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

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

Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome

Tartaglia, M., Mehler, E. L., Goldberg, R. B., Zampino, G., Brunner, H. G., Kremer, H., van der Burgt, I., Crosby, A. H., Ion, A., Jeffery, S., et al. (2001) · Nature Genetics · doi:10.1038/ng772 · Cited by 1,736 · see citing works

Proteasome inhibitors: a novel class of potent and effective antitumor agents.

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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

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

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

Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia

Tartaglia, M., Niemeyer, C. M., Fragale, A., Song, X., Buechner, J., Jung, A., Hählen, K., Hasle, H., Licht, J. D., & Gelb, B. D. (2003) · Nature Genetics · doi:10.1038/ng1156 · Cited by 1,033 · see citing works

Allosteric inhibition of SHP2 phosphatase inhibits cancers driven by receptor tyrosine kinases

Chen, Y.-N. P., LaMarche, M. J., Chan, H. M., Fekkes, P., Garcia-Fortanet, J., Acker, M. G., Antonakos, B., Chen, C. H.-T., Chen, Z., Cooke, V. G., et al. (2016) · Nature · doi:10.1038/nature18621 · Cited by 925 · 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

Small‐Molecule PROTACS: New Approaches to Protein Degradation

Toure, M., & Crews, C. M. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201507978 · Cited by 674 · see citing works

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

Mutations in PTPN11 implicate the SHP-2 phosphatase in leukemogenesis

Loh, M. L. (2003) · Blood · doi:10.1182/blood-2003-09-3287 · 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

PTPN11 is the first identified proto-oncogene that encodes a tyrosine phosphatase

Chan, R. J., & Feng, G. (2006) · Blood · doi:10.1182/blood-2006-07-028829 · Cited by 378 · see citing works

Mutant KRAS-driven cancers depend on PTPN11/SHP2 phosphatase

Ruess, D. A., Heynen, G. J., Ciecielski, K. J., Ai, J., Berninger, A., Kabacaoglu, D., Görgülü, K., Dantes, Z., Wörmann, S. M., Diakopoulos, K. N., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0024-8 · Cited by 370 · see citing works

SHP2 is required for growth of KRAS-mutant non-small-cell lung cancer in vivo

Mainardi, S., Mulero-Sánchez, A., Prahallad, A., Germano, G., Bosma, A., Krimpenfort, P., Lieftink, C., Steinberg, J. D., de Wit, N., Gonçalves-Ribeiro, S., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0023-9 · Cited by 320 · see citing works

Allosteric inhibition of SHP2: identification of a potent, selective, and orally efficacious phosphatase inhibitor

Garcia Fortanet, J., Chen, C. H.-T., Chen, Y.-N. P., Chen, Z., Deng, Z., Firestone, B., Fekkes, P., Fodor, M., Fortin, P. D., Fridrich, C., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00680 · Cited by 298 · 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

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

Qin, C., Hu, Y., Zhou, B., Fernandez-Salas, E., Yang, C.-Y., Liu, L., McEachern, D., Przybranowski, S., Wang, M., Stuckey, J., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00506 · Cited by 281 · see citing works

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

Schiedel, M., Herp, D., Hammelmann, S., Swyter, S., Lehotzky, A., Robaa, D., Oláh, J., Ovádi, J., Sippl, W., & Jung, M. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01872 · Cited by 275 · 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

PD-1/SHP-2 Inhibits Tc1/Th1 Phenotypic Responses and the Activation of T Cells in the Tumor Microenvironment

Li, J., Jie, H.-B., Lei, Y. L., Gildener‐Leapman, N., Trivedi, S., Green, T., Kane, L., & Ferris, R. L. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-1215 · Cited by 252 · see citing works

Structure-Based Discovery of SD-36 as a Potent, Selective, and Efficacious PROTAC Degrader of STAT3 Protein

Zhou, H., Bai, L., Xu, R., Zhao, Y., Chen, J., McEachern, D., Chinnaswamy, K., Wen, B., Dai, L., Kumar, P., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01530 · Cited by 233 · see citing works

Identification of TNO155, an Allosteric SHP2 Inhibitor for the Treatment of Cancer

LaMarche, M. J., Acker, M., Argintaru, A., Bauer, D., Boisclair, J., Chan, H., Chen, C. H.-T., Chen, Y.-N., Chen, Z., Deng, Z., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01170 · Cited by 231 · see citing works

Discovery of Highly Potent and Efficient PROTAC Degraders of Androgen Receptor (AR) by Employing Weak Binding Affinity VHL E3 Ligase Ligands

Han, X., Zhao, L., Xiang, W., Qin, C., Miao, B., Xu, T., Wang, M., Yang, C., Chinnaswamy, K., Stuckey, J. A., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01393 · Cited by 229 · see citing works

Chemically Induced Degradation of Anaplastic Lymphoma Kinase (ALK)

Powell, C. E., Gao, Y., Tan, L., Donovan, K. A., Nowak, R. P., Loehr, A., Bahcall, M., Fischer, E. S., Jänne, P. A., George, R. E., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01655 · Cited by 198 · see citing works

Development of Multifunctional Histone Deacetylase 6 Degraders with Potent Antimyeloma Activity

Wu, H., Yang, K., Zhang, Z., Leisten, E. D., Li, Z., Xie, H., Liu, J., Smith, K. A., Novakova, Z., Barinka, C., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00516 · Cited by 180 · see citing works

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

Burslem, G. M., Song, J., Chen, X., Hines, J., & Crews, C. M. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b10320 · Cited by 176 · see citing works

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

Wang, M., Lu, J., Wang, M., Yang, C.-Y., & Wang, S. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00471 · Cited by 172 · see citing works

Bruton tyrosine kinase degradation as a therapeutic strategy for cancer

Dobrovolsky, D., Wang, E. S., Morrow, S., Leahy, C., Faust, T., Nowak, R. P., Donovan, K. A., Yang, G., Li, Z., Fischer, E. S., et al. (2019) · Blood · doi:10.1182/blood-2018-07-862953 · Cited by 169 · see citing works

Development of a Novel B-Cell Lymphoma 6 (BCL6) PROTAC To Provide Insight into Small Molecule Targeting of BCL6

McCoull, W., Cheung, T., Anderson, E., Barton, P., Burgess, J., Byth, K., Cao, Q., Castaldi, M. P., Chen, H., Chiarparin, E., et al. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00698 · Cited by 139 · see citing works

Chlorogenic Acid Prevents Osteoporosis by Shp2/PI3K/Akt Pathway in Ovariectomized Rats

Zhou, R. P., Lin, S. J., Wan, W. B., Zuo, H. L., Yao, F. F., Ruan, H. B., Xu, J., Song, W., Zhou, Y., Wen, S. Y., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0166751 · Cited by 108 · see citing works

Isolation of a distinct class of gain-of-function SHP-2 mutants with oncogenic RAS-like transforming activity from solid tumors

Miyamoto, D., Miyamoto, M., Takahashi, A., Yomogita, Y., Higashi, H., Kondo, S., & Hatakeyama, M. (2008) · Oncogene · doi:10.1038/sj.onc.1211019 · Cited by 105 · see citing works

Optimization of Fused Bicyclic Allosteric SHP2 Inhibitors

Bagdanoff, J. T., Chen, Z., Acker, M., Chen, Y., Chan, H., Dore, M., Firestone, B., Fodor, M., García‐Fortanet, J., Hentemann, M., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01725 · Cited by 91 · see citing works

6-Amino-3-methylpyrimidinones as Potent, Selective, and Orally Efficacious SHP2 Inhibitors

Sarver, P., Acker, M., Bagdanoff, J. T., Chen, Z., Chen, Y.-N., Chan, H., Firestone, B., Fodor, M., Fortanet, J., Hao, H., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01726 · Cited by 87 · see citing works

Targeting Protein Tyrosine Phosphatase SHP2 for Therapeutic Intervention

Butterworth, S., Overduin, M., & Barr, A. (2014) · Future Medicinal Chemistry · doi:10.4155/fmc.14.88 · Cited by 78 · see citing works

Dietary quercetin potentiates the antiproliferative effect of interferon-α in hepatocellular carcinoma cells through activation of JAK/STAT pathway signaling by inhibition of SHP2 phosphatase

Igbe, I., Shen, X., Jiao, W., Qiang, Z., Deng, T., Li, S., Liu, W., Liu, H.-W., Zhang, G., & Wang, F. (2017) · Oncotarget · doi:10.18632/oncotarget.22556 · Cited by 53 · see citing works

Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials

Xie, X., Yu, T., Li, X., Zhang, N., Foster, L. J., Peng, C., Huang, W., & He, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01589-z · Cited by 396 · 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

Double-edged roles of protein tyrosine phosphatase SHP2 in cancer and its inhibitors in clinical trials

Song, Y., Zhao, M., Zhang, H., & Yu, B. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107966 · Cited by 125 · see citing works

A comprehensive review of SHP2 and its role in cancer

Asmamaw, M. D., Shi, X.-J., Zhang, L.-R., & Liu, H.-M. (2022) · Cellular Oncology · doi:10.1007/s13402-022-00698-1 · Cited by 119 · see citing works

Targeted Degradation of the Oncogenic Phosphatase SHP2

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Structure-based design, synthesis and biological evaluation of aminopyrazines as highly potent, selective, and cellularly active allosteric SHP2 inhibitors

Tang, K., Zhao, M., Wu, Y.-H., Wu, Q., Wang, S., Dong, Y., Yu, B., Song, Y., & Liu, H.-M. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114106 · Cited by 20 · see citing works

Analysis and Control of Proteolysis of Recombinant Proteins in Escherichia coli

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Proteolysis in alfalfa silage and its inhibiting method

Guo, X., He, Z., & Liu, G. (2005) · Caoye kexue

Progress on Proteolysis in Bacterial Cells

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Proteolysis Associated with Thymidine-Induced Selective Cell Death in L-Cell Cultures

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Intracellular proteolysis: Signals of selective protein degradation

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