Monomeric Targeted Protein Degraders
Abstract
The discovery and development of targeted protein degraders have become important areas of research in the field of medicinal chemistry. Inducing degradation of a target protein presents several advantages relative to simple inhibition including a potential for extended duration of action and more profound pharmacology. While engineered heterodimeric molecules have recently been a major focus within industry and academia, this Perspective highlights examples of targeted protein degradation observed for smaller, monomeric molecules. Methods and tools for evaluating protein degradation as well as a discussion of physical properties of monomeric vs engineered heterodimeric degraders are presented.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
MG degraders have favorable drug-like properties that often fall within Lipinski's rule of 5.
“(i) favorable drug-like properties that often fall within the Lipinski's ''rule of 5'' (Fig. 2); 35”
From Chasing molecular glue degraders: screening approaches (2022) · cites this paper as [35]
Cites
Lipinski, C. A., Lombardo, F., Dominy, B. W., & Feeney, P. J. (2001) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(00)00129-0 · Cited by 18,139 · see citing works
The phosphatidylinositol 3-Kinase–AKT pathway in human cancer
Vivanco, I., & Sawyers, C. L. (2002) · Nature reviews. Cancer · doi:10.1038/nrc839 · Cited by 6,041 · see citing works
The phosphoinositide 3-kinase pathway
Cantley, L. C. (2002) · Science · doi:10.1126/science.296.5573.1655 · Cited by 5,621 · see citing works
Jones, P. A., & Baylin, S. B. (2007) · Cell · doi:10.1016/j.cell.2007.01.029 · Cited by 4,515 · see citing works
Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing
Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R. S., & Zhang, Y. (2002) · Science · doi:10.1126/science.1076997 · Cited by 3,775 · see citing works
High Frequency of Mutations of the PIK3CA Gene in Human Cancers
Samuels, Y., Wang, Z., Bardelli, A., Silliman, N., Ptak, J., Szabo, S., Yan, H., Gazdar, A. F., Powell, S. M., Riggins, G. J., et al. (2004) · Science · doi:10.1126/science.1096502 · Cited by 3,448 · see citing works
Ertl, P., Rohde, B., & Selzer, P. M. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm000942e · Cited by 3,149 · see citing works
Targeting the phosphoinositide 3-kinase pathway in cancer
Liu, P., Cheng, H.-L. M., Roberts, T. M., & Zhao, J. J. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2926 · Cited by 2,722 · see citing works
The polycomb group protein EZH2 is involved in progression of prostate cancer
Varambally, S., Dhanasekaran, S. M., Zhou, M., Barrette, T. R., Kumar-Sinha, C., Sanda, M. G., Ghosh, D., Pienta, K. J., Sewalt, R. G. A. B., Otte, A. P., et al. (2002) · Nature · doi:10.1038/nature01075 · Cited by 2,717 · see citing works
Rock, K. L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., & Goldberg, A. L. (1994) · Cell · doi:10.1016/s0092-8674(94)90462-6 · Cited by 2,524 · see citing works
Thalidomide is an inhibitor of angiogenesis.
D'Amato, R. J., Loughnan, M. S., Flynn, E., & Folkman, J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.9.4082 · Cited by 2,454 · see citing works
Amplification of N- myc in Untreated Human Neuroblastomas Correlates with Advanced Disease Stage
Brodeur, G. M., Seeger, R. C., Schwab, M., VARMUS, H. E., & Bishop, J. M. (1984) · Science · doi:10.1126/science.6719137 · Cited by 2,261 · 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
An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
Soucy, T. A., Smith, P. G., Milhollen, M. A., Berger, A. J., Gavin, J. M., Adhikari, S., Brownell, J. E., Burke, K. E., Cardin, D. P., Critchley, S., et al. (2009) · Nature · doi:10.1038/nature07884 · Cited by 1,990 · 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
EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations
McCabe, M. T., Ott, H. M., Ganji, G., Korenchuk, S., Thompson, C., Van Aller, G. S., Liu, Y., Graves, A. P., III, A. D. P., Diaz, E., et al. (2012) · Nature · doi:10.1038/nature11606 · Cited by 1,786 · see citing works
IAP proteins: blocking the road to death's door
Salvesen, G. S., & Duckett, C. S. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm830 · Cited by 1,756 · see citing works
PI3K and cancer: lessons, challenges and opportunities
Fruman, D. A., & Rommel, C. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4204 · Cited by 1,716 · see citing works
Kleer, C. G., Cao, Q., Varambally, S., Shen, R., Ota, I., Tomlins, S. A., Ghosh, D., Sewalt, R. G. A. B., Otte, A. P., Hayes, D. F., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1933744100 · Cited by 1,649 · see citing works
Engineered Luciferase Reporter from a Deep Sea Shrimp Utilizing a Novel Imidazopyrazinone Substrate
Hall, M. P., Unch, J., Binkowski, B. F., Valley, M. P., Butler, B. L., Wood, M. G., Otto, P., Zimmerman, K., Vidugiris, G. J. A., Machleidt, T., et al. (2012) · ACS Chemical Biology · doi:10.1021/cb3002478 · Cited by 1,588 · 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
Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540 · see citing works
The JAK-STAT Pathway: Impact on Human Disease and Therapeutic Intervention
O'Shea, J., Schwartz, D., Villarino, A. V., Gadina, M., Mcinnes, I., & Laurence, A. (2015) · Annual Review of Medicine · doi:10.1146/annurev-med-051113-024537 · Cited by 1,472 · see citing works
Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8324 · Cited by 1,444 · see citing works
The discovery of artemisinin (qinghaosu) and gifts from Chinese medicine
Tu, Y. (2011) · Nature Medicine · doi:10.1038/nm.2471 · Cited by 1,397 · see citing works
Polycomb silencers control cell fate, development and cancer
Sparmann, A., & van Lohuizen, M. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1991 · Cited by 1,294 · see citing works
ESR1 ligand-binding domain mutations in hormone-resistant breast cancer
Toy, W., Shen, Y., Won, H. H., Green, B., Sakr, R. A., Will, M., Li, Z., Gala, K. P., Fanning, S. W., King, T. A., et al. (2013) · Nature Genetics · doi:10.1038/ng.2822 · Cited by 1,252 · see citing works
Mechanisms and consequences of Jak–STAT signaling in the immune system
Villarino, A. V., Kanno, Y., & O'Shea, J. J. (2017) · Nature Immunology · doi:10.1038/ni.3691 · Cited by 1,221 · see citing works
IAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNFα-Dependent Apoptosis
Varfolomeev, E., Blankenship, J. W., Wayson, S. M., Fedorova, A. V., Kayagaki, N., Garg, P., Zobel, K., Dynek, J. N., Elliott, L. O., Wallweber, H. J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.030 · Cited by 1,218 · see citing works
Sampaio, E. P., Sarno, E. N., Gallily, R., Cohn, Z. A., & Kaplan, G. (1991) · The Journal of Experimental Medicine · doi:10.1084/jem.173.3.699 · Cited by 1,191 · see citing works
A Pharmacological Map of the PI3-K Family Defines a Role for p110α in Insulin Signaling
Knight, Z. A., Gonzalez, B., Feldman, M. E., Zunder, E. R., Goldenberg, D. D., Williams, O., Loewith, R., Stokoe, D., Balla, A., Toth, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.03.035 · Cited by 1,174 · see citing works
Activating ESR1 mutations in hormone-resistant metastatic breast cancer
Robinson, D. R., Wu, Y.-M., Vats, P., Su, F., Lonigro, R. J., Cao, X., Kalyana-Sundaram, S., Wang, R., Ning, Y., Hodges, L., et al. (2013) · Nature Genetics · doi:10.1038/ng.2823 · Cited by 1,145 · see citing works
Advani, R. H., Buggy, J. J., Sharman, J. P., Smith, S. M., Boyd, T. E., Grant, B., Kolibaba, K. S., Furman, R. R., Rodriguez, S., Chang, B. Y., et al. (2013) · Journal of Clinical Oncology · doi:10.1200/jco.2012.42.7906 · Cited by 1,128 · see citing works
(1991) · PubMed · Cited by 1,101 · see citing works
IAP Antagonists Target cIAP1 to Induce TNFα-Dependent Apoptosis
Vince, J. E., Wong, W. W.-L., Khan, N. R., Feltham, R., Chau, D., Ahmed, A. U., Benetatos, C. A., Chunduru, S. K., Condon, S. M., McKinlay, M. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.037 · Cited by 1,061 · see citing works
An integrative genomic and proteomic analysis of pik3ca, pten, and akt mutations in breast cancer.
Stemke-Hale, K., Gonzalez-Angulo, A. M., Lluch, A., Neve, R. M., Kuo, W.-L., Davies, M., Carey, M., Hu, Z., Guan, Y., Sahin, A., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-6854 · Cited by 1,054 · see citing works
Inhibition of eukaryotic translation elongation by cycloheximide and lactimidomycin
Schneider‐Poetsch, T., Ju, J., Eyler, D. E., Dang, Y., Bhat, S., Merrick, W. C., Green, R., Shen, B., & Liu, J. O. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.304 · Cited by 1,020 · see citing works
Rodal, S. K., Skretting, G., Garred, Ø., Vilhardt, F., van Deurs, B., & Sandvig, K. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.4.961 · Cited by 1,009 · see citing works
Flow cytometry: basic principles and applications
Adan, A., Alizada, G., Kiraz, Y., Baran, Y., & Nalbant, A. (2016) · Critical Reviews in Biotechnology · doi:10.3109/07388551.2015.1128876 · Cited by 925 · see citing works
Mutant PIK3CA promotes cell growth and invasion of human cancer cells.
Samuels, Y., Diaz, L. A., Schmidt-Kittler, O., Cummins, J. M., DeLong, L., Cheong, I., Rago, C., Huso, D. L., Lengauer, C., Kinzler, K. W., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.05.014 · Cited by 915 · see citing works
EZH2 Oncogenic Activity in Castration-Resistant Prostate Cancer Cells Is Polycomb-Independent
Xu, K., Wu, Z. J., Groner, A. C., He, H. H., Cai, C., Lis, R. T., Wu, X., Stack, E. C., Loda, M. F., Liu, T., et al. (2012) · Science · doi:10.1126/science.1227604 · Cited by 877 · see citing works
Saal, L. H., Holm, K., Maurer, M. S., Memeo, L., Su, T., Wang, X., Yu, J. S., Malmström, P.-O., MANSUKHANI, M. M., Enoksson, J., et al. (2005) · Cancer Research · doi:10.1158/0008-5472-can-04-3913 · Cited by 877 · see citing works
Self-citationLenalidomide 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
Duda, D. M., Borg, L. A., Scott, D. C., Hunt, H. W., Hammel, M., & Schulman, B. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.022 · Cited by 767 · 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
Human Caspases: Activation, Specificity, and Regulation
Pop, C., & Salvesen, G. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r800084200 · Cited by 757 · 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
Antitumor Activity of PR-171, a Novel Irreversible Inhibitor of the Proteasome
Demo, S. D., Kirk, C. J., Aujay, M. A., Buchholz, T. J., Dajee, M., Ho, M. N., Jiang, J., Laidig, G. J., Lewis, E. R., Parlati, F., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4086 · Cited by 681 · see citing works
Quah, B., Warren, H. S., & Parish, C. R. (2007) · Nature Protocols · doi:10.1038/nprot.2007.296 · Cited by 628 · see citing works
Aydin, S. (2015) · Peptides · doi:10.1016/j.peptides.2015.04.012 · Cited by 626 · see citing works
Li, S., Shen, D., Shao, J., Crowder, R. J., Liu, W., Prat, A., He, X., Liu, S., Hoog, J., Lu, C., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.022 · Cited by 623 · 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
Kondo, Y., Shen, L., Cheng, A. S. L., Ahmed, S., Boumber, Y., Charo, C., Yamochi, T., Urano, T., Furukawa, K., Kwabi‐Addo, B., et al. (2008) · Nature Genetics · doi:10.1038/ng.159 · Cited by 618 · see citing works
Discovery and Development of Janus Kinase (JAK) Inhibitors for Inflammatory Diseases
Clark, J. D., Flanagan, M. E., & Telliez, J. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401490p · Cited by 615 · see citing works
IAPs, RINGs and ubiquitylation
Vaux, D. L., & Silke, J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1621 · Cited by 611 · see citing works
Ezh2 Orchestrates Gene Expression for the Stepwise Differentiation of Tissue-Specific Stem Cells
Ezhkova, E., Pasolli, H. A., Parker, J. S., Stokes, N., Su, I.-H., Hannon, G. J., Tarakhovsky, A., & Fuchs, E. V. (2009) · Cell · doi:10.1016/j.cell.2008.12.043 · Cited by 599 · see citing works
Targeted protein degradation by PROTACs
Neklesa, T. K., Winkler, J. D., & Crews, C. M. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.02.027 · Cited by 599 · see citing works
Isobaric Labeling-Based Relative Quantification in Shotgun Proteomics
Rauniyar, N., & Yates, J. R. (2014) · Journal of Proteome Research · doi:10.1021/pr500880b · Cited by 597 · see citing works
Acute cholesterol depletion inhibits clathrin-coated pit budding
Subtil, A., Gaidarov, I., Kobylarz, K. A., Lampson, M. A., Keen, J. H., & McGraw, T. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.6775 · Cited by 577 · see citing works
Stabilization of N-Myc Is a Critical Function of Aurora A in Human Neuroblastoma
Otto, T., Horn, S., Brockmann, M., Eilers, U., Schüttrumpf, L., Popov, N., Kenney, A. M., Schulte, J. H., Beijersbergen, R. L., Christiansen, H., et al. (2009) · Cancer Cell · doi:10.1016/j.ccr.2008.12.005 · Cited by 574 · see citing works
Haslett, P. A. J., Corral, L. G., Albert, M. L., & Kaplan, G. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.11.1885 · Cited by 572 · see citing works
The inhibitors of apoptosis (IAPs) as cancer targets
Hunter, A. M., LaCasse, E. C., & Korneluk, R. G. (2007) · Apoptosis · doi:10.1007/s10495-007-0087-3 · Cited by 565 · see citing works
Polycomb group proteins: navigators of lineage pathways led astray in cancer
Bracken, A. P., & Helin, K. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2736 · Cited by 562 · see citing works
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
Knutson, S. K., Kawano, S., Minoshima, Y., Warholic, N. M., Huang, K., Xiao, Y., Kadowaki, T., Uesugi, M., Kuznetsov, G., Kumar, N., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0773 · Cited by 529 · see citing works
Beyond chemotherapy: targeted therapies in ovarian cancer
Yap, T. A., Carden, C. P., & Kaye, S. B. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2583 · Cited by 495 · see citing works
Protac-Induced Protein Degradation in Drug Discovery: Breaking the Rules or Just Making New Ones?
Churcher, I. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01272 · Cited by 491 · see citing works
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
The proteasome inhibitor PS-341 in cancer therapy.
Teicher, B. A., Ara, G., Herbst, R. S., Palombella, V. J., & Adams, J. (1999) · PubMed · Cited by 472 · see citing works
Meyer, D. M., Jesson, M. I., Li, X., Elrick, M. M., Funckes-Shippy, C. L., Warner, J. D., Gross, C. J., Dowty, M. E., Ramaiah, S. K., Hirsch, J. L., et al. (2010) · Journal of Inflammation · doi:10.1186/1476-9255-7-41 · Cited by 464 · see citing works
Critical role for the p110α phosphoinositide-3-OH kinase in growth and metabolic regulation
Foukas, L. C., Claret, M., Pearce, W., Okkenhaug, K., Meek, S., Peskett, E., Sancho, S., Smith, A. J. H., Withers, D. J., & Vanhaesebroeck, B. (2006) · Nature · doi:10.1038/nature04694 · Cited by 463 · see citing works
A small-molecule inhibitor of the ubiquitin activating enzyme for cancer treatment
Hyer, M. L., Milhollen, M. A., Ciavarri, J., Fleming, P., Traore, T., Sappal, D., Huck, J., Shi, J., Gavin, J., Brownell, J., et al. (2018) · Nature Medicine · doi:10.1038/nm.4474 · Cited by 447 · see citing works
CRISPR-Mediated Tagging of Endogenous Proteins with a Luminescent Peptide
Schwinn, M. K., Machleidt, T., Zimmerman, K., Eggers, C. T., Dixon, A. S., Hurst, R., Hall, M. P., Encell, L. P., Binkowski, B. F., & Wood, K. V. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.7b00549 · Cited by 434 · see citing works
Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2
Deng, X., Dzamko, N. L., Prescott, A. R., Davies, P., Liu, Q., Yang, Q., Lee, J., Patricelli, M. P., Nomanbhoy, T. K., Alessi, D. R., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.538 · Cited by 424 · see citing works
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
Antitumor activity of MLN8054, an orally active small-molecule inhibitor of Aurora A kinase
Manfredi, M. G., Ecsedy, J., Meetze, K. A., Balani, S. K., Burenkova, O. V., Chen, W., Galvin, K. M., Hoar, K. M., Huck, J. J., Leroy, P. J., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608798104 · Cited by 412 · see citing works
SWI/SNF-mutant cancers depend on catalytic and non-catalytic activity of EZH2
Kim, K. H., Kim, W., Howard, T. P., Vázquez, F., Tsherniak, A., Wu, J. N., Wang, W., Haswell, J. R., Walensky, L. D., Hahn, W. C., et al. (2015) · Nature Medicine · doi:10.1038/nm.3968 · Cited by 407 · see citing works
Merenbakh-Lamin, K., Ben-Baruch, N. E., Yeheskel, A., Dvir, A., Soussan‐Gutman, L., Jeselsohn, R. M., Yelensky, R., Brown, M. A., Miller, V. A., Sarid, D. L., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-1197 · Cited by 397 · see citing works
Dzamko, N. L., Deák, M., Hentati, F., Reith, A. D., Prescott, A. R., Alessi, D. R., & Nichols, R. J. (2010) · Biochemical Journal · doi:10.1042/bj20100784 · Cited by 379 · see citing works
Herzig, M. C., Kolly, C., Persohn, E., Theil, D. J., Schweizer, T., Hafner, T., Stemmelen, C., Troxler, T. J., Schmid, P., Danner, S., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr348 · Cited by 360 · see citing works
Effect of selective LRRK2 kinase inhibition on nonhuman primate lung
Fuji, R. N., Flagella, M., Baca, M., Baptista, M. A. S., Brodbeck, J., Chan, B. K., Fiske, B. K., Honigberg, L. A., Jubb, A. M., Katavolos, P., et al. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aaa3634 · Cited by 357 · see citing works
Amino-substituted thalidomide analogs: Potent inhibitors of TNF-α production
Muller, G. W., Chen, R., Huang, S., Corral, L. G., Wong, L. M., Patterson, R. T., Chen, Y., Kaplan, G., & Stirling, D. (1999) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00250-4 · Cited by 341 · see citing works
Flanagan, M., Blumenkopf, T., Brissette, W., Brown, M. F., Casavant, J. M., Chang, S.-P., Doty, J. L., Elliott, E., Fisher, M., Hines, M., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm1004286 · Cited by 334 · see citing works
Discovery of Novel Antitumor Sulfonamides Targeting G1 Phase of the Cell Cycle
Owa, T., Yoshino, H., Okauchi, T., Yoshimatsu, K., Ozawa, Y., Sugi, N. H., Nagasu, T., Koyanagi, N., & Kitoh, K. (1999) · Journal of Medicinal Chemistry · doi:10.1021/jm9902638 · Cited by 322 · see citing works
Fell, M. J., Mirescu, C., Basu, K., Cheewatrakoolpong, B., DeMong, D. E., Ellis, J. M., Hyde, L. A., Lin, Y., Markgraf, C. G., Mei, H., et al. (2015) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.115.227587 · Cited by 310 · see citing works
A Cereblon Modulator (CC-220) with Improved Degradation of Ikaros and Aiolos
Matyskiela, M. E., Zhang, W., Man, H.-W., Muller, G., Khambatta, G., Baculi, F., Hickman, M., LeBrun, L., Pagarigan, B., Carmel, G., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01921 · Cited by 309 · see citing works
Quantitative Live-Cell Kinetic Degradation and Mechanistic Profiling of PROTAC Mode of Action
Riching, K. M., Mahan, S. D., Corona, C. R., McDougall, M. G., Vasta, J. D., Robers, M. B., Urh, M., & Daniels, D. L. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00692 · Cited by 307 · see citing works
Brockmann, M., Poon, E., Berry, T., Carstensen, A., Deubzer, H. E., Rycak, L., Jamin, Y., Thway, K., Robinson, S. P., Roels, F., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.05.005 · Cited by 300 · see citing works
Inhibition of Myc family proteins eradicates KRas-driven lung cancer in micePreprint
Soucek, L., Whitfield, J. R., Sodir, N. M., Massó-Vallés, D., Serrano, E., Karnezis, A. N., Swigart, L. B., & Evan, G. I. (2013) · Genes & Development · doi:10.1101/gad.205542.112 · Cited by 299 · see citing works
Drugging MYCN through an Allosteric Transition in Aurora Kinase A
Gustafson, W. C., Meyerowitz, J., Nekritz, E. A., Chen, J., Benes, C. H., Charron, E., Simonds, E. F., Seeger, R. C., Matthay, K. K., Hertz, N. T., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.07.015 · Cited by 280 · see citing works
Cai, Q., Sun, H., Peng, Y., Lü, J., Nikolovska‐Coleska, Z., McEachern, D., Liu, L., Qiu, S., Yang, C., Miller, R. S., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm101505d · Cited by 274 · see citing works
The Use of AlphaScreen Technology in HTS: Current Status
Eglen, R. M., Reisine, T., Roby, P., Rouleau, N., Illy, C., Bossé, R., & Bielefeld, M. (2008) · Current Chemical Genomics · doi:10.2174/1875397300801010002 · Cited by 261 · see citing works
Lai, A. G., Kahraman, M., Govek, S. P., Nagasawa, J. Y., Bonnefous, C., Julien, J., Douglas, K. L., Sensintaffar, J., Lu, N., Lee, K., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00054 · Cited by 253 · see citing works
Flygare, J. A., Beresini, M., Budha, N., Chan, H., Chan, I. T., Cheeti, S., Cohen, F., Deshayes, K., Doerner, K., Eckhardt, S. G., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300060k · Cited by 252 · see citing works
Receptor tyrosine kinase (c-Kit) inhibitors: a potential therapeutic target in cancer cells
Babaei, M. A., Kamalıdehghan, B., Saleem, M., et al. (2016) · Drug Design Development and Therapy · doi:10.2147/dddt.s89114 · Cited by 252 · see citing works
Development of artemisinin compounds for cancer treatment
Lai, H. C., Singh, N. P., & Sasaki, T. (2012) · Investigational New Drugs · doi:10.1007/s10637-012-9873-z · Cited by 235 · see citing works
Antagonists Induce a Conformational Change in cIAP1 That Promotes Autoubiquitination
Dueber, E. C., Schoeffler, A. J., Lingel, A., Elliott, J. M., Fedorova, A. V., Giannetti, A. M., Zobel, K., Maurer, B., Varfolomeev, E. E., Wu, P., et al. (2011) · Science · doi:10.1126/science.1207862 · Cited by 232 · see citing works
van Kruchten, M., de Vries, E. G. E., Glaudemans, A. W. J. M., van Lanschot, M. C. J., van Faassen, M., Kema, I. P., Brown, M., Schröder, C. P., de Vries, E. F., & Hospers, G. A. P. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-14-0697 · Cited by 229 · see citing works
Vaswani, R. G., Gehling, V. S., Dakin, L. A., Cook, A. S., Nasveschuk, C. G., Duplessis, M., Iyer, P., Balasubramanian, S., Zhao, F., Good, A. C., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01315 · Cited by 226 · see citing works
Therapeutic Ligands Antagonize Estrogen Receptor Function by Impairing Its Mobility
Guan, J., Zhou, W. J., Hafner, M. A., Blake, R. A., Chalouni, C. M., Chen, I. P., Bruyn, T. D., Giltnane, J. M., Hartman, S. J., Heidersbach, A. J., et al. (2019) · Cell · doi:10.1016/j.cell.2019.06.026 · Cited by 216 · see citing works
Self-citationChemically Induced Degradation of the Oncogenic Transcription Factor BCL6
Kerres, N., Steurer, S., Schlager, S., Bader, G., Berger, H., Caligiuri, M., Dank, C., Engen, J. R., Ettmayer, P., Fischerauer, B., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.081 · Cited by 207 · see citing works
Hagner, P. R., Man, H.-W., Fontanillo, C., Wang, M., Couto, S., Breider, M., Bjorklund, C., Havens, C. G., Lu, G., Rychak, E., et al. (2015) · Blood · doi:10.1182/blood-2015-02-628669 · Cited by 203 · see citing works
Myc proteins as therapeutic targets
Gustafson, W. C., & Weiss, W. A. (2010) · Oncogene · doi:10.1038/onc.2009.512 · Cited by 199 · see citing works
PROTAC-Mediated Degradation of Bruton’s Tyrosine Kinase Is Inhibited by Covalent Binding
Tinworth, C. P., Lithgow, H., Dittus, L., Bassi, Z. I., Hughes, S. E., Muelbaier, M., Dai, H., Smith, I. E. D., Kerr, W. J., Burley, G. A., et al. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.8b01094 · Cited by 195 · see citing works
Takawa, M., Masuda, K., Kunizaki, M., Daigo, Y., Takagi, K., Iwai, Y., Cho, H., Toyokawa, G., Yamane, Y., Maejima, K., et al. (2011) · Cancer Science · doi:10.1111/j.1349-7006.2011.01958.x · Cited by 192 · see citing works
Dietrich, J. D., Hulme, C., & Hurley, L. H. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.05.063 · Cited by 188 · see citing works
Molecular chaperones and protein kinase quality control
Caplan, A. J., Mandal, A. K., & Theodoraki, M. A. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.12.002 · Cited by 185 · see citing works
Ndubaku, C. O., Heffron, T. P., Staben, S. T., Baumgardner, M., Blaquière, N., Bradley, E. K., Bull, R., Do, S., Dotson, J., Dudley, D. A., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm4003632 · Cited by 182 · see citing works
Self-citationChen, T., Li, M., Zhang, R., & Wang, H. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00360.x · Cited by 181 · see citing works
Kim, Y. H., Girard, L., Giacomini, C. P., Wang, P., Hernandez‐Boussard, T., Tibshirani, R. J., Minna, J. D., & Pollack, J. R. (2005) · Oncogene · doi:10.1038/sj.onc.1208997 · Cited by 181 · see citing works
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
Baptista, M. A. S., Dave, K. D., Frasier, M. A., Sherer, T., Greeley, M. A., Beck, M. J., Varsho, J. S., Parker, G. A., Moore, C., Churchill, M. J., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080705 · Cited by 178 · see citing works
McDonnell, D. P., Wardell, S. E., & Norris, J. D. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00760 · Cited by 178 · see citing works
The development of Bruton's tyrosine kinase (BTK) inhibitors from 2012 to 2017: A mini-review
Liang, C., Tian, D., Ren, X., Ding, S., Jia, M., Xin, M., & Thareja, S. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.03.062 · Cited by 178 · see citing works
Savi, C. D., Bradbury, R. H., Rabow, A. A., Norman, R. A., de Almeida, C., Andrews, D. M., Ballard, P. G., Buttar, D., Callis, R. J., Currie, G. S., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00984 · Cited by 169 · see citing works
Ihle, N. T., & Powis, G. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-0801 · Cited by 166 · see citing works
Yan, J., Ng, S., Tay, J. L.-S., Lin, B., Koh, T. L., Tan, J. M.-L., Selvarajan, V., Liu, S.-C., Bi, C., Wang, S., et al. (2013) · Blood · doi:10.1182/blood-2012-08-450494 · Cited by 165 · see citing works
Detection of Intracellular Cytokines by Flow Cytometry
Yin, Y., Mitson‐Salazar, A., & Prussin, C. (2015) · Current Protocols in Immunology · doi:10.1002/0471142735.im0624s110 · Cited by 162 · see citing works
Prochownik, E. V., & Vogt, P. K. (2010) · Genes & Cancer · doi:10.1177/1947601910377494 · Cited by 150 · see citing works
Deisseroth, A., Kaminskas, E., Grillo, J. A., Chen, W., Saber, H., Lu, H., Rothmann, M. D., Brar, S. S., Wang, J., Garnett, C. E., et al. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-0653 · Cited by 149 · see citing works
The N-myc Oncogene: Maximizing its Targets, Regulation, and Therapeutic Potential
Beltran, H. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0536 · Cited by 148 · see citing works
Sjostrom, S. K., Finn, G., Hahn, W. C., Rowitch, D. H., & Kenney, A. M. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.07.014 · Cited by 147 · see citing works
Dihydroartemisinin is an inhibitor of ovarian cancer cell growth
Jiao, Y., Ge, C., Meng, Q., Cao, J., Tong, J., & Fan, S. (2007) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2007.00612.x · Cited by 146 · see citing works
BTK Signaling in B Cell Differentiation and Autoimmunity
Corneth, O. B. J., Wolterink, R. G. J. K., & Hendriks, R. W. (2015) · Current topics in microbiology and immunology · doi:10.1007/82_2015_478 · Cited by 140 · see citing works
ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system
Polier, S., Samant, R. S., Clarke, P. A., Workman, P., Prodromou, C., & Pearl, L. H. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1212 · Cited by 140 · see citing works
Gloeckner, C. J., Boldt, K., von Zweydorf, F., Helm, S., Wiesent, L., Sarioglu, H., & Ueffing, M. (2010) · Journal of Proteome Research · doi:10.1021/pr9008578 · Cited by 139 · see citing works
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
Skibinski, G., Nakamura, K., Cookson, M., & Finkbeiner, S. M. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2712-13.2014 · Cited by 138 · see citing works
Kung, P., Bingham, P., Brooun, A., Collins, M. R., Deng, Y., Dinh, D. M., Fan, C., Gajiwala, K. S., Grantner, R., Gukasyan, H. J., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01375 · Cited by 138 · see citing works
Baselga, J. M., Dent, S. F., Cortés, J., Im, Y., Dieras, V. C., Harbeck, N., Krop, I. E., Verma, S., Wilson, T. R., Jin, H., et al. (2018) · Journal of Clinical Oncology · doi:10.1200/jco.2018.36.18_suppl.lba1006 · Cited by 138 · see citing works
Enzyme‐Linked Immunosorbent Assays
Hornbeck, P. V. (2015) · Current Protocols in Immunology · doi:10.1002/0471142735.im0201s110 · Cited by 137 · see citing works
Tria, G. S., Abrams, T. J., Baird, J., Burks, H. E., Firestone, B., Gaither, L. A., Hamann, L. G., He, G., Kirby, C. A., Kim, S., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01682 · Cited by 134 · see citing works
Protein Detection by Simple Western™ Analysis
Harris, V. M. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2694-7_47 · Cited by 125 · see citing works
Amaravadi, R. K., & Winkler, J. D. (2012) · Autophagy · doi:10.4161/auto.20958 · Cited by 123 · see citing works
Joseph, J. D., Darimont, B. D., Zhou, W. J., Arrazate, A., Young, A. E., Ingalla, E., Walter, K., Blake, R. A., Nonomiya, J., Guan, Z., et al. (2016) · eLife · doi:10.7554/elife.15828 · Cited by 122 · see citing works
Self-citationSloane, D. A., Trikić, M. Z., Chu, M. L.-H., et al. (2010) · ACS Chemical Biology · doi:10.1021/cb100053q · Cited by 119 · see citing works
Cong, H., Xu, L., Wu, Y., Qu, Z., Bian, T., Zhang, W., Xing, C., & Zhuang, C. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01668 · Cited by 113 · see citing works
Protein degradation through covalent inhibitor-based PROTACs
Xue, G., Chen, J., Liu, L., Zhou, D., Zuo, Y., Fu, T., & Pan, Z. (2020) · Chemical Communications · doi:10.1039/c9cc08238g · Cited by 109 · see citing works
Ahlberg, J., Berkenstam, A. L., Henell, F., & Glaumann, H. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89099-8 · Cited by 107 · see citing works
Purushottamachar, P., Godbole, A. M., Gediya, L. K., Martin, M. S., Vasaitis, T. S., Kwegyir‐Afful, A. K., Ramalingam, S., Ateş‐Alagöz, Z., & Njar, V. C. O. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400048v · Cited by 104 · 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
Dieck, S. T., Müller, A., Nehring, A., Hinz, F. I., Bartnik, I., Schuman, E. M., & Dieterich, D. C. (2012) · Current Protocols in Cell Biology · doi:10.1002/0471143030.cb0711s56 · Cited by 99 · see citing works
A covalently bound inhibitor triggers EZH2 degradation through CHIP‐mediated ubiquitination
Wang, X., Cao, W., Zhang, J., Yan, M., Xu, Q., Wu, X., Wan, L., Zhang, Z., Zhang, C., Qin, X., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201694058 · Cited by 99 · see citing works
Self-citationHow Hsp90 and Cdc37 Lubricate Kinase Molecular Switches
Verba, K. A., & Agard, D. A. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.07.002 · Cited by 98 · see citing works
The specificity of JAK3 kinase inhibitors
Changelian, P. S., Moshinsky, D. J., Kuhn, C. F., et al. (2007) · Blood · doi:10.1182/blood-2007-09-115030 · Cited by 95 · see citing works
Zhang, Y., Zhang, J., Liu, C., et al. (2016) · Cancer Letters · doi:10.1016/j.canlet.2016.08.026 · Cited by 95 · see citing works
Ponnusamy, S., Coss, C. C., Thiyagarajan, T., Watts, K., Hwang, D., He, Y., Selth, L. A., McEwan, I. J., Duke, C. B., Pagadala, J., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-0976 · Cited by 95 · see citing works
Dodson, C. A., Kosmopoulou, M. N., Richards, M. W., Atrash, B., Bavetsias, V., Blagg, J., & Bayliss, R. W. (2010) · Biochemical Journal · doi:10.1042/bj20091530 · Cited by 94 · see citing works
C-KIT Signaling in Cancer Treatment
Stankov, K., Popović, S., & Mikov, M. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113199990593 · Cited by 94 · see citing works
Chen, J. J., Tsu, C. A., Gavin, J. M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.279984 · Cited by 93 · see citing works
El‐Ahmad, Y., Tabart, M., Halley, F., Certal, V., Thompson, F., Filoche-Rommé, B., Gruss-Leleu, F., Muller, C., Brollo, M., Fabien, L., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01293 · Cited by 90 · see citing works
Basic Multicolor Flow Cytometry
Maciorowski, Z., Chattopadhyay, P. K., & Jain, P. (2017) · Current Protocols in Immunology · doi:10.1002/cpim.26 · Cited by 87 · see citing works
Liu, J., Zheng, S., Akerstrom, V. L., Yuan, C., Ma, Y., Zhong, Q., Zhang, C., Zhang, Q., Guo, S., Ma, P., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00753 · Cited by 86 · see citing works
Yu, X., Han, Q., Wen, Z., Ma, L., Gao, J., & Zhou, G. (2012) · Cancer Letters · doi:10.1016/j.canlet.2012.03.004 · Cited by 83 · see citing works
The search for ESR1 mutations in breast cancer
Oesterreich, S., & Davidson, N. E. (2013) · Nature Genetics · doi:10.1038/ng.2831 · Cited by 82 · see citing works
LRRK2 Kinase Inhibition as a Therapeutic Strategy for Parkinson's Disease, Where Do We Stand?
Taymans, J., & Greggio, E. (2016) · Current Neuropharmacology · doi:10.2174/1570159x13666151030102847 · Cited by 81 · see citing works
Loddick, S. A., Ross, S. J., Thomason, A. G., Robinson, D. M., Walker, G. E., Dunkley, T. P. J., Brave, S. R., Broadbent, N., Stratton, N. C., Trueman, D., et al. (2013) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-12-1174 · Cited by 79 · see citing works
Kahraman, M., Govek, S. P., Nagasawa, J. Y., Lai, A. G., Bonnefous, C., Douglas, K. L., Sensintaffar, J., Liu, N., Lee, K., Aparicio, A. M., et al. (2018) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.8b00414 · Cited by 78 · see citing works
Discovery of a Potent, Covalent BTK Inhibitor for B-Cell Lymphoma
Wu, H., Wang, W., Liu, F., Weisberg, E., Tian, B., Chen, Y., Li, B., Wang, A., Wang, B., Zhao, Z., et al. (2014) · ACS Chemical Biology · doi:10.1021/cb4008524 · Cited by 76 · see citing works
Self-citationZhou, M., Wu, X., & Ginsberg, H. N. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.40.24769 · Cited by 75 · see citing works
Lobbestael, E., Civiero, L., Wit, T. D., Taymans, J., Greggio, E., & Baekelandt, V. (2016) · Scientific Reports · doi:10.1038/srep33897 · Cited by 73 · see citing works
Hwang, D., He, Y., Ponnusamy, S., Mohler, M. L., Thiyagarajan, T., McEwan, I. J., Narayanan, R., & Miller, D. D. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00973 · Cited by 73 · see citing works
LRRK2 dephosphorylation increases its ubiquitination
Zhao, J., Molitor, T. P., Langston, J. W., & Nichols, R. J. (2015) · Biochemical Journal · doi:10.1042/bj20141305 · Cited by 69 · see citing works
Small-Molecule Kinase Downregulators
Jones, L. H. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.10.011 · Cited by 69 · see citing works
Evolution of Cereblon-Mediated Protein Degradation as a Therapeutic Modality
Chamberlain, P. P., D’Agostino, L. A., Ellis, J. M., Hansen, J. D., Matyskiela, M. E., McDonald, J. J., Riggs, J. R., & Hamann, L. G. (2019) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00425 · Cited by 69 · see citing works
Yan, F., Wang, M., Chen, H., Su, J., Wang, X., Wang, F., Xia, L., & Li, Q. (2010) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2010.11.018 · Cited by 67 · see citing works
Self-citationLi, X., Ba, Q., Liu, Y., et al. (2017) · Cell Discovery · doi:10.1038/celldisc.2017.42 · Cited by 64 · see citing works
Fanning, S. W., Hodges-Gallagher, L., Myles, D. C., Sun, R., Fowler, C. E., Plant, I. N., Green, B. D., Harmon, C. L., Greene, G. L., & Kushner, P. J. (2018) · Nature Communications · doi:10.1038/s41467-018-04413-3 · Cited by 64 · see citing works
Wang, M., Shen, A., Zhang, C., Song, Z., Ai, J., Liu, H., Sun, L., Ding, J., Geng, M., & Zhang, A. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01106 · Cited by 62 · see citing works
Bradbury, R. H., Acton, D. G., Broadbent, N., Brooks, A. N., Carr, G. R., Hatter, G., Hayter, B. R., Hill, K. J., Howe, N. J., Jones, R. D. O., et al. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.02.056 · Cited by 56 · see citing works
Vancraenenbroeck, R., Raeymaecker, J. D., Lobbestael, E., et al. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00051 · Cited by 56 · see citing works
A Biologist's Field Guide to Multiplexed Quantitative Proteomics
Bakalarski, C. E., & Kirkpatrick, D. S. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o115.056986 · Cited by 56 · see citing works
Bryant, C., Scriven, K., & Massey, A. J. (2014) · Molecular Cancer · doi:10.1186/1476-4598-13-147 · Cited by 54 · see citing works
Johnson, C. N., Ahn, J. S., Buck, I. M., Chiarparin, E., Day, J. E. H., Hopkins, A., Howard, S., Lewis, E. J., Martins, V., Millemaggi, A., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00900 · Cited by 53 · see citing works
Nonradioactive quantification of autophagic protein degradation with L-azidohomoalanine labeling
Wang, J., Zhang, J., Lee, Y. M., Ng, S., Shi, Y. P., Hua, Z., Lin, Q., & Shen, H. (2017) · Nature Protocols · doi:10.1038/nprot.2016.160 · Cited by 52 · see citing works
Quantitative analysis of newly synthesized proteins
Ma, Y., McClatchy, D. B., Barkallah, S., Wood, W. W., & Yates, J. R. (2018) · Nature Protocols · doi:10.1038/s41596-018-0012-y · Cited by 51 · see citing works
Bachman, A. B., Keramisanou, D., Xu, W., Beebe, K. E., Moses, M. A., Kumar, M. V. V., Gray, G., Noor, R. E., van der Vaart, A., Neckers, L., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02711-w · Cited by 50 · see citing works
MYC is a critical target of FBXW7
Sato, M., Barrueco, R. R., Yu, J., Do, C., Silva, J. M., & Gautier, J. (2014) · Oncotarget · doi:10.18632/oncotarget.3203 · Cited by 49 · see citing works
Bradbury, R. H., Hales, N. J., Rabow, A. A., Walker, G. E., Acton, D. G., Andrews, D. M., Ballard, P. G., Brooks, N. A. N., Colclough, N., Girdwood, A., et al. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.06.122 · Cited by 47 · see citing works
Burks, H. E., Abrams, T. J., Kirby, C. A., Baird, J., Fekete, A., Hamann, L. G., Kim, S., Lombardo, F., Loo, A. T., Lubicka, D., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01468 · Cited by 47 · see citing works
Phosphorylation of LRRK2: from kinase to substrate
Lobbestael, E., Baekelandt, V., & Taymans, J. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120128 · Cited by 45 · see citing works
Identification of novel,in vivoactive Chk1 inhibitors utilizing structure guided drug design
Massey, A. J., Stokes, S. P., Browne, H. L., Foloppe, N., Fiumana, A., Scrace, S., Fallowfield, M., Bedford, S. T., Webb, P., Baker, L. M., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.5929 · Cited by 45 · see citing works
Nagasawa, J. Y., Govek, S. P., Kahraman, M., Lai, A. G., Bonnefous, C., Douglas, K. L., Sensintaffar, J., Lu, N., Lee, K., Aparicio, A. M., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00921 · Cited by 44 · see citing works
Tricyclic Indazoles—A Novel Class of Selective Estrogen Receptor Degrader Antagonists
Scott, J. S., Bailey, A., Buttar, D., Carbajo, R. J., Curwen, J., Davey, P. R. J., Davies, R. D. M., Degorce, S. L., Donald, C. S., Gangl, E. T., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01837 · Cited by 41 · see citing works
Insights into MAPK p38α DFG flip mechanism by accelerated molecular dynamics
Filomia, F., Rienzo, F. D., & Menziani, M. C. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.07.047 · Cited by 39 · see citing works
High-throughput flow cytometry for drug discovery: principles, applications, and case studies
Ding, M., Kaspersson, K., Murray, D., & Bardelle, C. (2017) · Drug Discovery Today · doi:10.1016/j.drudis.2017.09.005 · Cited by 38 · see citing works
Teramura, Y., Asif, S., Ekdahl, K. N., et al. (2016) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b14584 · Cited by 36 · see citing works
Ma, Y., & Yates, J. R. (2018) · Expert Review of Proteomics · doi:10.1080/14789450.2018.1500902 · Cited by 36 · see citing works
Cellular screening assays using fluorescence microscopy
Blake, R. (2001) · Current Opinion in Pharmacology · doi:10.1016/s1471-4892(01)00092-3 · Cited by 35 · see citing works
Self-citationBate-Eya, L. T., Gierman, H. J., Ebus, M. E., Köster, J., Caron, H. N., Versteeg, R., Dolman, M. E. M., & Molenaar, J. J. (2017) · European Journal of Cancer · doi:10.1016/j.ejca.2016.12.019 · Cited by 35 · see citing works
Min, J., Guillen, V. S., Sharma, A., Zhao, Y., Ziegler, Y., Gong, P., Mayne, C. G., Srinivasan, S., Kim, S. H., Carlson, K. E., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00585 · Cited by 35 · see citing works
Kato, K., Hamaguchi, Y., OKAWA, S., Ishikawa, E., Kobayashi, K., & Katunuma, N. (1977) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a131678 · Cited by 34 · see citing works
Cellular and lysosomal uptake of methylamine in isolated rat hepatocytes
Solheim, A. E., & Seglen, P. O. (1983) · Biochemical Journal · doi:10.1042/bj2100929 · Cited by 33 · see citing works
High-Content Analysis in Preclinical Drug Discovery
Denner, P., Schmalowsky, J., & Prechtl, S. (2008) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/138620708783877780 · Cited by 33 · see citing works
Synthetic study of peptide aldehydes.
Itô, A., Takahashi, R., MIURA, C., et al. (1975) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.23.3106 · Cited by 32 · see citing works
Hong, R., Edgar, K. A., Song, K., Steven, S., Young, A. E., Hamilton, P., Arrazate, A., de la Cruz, C., Chan, C., Pang, J., et al. (2018) · Cancer Research · doi:10.1158/1538-7445.sabcs17-pd4-14 · Cited by 27 · see citing works
Self-citationImmunodetection of Proteins by Western Blotting
Henderson, C. J., & Wolf, C. R. (2003) · Humana Press eBooks · doi:10.1385/0-89603-204-3:221 · Cited by 26 · see citing works
Purushottamachar, P., Kwegyir‐Afful, A. K., Martin, M. S., et al. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.6b00137 · Cited by 25 · see citing works
Tyrosine Kinase Inhibitors Induce Down-Regulation of c-Kit by Targeting the ATP Pocket
d’Allard, D., Gay, J., Descarpentries, C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060961 · Cited by 23 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Targeted protein degradation via intramolecular bivalent glues
Hsia, O., Hinterndorfer, M., Cowan, A. D., Iso, K., Ishida, T., Sundaramoorthy, R., Nakasone, M. A., Imrichova, H., Schätz, C., Rukavina, A., et al. (2024) · Nature · doi:10.1038/s41586-024-07089-6 · Cited by 222 · see citing works
Chasing molecular glue degraders: screening approaches
Domostegui, A., Nieto-Barrado, L., Perez-Lopez, C., & Mayor-Ruiz, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00197g · Cited by 200 · 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
Haven't got a glue: Protein surface variation for the design of molecular glue degraders
Kozicka, Z., & Thomä, N. H. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2021.04.009 · Cited by 170 · see citing works
Progress and Challenges in Targeted Protein Degradation for Neurodegenerative Disease Therapy
Fang, Y., Wang, J., Zhao, M., Zheng, Q., Ren, C., Wang, Y., & Zhang, J. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00844 · Cited by 100 · see citing works
Development of PDE6D and CK1α Degraders through Chemical Derivatization of FPFT-2216
Teng, M., Lu, W., Donovan, K. A., Sun, J., Krupnick, N. M., Nowak, R. P., Li, Y.-D., Sperling, A. S., Zhang, T., Ebert, B. L., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01832 · Cited by 63 · see citing works
Prospecting for molecular glues
den Besten, W., & Lipford, J. R. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0620-z · Cited by 55 · see citing works
Improved Proteomics-Based Drug Mechanism-of-Action Studies Using 16-Plex Isobaric Mass Tags
Zinn, N., Werner, T., Doce, C., Mathieson, T., Boecker, C., Sweetman, G., Fufezan, C., & Bantscheff, M. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00900 · Cited by 49 · see citing works
Unifying Catalysis Framework to Dissect Proteasomal Degradation Paradigms
Rodriguez-Rivera, F. P., & Levi, S. M. (2021) · ACS Central Science · doi:10.1021/acscentsci.1c00389 · Cited by 30 · see citing works
- Authors
- Hanan, E. J., Liang, J., Wang, X., Blake, R. A., Blaquiere, N., & Staben, S. T.
- Affiliations
- Genentech (US)
- Genentech, Inc. , , 1 DNA Way , , ,
- Corresponding author
- Staben, Steven T.
- Venue
- Journal of Medicinal Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2020-04-30
- Volume
- 63
- Issue
- 20
- Pages
- 11330-11361
- ISSN
- 0022-2623 (ISSN-L)
- 1520-4804
- OpenAlex
- W3023538604
- Cited by
- 69
- References
- 218
- Citations by year
- 2026: 6 · 2025: 6 · 2024: 8 · 2023: 13 · 2022: 13 · 2021: 13 · 2020: 8
- FWCI
- 1.20
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Journal of Medicinal Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- targeted protein degradation, duration of action
- MeSH terms
- Binding Sites, Humans, Protein Binding, Proteins, Molecular Structure, Ubiquitin-Protein Ligases, Cell Line, Tumor, Small Molecule Libraries, Drug Discovery, Proteolysis
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review