Ligandability of E3 Ligases for Targeted Protein Degradation Applications

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

C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00507-4 · Cited by 3,333 · 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

Identification of a Primary Target of Thalidomide Teratogenicity

Ito, T., Ando, H., Suzuki, T., Ogura, T., Hotta, K., Imamura, Y., Yamaguchi, Y., & Handa, H. (2010) · Science · doi:10.1126/science.1177319 · Cited by 2,136 · 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

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

Quantitative reactivity profiling predicts functional cysteines in proteomes

Weerapana, E., Wang, C., Simon, G. M., Richter, F., Khare, S., Dillon, M. B. D., Bachovchin, D. A., Mowen, K., Baker, D., & Cravatt, B. F. (2010) · Nature · doi:10.1038/nature09472 · Cited by 1,684 · see citing works

The Myeloma Drug Lenalidomide Promotes the Cereblon-Dependent Destruction of Ikaros Proteins

Lu, G., Middleton, R. E., Sun, H., Naniong, M., Ott, C. J., Mitsiades, C. S., Wong, K.-K., Bradner, J. E., & Kaelin, W. G. (2014) · Science · doi:10.1126/science.1244917 · Cited by 1,583 · 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

Lysosome-targeting chimaeras for degradation of extracellular proteins

Banik, S. M., Pedram, K., Wisnovsky, S., Ahn, G., Riley, N. M., & Bertozzi, C. R. (2020) · Nature · doi:10.1038/s41586-020-2545-9 · Cited by 1,199 · 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

Proteolysis-Targeting Chimeras as Therapeutics and Tools for Biological Discovery

Burslem, G. M., & Crews, C. M. (2020) · Cell · doi:10.1016/j.cell.2019.11.031 · Cited by 1,079 · see citing works

Selective Small Molecule Induced Degradation of the BET Bromodomain Protein BRD4

Zengerle, M., Chan, K.-H., & Ciulli, A. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00216 · Cited by 1,056 · 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

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

Nonproteolytic Functions of Ubiquitin in Cell Signaling

Chen, Z. J., & Sun, L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.014 · Cited by 921 · see citing works

Lenalidomide induces ubiquitination and degradation of CK1α in del(5q) MDS

Krönke, J., Fink, E. C., Hollenbach, P. W., MacBeth, K. J., Hurst, S. N., Udeshi, N. D., Chamberlain, P. P., Mani, D. R., Man, H. W., Gandhi, A. K., et al. (2015) · Nature · doi:10.1038/nature14610 · Cited by 863 · see citing works

PROteolysis TArgeting Chimeras (PROTACs) — Past, present and future

Pettersson, M., & Crews, C. M. (2019) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2019.01.002 · Cited by 818 · see citing works

Cereblon is a direct protein target for immunomodulatory and antiproliferative activities of lenalidomide and pomalidomide

Lopez-Girona, A., Mendy, D., Ito, T., Miller, K., Gandhi, A. K., Kang, J., Karasawa, S., Carmel, G., Jackson, P., Abbasian, M., et al. (2012) · Leukemia · doi:10.1038/leu.2012.119 · Cited by 814 · see citing works

Anticancer sulfonamides target splicing by inducing RBM39 degradation via recruitment to DCAF15

Han, T., Goralski, M., Gaskill, N., Capota, E., Kim, J., Ting, T. C., Xie, Y., Williams, N. S., & Nijhawan, D. (2017) · Science · doi:10.1126/science.aal3755 · Cited by 762 · see citing works

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

Hon, W.-C., Wilson, M. I., Harlos, K., Claridge, T. D. W., Schofield, C. J., Pugh, C. W., Maxwell, P. H., Ratcliffe, P. J., Stuart, D. I., & Jones, E. Y. (2002) · Nature · doi:10.1038/nature00767 · Cited by 751 · 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

AUTACs: Cargo-Specific Degraders Using Selective Autophagy

Takahashi, D., Moriyama, J., Nakamura, T., Miki, E., Takahashi, E., Sato, A., Akaike, T., Itto-Nakama, K., & Arimoto, H. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.009 · Cited by 675 · see citing works

Advancing targeted protein degradation for cancer therapy

Dale, B., Cheng, M., Park, K., Kanıskan, H. Ü., Xiong, Y., & Jin, J. J. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00365-x · Cited by 671 · see citing works

A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes

Ciehanover, A., Hod, Y., & Hershko, A. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)91249-4 · Cited by 649 · 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

The Rise of Molecular Glues

Schreiber, S. L. (2021) · Cell · doi:10.1016/j.cell.2020.12.020 · Cited by 598 · 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

Mechanism-Based Profiling of Enzyme Families

Evans, M. J., & Cravatt, B. F. (2006) · Chemical Reviews · doi:10.1021/cr050288g · Cited by 568 · see citing works

Defining the human C2H2 zinc finger degrome targeted by thalidomide analogs through CRBN

Sievers, Q. L., Petzold, G., Bunker, R. D., Renneville, A., Słabicki, M., Liddicoat, B. J., Abdulrahman, W., Mikkelsen, T., Ebert, B. L., & Thomä, N. H. (2018) · Science · doi:10.1126/science.aat0572 · Cited by 537 · see citing works

Structure of the human Cereblon-DDB1-lenalidomide complex reveals basis for responsiveness to thalidomide analogs

Chamberlain, P. P., Lopez-Girona, A., Miller, K., Carmel, G., Pagarigan, B., Chie-Leon, B., Rychak, E., Corral, L. G., Ren, Y. J., Wang, M., et al. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2874 · Cited by 531 · see citing works

PROTACs: An Emerging Therapeutic Modality in Precision Medicine

Nalawansha, D. A., & Crews, C. M. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.07.020 · Cited by 514 · see citing works

Thalidomide promotes degradation of SALL4, a transcription factor implicated in Duane Radial Ray syndrome

Donovan, K. A., An, J., Nowak, R. P., Yuan, J. C., Fink, E. C., Berry, B. C., Ebert, B. L., & Fischer, E. S. (2018) · eLife · doi:10.7554/elife.38430 · Cited by 509 · 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

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

Global profiling of lysine reactivity and ligandability in the human proteome

Hacker, S. M., Backus, K. M., Lazear, M. R., Forli, S., Correia, B. E., & Cravatt, B. F. (2017) · Nature Chemistry · doi:10.1038/nchem.2826 · Cited by 485 · see citing works

Targeted Degradation of Oncogenic KRAS ^G12C by VHL-Recruiting PROTACs

Bond, M. J., Chu, L., Nalawansha, D. A., Li, K., & Crews, C. M. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00411 · Cited by 450 · 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

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

Targeted Protein Degradation: from Chemical Biology to Drug Discovery

Cromm, P. M., & Crews, C. M. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.05.024 · Cited by 423 · 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

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

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

An Activity-Guided Map of Electrophile-Cysteine Interactions in Primary Human T Cells

Vinogradova, E. V., Zhang, X., Remillard, D., Lazar, D. C., Suciu, R. M., Wang, Y., Bianco, G., Yamashita, Y., Crowley, V. M., Schafroth, M. A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.07.001 · Cited by 351 · 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

Deubiquitinase-targeting chimeras for targeted protein stabilization

Henning, N. J., Boike, L., Spradlin, J. N., Ward, C. C., Liu, G., Zhang, E., Belcher, B. P., Brittain, S. M., Hesse, M. J., Dovala, D., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-00971-2 · Cited by 344 · see citing works

Activity-based protein profiling for biochemical pathway discovery in cancer

Nomura, D. K., Dix, M. M., & Cravatt, B. F. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2901 · Cited by 342 · see citing works

SALL4 mediates teratogenicity as a thalidomide-dependent cereblon substrate

Matyskiela, M. E., Couto, S., Zheng, X., Lu, G., Hui, J., Stamp, K., Drew, C., Ren, Y., Wang, M., Carpenter, A., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0129-x · Cited by 338 · 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

Reimagining high-throughput profiling of reactive cysteines for cell-based screening of large electrophile libraries

Kuljanin, M., Mitchell, D. C., Schweppe, D. K., Gikandi, A. S., Nusinow, D. P., Bulloch, N. J., Vinogradova, E. V., Wilson, D. L., Kool, E. T., Mancias, J. D., et al. (2021) · Nature Biotechnology · doi:10.1038/s41587-020-00778-3 · Cited by 305 · see citing works

A chemoproteomic platform to quantitatively map targets of lipid-derived electrophiles

Wang, C., Weerapana, E., Blewett, M. M., & Cravatt, B. F. (2013) · Nature Methods · doi:10.1038/nmeth.2759 · Cited by 303 · 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

Chemical Proteomics Identifies Druggable Vulnerabilities in a Genetically Defined Cancer

Bar-Peled, L., Kemper, E. K., Suciu, R. M., Vinogradova, E. V., Backus, K. M., Horning, B. D., Paul, T. A., Ichu, T.-A., Svensson, R. U., Olucha, J., et al. (2017) · Cell · doi:10.1016/j.cell.2017.08.051 · Cited by 262 · see citing works

Structural basis of indisulam-mediated RBM39 recruitment to DCAF15 E3 ligase complex

Bussiere, D. E., Xie, L., Srinivas, H., Shu, W., Burke, A., Be, C., Zhao, J., Godbole, A., King, D., Karki, R. G., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-019-0411-6 · Cited by 257 · 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

Proteolysis targeting chimeras (PROTACs) come of age: entering the third decade of targeted protein degradation

Bond, M. J., & Crews, C. M. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00011j · Cited by 227 · see citing works

Resolution of the ATP-dependent proteolytic system from reticulocytes: a component that interacts with ATP.

Hershko, A., Ciechanover, A. J., & Rose, I. A. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.7.3107 · Cited by 224 · see citing works

Discovery of a Covalent FEM1B Recruiter for Targeted Protein Degradation Applications

Henning, N. J., Manford, A. G., Spradlin, J. N., Brittain, S. M., Zhang, E., McKenna, J. M., Tallarico, J. A., Schirle, M., Rape, M., & Nomura, D. K. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c03980 · Cited by 221 · see citing works

Structural complementarity facilitates E7820-mediated degradation of RBM39 by DCAF15

Faust, T. B., Yoon, H., Nowak, R. P., Donovan, K. A., Li, Z., Cai, Q., Eleuteri, N. A., Zhang, T., Gray, N. S., & Fischer, E. S. (2020) · Nature Chemical Biology · doi:10.1038/s41589-019-0378-3 · Cited by 218 · see citing works

DCAF11 Supports Targeted Protein Degradation by Electrophilic Proteolysis-Targeting Chimeras

Zhang, X., Luukkonen, L. M., Eissler, C. L., Crowley, V. M., Yamashita, Y., Schafroth, M. A., Kikuchi, S., Weinstein, D. S., Symons, K. T., Nordin, B. E., et al. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c00990 · Cited by 199 · see citing works

Phosphorylation-Inducing Chimeric Small Molecules

Siriwardena, S. U., Godage, D. N. P. M., Shoba, V. M., Lai, S., Shi, M., Wu, P., Chaudhary, S. K., Schreiber, S. L., & Choudhary, A. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c05537 · Cited by 196 · see citing works

BacPROTACs mediate targeted protein degradation in bacteria

Morreale, F. E., Kleine, S., Leodolter, J., Junker, S., Hoi, D. M., Ovchinnikov, S., Okun, A., Kley, J., Kurzbauer, R., Junk, L., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.009 · Cited by 196 · see citing works

Chemoproteomics-enabled discovery of covalent RNF114-based degraders that mimic natural product function

Luo, M., Spradlin, J. N., Boike, L., Tong, B., Brittain, S. M., McKenna, J. M., Tallarico, J. A., Schirle, M., Maimone, T. J., & Nomura, D. K. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2021.01.005 · Cited by 186 · see citing works

A Cellular Mechanism to Detect and Alleviate Reductive Stress.

Manford, A., Rodríguez-Pérez, F., Shih, K. Y., Shi, Z., Berdan, C. A., Choe, M., Titov, D., Nomura, D., & Rapé, M. (2020) · Cell · doi:10.1016/j.cell.2020.08.034 · Cited by 185 · see citing works

How Chemoproteomics Can Enable Drug Discovery and Development

Moellering, R. E., & Cravatt, B. F. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.01.001 · Cited by 182 · see citing works

Targeted degradation of transcription factors by TRAFTACs: TRAnscription Factor TArgeting Chimeras

Samarasinghe, K. T. G., Jaime-Figueroa, S., Burgess, M., Nalawansha, D. A., Dai, K., Hu, Z., Bebenek, A., Holley, S. A., & Crews, C. M. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2021.03.011 · Cited by 182 · see citing works

Structural Basis and Kinetic Pathway of RBM39 Recruitment to DCAF15 by a Sulfonamide Molecular Glue E7820

Du, X., Volkov, O. A., Czerwinski, R. M., Tan, H., Huerta, C., Morton, E. R., Rizzi, J. P., Wehn, P. M., Xu, R., Nijhawan, D., et al. (2019) · Structure · doi:10.1016/j.str.2019.10.005 · Cited by 181 · see citing works

Reimagining Druggability Using Chemoproteomic Platforms

Spradlin, J. N., Zhang, E., & Nomura, D. K. (2021) · Accounts of Chemical Research · doi:10.1021/acs.accounts.1c00065 · Cited by 176 · see citing works

Small Molecules Destabilize cIAP1 by Activating Auto-ubiquitylation

Sekine, K., Takubo, K., Kikuchi, R., Nishimoto, M., Kitagawa, M., Abe, F., Nishikawa, K., Tsuruo, T., & Naito, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709525200 · Cited by 173 · see citing works

Covalent Targeting of the Vacuolar H+-ATPase Activates Autophagy Via mTORC1 Inhibition

Chung, C., Shin, H. R., Berdan, C. A., Ford, B., Ward, C. C., Olzmann, J. A., Zoncu, R., & Nomura, D. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0308-4 · Cited by 173 · see citing works

NHS-Esters As Versatile Reactivity-Based Probes for Mapping Proteome-Wide Ligandable Hotspots

Ward, C. C., Kleinman, J. I., & Nomura, D. K. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00125 · Cited by 158 · see citing works

Discovery of a Functional Covalent Ligand Targeting an Intrinsically Disordered Cysteine within MYC

Boike, L., Cioffi, A. G., Majewski, F. C., Co, J., Henning, N. J., Jones, M. D., Liu, G., McKenna, J. M., Tallarico, J. A., Schirle, M., et al. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2020.09.001 · Cited by 154 · see citing works

Bardoxolone conjugation enables targeted protein degradation of BRD4

Tong, B., Luo, M., Xie, Y., Spradlin, J. N., Tallarico, J. A., McKenna, J. M., Schirle, M., Maimone, T. J., & Nomura, D. K. (2020) · Scientific Reports · doi:10.1038/s41598-020-72491-9 · Cited by 149 · see citing works

Expanding the arsenal of E3 ubiquitin ligases for proximity-induced protein degradation

Kannt, A., & Đikić, I. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.007 · Cited by 148 · see citing works

RBR E3‐ligases at work

Smit, J. J., & Sixma, T. K. (2014) · EMBO Reports · doi:10.1002/embr.201338166 · Cited by 146 · see citing works

Heterobifunctional Molecules Induce Dephosphorylation of Kinases–A Proof of Concept Study

Yamazoe, S., Tom, J., Fu, Y., Wu, W., Zeng, L., Sun, C., Liu, Q., Lin, J. M., Lin, K., Fairbrother, W. J., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01167 · Cited by 145 · see citing works

An E3 ligase guide to the galaxy of small-molecule-induced protein degradation

Jevtić, P., Haakonsen, D. L., & Rapé, M. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.002 · Cited by 144 · see citing works

Design, synthesis and biological evaluation of nuclear receptor-degradation inducers

Itoh, Y., Kitaguchi, R., Ishikawa, M., Naito, M., & Hashimoto, Y. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.09.041 · Cited by 142 · see citing works

Degrons in cancer

Mészáros, B., Kumar, M., Gibson, T. J., Uyar, B., & Dosztányi, Z. (2017) · Science Signaling · doi:10.1126/scisignal.aak9982 · Cited by 139 · see citing works

Covalent Ligand Discovery against Druggable Hotspots Targeted by Anti-cancer Natural Products

Grossman, E. A., Ward, C. C., Spradlin, J. N., Bateman, L. A., Huffman, T. R., Miyamoto, D. K., Kleinman, J. I., & Nomura, D. K. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.08.013 · Cited by 124 · see citing works

Manumycin polyketides act as molecular glues between UBR7 and P53

Isobe, Y., Okumura, M., McGregor, L. M., Brittain, S. M., Jones, M. D., Liang, X., White, R., Forrester, W., McKenna, J. M., Tallarico, J. A., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0557-2 · Cited by 124 · see citing works

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

Tong, B., Spradlin, J. N., Novaes, L. F. T., Zhang, E., Hu, X., Moeller, M., Brittain, S. M., McGregor, L. M., McKenna, J. M., Tallarico, J. A., et al. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00348 · Cited by 118 · see citing works

Chemoproteomic Screening of Covalent Ligands Reveals UBA5 As a Novel Pancreatic Cancer Target

Roberts, A. M., Miyamoto, D. K., Huffman, T. R., Bateman, L. A., Ives, A. N., Akopian, D., Heslin, M. J., Contreras, C. M., Rapé, M., Skibola, C. F., et al. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00020 · Cited by 113 · see citing works

Liganding Functional Tyrosine Sites on Proteins Using Sulfur–Triazole Exchange Chemistry

Brulet, J. W., Borne, A. L., Yuan, K., Libby, A. H., & Hsu, K. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c00648 · Cited by 105 · see citing works

Identification of Potent, Selective, and Orally Bioavailable Small-Molecule GSPT1/2 Degraders from a Focused Library of Cereblon Modulators

Nishiguchi, G., Keramatnia, F., Min, J., Chang, Y., Jonchère, B., Das, S., Actis, M., Price, J. E., Chepyala, D., Young, B. M., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01313 · Cited by 103 · see citing works

Cancer cell death induced by novel small molecules degrading the TACC3 protein via the ubiquitin–proteasome pathway

Ohoka, N., Nagai, K., Hattori, T., Okuhira, K., Shibata, N., Cho, N. J., & Naito, M. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.471 · Cited by 100 · see citing works

Mapping Proteome-wide Targets of Glyphosate in Mice

Ford, B., Bateman, L. A., Gutierrez-Palominos, L., Park, R., & Nomura, D. K. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2016.12.013 · Cited by 96 · see citing works

In vivo target protein degradation induced by PROTACs based on E3 ligase DCAF15

Li, L., Mi, D., Pei, H., Duan, Q., Wang, X., Zhou, W., Jin, J., Li, D., Liu, M., & Chen, Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00245-0 · Cited by 94 · see citing works

Parthenolide Covalently Targets and Inhibits Focal Adhesion Kinase in Breast Cancer Cells

Berdan, C. A., Ho, R. Y., Lehtola, H. S., To, M., Hu, X., Huffman, T. R., Petri, Y. D., Altobelli, C. R., Demeulenaere, S. K., Olzmann, J. A., et al. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.03.016 · Cited by 92 · see citing works

Selective Degradation of GSPT1 by Cereblon Modulators Identified via a Focused Combinatorial Library

Powell, C. E., Du, G., Che, J., He, Z., Donovan, K. A., Yue, H., Wang, E. S., Nowak, R. P., Zhang, T., Fischer, E. S., et al. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00520 · Cited by 88 · see citing works

Development of target protein-selective degradation inducer for protein knockdown

Itoh, Y., Ishikawa, M., Kitaguchi, R., Sato, S., Naito, M., & Hashimoto, Y. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.03.057 · Cited by 87 · see citing works

Targeted Degradation of the Oncogenic MicroRNA 17-92 Cluster by Structure-Targeting Ligands

Liu, X., Haniff, H. S., Childs‐Disney, J. L., et al. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b13159 · Cited by 84 · see citing works

New strategy for renal fibrosis: Targeting Smad3 proteins for ubiquitination and degradation

Wang, X., Feng, S., Fan, J., Li, X., Wen, Q., & Luo, N. (2016) · Biochemical Pharmacology · doi:10.1016/j.bcp.2016.07.017 · Cited by 79 · see citing works

Proteostasis regulation by the ubiquitin system

Bett, J. S. (2016) · Essays in Biochemistry · doi:10.1042/ebc20160001 · Cited by 78 · see citing works

Chemoproteomics-enabled covalent ligand screen reveals a cysteine hotspot in reticulon 4 that impairs ER morphology and cancer pathogenicity

Bateman, L. A., Nguyen, T., Roberts, A. M., Miyamoto, D. K., Ku, W.-M., Huffman, T. R., Petri, Y. D., Heslin, M. J., Contreras, C. M., Skibola, C. F., et al. (2017) · Chemical Communications · doi:10.1039/c7cc01480e · Cited by 73 · see citing works

Phase I Study of E7820, an Oral Inhibitor of Integrin α-2 Expression with Antiangiogenic Properties, in Patients with Advanced Malignancies

Mita, M., Kelly, K. R., Mita, A., Ricart, A. D., Romero, O., Tolcher, A., Hook, L., Okereke, C., Krivelevich, I., Rossignol, D. P., et al. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-0010 · Cited by 71 · see citing works

Use of PROTACS as molecular probes of angiogenesis

Bargagna‐Mohan, P., Baek, S., Lee, H., Kim, K., & Mohan, R. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.04.008 · Cited by 70 · see citing works

Exploiting ubiquitin ligase cereblon as a target for small-molecule compounds in medicine and chemical biology

Ito, T., Yamaguchi, Y., & Handa, H. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.012 · Cited by 60 · see citing works

Chemoproteomics-Enabled Covalent Ligand Screening Reveals ALDH3A1 as a Lung Cancer Therapy Target

Counihan, J. L., Wiggenhorn, A. L., Anderson, K. E., & Nomura, D. K. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00381 · Cited by 53 · see citing works

Deubiquitinase-Targeting Chimeras for Targeted Protein StabilizationPreprint

Henning, N. J., Boike, L., Spradlin, J. N., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.30.441959 · Cited by 32 · see citing works

Chemoproteomic Profiling of Acetanilide Herbicides Reveals Their Role in Inhibiting Fatty Acid Oxidation

Counihan, J. L., Duckering, M., Dalvie, E. D., Ku, W.-M., Bateman, L. A., Fisher, K. J., & Nomura, D. K. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.6b01001 · Cited by 29 · see citing works

CYP27A1-dependent anti-melanoma activity of limonoid natural products targets mitochondrial metabolism

Cho, H., Shen, Q. “., Zhang, L. H., Okumura, M., Kawakami, A., Ambrose, J., Sigoillot, F. D., Miller, H., Gleim, S., Cobos‐Correa, A., et al. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.03.004 · Cited by 27 · see citing works

Mapping Novel Metabolic Nodes Targeted by Anti-Cancer Drugs that Impair Triple-Negative Breast Cancer Pathogenicity

Roberts, L. S., Yan, P., Bateman, L. A., & Nomura, D. K. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.6b01159 · Cited by 23 · see citing works

Primary Amine Tethered Small Molecules Promote the Degradation of X-Linked Inhibitor of Apoptosis Protein

den Besten, W., Verma, K., Yamazoe, S., Blaquière, N., Phung, W., Izrael-Tomasevic, A., Mulvihill, M. M., Helgason, E., Prakash, S., Goncharov, T., et al. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c05269 · Cited by 19 · see citing works

Reprint of “A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes”

Ciechanover, A. J. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.08.025 · Cited by 17 · see citing works

Clinical complete long-term remission of a patient with metastatic malignant melanoma under therapy with indisulam (E7070)

Baur, M., Gneist, M., Owa, T., & Dittrich, C. (2007) · Melanoma Research · doi:10.1097/cmr.0b013e3282ef4189 · Cited by 16 · see citing works

A phase II study of chloroquinoxaline sulfonamide (CQS) in patients with metastatic colorectal carcinoma (MCRC)

Bekaii‐Saab, T., Mortazavi, A., Hicks, L. G., Zalupski, M. M., Pelley, R. J., Chan, K. K., & Kraut, E. H. (2006) · Investigational New Drugs · doi:10.1007/s10637-005-4827-3 · Cited by 15 · see citing works

Advances in covalent drug discovery

Boike, L., Henning, N. J., & Nomura, D. K. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00542-z · Cited by 823 · 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

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

Proteasomes: protein degradation machines of the cell

Peters, J. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90115-5 · Cited by 311 · see citing works

Regulation of Protein Degradation by Proteasomes in Cancer

Jang, H. H. (2018) · Journal of Cancer Prevention · doi:10.15430/jcp.2018.23.4.153 · Cited by 101 · see citing works

Protein Degradation by the 26S Proteasome System in the Normal and Stressed Myocardium

Gomes, A. V., Zong, C., & Ping, P. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1677 · Cited by 37 · see citing works

Proteasomal and lysosomal protein degradation and heart disease

Wang, X., & Robbins, J. M. (2013) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.11.006 · Cited by 169 · see citing works

Ubiquitin-like Protein FAT10-mediated Proteasome Degradation

Jun, H. (2014) · Zhongguo shengwu huaxue yu fenzi shengwu xuebao