquitin code

Yau, R., & Rape, M. (2016) · Nature Cell Biology · doi:10.1038/ncb3358 · Cited by 1,054 · see citing works

A new era for understanding amyloid structures and disease

Iadanza, M. G., Jackson, M. P., Hewitt, E. W., Ranson, N. A., & Radford, S. E. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0060-8 · Cited by 969 · 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

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

Human chronic myeloid leukemia stem cells are insensitive to imatinib despite inhibition of BCR-ABL activity

Corbin, A. S., Agarwal, A., Loriaux, M., Cortes, J., Deininger, M. W., & Druker, B. J. (2011) · Journal of Clinical Investigation · doi:10.1172/jci35721 · Cited by 765 · see citing works

Validation of ITD mutations in FLT3 as a therapeutic target in human acute myeloid leukaemia

Smith, C. C., Wang, Q., Chin, C.-S., Salerno, S. N., Damon, L. E., Levis, M. J., Perl, A. E., Travers, K. J., Wang, S., Hunt, J. P., et al. (2012) · Nature · doi:10.1038/nature11016 · Cited by 738 · see citing works

A novel cereblon modulator recruits GSPT1 to the CRL4CRBN ubiquitin ligase

Matyskiela, M. E., Lu, G., Ito, T., Pagarigan, B., Lu, C.-C., Miller, K., Fang, W., Wang, N.-Y., Nguyen, D., Houston, J., et al. (2016) · Nature · doi:10.1038/nature18611 · Cited by 701 · 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

Project DRIVE: a compendium of cancer dependencies and synthetic lethal relationships uncovered by large-scale, deep RNAi screening

McDonald, E. R., de Weck, A., Schlabach, M. R., Billy, E., Mavrakis, K. J., Hoffman, G. R., Belur, D., Castelletti, D., Frias, E., Gampa, K., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.005 · Cited by 658 · see citing works

Road to Ruin: Targeting Proteins for Degradation in the Endoplasmic Reticulum

Smith, M. H., Ploegh, H. L., & Weissman, J. S. (2011) · Science · doi:10.1126/science.1209235 · Cited by 648 · see citing works

AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML)

Zarrinkar, P. P., Gunawardane, R. N., Cramer, M. D., Gardner, M. F., Brigham, D., Belli, B., Karaman, M. W., Pratz, K. W., Pallares, G., Chao, Q., et al. (2009) · Blood · doi:10.1182/blood-2009-05-222034 · Cited by 641 · see citing works

Targeted intracellular protein degradation induced by a small molecule: En route to chemical proteomics

Schneekloth, A. R., Pucheault, M., Tae, H. S., & Crews, C. M. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.07.114 · Cited by 635 · 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

Targeting the von Hippel-Lindau E3 ubiquitin ligase using small molecules to disrupt the VHL/HIF-1α interaction

Buckley, D. L., Van Molle, I., Gareiss, P. C., Tae, H. S., Michel, J., Noblin, D. J., Jorgensen, W. L., Ciulli, A., & Crews, C. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja209924v · Cited by 569 · 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

Redesigning an FKBP–ligand interface to generate chemical dimerizers with novel specificity

Clackson, T., Yang, W., Rozamus, L. W., Hatada, M., Amara, J. F., Rollins, C. T., Stevenson, L. F., Magari, S. R., Wood, S. A., Courage, N. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10437 · Cited by 558 · see citing works

A Method for the Acute and Rapid Degradation of Endogenous Proteins

Clift, D., McEwan, W. A., Labzin, L. I., Konieczny, V., Mogessie, B., James, L. C., & Schuh, M. (2017) · Cell · doi:10.1016/j.cell.2017.10.033 · Cited by 531 · 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

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

Protein quality control and elimination of protein waste: The role of the ubiquitin–proteasome system

Amm, I., Sommer, T., & Wolf, D. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.031 · Cited by 493 · see citing works

HaloPROTACS: Use of Small Molecule PROTACs to Induce Degradation of HaloTag Fusion Proteins

Buckley, D. L., Raina, K., Darricarrere, N., Hines, J., Gustafson, J. L., Smith, I. E., Miah, A. H., Harling, J. D., & Crews, C. M. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00442 · Cited by 488 · see citing works

Electrophilic PROTACs that degrade nuclear proteins by engaging DCAF16

Zhang, X., Crowley, V. M., Wucherpfennig, T. G., Dix, M. M., & Cravatt, B. F. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0279-5 · Cited by 487 · 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

Substrate-Assisted Inhibition of Ubiquitin-like Protein-Activating Enzymes: The NEDD8 E1 Inhibitor MLN4924 Forms a NEDD8-AMP Mimetic In Situ

Brownell, J. E., Sintchak, M. D., Gavin, J. M., Liao, H., Bruzzese, F. J., Bump, N. J., Soucy, T. A., Milhollen, M. A., Yang, X., Burkhardt, A. L., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2009.12.024 · Cited by 468 · 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

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

Small-molecule hydrophobic tagging–induced degradation of HaloTag fusion proteins

Neklesa, T. K., Tae, H. S., Schneekloth, A. R., Stulberg, M. J., Corson, T. W., Sundberg, T. B., Raina, K., Holley, S. A., & Crews, C. M. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.597 · Cited by 429 · see citing works

Selective estrogen receptor modulators (SERMs) and selective estrogen receptor degraders (SERDs) in cancer treatment.

Patel, H., & Bihani, T. (2017) · Pharmacology and Therapeutics · doi:10.1016/j.pharmthera.2017.12.012 · Cited by 423 · see citing works

A non-canonical SWI/SNF complex is a synthetic lethal target in cancers driven by BAF complex perturbation

Michel, B. C., D’Avino, A. R., Cassel, S. H., Mashtalir, N., McKenzie, Z. M., McBride, M. J., Valencia, A. M., Zhou, Q., Bocker, M., Soares, L. M. M., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0221-1 · Cited by 423 · 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

Perilous journey: a tour of the ubiquitin–proteasome system

Kleiger, G., & Mayor, T. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.12.003 · Cited by 409 · see citing works

Protein Knockdown Using Methyl Bestatin−Ligand Hybrid Molecules: Design and Synthesis of Inducers of Ubiquitination-Mediated Degradation of Cellular Retinoic Acid-Binding Proteins

Itoh, Y., Ishikawa, M., Naito, M., & Hashimoto, Y. (2010) · Journal of the American Chemical Society · doi:10.1021/ja100691p · Cited by 404 · see citing works

Discovery of ARD-69 as a Highly Potent Proteolysis Targeting Chimera (PROTAC) Degrader of Androgen Receptor (AR) for the Treatment of Prostate Cancer

Han, X., Wang, C., Qin, C., Xiang, W., Fernández‐Salas, E., Yang, C., Wang, M., Zhao, L., Xu, T., Chinnaswamy, K., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01631 · Cited by 404 · see citing works

E3 ubiquitin ligases

Ardley, H. C., & Robinson, P. A. (2005) · Essays in Biochemistry · doi:10.1042/eb0410015 · Cited by 392 · 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

Pnpla3I148M knockin mice accumulate PNPLA3 on lipid droplets and develop hepatic steatosis

Smagris, E., BasuRay, S., Li, J., Huang, Y., Lai, K. V., Gromada, J., Cohen, J. C., & Hobbs, H. H. (2015) · Hepatology · doi:10.1002/hep.27242 · Cited by 379 · see citing works

The recognition of ubiquitinated proteins by the proteasome

Grice, G. L., & Nathan, J. A. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2255-5 · Cited by 370 · see citing works

Acquired Resistance to BET-PROTACs (Proteolysis-Targeting Chimeras) Caused by Genomic Alterations in Core Components of E3 Ligase Complexes

Zhang, L., Riley-Gillis, B., Vijay, P., & Shen, Y. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-18-1129 · Cited by 365 · see citing works

Androgen receptor degradation by the proteolysis-targeting chimera ARCC-4 outperforms enzalutamide in cellular models of prostate cancer drug resistance

Salami, J., Alabi, S., Willard, R. R., Vitale, N. J., Wang, J., Dong, H., Jin, M., McDonnell, D. P., Crew, A. P., Neklesa, T. K., et al. (2018) · Communications Biology · doi:10.1038/s42003-018-0105-8 · Cited by 349 · see citing works

MDM2-Recruiting PROTAC Offers Superior, Synergistic Antiproliferative Activity via Simultaneous Degradation of BRD4 and Stabilization of p53

Hines, J., Lartigue, S., Dong, H., Qian, Y., & Crews, C. M. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-2918 · Cited by 348 · 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

PHOTACs enable optical control of protein degradation

Reynders, M., Matsuura, B. S., Bérouti, M., Simoneschi, D., Marzio, A., Pagano, M., & Trauner, D. H. (2020) · Science Advances · doi:10.1126/sciadv.aay5064 · Cited by 333 · see citing works

Mutant NPM1 Maintains the Leukemic State through HOX Expression

Brunetti, L., Gundry, M. C., Sorcini, D., Guzman, A. G., Huang, Y., Ramabadran, R., Gionfriddo, I., Mezzasoma, F., Milano, F., Nabet, B., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.08.005 · Cited by 317 · see citing works

HaloTag Technology: A Versatile Platform for Biomedical Applications

England, C. G., Luo, H., & Cai, W. (2015) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.5b00191 · Cited by 313 · see citing works

Transcription control by the ENL YEATS domain in acute leukaemia

Erb, M. A., Scott, T. G., Li, B. E., Xie, H., Paulk, J., Seo, H., Souza, A., Roberts, J. M., Dastjerdi, S., Buckley, D. L., et al. (2017) · Nature · doi:10.1038/nature21688 · Cited by 313 · see citing works

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

Riching, K. M., Mahan, S. D., Corona, C. R., McDougall, M. G., Vasta, J. D., Robers, M. B., Urh, M., & Daniels, D. L. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00692 · Cited by 307 · 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 International Edition · doi:10.1002/anie.201611281 · Cited by 294 · 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 · cited 1× · see citing works

Discovery of ERD-308 as a Highly Potent Proteolysis Targeting Chimera (PROTAC) Degrader of Estrogen Receptor (ER)

Hu, J., Hu, B., Wang, M., Xu, F., Miao, B., Yang, C., Wang, M., Liu, Z., Hayes, D. F., Chinnaswamy, K., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01572 · Cited by 286 · see citing works

Accumulation of PNPLA3 on lipid droplets is the basis of associated hepatic steatosis

BasuRay, S., Wang, Y., Šmagris, Ē., Cohen, J. C., & Hobbs, H. H. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1901974116 · Cited by 285 · see citing works

Targeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models

Silva, M. C., Ferguson, F. M., Cai, Q., Donovan, K. A., Nandi, G., Patnaik, D., Zhang, T., Huang, H.-T., Lucente, D. E., Dickerson, B. C., et al. (2019) · eLife · doi:10.7554/elife.45457 · Cited by 283 · see citing works

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

Crew, A. P., Raina, K., Dong, H., Qian, Y., Wang, J., Vigil, D., Serebrenik, Y. V., Hamman, B. D., Morgan, A., Ferraro, C., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00635 · Cited by 257 · see citing works

Small-Molecule Modulation of Protein Homeostasis.

Burslem, G., & Crews, C. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00077 · Cited by 256 · see citing works

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

Chu, T.-T., Gao, N., Li, Q.-Q., Chen, P.-G., Yang, X.-F., Chen, Y.-X., Zhao, Y.-F., & Li, Y.-M. (2016) · Cell Chemical Biology · doi:10.1016/j.chembiol.2016.02.016 · Cited by 247 · see citing works

Bortezomib

Paramore, A., & Frantz, S. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1159 · Cited by 244 · see citing works

Potent and selective chemical probe of hypoxic signalling downstream of HIF-α hydroxylation via VHL inhibition

Frost, J., Galdeano, C., Soares, P., Gadd, M. S., Grzes, K. M., Ellis, L. C. J., Epemolu, O., Shimamura, S., Bantscheff, M., Grandi, P., et al. (2016) · Nature Communications · doi:10.1038/ncomms13312 · Cited by 242 · see citing works

A scalable strategy for high-throughput GFP tagging of endogenous human proteins

Leonetti, M. D., Sekine, S., Kamiyama, D., Weissman, J. S., & Huang, B. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606731113 · Cited by 225 · see citing works

Functional TRIM24 degrader via conjugation of ineffectual bromodomain and VHL ligands

Gechijian, L. N., Buckley, D. L., Lawlor, M. A., Reyes, J. M., Paulk, J., Ott, C. J., Winter, G. E., Erb, M. A., Scott, T. G., Xu, M., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0010-y · Cited by 222 · see citing works

ARV-110: An oral androgen receptor PROTAC degrader for prostate cancer.

Neklesa, T. K., Snyder, L. B., Willard, R. R., Vitale, N., Pizzano, J., Gordon, D., Bookbinder, M., Macaluso, J., Dong, H., Ferraro, C., et al. (2019) · Journal of Clinical Oncology · doi:10.1200/jco.2019.37.7_suppl.259 · Cited by 219 · see citing works

Multiplexed Proteome Dynamics Profiling Reveals Mechanisms Controlling Protein Homeostasis

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Targeted degradation of BRD9 reverses oncogenic gene expression in synovial sarcoma

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A direct high-throughput protein quantification strategy facilitates discovery and characterization of a celastrol-derived BRD4 degrader

Payne, N. C., Maksoud, S., Tannous, B. A., & Mazitschek, R. (2022) · Cell Chemical Biology · doi:10.1016/j.chembiol.2022.05.003 · Cited by 44 · see citing works

Targeting oncoproteins with a positive selection assay for protein degraders

Koduri, V., Duplaquet, L., Lampson, B. L., Wang, A. C., Sabet, A. H., Ishoey, M., Paulk, J., Teng, M., Harris, I. S., Endress, J. E., et al. (2021) · Science Advances · doi:10.1126/sciadv.abd6263 · Cited by 44 · see citing works

Development of NanoLuc-targeting protein degraders and a universal reporter system to benchmark tag-targeted degradation platforms

Grohmann, C., Magtoto, C. M., Walker, J. R., Chua, N. K., Gabrielyan, A., Hall, M., Cobbold, S. A., Mieruszynski, S., Brzozowski, M., Simpson, D. S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29670-1 · Cited by 43 · see citing works

An IMiD-induced SALL4 degron system for selective degradation of target proteins

Yamanaka, S., Shoya, Y., Matsuoka, S., Nishida-Fukuda, H., Shibata, N., & Sawasaki, T. (2020) · Communications Biology · doi:10.1038/s42003-020-01240-5 · Cited by 29 · see citing works

Peptide-Based PROTAC: The Predator of Pathological Proteins

Au, Y. Z., Wang, T., Sigua, L. H., & Qi, J. (2020) · Cell Chemical Biology · doi:10.1016/j.chembiol.2020.06.002 · Cited by 28 · 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

Scrutinizing the Therapeutic Potential of PROTACs in the Management of Alzheimer’s Disease

Bhatia, S., Singh, M., Singh, T., & Singh, V. (2023) · Neurochemical Research · doi:10.1007/s11064-022-03722-w · Cited by 22 · 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

Dissecting Intracellular Proteolysis Using Small Molecule Inhibitors and Molecular Probes

Ovaa, H., Overkleeft, H. S., Kessler, B. M., & Ploegh, H. L. (2005) · doi:10.1002/9783527620210.ch3 · Cited by 2 · see citing works

Dissecting Intracellular Proteolysis Using Small Molecule Inhibitors and Molecular Probes

Ovaa, H., Overkleeft, H. S., Kessler, B. M., & Ploegh, H. L. (2007) · doi:10.1002/9783527619320.ch3a

Autoregulation of the 26S proteasome by in situ ubiquitination

Jacobson, A. D., MacFadden, A., Wu, Z., et al. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-10-0585 · Cited by 70 · see citing works

Regulation of proteolysis

Attaix, D., Combaret, L., Pouch-Pélissier, M.-N., & Taillandier, D. (2001) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-200101000-00009 · Cited by 74 · see citing works

Ubiquitin pools, ubiquitin mRNA levels, and ubiquitin-mediated proteolysis in aging human fibroblasts

Pan, J.-X., Short, S. R., Goff, S. A., & Dice, J. F. (1993) · Experimental Gerontology · doi:10.1016/0531-5565(93)90018-9 · Cited by 30 · see citing works