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

Cell cycle, CDKs and cancer: a changing paradigm

Malumbres, M., & Barbacid, M. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2602 · Cited by 3,957 · see citing works

Palbociclib and letrozole in advanced breast cancer

Finn, R. S., Martin, M., Rugo, H. S., Jones, S., Im, S.-A., Gelmon, K., Harbeck, N., Lipatov, O. N., Walshe, J. M., Moulder, S., et al. (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1607303 · Cited by 3,007 · see citing works

Computational correction of copy number effect improves specificity of CRISPR-Cas9 essentiality screens in cancer cells

Meyers, R. M., Bryan, J. G., McFarland, J. M., Weir, B. A., Sizemore, A. E., Xu, H., Dharia, N. V., Montgomery, P. G., Cowley, G. S., Pantel, S., et al. (2017) · Nature Genetics · doi:10.1038/ng.3984 · Cited by 1,952 · 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

Fulvestrant plus palbociclib versus fulvestrant plus placebo for treatment of hormone-receptor-positive, HER2-negative metastatic breast cancer that progressed on previous endocrine therapy (PALOMA-3): final analysis of the multicentre, double-blind, phase 3 randomised controlled trial

Cristofanilli, M., Turner, N. C., Bondarenko, I., Ro, J., Im, S.-A., Masuda, N., Colleoni, M., DeMichele, A., Loi, S., Verma, S., et al. (2016) · The Lancet Oncology · doi:10.1016/s1470-2045(15)00613-0 · Cited by 1,827 · 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 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

New functional activities for the p21 family of CDK inhibitors.

LaBaer, J., Garrett, M. D., Stevenson, L. F., Slingerland, J. M., Sandhu, C., Chou, H. S., Fattaey, A., & Harlow, E. (1997) · Genes & Development · doi:10.1101/gad.11.7.847 · Cited by 1,402 · see citing works

PD 0332991, a selective cyclin D kinase 4/6 inhibitor, preferentially inhibits proliferation of luminal estrogen receptor-positive human breast cancer cell lines in vitro

Finn, R. S., Dering, J., Conklin, D., Kalous, O., Cohen, D. J., Desai, A. J., Ginther, C., Atefi, M., Chen, I., Fowst, C., et al. (2009) · Breast Cancer Research · doi:10.1186/bcr2419 · Cited by 1,398 · see citing works

Treating cancer with selective CDK4/6 inhibitors

O'Leary, B., Finn, R. S., & Turner, N. C. (2016) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2016.26 · Cited by 1,137 · see citing works

Kinase inhibitors: the road ahead

Ferguson, F. M., & Gray, N. S. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.21 · Cited by 1,009 · 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

Targeting CDK4 and CDK6: From Discovery to Therapy

Sherr, C. J., Beach, D., & Shapiro, G. I. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-0894 · Cited by 936 · 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

Structural basis of lenalidomide-induced CK1α degradation by the CRL4CRBN ubiquitin ligase

Petzold, G., Fischer, E. S., & Thomä, N. H. (2016) · Nature · doi:10.1038/nature16979 · Cited by 620 · see citing works

Discovery of RG7388, a Potent and Selective p53–MDM2 Inhibitor in Clinical Development

Ding, Q., Zhang, Z., Liu, J.-J., Jiang, N., Zhang, J., Ross, T. M., Chu, X.-J., Bartkovitz, D., Podlaski, F., Janson, C., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400487c · Cited by 595 · 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

Discovery of a potent and selective inhibitor of cyclin-dependent kinase 4/6

Toogood, P. L., Harvey, P. J., Repine, J. T., Sheehan, D. J., VanderWel, S. N., Zhou, H., Keller, P. R., McNamara, D. J., Sherry, D., Zhu, T., et al. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049354h · Cited by 513 · see citing works

CDK4/6 Inhibition in Cancer: Beyond Cell Cycle Arrest

Goel, S., DeCristo, M. J., McAllister, S. S., & Zhao, J. J. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.07.002 · Cited by 494 · 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

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

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

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

CDK4/6 Inhibitors: The Mechanism of Action May Not Be as Simple as Once Thought

Klein, M. E., Kovatcheva, M., Davis, L. E., Tap, W. D., & Koff, A. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.03.023 · Cited by 378 · see citing works

Discovery of Potent Antagonists of the Antiapoptotic Protein XIAP for the Treatment of Cancer

Oost, T. K., Sun, C. C., Armstrong, R. C., Al-Assaad, A.-S., Betz, S. F., Deckwerth, T. L., Ding, H., Elmore, S. W., Meadows, R. P., Olejniczak, E. T., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm040037k · Cited by 367 · 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

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

The metabolic function of cyclin D3-CDK6 kinase in cancer cell survival

Wang, H., Nicolay, B. N., Chick, J. M., Gao, X., Geng, Y., Ren, H., Gao, H., Yang, G., Williams, J. A., Suski, J. M., et al. (2017) · Nature · doi:10.1038/nature22797 · Cited by 347 · 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

A Kinase-Independent Function of CDK6 Links the Cell Cycle to Tumor Angiogenesis

Kollmann, K., Heller, G., Schneckenleithner, C., Warsch, W., Scheicher, R., Ott, R. G., Schäfer, M., Fajmann, S., Schlederer, M., Schiefer, A.-I., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.07.012 · Cited by 313 · 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

PROTAC-induced BTK degradation as a novel therapy for mutated BTK C481S induced ibrutinib-resistant B-cell malignancies

Sun, Y., Zhao, X., Ding, N., Gao, H., Wu, Y., Yang, Y., Zhao, M., Hwang, J., Song, Y., Liu, W., et al. (2018) · Cell Research · doi:10.1038/s41422-018-0055-1 · Cited by 295 · see citing works

Development of dual and selective degraders of cyclin-dependent kinases 4 and 6

Jiang, B., Wang, E. S., Donovan, K. A., Liang, Y., Fischer, E. S., Zhang, T., & Gray, N. S. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201901336 · Cited by 272 · see citing works

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

Brand, M., Jiang, B., Bauer, S., Donovan, K. A., Liang, Y., Wang, E. S., Nowak, R. P., Yuan, J. C., Zhang, T., Kwiatkowski, N., et al. (2019) · Cell Chemical Biology · doi:10.1016/j.chembiol.2018.11.006 · Cited by 258 · see citing works

Targeted sequencing of refractory myeloma reveals a high incidence of mutations in CRBN and Ras pathway genes

Kortüm, K. M., Mai, E. K., Hanafiah, N. H., Shi, C.-X., Zhu, Y.-X., Bruins, L., Barrio, S., Jedlowski, P., Merz, M., Xu, J., et al. (2016) · Blood · doi:10.1182/blood-2016-02-698092 · Cited by 255 · see citing works

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

Maniaci, C., Hughes, S. J., Testa, A., Chen, W., Lamont, D. J., Rocha, S., Alessi, D. R., Romeo, R., & Ciulli, A. (2017) · Nature Communications · doi:10.1038/s41467-017-00954-1 · Cited by 245 · see citing works

p27 allosterically activates cyclin-dependent kinase 4 and antagonizes palbociclib inhibition

Guiley, K. Z., Stevenson, J. W., Lou, K., Barkovich, K. J., Kumarasamy, V. M., Wijeratne, T. U., Bunch, K. L., Tripathi, S. M., Knudsen, E. S., Witkiewicz, A. K., et al. (2019) · Science · doi:10.1126/science.aaw2106 · Cited by 225 · see citing works

Targeting BCR-ABL1 in Chronic Myeloid Leukemia by PROTAC-Mediated Targeted Protein Degradation

Burslem, G. M., Schultz, A. R., Bondeson, D. P., Eide, C. A., Savage Stevens, S. L., Druker, B. J., & Crews, C. M. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1236 · Cited by 212 · see citing works

Potent and Preferential Degradation of CDK6 via Proteolysis Targeting Chimera Degraders

Su, S., Yang, Z., Gao, H., Yang, H., Zhu, S., An, Z., Wang, J., Li, Q., Chandarlapaty, S., Deng, H., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00871 · Cited by 209 · see citing works

CDK6—a review of the past and a glimpse into the future: from cell-cycle control to transcriptional regulation

Tigan, A.-S., Bellutti, F., Kollmann, K., Tebb, G., & Sexl, V (2016) · Oncogene · doi:10.1038/onc.2015.407 · Cited by 204 · see citing works

Cyclin dependent kinase (CDK) inhibitors as anticancer drugs: Recent advances (2015–2019)

Sánchez-Martínez, C., Lallena, M. J., Sanfeliciano, S. G., & de Dios, A. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2019.126637 · Cited by 200 · see citing works

CDK 4/6 Inhibitors in Breast Cancer: Current Controversies and Future Directions

Spring, L. M., Wander, S. A., Zangardi, M. L., & Bardia, A. (2019) · Current Oncology Reports · doi:10.1007/s11912-019-0769-3 · Cited by 172 · see citing works

Updates on the CDK4/6 Inhibitory Strategy and Combinations in Breast Cancer

Sobhani, N., D’Angelo, A., Pittacolo, M., Roviello, G., Miccoli, A., Corona, S. P., Bernocchi, O., Generali, D., & Otto, T. (2019) · Cells · doi:10.3390/cells8040321 · Cited by 168 · see citing works

SNIPERs—Hijacking IAP activity to induce protein degradation

Naito, M., Ohoka, N., & Shibata, N. (2019) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2018.12.002 · Cited by 167 · see citing works

Targeting CDK6 in cancer: State of the art and new insights

Tadesse, S., Yu, M., Kumarasiri, M., Le, B. T., & Wang, S. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1084445 · Cited by 166 · see citing works

THE METABOLISM OF THALIDOMIDE: THE SPONTANEOUS HYDROLYSIS OF THALIDOMIDE IN SOLUTION

Schumacher, H., Smith, R. L., & Williams, R. T. (1965) · British Journal of Pharmacology and Chemotherapy · doi:10.1111/j.1476-5381.1965.tb02053.x · Cited by 162 · see citing works

Developing degraders: principles and perspectives on design and chemical space

Maple, H. J., Clayden, N., Baron, A., Stacey, C., & Felix, R. L. (2019) · MedChemComm · doi:10.1039/c9md00272c · Cited by 159 · see citing works

Cereblon versus VHL: Hijacking E3 ligases against each other using PROTACs

Girardini, M., Maniaci, C., Hughes, S. J., Testa, A., & Ciulli, A. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.02.048 · Cited by 157 · see citing works

Degradation of Bruton’s tyrosine kinase mutants by PROTACs for potential treatment of ibrutinib-resistant non-Hodgkin lymphomas

Sun, Y., Ding, N., Song, Y., Yang, Z., Liu, W., Zhu, J., & Rao, Y. (2019) · Leukemia · doi:10.1038/s41375-019-0440-x · Cited by 148 · see citing works

Rapid and Reversible Knockdown of Endogenously Tagged Endosomal Proteins via an Optimized HaloPROTAC Degrader

Tovell, H., Testa, A., Maniaci, C., Zhou, H., Prescott, A. R., Macartney, T., Ciulli, A., & Alessi, D. R. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.8b01016 · Cited by 146 · see citing works

Chemical approaches to targeted protein degradation through modulation of the ubiquitin–proteasome pathway

Collins, I., Wang, H., Caldwell, J., & Chopra, R. (2017) · Biochemical Journal · doi:10.1042/bcj20160762 · Cited by 135 · see citing works

Selective degradation of CDK6 by a palbociclib based PROTAC

Rana, S., Bendjennat, M., Kour, S., King, H. M., Kizhake, S., Zahid, M., & Natarajan, A. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2019.03.035 · Cited by 135 · see citing works

FDA Approval of Palbociclib in Combination with Fulvestrant for the Treatment of Hormone Receptor–Positive, HER2-Negative Metastatic Breast Cancer

Walker, A. J., Wedam, S. B., Amiri‐Kordestani, L., Bloomquist, E. W., Tang, S., Sridhara, R., Chen, W., Palmby, T. R., Zirkelbach, J. F., Fu, W., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-0493 · Cited by 133 · see citing works

PROTACs suppression of CDK4/6, crucial kinases for cell cycle regulation in cancer

Zhao, B., & Burgess, K. (2019) · Chemical Communications · doi:10.1039/c9cc00163h · Cited by 130 · see citing works

MDM2 antagonists overcome intrinsic resistance to CDK4/6 inhibition by inducing p21

Vilgelm, A. E., Saleh, N., Shattuck-Brandt, R. L., Riemenschneider, K., Slesur, L., Chen, S., Johnson, C. A., Yang, J., Blevins, A., Yan, C. W., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aav7171 · Cited by 123 · see citing works

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

Mayor-Ruiz, C., Jaeger, M. G., Bauer, S., Brand, M., Sin, C., Hanzl, A., Mueller, A. C., Menche, J., & Winter, G. E. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.07.013 · Cited by 119 · see citing works

A chemical approach for global protein knockdown from mice to non-human primates

Sun, X., Wang, J., Yao, X., Zheng, W., Mao, Y., Lan, T., Wang, L., Sun, Y., Zhang, X., Zhao, Q., et al. (2019) · Cell Discovery · doi:10.1038/s41421-018-0079-1 · Cited by 118 · see citing works

Derivatization of inhibitor of apoptosis protein (IAP) ligands yields improved inducers of estrogen receptor α degradation

Ohoka, N., Morita, Y., Nagai, K., Shimokawa, K., Ujikawa, O., Fujimori, I., Ito, M., Hayase, Y., Okuhira, K., Shibata, N., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001091 · Cited by 105 · see citing works

PROTAC-mediated crosstalk between E3 ligases

Steinebach, C., Kehm, H., Lindner, S., Vu, L. P., Köpff, S., Mármol, Á. L., Weiler, C., Wagner, K. G., Reichenzeller, M., Krönke, J., et al. (2019) · Chemical Communications · doi:10.1039/c8cc09541h · Cited by 101 · 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

Demonstrating In-Cell Target Engagement Using a Pirin Protein Degradation Probe (CCT367766)

Chessum, N. E. A., Sharp, S. Y., Caldwell, J., Pasqua, E., Wilding, B., Colombano, G., Collins, I., Özer, B., Richards, M., Rowlands, M., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01406 · Cited by 90 · see citing works

PROTACs as Potential Therapeutic Agents for Cancer Drug Resistance

Sun, X., & Rao, Y. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00848 · Cited by 87 · see citing works

CDK6 Antagonizes p53-Induced Responses during Tumorigenesis

Bellutti, F., Tigan, A.-S., Nebenfuehr, S., Dolezal, M., Zojer, M., Grausenburger, R., Hartenberger, S., Kollmann, S., Doma, E., Prchal‐Murphy, M., et al. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-17-0912 · Cited by 76 · see citing works

Highly Potent, Selective, and Orally Bioavailable 4-Thiazol- N -(pyridin-2-yl)pyrimidin-2-amine Cyclin-Dependent Kinases 4 and 6 Inhibitors as Anticancer Drug Candidates: Design, Synthesis, and Evaluation

Tadesse, S., Yu, M., Mekonnen, L. B., Lam, F., Islam, S., Tomusange, K., Rahaman, M. H., Noll, B. D., Basnet, S. K. C., Teo, T., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01670 · Cited by 74 · see citing works

Targeted protein degradation in vivo with Proteolysis Targeting Chimeras: Current status and future considerations

Watt, G. F., Scott‐Stevens, P., & Gaohua, L. (2019) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2019.02.005 · Cited by 72 · see citing works

A MedChem toolbox for cereblon-directed PROTACs

Steinebach, C., Sosič, I., Lindner, S., Bricelj, A., Kohl, F., Ng, Y. L. D., Monschke, M., Wagner, K. G., Krönke, J., & Gütschow, M. (2019) · MedChemComm · doi:10.1039/c9md00185a · Cited by 66 · see citing works

Ligand-mediated protein degradation reveals functional conservation among sequence variants of the CUL4-type E3 ligase substrate receptor cereblon

Akuffo, A. A., Alontaga, A. Y., Metcalf, R. S., Beatty, M. S., Becker, A., McDaniel, J. M., Hesterberg, R. S., Goodheart, W. E., Gunawan, S., Ayaz, M., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.816868 · Cited by 55 · see citing works

The interplay of CDK4 and CDK6 in melanoma

Kollmann, K., Briand, C., Bellutti, F., Schicher, N., Blunder, S., Zojer, M., & Höeller, C. (2019) · Oncotarget · doi:10.18632/oncotarget.26515 · Cited by 55 · see citing works

A critical evaluation of the approaches to targeted protein degradation for drug discovery

Chopra, R., Sadok, A., & Collins, I. (2019) · Drug Discovery Today: Technologies · doi:10.1016/j.ddtec.2019.02.002 · Cited by 53 · see citing works

Pharmacological difference between degrader and inhibitor against oncogenic BCR-ABL kinase

Shibata, N., Shimokawa, K., Nagai, K., Ohoka, N., Hattori, T., Miyamoto, N., Ujikawa, O., Sameshima, T., Nara, H., Cho, N., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-31913-5 · Cited by 52 · see citing works

Inhibition of cyclin-dependent kinase 4 as a potential therapeutic strategy for treatment of synovial sarcoma

Li, X., Seebacher, N. A., Garbutt, C. C., Ma, H., Gao, P., Xiao, T., Hornicek, F. J., & Duan, Z. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0474-4 · Cited by 42 · see citing works

When Kinases Meet PROTACs

Tan, L., & Gray, N. S. (2018) · Chinese Journal of Chemistry · doi:10.1002/cjoc.201800293 · Cited by 33 · see citing works

Small molecule-mediated protein knockdown as a new approach to drug discovery

Tinworth, C. P., Lithgow, H., & Churcher, I. (2016) · MedChemComm · doi:10.1039/c6md00347h · Cited by 32 · see citing works

The hydrophobically-tagged MDM2–p53 interaction inhibitor Nutlin-3a-HT is more potent against tumor cells than Nutlin-3a

Nietzold, F., Rubner, S., & Berg, T. (2019) · Chemical Communications · doi:10.1039/c9cc07795b · Cited by 27 · see citing works

Development of a Potent Protein Degrader against Oncogenic BCR-ABL Protein

Shibata, N., Ohoka, N., Hattori, T., & Naito, M. (2019) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c18-00703 · Cited by 21 · see citing works

A Novel Series of N -(Pyridin-2-Yl)-4-(Thiazol-5-Yl)Pyrimidin-2-Amines as Highly Potent Cdk4/6 Inhibitors

Tadesse, S., Zhu, G., Mekonnen, L. B., Lenjisa, J. L., Yu, M., Brown, M. P., & Wang, S. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0076 · Cited by 16 · 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

Proteolysis-targeting chimeras (PROTACs) in cancer therapy

Li, X., Pu, W., Zheng, Q., Ai, M., Chen, S., & Peng, Y. (2022) · Molecular Cancer · doi:10.1186/s12943-021-01434-3 · Cited by 374 · see citing works

Target and tissue selectivity of PROTAC degraders

Guenette, R. G., Yang, S. W., Min, J., Pei, B., & Potts, P. R. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00200k · Cited by 324 · 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 chimera (PROTAC) in drug discovery paradigm: Recent progress and future challenges

Zeng, S., Huang, W., Zheng, X., Cheng, L., Zhang, Z., Wang, J., & Shen, Z. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112981 · Cited by 262 · see citing works

Discovery of small molecule ligands for the von Hippel-Lindau (VHL) E3 ligase and their use as inhibitors and PROTAC degraders

Diehl, C. J., & Ciulli, A. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00387b · Cited by 259 · see citing works

Unraveling the Role of Linker Design in Proteolysis Targeting Chimeras

Bemis, T. A., Clair, J. J. L., & Burkart, M. D. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00482 · Cited by 244 · 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

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

E3 Ligase Ligands in Successful PROTACs: An Overview of Syntheses and Linker Attachment Points

Bricelj, A., Steinebach, C., Kuchta, R. D., Gütschow, M., & Sosič, I. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.707317 · Cited by 226 · see citing works

From Conception to Development: Investigating PROTACs Features for Improved Cell Permeability and Successful Protein Degradation

Cecchini, C., Pannilunghi, S., Tardy, S., & Scapozza, L. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.672267 · Cited by 198 · see citing works

The roles of E3 ubiquitin ligases in cancer progression and targeted therapy

Sampson, C., Wang, Q., Otkur, W., Zhao, H., Lu, Y., Liu, X., & Piao, H. (2023) · Clinical and Translational Medicine · doi:10.1002/ctm2.1204 · Cited by 186 · see citing works

E3 ligase ligand chemistries: from building blocks to protein degraders

Sosič, I., Bricelj, A., & Steinebach, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00148a · Cited by 173 · see citing works

Understanding the Metabolism of Proteolysis Targeting Chimeras (PROTACs): The Next Step toward Pharmaceutical Applications

Goracci, L., Desantis, J., Valeri, A., Castellani, B., Eleuteri, M., & Cruciani, G. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00793 · Cited by 160 · 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

Developments of CRBN-based PROTACs as potential therapeutic agents

Wang, C., Zhang, Y., Wu, Y., & Xing, D. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113749 · Cited by 152 · see citing works

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

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

A bibliometric analysis of PROTAC from 2001 to 2021

Li, D., Yu, D., Li, Y., & Yang, R. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114838 · Cited by 122 · see citing works

Sequential responsive nano-PROTACs for precise intracellular delivery and enhanced degradation efficacy in colorectal cancer therapy

Yang, L., Yang, Y., Zhang, J., Li, M., Yang, L., Wang, X., Chen, M., Zhang, H., He, B., Wang, X., et al. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01983-1 · Cited by 113 · see citing works

CDK4: a master regulator of the cell cycle and its role in cancer

Baker, S. J., Poulikakos, P. I., Irie, H. Y., Parekh, S. S., & Reddy, E. P. (2022) · Genes & Cancer · doi:10.18632/genesandcancer.221 · Cited by 84 · see citing works

Overview of epigenetic degraders based on PROTAC, molecular glue, and hydrophobic tagging technologies

Peng, X., Hu, Z., Zeng, L., Zhang, M., Xu, C., Lu, B., Tao, C., Chen, W., Hou, W., Cheng, K., et al. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.09.003 · Cited by 85 · see citing works

Influence of Linker Attachment Points on the Stability and Neosubstrate Degradation of Cereblon Ligands

Bricelj, A., Ng, Y. L. D., Ferber, D., Kuchta, R. D., Müller, S., Monschke, M., Wagner, K. G., Krönke, J., Sosič, I., Gütschow, M., et al. (2021) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.1c00368 · Cited by 71 · see citing works

The Renaissance of Cyclin Dependent Kinase Inhibitors

Ettl, T., Schulz, D., & Bauer, R. J. (2022) · Cancers · doi:10.3390/cancers14020293 · Cited by 71 · see citing works

VHL-based PROTACs as potential therapeutic agents: Recent progress and perspectives

Wang, C., Zhang, Y., Wang, J., & Xing, D. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113906 · Cited by 71 · see citing works

Proteomic profiling reveals CDK6 upregulation as a targetable resistance mechanism for lenalidomide in multiple myeloma

Ng, Y. L. D., Ramberger, E., Bohl, S., Dolnik, A., Steinebach, C., Conrad, T., Müller, S., Popp, O., Kull, M., Haji, M., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28515-1 · Cited by 68 · see citing works

Recent Advances of Degradation Technologies Based on PROTAC Mechanism

Xiao, M., Zhao, J., Wang, Q., Liu, J., & Ma, L. (2022) · Biomolecules · doi:10.3390/biom12091257 · Cited by 66 · see citing works

Targeted protein degradation in cancers: Orthodox PROTACs and beyond

Li, J., Chen, X., Lü, A., & Liang, C. (2023) · The Innovation · doi:10.1016/j.xinn.2023.100413 · Cited by 66 · see citing works

A beginner’s guide to current synthetic linker strategies towards VHL-recruiting PROTACs

Zografou-Barredo, N. A., Hallatt, A. J., Goujon-Ricci, J., & Cano, C. (2023) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2023.117334 · Cited by 64 · see citing works

Resistance mechanisms and therapeutic strategies of CDK4 and CDK6 kinase targeting in cancer

Asciolla, J. J., Wu, X., Adamopoulos, C., Gavathiotis, E., & Poulikakos, P. I. (2025) · Nature Cancer · doi:10.1038/s43018-024-00893-z · Cited by 62 · see citing works

Optimization of PROTAC Ternary Complex Using DNA Encoded Library Approach

Chen, Q., Liu, C., Wang, W., Meng, X., Cheng, X., Li, X.-Y., Cai, L., Luo, L., He, X., Qu, H., et al. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.2c00797 · Cited by 55 · see citing works

Current advances of small molecule E3 ligands for proteolysis-targeting chimeras design

Mi, D., Li, Y., Gu, H., Li, Y., & Chen, Y. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115444 · Cited by 57 · see citing works

DNA framework-engineered chimeras platform enables selectively targeted protein degradation

Zhou, L.-M., Yu, B., Gao, M., Chen, R., Li, Z., Gu, Y., Bian, J., & Ma, Y. (2023) · Nature Communications · doi:10.1038/s41467-023-40244-7 · Cited by 57 · see citing works

Enriching Proteolysis Targeting Chimeras with a Second Modality: When Two Are Better Than One

Salerno, A., Seghetti, F., Caciolla, J., Uliassi, E., Testi, E., Guardigni, M., Roberti, M., Milelli, A., & Bolognesi, M. L. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00302 · Cited by 55 · see citing works

Targeting Protein Kinases Degradation by PROTACs

Yu, F., Cai, M., Shao, L., & Zhang, J. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.679120 · Cited by 54 · see citing works

Leveraging Ligand Affinity and Properties: Discovery of Novel Benzamide-Type Cereblon Binders for the Design of PROTACs

Steinebach, C., Bricelj, A., Murgai, A., Sosič, I., Bischof, L., Ng, Y. L. D., Heim, C., Maiwald, S. A., Proj, M., Voget, R., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00851 · Cited by 54 · see citing works

Identification of a selective BRD4 PROTAC with potent antiproliferative effects in AR-positive prostate cancer based on a dual BET/PLK1 inhibitor

Hu, R., Wang, W., Yang, Y.-Y., Hu, X.-T., Wang, Q., Zuo, W., Xu, Y., Feng, Q., & Wang, N. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113922 · Cited by 53 · see citing works

MDM2-Based Proteolysis-Targeting Chimeras (PROTACs): An Innovative Drug Strategy for Cancer Treatment

Vicente, A. T. S., & Salvador, J. A. R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911068 · Cited by 53 · see citing works

Targeting the Epidermal Growth Factor Receptor with Molecular Degraders: State-of-the-Art and Future Opportunities

Maity, P., Chatterjee, J., Patil, K. T., Arora, S., Katiyar, M. K., Kumar, M., Samarbakhsh, A., Joshi, G., Bhutani, P., Chugh, M., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01242 · Cited by 51 · see citing works

Recent advances in IAP-based PROTACs (SNIPERs) as potential therapeutic agents

Wang, C., Zhang, Y., Shi, L., Yang, S., Chang, J., Zhong, Y., Li, Q., & Xing, D. (2022) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2022.2074414 · Cited by 49 · see citing works

Targeting CDK4/6 for Anticancer Therapy

Qi, J., & Ouyang, Z. (2022) · Biomedicines · doi:10.3390/biomedicines10030685 · Cited by 47 · see citing works

The impact of E3 ligase choice on PROTAC effectiveness in protein kinase degradation

Sobierajski, T., Małolepsza, J., Pichlak, M., Gendaszewska‐Darmach, E., & Błażewska, K. M. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.104032 · Cited by 48 · see citing works

PROTACs bearing piperazine-containing linkers: what effect on their protonation state?

Desantis, J., Mammoli, A., Eleuteri, M., Coletti, A., Croci, F., Macchiarulo, A., & Goracci, L. (2022) · RSC Advances · doi:10.1039/d2ra03761k · Cited by 46 · see citing works

Development of CDK4/6 Inhibitors: A Five Years Update

Ammazzalorso, A., Agamennone, M., Filippis, B. D., & Fantacuzzi, M. (2021) · Molecules · doi:10.3390/molecules26051488 · Cited by 43 · see citing works

Inhibitors, PROTACs and Molecular Glues as Diverse Therapeutic Modalities to Target Cyclin-Dependent Kinase

Rana, S., Mallareddy, J. R., Singh, S., Boghean, L., & Natarajan, A. (2021) · Cancers · doi:10.3390/cancers13215506 · Cited by 42 · see citing works

Recent advances in targeted protein degraders as potential therapeutic agents

Yang, N., Kong, B., Zhu, Z., Huang, F., Zhang, L., Lu, T., Chen, Y., Zhang, Y., & Jiang, Y. (2023) · Molecular Diversity · doi:10.1007/s11030-023-10606-w · Cited by 41 · see citing works

Solubility Enhanced Formulation Approaches to Overcome Oral Delivery Obstacles of PROTACs

Pöstges, F., Kayser, K., Appelhaus, J., Monschke, M., Gütschow, M., Steinebach, C., & Wagner, K. G. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15010156 · Cited by 40 · see citing works

Discovery of highly potent and selective KRASG12C degraders by VHL-recruiting PROTACs for the treatment of tumors with KRASG12C-Mutation

Yang, N., Fan, Z., Sun, S., Hu, X., Mao, Y., Jia, C., Cai, X., Xu, T., Li, B., Li, Y., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115857 · Cited by 40 · see citing works

Targeting androgen receptor and the variants by an orally bioavailable Proteolysis Targeting Chimeras compound in castration resistant prostate cancer

Hung, C.-L., Liu, H.-H., Fu, C., Yeh, H.-H., Hu, T.-L., Kuo, Z., Lin, Y.-C., Jhang, M.-R., Hwang, C.-S., Hsu, H., et al. (2023) · EBioMedicine · doi:10.1016/j.ebiom.2023.104500 · Cited by 39 · see citing works

Designing HDAC-PROTACs: Lessons Learned So Far

Fischer, F., Avelar, L. A. A., Murray, L., & Kurz, T. (2021) · Future Medicinal Chemistry · doi:10.4155/fmc-2021-0206 · Cited by 38 · see citing works

PROTAC: targeted drug strategy. Principles and limitations

Koroleva, O. A., Dutikova, Y. V., Trubnikov, A. V., Zenov, F. A., Manasova, E. V., Shtil, A. A., & Kurkin, A. V. (2022) · Russian Chemical Bulletin · doi:10.1007/s11172-022-3659-z · Cited by 38 · see citing works

CRL4CRBN E3 Ligase Complex as a Therapeutic Target in Multiple Myeloma

Barankiewicz, J., Salomon‐Perzyński, A., Misiewicz-Krzemińska, I., & Lech‐Marańda, E. (2022) · Cancers · doi:10.3390/cancers14184492 · Cited by 35 · see citing works

Ubiquitination and Ubiquitin-Like Modifications in Multiple Myeloma: Biology and Therapy

Wirth, M., Schick, M., Keller, U. B., & Krönke, J. (2020) · Cancers · doi:10.3390/cancers12123764 · Cited by 34 · see citing works

HaloTag‐Targeted Sirtuin‐Rearranging Ligand (SirReal) for the Development of Proteolysis‐Targeting Chimeras (PROTACs) against the Lysine Deacetylase Sirtuin 2 (Sirt2)**

Schiedel, M., Lehotzky, A., Szunyogh, S., Oláh, J., Hammelmann, S., Wössner, N., Robaa, D., Einsle, O., Sippl, W., Ovádi, J., et al. (2020) · ChemBioChem · doi:10.1002/cbic.202000351 · Cited by 31 · see citing works

Recent Progress in CDK4/6 Inhibitors and PROTACs

Wang, H., Ba, J., Kang, Y., Gong, Z., Liang, T., Zhang, Y., Qi, J., & Wang, J. (2023) · Molecules · doi:10.3390/molecules28248060 · Cited by 32 · see citing works

Progress of small molecules for targeted protein degradation: PROTACs and other technologies

Zhao, H., Xin, M., & Zhang, S. (2023) · Drug Development Research · doi:10.1002/ddr.22026 · Cited by 31 · see citing works

Current strategies for improving limitations of proteolysis targeting chimeras

Pu, C., Wang, S., Liu, L., Feng, Z., Zhang, H., Gong, Q., Sun, Y., Guo, Y., & Li, R. (2022) · Chinese Chemical Letters · doi:10.1016/j.cclet.2022.107927 · Cited by 29 · see citing works

Therapeutic potential of CDK4/6 inhibitors in renal cell carcinoma

Sager, R., Backe, S. J., Ahanin, E. F., Smith, G., Nsouli, I. S., Woodford, M. R., Bratslavsky, G., Bourboulia, D., & Mollapour, M. (2022) · Nature Reviews Urology · doi:10.1038/s41585-022-00571-8 · Cited by 29 · see citing works

Molecular glues: enhanced protein-protein interactions and cell proteome editing

Weagel, E. G., Foulks, J. M., Siddiqui, A. Q., & Warner, S. L. (2022) · Medicinal Chemistry Research · doi:10.1007/s00044-022-02882-2 · Cited by 29 · see citing works

Targeting CDKs in cancer therapy: advances in PROTACs and molecular glues

Marei, H. E. S., Bedair, K., Hasan, A., Al-Mansoori, L., Gaiba, A., Morrione, A., Cenciarelli, C., & Giordano, A. (2025) · npj Precision Oncology · doi:10.1038/s41698-025-00931-8 · Cited by 30 · see citing works

Sweet and Blind Spots in E3 Ligase Ligand Space Revealed by a Thermophoresis-Based Assay

Maiwald, S. A., Heim, C., Alvarez, B. H., & Hartmann, M. D. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00440 · Cited by 26 · see citing works

Translating PROTAC chemical series optimization into functional outcomes underlying BRD7 and BRD9 protein degradation

Riching, K. M., Vasta, J. D., Hughes, S. J., Zoppi, V., Maniaci, C., Testa, A., Urh, M., Ciulli, A., & Daniels, D. L. (2021) · Current Research in Chemical Biology · doi:10.1016/j.crchbi.2021.100009 · Cited by 25 · see citing works

PROTAC: Novel degradable approach for different targets to treat breast cancer

Wang, Z., Che, S., & Yu, Z. (2024) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2024.106793 · Cited by 25 · see citing works

Design, synthesis, and characterization of PROTACs targeting the androgen receptor in prostate and lung cancer models

Gockel, L. M., Pfeifer, V., Baltes, F., Bachmaier, R. D., Wagner, K. G., Bendas, G., Gütschow, M., Sosič, I., & Steinebach, C. (2022) · Archiv der Pharmazie · doi:10.1002/ardp.202100467 · Cited by 24 · see citing works

Synthesis, biological evaluation and clinical trials of Cereblon-based PROTACs

Vicente, A. T. S., Moura, S. P. S. P., & Salvador, J. A. R. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01598-9 · Cited by 23 · see citing works

3-Aminophthalic acid, a new cereblon ligand for targeted protein degradation by O’PROTAC

Yan, Y., Shao, J., Ding, D., Pan, Y., Tran, P., Yan, W., Wang, Z., Li, H., & Huang, H. (2022) · Chemical Communications · doi:10.1039/d1cc06525d · Cited by 21 · see citing works

Expanding the Structural Diversity at the Phenylene Core of Ligands for the von Hippel–Lindau E3 Ubiquitin Ligase: Development of Highly Potent Hypoxia-Inducible Factor-1α Stabilizers

Vu, L. P., Diehl, C. J., Casement, R., Bond, A. G., Steinebach, C., Strašek, N., Bricelj, A., Perdih, A., Schnakenburg, G., Sosič, I., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00434 · Cited by 20 · see citing works

Proteolysis Targeting Chimeras (PROTACs) in Breast Cancer Therapy

Jin, Y., & Lee, Y. (2024) · ChemMedChem · doi:10.1002/cmdc.202400267 · Cited by 18 · see citing works

Targeting micro-environmental pathways by PROTACs as a therapeutic strategy

Liu, J., Peng, Y., Inuzuka, H., & Wei, W. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2022.07.001 · Cited by 20 · see citing works

On the correlation of cereblon binding, fluorination and antiangiogenic properties of immunomodulatory drugs

Heim, C., Maiwald, S. A., Steinebach, C., Collins, M. K., Strope, J. D., Chau, C. H., Figg, W. D., Gütschow, M., & Hartmann, M. D. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.11.117 · Cited by 19 · see citing works

Development of Degraders of Cyclin-Dependent Kinases 4 and 6 Based on Rational Drug Design

He, H., Zhang, X., Wang, J., Liu, Q., Zhang, L., Lu, C., Yuan, Y., Zhao, Z., Li, H., & Chen, Z. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00965 · Cited by 18 · see citing works

Proteolysis-targeting chimeras in biotherapeutics: Current trends and future applications

Li, Q., Zhou, L., Qin, S., Huang, Z., Li, B., Li, B., Yang, M., Nice, E. C., Zhu, H., & Huang, C. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115447 · Cited by 17 · see citing works

Development of PROTACS degrading KRAS and SOS1

Hamilton, G., Eggerstorfer, M.-T., & Stickler, S. (2024) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.32604/or.2024.051653 · Cited by 16 · see citing works

Discovery of HyT‐Based Degraders of CDK9‐Cyclin T1 Complex

Lin, R., Yang, J., Liu, T., Wang, M., Ke, C., Luo, C., Lin, J. H., Li, J., & Lin, H. (2023) · Chemistry & Biodiversity · doi:10.1002/cbdv.202300769 · Cited by 15 · see citing works

PROteolysis‐Targeting Chimeras (PROTACs) in leukemia: overview and future perspectives

Vicente, A. T. S., & Salvador, J. A. R. (2024) · MedComm · doi:10.1002/mco2.575 · Cited by 14 · see citing works

Small-Molecule Degraders of Cyclin-Dependent Kinase Protein: A Review

Yu, B., Du, Z., Zhang, Y., Li, Z., & Bian, J. (2021) · Future Medicinal Chemistry · doi:10.4155/fmc-2021-0154 · Cited by 13 · see citing works

PROTACs: The Future of Leukemia Therapeutics

Anwar, Z., Ali, M. S., Galvano, A., Perez, A., Mantia, M. L., Bukhari, I., & Świątczak, B. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.851087 · Cited by 13 · see citing works

Covalent fragment-based ligand screening approaches for identification of novel ubiquitin proteasome system modulators

Rothweiler, E. M., Brennan, P. E., & Huber, K. (2022) · Biological Chemistry · doi:10.1515/hsz-2021-0396 · Cited by 12 · see citing works

Development and Characterization of the First Selective Class IIb Histone Deacetylase Degraders

Zhai, S., Honin, I., Schäker‐Hübner, L., Hanl, M., Jacobi, L., Dressler, F., Pieńkowska, D. E., König, P., Gerhartz, J., Voget, R., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00674 · Cited by 11 · see citing works

Encoding BRAF inhibitor functions in protein degraders

Miller, D. S. J., Voell, S. A., Sosič, I., Proj, M., Rossanese, O. W., Schnakenburg, G., Gütschow, M., Collins, I., & Steinebach, C. (2022) · RSC Medicinal Chemistry · doi:10.1039/d2md00064d · Cited by 11 · see citing works

Heterobifunctional Ligase Recruiters Enable pan-Degradation of Inhibitor of Apoptosis Proteins

Ng, Y. L. D., Bricelj, A., Jansen, J. A., Murgai, A., Peter, K., Donovan, K. A., Gütschow, M., Krönke, J., Steinebach, C., & Sosič, I. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01817 · Cited by 11 · see citing works

Targeting the cell-cycle machinery for cancer therapy

Peng, Y., Liu, J., Inuzuka, H., Liu, J., & Wei, W. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.08.008 · Cited by 10 · see citing works

Targeting the ubiquitin pathway in lymphoid malignancies

Li, B., Eichhorn, P. J. A., & Chng, W. J. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.216978 · Cited by 10 · see citing works

Exploiting targeted degradation of cyclins and cyclin-dependent kinases for cancer therapeutics: a review

Zheng, S., Chen, Y., Zhu, Z., Li, N., He, C., Koeffler, H. P., Han, X., Wei, Q., & Xu, L. (2025) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2500021 · Cited by 9 · see citing works

A narrative review of proteolytic targeting chimeras (PROTACs): future perspective for prostate cancer therapy

Chen, X., Haishan, S., Shao, Y., Ma, Q., Niu, Y., & Shang, Z. (2021) · Translational Andrology and Urology · doi:10.21037/tau-20-1357 · Cited by 9 · see citing works

Accessing three-branched high-affinity cereblon ligands for molecular glue and protein degrader design

Kuchta, R. D., Heim, C., Herrmann, A., Maiwald, S. A., Ng, Y. L. D., Sosič, I., Keuler, T., Krönke, J., Gütschow, M., Hartmann, M. D., et al. (2023) · RSC Chemical Biology · doi:10.1039/d2cb00223j · Cited by 9 · see citing works

FDA-approved kinase inhibitors in PROTAC design, development and synthesis

Kossakowski, K., Cherniienko, A., Zaprutko, L., & Pawełczyk, A. (2025) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2025.2542357 · Cited by 8 · see citing works

Enhancing Solubility in VHL-Based PROTACs: Optimized USP7 Degraders for Improved Developability

Wittenburg, S., Zuleeg, M. R., Peter, K., Lemnitzer, P., Voget, R., Bricelj, A., Gobec, M., Dierlamm, N., Braun, M. B., Geiger, T. M., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00718 · Cited by 7 · see citing works

Molecules Inducing Specific Cyclin-Dependent Kinase Degradation and their Possible Use in Cancer Therapy

Zheng, M., Zhang, X., Chen, W., Xia, F., Yang, H., Yuan, K., & Yang, P. (2024) · Future Medicinal Chemistry · doi:10.4155/fmc-2023-0259 · Cited by 7 · see citing works

Targeted degradation of CDK4/6 by LA-CB1 inhibits EMT and suppresses tumor growth in orthotopic breast cancer

He, J., Liu, S., Zhang, S., Gao, Q., Zhu, L., Xu, N., Hu, Z., Zhang, X., Ma, S., Wang, X., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-92494-8 · Cited by 7 · see citing works

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Adhikari, B., Schneider, K., Diebold, M., Sotriffer, C., & Wolf, E. (2024) · eLife · doi:10.7554/elife.98450.3 · Cited by 6 · see citing works

Research Progress of PROTACs in Breast Cancer: Subtype-Oriented Target Landscape, Clinical Stratification Evidence, and Engineering Strategies for Translation

Guo, S., Liu, J., Zheng, H., & Wu, X. (2026) · Biomedicines · doi:10.3390/biomedicines14040835 · Cited by 5 · see citing works

Targeted protein degraders from an oncologist point of view: The Holy Grail of cancer therapy?

Ambrosini, M., Fucà, G., Duca, M., Damian, S., Santis, F. D., Corti, F., Cresta, S., de Braud, F., & Nicola, M. D. (2021) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2021.103532 · Cited by 5 · see citing works

Selective CDK6 Degradation via the KLHDC2 E3 Ubiquitin Ligase

Jeon, E., Kim, Y., Ahn, H., Martinez, M. J., Hwang, K., Cho, S., Dwyer, B. G., Romero, B. A., Hinshaw, S. M., Gray, N. S., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c02713 · Cited by 4 · see citing works

Emerging Strategies to Inhibit the G1/S Transition for Cancer Therapy

Rubin, S. M., Sage, J., & Skotheim, J. M. (2026) · Cancer Research · doi:10.1158/0008-5472.can-25-0916 · Cited by 5 · see citing works

Design and synthesis of JNK1-targeted PROTACs and research on the activity

Guo, Y., Liu, F., Chi, M., Qian, H., Zhang, Y., Yuan, Y., Hou, S., Chen, X., & Ma, L. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.108044 · Cited by 4 · see citing works

PROTAC-Mediated GSPT1 Degradation Impairs the Expression of Fusion Genes in Acute Myeloid Leukemia

Perzolli, A., Steinebach, C., Krönke, J., Gütschow, M., Zwaan, C. M., Barneh, F., & Heidenreich, O. T. (2025) · Cancers · doi:10.3390/cancers17020211 · Cited by 4 · see citing works

Identification of suitable target/E3 ligase pairs for PROTAC development using a rapamycin-induced proximity assay (RiPA)

Adhikari, B., Schneider, K., Diebold, M., Sotriffer, C., & Wolf, E. (2024) · eLife · doi:10.7554/elife.98450 · Cited by 4 · see citing works

Palbociclib as an Antitumor Drug: A License to Kill

Łupicka‐Słowik, A., Cossu, F., & Sieńczyk, M. (2024) · Molecules · doi:10.3390/molecules29225334 · Cited by 3 · see citing works

PROTACs improve selectivity for targeted proteins

Liu, L., Guan, X., Zhuo, J., Wu, X., & Han, X. (2025) · Acta Materia Medica · doi:10.15212/amm-2025-0015 · Cited by 3 · see citing works

Selective CDK6 degradation mediated by cereblon, VHL, and novel IAP-recruiting PROTACs

Anderson, N. A., Cryan, J., Ahmed, A., Dai, H., McGonagle, G. A., Rozier, C., & Benowitz, A. B. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127106 · Cited by 69 · see citing works

Potent and Preferential Degradation of CDK6 via Proteolysis Targeting Chimera Degraders

Su, S., Yang, Z., Gao, H., Yang, H., Zhu, S., An, Z., Wang, J., Li, Q., Chandarlapaty, S., Deng, H., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00871 · Cited by 209 · see citing works

Selective CDK6 Degradation via the KLHDC2 E3 Ubiquitin Ligase

Jeon, E., Kim, Y., Ahn, H., Martinez, M. J., Hwang, K., Cho, S., Dwyer, B. G., Romero, B. A., Hinshaw, S. M., Gray, N. S., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c02713 · Cited by 4 · see citing works

Selective degradation of CDK6 by a palbociclib based PROTAC

Rana, S., Bendjennat, M., Kour, S., King, H. M., Kizhake, S., Zahid, M., & Natarajan, A. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2019.03.035 · Cited by 135 · see citing works

A Type II CDK6 Degrader Enables Cellular Targeting beyond the Limits of Type II Inhibition

Kim, J. H., Mills, C. E., Kozicka, Z., Scott, D. C., Jin, C., Jiang, Z., Dwyer, B. G., Geng, Q., Toenjes, S. T., Byun, W. S., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c10277 · Cited by 2 · see citing works