IFITM proteins assist cellular uptake of diverse linked chemotypes
Open accessAbstract
The search for cell-permeable drugs has conventionally focused on low-molecular weight (MW), nonpolar, rigid chemical structures. However, emerging therapeutic strategies break traditional drug design rules by employing flexibly linked chemical entities composed of more than one ligand. Using complementary genome-scale chemical-genetic approaches we identified an endogenous chemical uptake pathway involving interferon-induced transmembrane proteins (IFITMs) that modulates the cell permeability of a prototypical biopic inhibitor of MTOR (RapaLink-1, MW: 1784 g/mol). We devised additional linked inhibitors targeting BCR-ABL1 (DasatiLink-1, MW: 1518 g/mol) and EIF4A1 (BisRoc-1, MW: 1466 g/mol), uptake of which was facilitated by IFITMs. We also found that IFITMs moderately assisted some proteolysis-targeting chimeras and examined the physicochemical requirements for involvement of this uptake pathway.
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CRISPRi experiments in other cancer cell types (AML, CML, pancreatic cancer and lung cancer cell lines) demonstrated that, unlike PSMA1, PTGES3 is not an essential gene upon knockdown.
“Furthermore, CRISPRi experiments in other cancer cell types (AML, CML, pancreatic cancer and lung cancer cell lines54–56) demonstrated that, unlike PSMA1, which is a positive control commonly essential gene, PTGES3 is not an essential gene upon knockdown (Extended Data Fig. 10d–g).”
From Genome-scale CRISPR screens identify PTGES3 as a direct modulator of androgen receptor function in advanced prostate cancer (2025) · cites this paper as [55]
The section on complementary genome-scale chemical-genetic approaches reports CRISPRi experiments in K562 chronic myeloid leukemia cells, supporting the CML portion of the cited cell-line description (page unavailable). It does not report PTGES3 or PSMA1 knockdown essentiality, or CRISPRi experiments in the other cancer cell types named in the claim. (LLM, conf=0.83)
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Wickham, H., Averick, M., Bryan, J., Chang, W., McGowan, L., François, R., Grolemund, G., Hayes, A., Henry, L., Hester, J., et al. (2019) · Journal of Open Source Software · doi:10.21105/joss.01686 · Cited by 22,138 · see citing works
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
Lipinski, C. A., Lombardo, F., Dominy, B. W., & Feeney, P. J. (1997) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(96)00423-1 · Cited by 11,484 · see citing works
Protein Identification and Analysis Tools on the ExPASy Server
Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M. R., Appel, R. D., & Bairoch, A. (2005) · Humana Press eBooks · doi:10.1385/1-59259-890-0:571 · Cited by 10,133 · see citing works
Molecular properties that influence the oral bioavailability of drug candidates
Veber, D. F., Johnson, S. R., Cheng, H.-Y., Smith, B. R., Ward, K. W., & Kopple, K. D. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm020017n · Cited by 8,420 · see citing works
PROTAC targeted protein degraders: the past is prologue
Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395 · see citing works
Next-generation characterization of the Cancer Cell Line Encyclopedia
Ghandi, M., Huang, F. W., Jané-Valbuena, J., Kryukov, G. V., Lo, C. C., McDonald, E. R., Barretina, J., Gelfand, E. T., Bielski, C. M., Li, H., et al. (2019) · Nature · doi:10.1038/s41586-019-1186-3 · Cited by 3,394 · see citing works
Ghose, A. K., Viswanadhan, V. N., & Wendoloski, J. J. (1998) · Journal of Combinatorial Chemistry · doi:10.1021/cc9800071 · Cited by 3,095 · see citing works
Cellular uptake of the tat protein from human immunodeficiency virus
Frankel, A. D., & Pabo, C. O. (1988) · Cell · doi:10.1016/0092-8674(88)90263-2 · Cited by 2,782 · see citing works
mTOR at the nexus of nutrition, growth, ageing and disease
Liu, G. Y., & Sabatini, D. M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0199-y · Cited by 2,737 · see citing works
Genome-Scale CRISPR-Mediated Control of Gene Repression and Activation
Gilbert, L. A., Horlbeck, M. A., Adamson, B., Villalta, J. E., Chen, Y., Whitehead, E. H., Guimaraes, C., Panning, B., Ploegh, H. L., Bassik, M. C., et al. (2014) · Cell · doi:10.1016/j.cell.2014.09.029 · Cited by 2,728 · see citing works
Self-citationSakamoto, 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
Systematic identification of genomic markers of drug sensitivity in cancer cells
Garnett, M. J., Edelman, E. J., Heidorn, S. J., Greenman, C. D., Dastur, A., Lau, K. W., Greninger, P., Thompson, I. R., Luo, X., Soares, J., et al. (2012) · Nature · doi:10.1038/nature11005 · Cited by 2,456 · see citing works
Self-citationA Landscape of Pharmacogenomic Interactions in Cancer
Iorio, F., Knijnenburg, T. A., Vis, D. J., Bignell, G. R., Menden, M. P., Schubert, M., Aben, N., Gonçalves, E., Barthorpe, S., Lightfoot, H., et al. (2016) · Cell · doi:10.1016/j.cell.2016.06.017 · Cited by 2,090 · see citing works
Self-citationA small molecule–kinase interaction map for clinical kinase inhibitors
Fabian, M. A., Biggs, W., Treiber, D. K., Atteridge, C. E., Azimioara, M. D., Benedetti, M. G., Carter, T. A., Ciceri, P., Edeen, P. T., Floyd, M. B., et al. (2005) · Nature Biotechnology · doi:10.1038/nbt1068 · Cited by 1,901 · see citing works
Structural Mechanism for STI-571 Inhibition of Abelson Tyrosine Kinase
Schindler, T. H., Bornmann, W. G., Pellicena, P., Miller, W. T., Clarkson, B., & Kuriyan, J. (2000) · Science · doi:10.1126/science.289.5486.1938 · Cited by 1,785 · see citing works
Green, M., & Loewenstein, P. M. (1988) · Cell · doi:10.1016/0092-8674(88)90262-0 · Cited by 1,551 · see citing works
Inducible Apoptosis as a Safety Switch for Adoptive Cell Therapy
Di Stasi, A., Tey, S.-K., Dotti, G., Fujita, Y., Kennedy-Nasser, A., Martinez, C., Straathof, K., Liu, E., Durett, A. G., Grilley, B., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1106152 · Cited by 1,512 · see citing works
Brass, A., Huang, I.-C., Benita, Y., John, S., Krishnan, M. N., Feeley, E., Ryan, B., Weyer, J., van der Weyden, L., Fikrig, E., et al. (2009) · Cell · doi:10.1016/j.cell.2009.12.017 · Cited by 1,292 · see citing works
Activity-Based Protein Profiling: From Enzyme Chemistry to Proteomic Chemistry
Cravatt, B. F., Wright, A. T., & Kozarich, J. W. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.124125 · Cited by 1,270 · see citing works
Adamson, B., Norman, T. M., Jost, M., Cho, M. Y., Nuñez, J. K., Chen, Y., Villalta, J. E., Gilbert, L. A., Horlbeck, M. A., Hein, M. Y., et al. (2016) · Cell · doi:10.1016/j.cell.2016.11.048 · Cited by 1,193 · see citing works
Self-citationDobson, C. M. (2004) · Nature · doi:10.1038/nature03192 · Cited by 1,003 · see citing works
Horlbeck, M. A., Gilbert, L. A., Villalta, J. E., Adamson, B., Pak, R. A., Chen, Y., Fields, A. P., Park, C. Y., Corn, J. E., Kampmann, M., et al. (2016) · eLife · doi:10.7554/elife.19760 · Cited by 894 · see citing works
Self-citationCorrelating chemical sensitivity and basal gene expression reveals mechanism of action
Rees, M. G., Seashore-Ludlow, B. A., Cheah, J. H., Adams, D., Price, E. V., Gill, S., Javaid, S., Coletti, M. E., Jones, V., Bodycombe, N. E., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1986 · Cited by 874 · see citing works
Controlling Signal Transduction with Synthetic Ligands
Spencer, D. M., Wandless, T. J., Schreiber, S. L., & Crabtree, G. R. (1993) · Science · doi:10.1126/science.7694365 · Cited by 845 · see citing works
Oral Druggable Space beyond the Rule of 5: Insights from Drugs and Clinical Candidates
Doak, B. C., Over, B., Giordanetto, F., & Kihlberg, J. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.08.013 · Cited by 835 · cited 1× · see citing works
“…molecular weight therapeutics such as natural products and synthetic macrocycles often comprise highly tailored arrangements of polar/non-polar functionality that allow switching between membrane-favored and aqueous-favored conformations to enable passive permeability through membranes (12).”
The Molecular Genetics of Philadelphia Chromosome–Positive Leukemias
Epstein, F. H., Kurzrock, R., Gutterman, J. U., & Talpaz, M. (1988) · New England Journal of Medicine · doi:10.1056/nejm198810133191506 · Cited by 833 · see citing works
The allosteric inhibitor ABL001 enables dual targeting of BCR–ABL1
Wylie, A. A., Schoepfer, J. G., Jahnke, W., Cowan‐Jacob, S. W., Loo, A. T., Furet, P., Marzinzik, A. L., Pellé, X., Donovan, J., Zhu, W. S., et al. (2017) · Nature · doi:10.1038/nature21702 · Cited by 622 · see citing works
Targeting Bcr–Abl by combining allosteric with ATP-binding-site inhibitors
Zhang, J., Adrián, F., Jahnke, W., Cowan‐Jacob, S. W., Li, A. G., Iacob, R. E., Sim, T., Powers, J. T., Dierks, C., Sun, F., et al. (2010) · Nature · doi:10.1038/nature08675 · Cited by 603 · see citing works
Response and Resistance to BCR-ABL1-Targeted Therapies
Braun, T. P., Eide, C. A., & Druker, B. J. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.03.006 · Cited by 488 · see citing works
Overcoming mTOR resistance mutations with a new-generation mTOR inhibitor
Rodrik-Outmezguine, V. S., Okaniwa, M., Yao, Z., Novotny, C. J., McWhirter, C., Banaji, A., Won, H., Wong, W., Berger, M., de Stanchina, E., et al. (2016) · Nature · doi:10.1038/nature17963 · Cited by 479 · see citing works
Self-citationIFITM-Family Proteins: The Cell's First Line of Antiviral Defense
Bailey, C. C., Zhong, G., Huang, I., & Farzan, M. (2014) · Annual Review of Virology · doi:10.1146/annurev-virology-031413-085537 · Cited by 470 · see citing works
Chemical genetics: ligand-based discovery of gene function
Stockwell, B. R. (2000) · Nature Reviews Genetics · doi:10.1038/35038557 · Cited by 418 · see citing works
Das, J., Chen, P., Norris, D. J., Padmanabha, R., Lin, J., Moquin, R. V., Shen, Z., Cook, L. S., Doweyko, A. M., Pitt, S., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060727j · Cited by 399 · see citing works
Broad-Spectrum Kinase Profiling in Live Cells with Lysine-Targeted Sulfonyl Fluoride Probes
Zhao, Q., Ouyang, X., Wan, X., Gajiwala, K. S., Kath, J. C., Jones, L. H., Burlingame, A. L., & Taunton, J. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.6b08536 · Cited by 388 · see citing works
Self-citationIFITM Proteins Restrict Viral Membrane Hemifusion
Li, K., Markosyan, R. M., Zheng, Y.-M., Golfetto, O., Bungart, B. L., Li, M., Ding, S., He, Y., Liang, C., Lee, J. C., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003124 · Cited by 358 · see citing works
Deubiquitinase-targeting chimeras for targeted protein stabilization
Henning, N. J., Boike, L., Spradlin, J. N., Ward, C. C., Liu, G., Zhang, E., Belcher, B. P., Brittain, S. M., Hesse, M. J., Dovala, D., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-00971-2 · Cited by 344 · see citing works
Cell Penetrating Peptides in Drug Delivery
Snyder, E. L., & Dowdy, S. F. (2004) · Pharmaceutical Research · doi:10.1023/b:pham.0000019289.61978.f5 · Cited by 324 · see citing works
Rocaglates convert DEAD-box protein eIF4A into a sequence-selective translational repressor
Iwasaki, S., Floor, S. N., & Ingolia, N. T. (2016) · Nature · doi:10.1038/nature17978 · Cited by 304 · see citing works
Jost, M., Chen, Y., Gilbert, L. A., Horlbeck, M. A., Krenning, L., Menchon, G., Rai, A., Cho, M. Y., Stern, J. J., Prota, A. E., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.09.012 · Cited by 241 · see citing works
Self-citationIFITM3 directly engages and shuttles incoming virus particles to lysosomes
Spence, J. S., He, R., Hoffmann, H.-H., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0213-2 · Cited by 225 · see citing works
High yield bacterial expression of active c‐Abl and c‐Src tyrosine kinases
Seeliger, M. A., Young, M. A., Henderson, M. N., Pellicena, P., King, D., Falick, A. M., & Kuriyan, J. (2005) · Protein Science · doi:10.1110/ps.051750905 · Cited by 220 · see citing works
Self-citationVajpai, N., Strauss, A., Fendrich, G., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801337200 · Cited by 212 · see citing works
Small Molecule Targeted Recruitment of a Nuclease to RNA
Costales, M. G., Matsumoto, Y., Velagapudi, S. P., & Disney, M. D. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b01233 · Cited by 212 · see citing works
Solution Conformations Shed Light on PROTAC Cell Permeability
Atilaw, Y., Poongavanam, V., Svensson Nilsson, C., Nguyen, D., Giese, A., Meibom, D., Erdelyi, M., & Kihlberg, J. (2021) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00556 · Cited by 208 · see citing works
PKIDB: A Curated, Annotated and Updated Database of Protein Kinase Inhibitors in Clinical Trials
Carles, F., Bourg, S., Meyer, C., & Bonnet, P. (2018) · Molecules · doi:10.3390/molecules23040908 · Cited by 202 · see citing works
Phosphorylation-Inducing Chimeric Small Molecules
Siriwardena, S. U., Godage, D. N. P. M., Shoba, V. M., Lai, S., Shi, M., Wu, P., Chaudhary, S. K., Schreiber, S. L., & Choudhary, A. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c05537 · Cited by 196 · see citing works
The Translation Inhibitor Rocaglamide Targets a Bimolecular Cavity between eIF4A and Polypurine RNA
Iwasaki, S., Iwasaki, W., Takahashi, M., Sakamoto, A., Watanabe, C., Shichino, Y., Floor, S. N., Fujiwara, K., Mito, M., Dodo, K., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.11.026 · Cited by 193 · see citing works
Interferon induction of IFITM proteins promotes infection by human coronavirus OC43
Zhao, X., Guo, F., Liu, F., Cuconati, A., Chang, J., Block, T. M., & Guo, J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1320856111 · Cited by 192 · see citing works
http://Mcule.com: a public web service for drug discovery
Kiss, R., Sándor, M., & Szalai, F. A. (2012) · Journal of Cheminformatics · doi:10.1186/1758-2946-4-s1-p17 · Cited by 187 · see citing works
A Kinase Inhibitor Targeted to mTORC1 Drives Regression in Glioblastoma
Fan, Q.-W., Aksoy, O., Wong, R. A., Ilkhanizadeh, S., Novotny, C. J., Gustafson, W. C., Truong, A. Y.-Q., Cayanan, G., Simonds, E. F., Haas-Kogan, D. A., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.01.014 · Cited by 184 · see citing works
Self-citationFundamental aspects of DMPK optimization of targeted protein degraders
Cantrill, C., Chaturvedi, P., Rynn, C., Schaffland, J. P., Walter, I., & Wittwer, M. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.03.012 · Cited by 169 · see citing works
IFITM proteins inhibit placental syncytiotrophoblast formation and promote fetal demise
Buchrieser, J., Degrelle, S. A., Couderc, T., Nevers, Q., Disson, O., Manet, C., Donahue, D. A., Porrot, F., Hillion, K.-H., Perthame, É., et al. (2019) · Science · doi:10.1126/science.aaw7733 · Cited by 161 · see citing works
Understanding and Improving the Membrane Permeability of VH032-Based PROTACs
Klein, V. G., Townsend, C. E., Testa, A., Zengerle, M., Maniaci, C., Hughes, S. J., Chan, K.-H., Ciulli, A., & Lokey, R. S. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00265 · Cited by 153 · see citing works
IFITM Genes, Variants, and Their Roles in the Control and Pathogenesis of Viral Infections
Zhao, X., Li, J., Winkler, C. A., An, P., & Guo, J. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.03228 · Cited by 151 · see citing works
Synthetic transcription elongation factors license transcription across repressive chromatin
Erwin, G. S., Grieshop, M. P., Ali, A., Qi, J., Lawlor, M. A., Kumar, D., Ahmad, I., McNally, A. G., Teider, N., Worringer, K. A., et al. (2017) · Science · doi:10.1126/science.aan6414 · Cited by 140 · see citing works
Condon, K. J., Orozco, J. M., Adelmann, C. H., Spinelli, J. B., van der Helm, P. W., Roberts, J. M., Kunchok, T., & Sabatini, D. M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2022120118 · Cited by 132 · see citing works
Erez, M., Takemori, A. E., & Portoghese, P. S. (1982) · Journal of Medicinal Chemistry · doi:10.1021/jm00349a016 · Cited by 126 · see citing works
Shi, G., Schwartz, O., & Compton, A. A. (2017) · Retrovirology · doi:10.1186/s12977-017-0377-y · Cited by 109 · see citing works
IFITM3 functions as a PIP3 scaffold to amplify PI3K signalling in B cells
Lee, J. W., Robinson, M. E., Ma, N., Artadji, D., Ahmed, M. A. H., Xiao, G., Sadras, T., Deb, G., Winchester, J., Cosgun, K. N., et al. (2020) · Nature · doi:10.1038/s41586-020-2884-6 · Cited by 109 · see citing works
Brain-restricted mTOR inhibition with binary pharmacology
Zhang, Z., Fan, Q.-W., Luo, X., Lou, K., Weiss, W. A., & Shokat, K. M. (2022) · Nature · doi:10.1038/s41586-022-05213-y · Cited by 98 · see citing works
Self-citationEvolutionary Dynamics of the Interferon-Induced Transmembrane Gene Family in Vertebrates
Zhang, Z., Liu, J., Li, M., Yang, H., & Zhang, C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049265 · Cited by 92 · see citing works
Self-citationFoley, C. A., Potjewyd, F., Lamb, K. N., James, L. I., & Frye, S. V. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.9b00972 · Cited by 89 · see citing works
CRISPR Approaches to Small Molecule Target Identification
Jost, M., & Weissman, J. S. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.7b00965 · Cited by 88 · see citing works
Selective inhibitors of mTORC1 activate 4EBP1 and suppress tumor growth
Lee, B. J., Boyer, J. A., Burnett, G. L., Thottumkara, A. P., Tibrewal, N., Wilson, S. L., Hsieh, T., Marquez, A., Lorenzana, E. G., Evans, J., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00813-7 · Cited by 85 · see citing works
Systematic Investigation of the Permeability of Androgen Receptor PROTACs
Scott, D. E., Rooney, T. P. C., Bayle, E. D., Mirza, T., Willems, H. M. G., Clarke, J. H., Andrews, S. P., & Skidmore, J. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00194 · Cited by 79 · see citing works
Allosteric Interactions between the Myristate- and ATP-Site of the Abl Kinase
Iacob, R. E., Zhang, J., Gray, N. S., & Engen, J. R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0015929 · Cited by 73 · see citing works
Bivalent inhibitors of protein kinases
Gower, C. M., Chang, M. E. K., & Maly, D. J. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.875513 · Cited by 72 · see citing works
Degraders early developability assessment: face-to-face with molecular properties
Ermondi, G., Vallaro, M., & Caron, G. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.06.015 · Cited by 40 · see citing works
S ‑Palmitoylation and Sterol Interactions Mediate Antiviral Specificity of IFITMs
Das, T., Yang, X., Lee, H.-Y., Garst, E. H., Valencia, E., Chandran, K., Im, W., & Hang, H. C. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00176 · Cited by 37 · see citing works
Backbone NMR resonance assignment of the Abelson kinase domain in complex with imatinib
Vajpai, N., Strauss, A., Fendrich, G., Cowan‐Jacob, S. W., Manley, P. W., Jahnke, W., & Grzesiek, S. (2008) · Biomolecular NMR Assignments · doi:10.1007/s12104-008-9079-7 · Cited by 36 · see citing works
Li, P., Shi, M., Shen, W., Zhang, Z., Xie, D., Zhang, X.-Y., He, C., Zhang, Y., & Zhao, Z. (2017) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2017.05.003 · Cited by 17 · see citing works
Self-citationGenome-Scale Perturbation of Long Noncoding RNA Expression Using CRISPR Interference
Liu, S. J., Horlbeck, M. A., Weissman, J. S., & Lim, D. A. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-1158-6_20 · Cited by 10 · see citing works
Dezan, E., van Stiphout, R., Gapp, B. V., Blomen, V., Brummelkamp, T., & Nijman, S. (2020) · Science Signaling · doi:10.1126/scisignal.aba5665 · Cited by 9 · see citing works
Burris, H. A., Ulahannan, S. V., Haura, E. B., Ou, S. I., Capasso, A., Münster, P. N., Kitai, H., Wang, Z., Hayes, J. L., Lin, T., et al. (2022) · Journal of Clinical Oncology · doi:10.1200/jco.2022.40.16_suppl.3098 · Cited by 7 · see citing works
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- Authors
- Lou, K., Wassarman, D. R., Yang, T., Paung, Y., Zhang, Z., O’Loughlin, T. A., Moore, M. K., Egan, R. K., Greninger, P., Benes, C. H., Seeliger, M. A., Taunton, J., Gilbert, L. A., & Shokat, K. M.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of California, San Francisco (US)
- Stony Brook University (US)
- Massachusetts General Hospital (US)
- Harvard University (US)
- Corresponding author
- Gilbert, Luke A.
- Shokat, Kevan M.
- ORCID
- Venue
- Science
- Published
- 2022-12-09
- Volume
- 378
- Issue
- 6624
- Pages
- 1097-1104
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC9924227
- OpenAlex
- W4311883476
- Cited by
- 42
- References
- 75
- Citations by year
- 2026: 12 · 2025: 14 · 2024: 6 · 2023: 9 · 2022: 1
- FWCI
- 3.14
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- Science (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion, cc-by)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- Funders
- Howard Hughes Medical Institute
- Wellcome Trust (102696)
- National Institutes of Health (5f31ca243439-02, 1s10od028478-01, 1s10od028511-01)
- National Cancer Institute (R01CA221969, DP2CA239597, F30CA239476, F31-CA243439, R01CA244550)
- National Institute of General Medical Sciences (R35GM119437, T32GM145460)
- National Institute of Allergy and Infectious Diseases (U19AI171110)
- Topics
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- interferon-induced transmembrane proteins, membrane permeability, mTOR inhibitors, BCR-ABL1 inhibitor, PROTACs, high molecular weight drugs, drug delivery
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 ›
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