Kinase-mediated RAS signaling via membraneless cytoplasmic protein granules
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Abstract
Receptor tyrosine kinase (RTK)-mediated activation of downstream effector pathways such as the RAS GTPase/MAP kinase (MAPK) signaling cascade is thought to occur exclusively from lipid membrane compartments in mammalian cells. Here, we uncover a membraneless, protein granule-based subcellular structure that can organize RTK/RAS/MAPK signaling in cancer. Chimeric (fusion) oncoproteins involving certain RTKs including ALK and RET undergo de novo higher-order assembly into membraneless cytoplasmic protein granules that actively signal. These pathogenic biomolecular condensates locally concentrate the RAS activating complex GRB2/SOS1 and activate RAS in a lipid membrane-independent manner. RTK protein granule formation is critical for oncogenic RAS/MAPK signaling output in these cells. We identify a set of protein granule components and establish structural rules that define the formation of membraneless protein granules by RTK oncoproteins. Our findings reveal membraneless, higher-order cytoplasmic protein assembly as a distinct subcellular platform for organizing oncogenic RTK and RAS signaling.
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The intracellular EML4-ALK fusion protein recruits RTK adaptor proteins, resulting in the elicitation of cytoplasmic KRAS localization.
“Related to this, the intracellular EML4-ALK fusion protein has been shown to recruit RTK adaptor proteins, resulting in the elicitation of cytoplasmic KRAS localization47.”
From Mechanisms of KRAS inhibitor resistance in KRAS-mutant colorectal cancer harboring Her2 amplification and aberrant KRAS localization (2025) · cites this paper as [47]
The Results section on GRB2/SOS1/GAB1 recruitment reports that EML4-ALK granules recruit RTK adaptor proteins. The Results section on local RAS activation reports activation of a cytosolic KRAS mutant and enrichment of a RAS-GTP reporter at the granules, but it describes a pre-existing cytosolic RAS pool—not EML4-ALK causing KRAS to relocate to the cytoplasm. Page numbers are not available in our copy. (LLM, conf=0.87)
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Cites
NIH Image to ImageJ: 25 years of image analysis
Schneider, C. A., Rasband, W. S., & Eliceiri, K. W. (2012) · Nature Methods · doi:10.1038/nmeth.2089 · Cited by 64,638 · see citing works
Cell Signaling by Receptor Tyrosine Kinases
Lemmon, M. A., & Schlessinger, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.011 · Cited by 7,929 · see citing works
Biomolecular condensates: organizers of cellular biochemistry
Banani, S. F., Lee, H. O., Hyman, A., & Rosen, M. (2017) · Nature reviews. Molecular cell biology · doi:10.1038/nrm.2017.7 · Cited by 5,574 · see citing works
Identification of the transforming EML4–ALK fusion gene in non-small-cell lung cancer
Soda, M., Choi, Y. L., Enomoto, M., Takada, S., Yamashita, Y., Ishikawa, S., Fujiwara, S.-I., Watanabe, H., Kurashina, K., Hatanaka, H., et al. (2007) · Nature · doi:10.1038/nature05945 · Cited by 5,439 · see citing works
Liquid phase condensation in cell physiology and disease
Shin, Y., & Brangwynne, C. P. (2017) · Science · doi:10.1126/science.aaf4382 · Cited by 4,184 · see citing works
Oncogenic Signaling Pathways in The Cancer Genome Atlas
Sanchez-Vega, F., Mina, M., Armenia, J., Chatila, W. K., Luna, A., La, K. C., Dimitriadoy, S., Liu, D. L., Kantheti, H. S., Saghafinia, S., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.035 · Cited by 3,201 · see citing works
Self-citationA Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927 · see citing works
Alberti, S., Gladfelter, A., & Mittag, T. (2019) · Cell · doi:10.1016/j.cell.2018.12.035 · Cited by 2,856 · see citing works
Molliex, A., Temirov, J. P., Lee, J., Coughlin, M., Kanagaraj, A., Kim, H. J., Mittag, T., & Taylor, J. P. (2015) · Cell · doi:10.1016/j.cell.2015.09.015 · Cited by 2,658 · see citing works
Advanced methods of microscope control using μManager software
Edelstein, A., Tsuchida, M. A., Amodaj, N., Pinkard, H., Vale, R. D., & Stuurman, N. (2014) · Journal of Biological Methods · doi:10.14440/jbm.2014.36 · Cited by 1,927 · see citing works
Erlotinib in Lung Cancer — Molecular and Clinical Predictors of Outcome
Tsao, M., Sakurada, A., Cutz, J.-C., Zhu, C., Kamel‐Reid, S., Squire, J. A., Lorimer, I. A. J., Zhang, T., Liu, G., Daneshmand, M., et al. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa050736 · Cited by 1,815 · see citing works
Computer Control of Microscopes Using µManager
Edelstein, A., Amodaj, N., Hoover, K., Vale, R. D., & Stuurman, N. (2010) · Current Protocols in Molecular Biology · doi:10.1002/0471142727.mb1420s92 · Cited by 1,678 · see citing works
The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
Lowenstein, E. J., Daly, R. J., Batzer, A., Li, W., Margolis, B. L., Lammers, R., Ullrich, A., Skolnik, E. Y., Bar‐Sagi, D., & Schlessinger, J. (1992) · Cell · doi:10.1016/0092-8674(92)90167-b · Cited by 1,632 · see citing works
ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure
Jain, S., Wheeler, J., Walters, R. W., Agrawal, A., Barsic, A. J., & Parker, R. (2016) · Cell · doi:10.1016/j.cell.2015.12.038 · Cited by 1,597 · see citing works
Phase separation of signaling molecules promotes T cell receptor signal transduction
Su, X., Ditlev, J. A., Hui, E., Xing, W., Banjade, S., Okrut, J., King, D., Taunton, J., Rosen, M. K., & Vale, R. D. (2016) · Science · doi:10.1126/science.aad9964 · Cited by 1,260 · see citing works
Mechanisms of receptor tyrosine kinase activation in cancer
Du, Z., & Lovly, C. M. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0782-4 · Cited by 1,066 · see citing works
The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
Rozakis-Adcock, M., Fernley, R. T., Wade, J. D., Pawson, T. J., & Bowtell, D. D. L. (1993) · Nature · doi:10.1038/363083a0 · Cited by 1,009 · see citing works
Understanding and targeting resistance mechanisms in NSCLC
Rotow, J. K., & Bivona, T. G. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2017.84 · Cited by 978 · see citing works
Self-citationLi, N., Batzer, A., Daly, R. J., Yajnik, V., Skolnik, E. Y., Chardin, P., Bar‐Sagi, D., Margolis, B. L., & Schlessinger, J. (1993) · Nature · doi:10.1038/363085a0 · Cited by 938 · see citing works
An Acylation Cycle Regulates Localization and Activity of Palmitoylated Ras Isoforms
Rocks, O., Peyker, A., Kahms, M., Verveer, P., Koerner, C., Lumbierres, M., Kuhlmann, J., Waldmann, H., Wittinghofer, A., & Bastiaens, P. (2005) · Science · doi:10.1126/science.1105654 · Cited by 866 · see citing works
γ-Secretase Cleavage and Nuclear Localization of ErbB-4 Receptor Tyrosine Kinase
Ni, C.-Y., Murphy, M. P., Golde, T. E., & Carpenter, G. F. (2001) · Science · doi:10.1126/science.1065412 · Cited by 858 · see citing works
Biochemical and Structural Analysis of Common Cancer-Associated KRAS Mutations
Hunter, J. C., Manandhar, A., Carrasco, M. A., Gurbani, D., Gondi, S., & Westover, K. D. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0203 · Cited by 786 · see citing works
Direct visualization of Ras proteins in spatially distinct cell surface microdomains
Prior, I. A., Muncke, C., Parton, R. G., & Hancock, J. F. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200209091 · Cited by 735 · see citing works
The Centrosome Is a Selective Condensate that Nucleates Microtubules by Concentrating Tubulin
Woodruff, J. B., Gomes, B. F., Widlund, P. O., Mahamid, J., Honigmann, A., & Hyman, A. A. (2017) · Cell · doi:10.1016/j.cell.2017.05.028 · Cited by 685 · see citing works
Monahan, Z. T., Ryan, V. H., Janke, A. M., Burke, K. A., Rhoads, S. N., Zerze, G. H., O’Meally, R. N., Dignon, G. L., Conicella, A. E., Zheng, W., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201696394 · Cited by 685 · see citing works
Ras signalling on the endoplasmic reticulum and the Golgi
Chiu, V. K., Bivona, T., Hach, A., Sajous, J. B., Silletti, J., Wiener, H., Johnson, R. L., Cox, A. D., & Philips, M. R. (2002) · Nature Cell Biology · doi:10.1038/ncb783 · Cited by 594 · see citing works
Self-citationThe p21 ras C-terminus is required for transformation and membrane association
Willumsen, B. M., Christensen, A., Hubbert, N. L., Papageorge, A. G., & Lowy, D. R. (1984) · Nature · doi:10.1038/310583a0 · Cited by 584 · see citing works
Kroschwald, S., Maharana, S., Matějů, D., Malinovska, L., Nüske, E., Poser, I., Richter, D., & Alberti, S. (2015) · eLife · doi:10.7554/elife.06807 · Cited by 545 · see citing works
Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells
Rizzuto, R., Brini, M., Pizzo, P., Murgia, M., & Pozzan, T. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00128-x · Cited by 499 · see citing works
The t(15;17) translocation alters a nuclear body in a retinoic acid‐reversible fashion.
Koken, M. H. M., Puvion-dutilleul, F., Guillemin, M.-C., Viron, A., Linares‐Cruz, G., Stuurman, N., de Jong, L., Szostecki, C., Calvo, F. M., & Chomienne, C. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06356.x · Cited by 496 · see citing works
Quantitative assessment of fluorescent proteins
Cranfill, P. J. C., Sell, B., Baird, M. A., Allen, J. R., Lavagnino, Z., de Gruiter, H. M., Kremers, G., Davidson, M. W., Ustione, A., & Piston, D. W. (2016) · Nature Methods · doi:10.1038/nmeth.3891 · Cited by 485 · see citing works
Cancer-Specific Retargeting of BAF Complexes by a Prion-like Domain
Boulay, G., Sandoval, G. J., Riggi, N., Iyer, S., Buisson, R., Naigles, B., Awad, M. E., Rengarajan, S., Volorio, A., McBride, M. J., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.036 · Cited by 474 · see citing works
Plowman, S. J., Muncke, C., Parton, R. G., & Hancock, J. F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504114102 · Cited by 468 · see citing works
McWhirter, J. R., Galasso, D. L., & Wang, J. Y. J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7587 · Cited by 422 · see citing works
Kinase-controlled phase transition of membraneless organelles in mitosis
Rai, A. K., Chen, J., Selbach, M., & Pelkmans, L. (2018) · Nature · doi:10.1038/s41586-018-0279-8 · Cited by 387 · see citing works
A molecular assembly phase transition and kinetic proofreading modulate Ras activation by SOS
Huang, W. Y. C., Alvarez, S. A., Kondo, Y., Lee, Y. K., Chung, J. K., Lam, H. Y. M., Biswas, K. H., Kuriyan, J., & Groves, J. T. (2019) · Science · doi:10.1126/science.aau5721 · Cited by 352 · see citing works
Targeting RAS Membrane Association: Back to the Future for Anti-RAS Drug Discovery?
Cox, A. D., Der, C. J., & Philips, M. R. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-3214 · Cited by 351 · see citing works
Farnesol modification of Kirsten-ras exon 4B protein is essential for transformation.
Jackson, J. H., Cochrane, C. G., Bourne, J. R., Solski, P. A., Buss, J. E., & Der, C. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.8.3042 · Cited by 338 · see citing works
ALK, ROS1, and NTRK Rearrangements in Metastatic Colorectal Cancer
Pietrantonio, F., Di Nicolantonio, F., Schrock, A. B., Lee, J., Tejpar, S., Sartore-Bianchi, A., Hechtman, J. F., Christiansen, J., Novara, L., Tebbutt, N., et al. (2017) · JNCI: Journal of the National Cancer Institute · doi:10.1093/jnci/djx089 · Cited by 317 · see citing works
Depalmitoylated Ras traffics to and from the Golgi complex via a nonvesicular pathway
Goodwin, J., Drake, K. R., Rogers, C., Wright, L. P., Lippincott-Schwartz, J., Philips, M., & Kenworthy, A. (2005) · Journal of Cell Biology · doi:10.1083/jcb.200502063 · Cited by 308 · see citing works
RET Aberrations in Diverse Cancers: Next-Generation Sequencing of 4,871 Patients
Kato, S., Subbiah, V., Marchlik, E., Elkin, S. K., Carter, J. L., & Kurzrock, R. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-1679 · Cited by 285 · see citing works
Mutant ras-encoded proteins with altered nucleotide binding exert dominant biological effects.
Sigal, I. S., Gibbs, W. W., D'Alonzo, J., Temeles, G. L., Wolanski, B., Socher, S. H., & Scolnick, E. M. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.4.952 · Cited by 267 · see citing works
RAS-MAPK dependence underlies a rational polytherapy strategy in EML4-ALK–positive lung cancer
Hrustanovic, G., Olivas, V. R., Pazarentzos, E., Tulpule, A., Asthana, S., Blakely, C. M., Okimoto, R. A., Lin, L., Neel, D. S., Sabnis, A. J., et al. (2015) · Nature Medicine · doi:10.1038/nm.3930 · Cited by 267 · see citing works
Self-citationImproved split fluorescent proteins for endogenous protein labeling
Feng, S., Sekine, S., Pessino, V., Li, H., Leonetti, M. D., & Huang, B. (2017) · Nature Communications · doi:10.1038/s41467-017-00494-8 · Cited by 264 · see citing works
Self-citationThe Dynamics of Mammalian P Body Transport, Assembly, and Disassembly In Vivo
Aizer, A., Brody, Y., Ler, L. W., Sonenberg, N., Singer, R. H., & Shav‐Tal, Y. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-05-0513 · Cited by 227 · see citing works
EML4-ALK Variants: Biological and Molecular Properties, and the Implications for Patients
Sabir, S. R., Yeoh, S., Jackson, G., & Bayliss, R. W. (2017) · Cancers · doi:10.3390/cancers9090118 · Cited by 225 · see citing works
PI(3,4,5)P 3 Engagement Restricts Akt Activity to Cellular Membranes
Ebner, M., Lučić, I., Leonard, T. A., & Yudushkin, I. A. (2017) · Molecular Cell · doi:10.1016/j.molcel.2016.12.028 · Cited by 220 · see citing works
Ras/MAPK signaling from endomembranes
Fehrenbacher, N., Bar‐Sagi, D., & Philips, M. R. (2009) · Molecular Oncology · doi:10.1016/j.molonc.2009.06.004 · Cited by 150 · see citing works
Visualizing Dynamics of Cell Signaling In Vivo with a Phase Separation-Based Kinase Reporter
Zhang, Q., Huang, H., Zhang, L., Wu, R. S., Chung, C.-I., Zhang, S., Torra, J., Schepis, A., Coughlin, S. R., Kornberg, T. B., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2017.12.008 · Cited by 149 · see citing works
Cussac, D., Frech, M., & Chardin, P. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06717.x · Cited by 125 · see citing works
Passive Noise Filtering by Cellular Compartmentalization
Stoeger, T., Battich, N., & Pelkmans, L. (2016) · Cell · doi:10.1016/j.cell.2016.02.005 · Cited by 115 · see citing works
Childress, M. A., Himmelberg, S. M., Chen, H., Deng, W., Davies, M. A., & Lovly, C. M. (2018) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-18-0171 · Cited by 108 · see citing works
Richards, M. W., O’Regan, L., Röth, D., Montgomery, J. M., Straube, A., Fry, A. M., & Bayliss, R. W. (2015) · Biochemical Journal · doi:10.1042/bj20150039 · Cited by 101 · see citing works
Tyrosine kinase gene fusions in cancer: translating mechanisms into targeted therapies
Medves, S., & Demoulin, J. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01415.x · Cited by 99 · see citing works
den Hertog, J., & Hunter, T. R. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00665.x · Cited by 86 · see citing works
Santos, R. C. D., Garay, C., & Antonescu, C. N. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.07.004 · Cited by 72 · see citing works
Spatial Regulation of EGFR Signaling by Sprouty2
Kim, H. J., Taylor, L. J., & Bar‐Sagi, D. (2007) · Current Biology · doi:10.1016/j.cub.2007.01.059 · Cited by 70 · see citing works
Quantitative microscopy reveals dynamics and fate of clustered IRE1α
Belyy, V., Tran, N.-H. T., & Walter, P. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1915311117 · Cited by 60 · see citing works
VPS35 binds farnesylated N-Ras in the cytosol to regulate N-Ras trafficking
Zhou, M., Wiener, H. H., Su, W., Zhou, Y., Liot, C., Ahearn, I. M., Hancock, J. F., & Philips, M. R. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201604061 · Cited by 56 · see citing works
Src‐dependent autophagic degradation of Ret in FAK‐signalling‐defective cancer cells
Sandilands, E., Serrels, B., Wilkinson, S., & Frame, M. C. (2012) · EMBO Reports · doi:10.1038/embor.2012.92 · Cited by 51 · see citing works
TCR-Induced Activation of Ras Proceeds at the Plasma Membrane and Requires Palmitoylation of N-Ras
Rubio, I., Grund, S., Song, S.-P., Biskup, C. U., Bandemer, S., Fricke, M., Förster, M., Graziani, A., Wittig, U., & Kliche, S. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000334 · Cited by 50 · see citing works
LC3C-Mediated Autophagy Selectively Regulates the Met RTK and HGF-Stimulated Migration and Invasion
Bell, E. S., Coelho, P. P., Ratcliffe, C. D. H., Rajadurai, C. V., Peschard, P., Vaillancourt, R., Zuo, D., & Park, M. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.11.063 · Cited by 49 · see citing works
Regulated Intramembrane Cleavage of the EGF Receptor
Liao, H., & Carpenter, G. F. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01371.x · Cited by 37 · see citing works
A Novel ALK Fusion in Pediatric Medullary Thyroid Carcinoma
Hillier, K., Hughes, A. L., Shamberger, R. C., Shusterman, S., Pérez‐Atayde, A. R., Wassner, A. J., Iafrate, A. J., Dubuc, A. M., Janeway, K. A., Rothenberg, S. M., et al. (2019) · Thyroid · doi:10.1089/thy.2019.0041 · Cited by 33 · see citing works
Receptor Tyrosine Kinases: Translocation Partners in Hematopoietic Disorders
Nelson, K. N., Peiris, M. N., Meyer, A. N., Siari, A., & Donoghue, D. J. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.11.002 · Cited by 33 · see citing works
Stop fRETting the Target: Next-Generation RET Inhibitors Have Arrived
Iams, W. T., & Lovly, C. M. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-0489 · Cited by 11 · see citing works
Real-Time Visualization and Quantification of Native Ras Activation in Single Living Cells
Biskup, C. U., & Rubio, I. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-791-4_19 · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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Huang, L., Guo, Z., Wang, F., & Fu, L. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00780-4 · Cited by 1,127 · see citing works
A framework for understanding the functions of biomolecular condensates across scales
Lyon, A. S., Peeples, W. B., & Rosen, M. K. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00303-z · Cited by 895 · see citing works
Liquid–liquid phase separation drives cellular function and dysfunction in cancer
Mehta, S., & Zhang, J. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00444-7 · Cited by 443 · see citing works
ALK-positive lung cancer: a moving target
Schneider, J. L., Lin, J. J., & Shaw, A. T. (2023) · Nature Cancer · doi:10.1038/s43018-023-00515-0 · Cited by 190 · see citing works
Wu, Y., Zhou, L., Zou, Y., Zhang, Y., Zhang, M., Xu, L., Zheng, L., He, W., Yu, K., Li, T., et al. (2023) · Nature Cancer · doi:10.1038/s43018-023-00522-1 · Cited by 126 · see citing works
Molecular Spies in Action: Genetically Encoded Fluorescent Biosensors Light up Cellular Signals
Gest, A. M. M., Sahan, A. Z., Zhong, Y., Lin, W., Mehta, S., & Zhang, J. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00293 · Cited by 110 · see citing works
Receptor tyrosine kinases regulate signal transduction through a liquid-liquid phase separated state
Lin, C., Suen, K. M., Jeffrey, P.-A., Wieteska, Ł., Lidster, J. A., Bao, P., Curd, A., Stainthorp, A. K., Seiler, C., Koss, H., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.02.005 · Cited by 101 · see citing works
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Cai, D., Liu, Z. J., & Lippincott‐Schwartz, J. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.01.002 · Cited by 98 · see citing works
Kinase regulation by liquid–liquid phase separation
López-Palacios, T. P., & Andersen, J. L. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.11.009 · Cited by 89 · see citing works
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Chen, L., Zhang, Y., Yin, L., Cai, B., Huang, P. C., Li, X., & Liang, G. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02156-6 · Cited by 93 · see citing works
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Lei, Y., Yan, L., Shi, X., & Wang, J. (2022) · Oncology Letters · doi:10.3892/ol.2022.13397 · Cited by 86 · see citing works
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Yin, G., Huang, J., Petela, J., Jiang, H., Zhang, Y., Gong, S., Wu, J., Liu, B., Shi, J., & Gao, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01441-4 · Cited by 87 · see citing works
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Boeynaems, S., Chong, S., Gsponer, J. A., Holt, L. J., Milovanović, D., Mitrea, D. M., Mueller‐Cajar, O., Portz, B., Reilly, J. F., Reinkemeier, C. D., et al. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.167971 · Cited by 80 · see citing works
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Tripathi, S., Shirnekhi, H. K., Gorman, S. D., Chandra, B., Baggett, D. W., Park, C., Somjee, R., Lang, B., Hosseini, S. M. H., Pioso, B. J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41655-2 · Cited by 75 · see citing works
Signaling pathways in liver cancer: pathogenesis and targeted therapy
Xue, Y., Ruan, Y., Wang, Y., Xiao, P., & Xu, J. (2024) · Molecular Biomedicine · doi:10.1186/s43556-024-00184-0 · Cited by 81 · see citing works
Li, Y., Liu, Y., Yu, X., Xu, Y., Pan, X., Sun, Y. E., Wang, Y., Song, Y.-H., & Shen, Z. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02013-w · Cited by 69 · see citing works
Santarpia, M., Ciappina, G., Spagnolo, C. C., Squeri, A., Passalacqua, M. I., Aguilar, A., Gonzalez-Cao, M., Giovannetti, E., Silvestris, N., & Rosell, R. (2023) · Translational Lung Cancer Research · doi:10.21037/tlcr-22-639 · Cited by 65 · see citing works
EML4‐ALK biology and drug resistance in non‐small cell lung cancer: a new phase of discoveries
Elshatlawy, M., Sampson, J., Clarke, K., & Bayliss, R. W. (2023) · Molecular Oncology · doi:10.1002/1878-0261.13446 · Cited by 69 · see citing works
Biomolecular condensates: Formation mechanisms, biological functions, and therapeutic targets
Niu, X., Zhang, L., Wu, Y., Zong, Z., Wang, B., Liu, J., Zhang, L., & Zhou, F. (2023) · MedComm · doi:10.1002/mco2.223 · Cited by 64 · see citing works
Zhang, J. Z., Mehta, S., & Zhang, J. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.07.003 · Cited by 64 · see citing works
FGFR2 Inhibition in Cholangiocarcinoma
Vogel, A., Segatto, O., Stenzinger, A., & Saborowski, A. L. (2022) · Annual Review of Medicine · doi:10.1146/annurev-med-042921-024707 · Cited by 63 · see citing works
Phase-separated foci of EML4-ALK facilitate signalling and depend upon an active kinase conformation
Sampson, J., Richards, M. W., Choi, J., Fry, A. M., & Bayliss, R. W. (2021) · EMBO Reports · doi:10.15252/embr.202153693 · Cited by 61 · see citing works
Phase separation drives the self-assembly of mitochondrial nucleoids for transcriptional modulation
Long, Q., Zhou, Y., Wu, H., Du, S., Hu, M., Qi, J., Li, W., Guo, J., Wu, Y., Yang, L., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00671-w · Cited by 57 · see citing works
The Configuration of GRB2 in Protein Interaction and Signal Transduction
Wang, D., Liu, G., Meng, Y., Chen, H., Ye, Z., & Ji, J. (2024) · Biomolecules · doi:10.3390/biom14030259 · Cited by 52 · see citing works
Targeting KRAS mutations: orchestrating cancer evolution and therapeutic challenges
Choucair, K., Imtiaz, H., Uddin, M. H., Nagasaka, M., Al-Hallak, M. N., Philip, P. A., El-Rayes, B., Pasche, B., & Azmi, A. S. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02473-8 · Cited by 57 · see citing works
The oncogenic fusion landscape in pediatric CNS neoplasms
Roosen, M. M., Odé, Z., Bunt, J., & Kool, M. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02405-8 · Cited by 52 · see citing works
Quantitative reconstitution of yeast RNA processing bodies
Currie, S. L., Xing, W., Muhlrad, D., Decker, C. J., Parker, R., & Rosen, M. K. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2214064120 · Cited by 51 · see citing works
Emerging Implications of Phase Separation in Cancer
Ren, J., Zhang, Z., Zong, Z., Zhang, L., & Zhou, F. (2022) · Advanced Science · doi:10.1002/advs.202202855 · Cited by 47 · see citing works
Molecular insights into the effect of 1,6-hexanediol on FUS phase separation
Zheng, T., Wake, N., Weng, S.-L., Perdikari, T. M., Murthy, A. C., Mittal, J., & Fawzi, N. L. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00431-2 · Cited by 46 · see citing works
Zheng, L., Liu, C., & Yu, K. (2023) · Journal of Hematology & Oncology · doi:10.1186/s13045-023-01522-5 · Cited by 45 · see citing works
Prognostic and predictive biomarkers in non-small cell lung carcinoma
Odintsov, I., & Sholl, L. M. (2023) · Pathology · doi:10.1016/j.pathol.2023.11.006 · Cited by 46 · see citing works
YAP condensates are highly organized hubs
Hao, S., Lee, Y. J., Goldfajn, N. B., Flores, E., Liang, J., Fuehrer, H., Demmerle, J., Lippincott‐Schwartz, J., Liu, Z. J., Sukenik, S., et al. (2024) · iScience · doi:10.1016/j.isci.2024.109927 · Cited by 43 · see citing works
Uniyal, P., Kashyap, V. K., Behl, T., Parashar, D., & Rawat, R. (2025) · Cancers · doi:10.3390/cancers17050785 · Cited by 45 · see citing works
Resistance Profile and Structural Modeling of Next-Generation ROS1 Tyrosine Kinase Inhibitors
Keddy, C., Shinde, P., Jones, K. L., Kaech, S., Somwar, R., Shinde, U. P., & Davare, M. A. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0395 · Cited by 42 · see citing works
ALK in cancer: from function to therapeutic targeting
Voena, C., Ambrogio, C., Iannelli, F., & Chiarle, R. (2025) · Nature reviews. Cancer · doi:10.1038/s41568-025-00797-9 · Cited by 45 · see citing works
The Role of Phase-Separated Condensates in Fusion Oncoprotein–Driven Cancers
Shirnekhi, H. K., Chandra, B., & Kriwacki, R. W. (2023) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-061421-122050 · Cited by 39 · see citing works
Liquid‒liquid phase separation: roles and implications in future cancer treatment
Liu, Z., Qin, Z., Liu, Y., Xia, X., He, L., Chen, N., Hu, X., & Peng, X. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.81521 · Cited by 39 · see citing works
Clinically relevant fusion oncogenes: detection and practical implications
Sorokin, M., Rabushko, E., Rozenberg, J. M., Mohammad, T., Seryakov, A., Sekacheva, M. I., & Buzdin, A. A. (2022) · Therapeutic Advances in Medical Oncology · doi:10.1177/17588359221144108 · Cited by 37 · see citing works
Biomolecular condensates in cancer biology
Suzuki, H. I., & Onimaru, K. (2021) · Cancer Science · doi:10.1111/cas.15232 · Cited by 35 · see citing works
Research progress of drug resistance mechanism of temozolomide in the treatment of glioblastoma
Wu, H., Gao, W., Chen, P., Wei, Y., Zhao, H., & Wang, F. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e39984 · Cited by 36 · see citing works
Phase separation enhances probability of receptor signalling and drug targeting
Ladbury, J. E., Lin, C., & Suen, K. M. (2023) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2023.01.005 · Cited by 36 · see citing works
Zhang, J. Z., Nguyen, W. H., Greenwood, N., Rose, J. C., Ong, S.-E., Maly, D. J., & Baker, D. (2024) · Nature Biotechnology · doi:10.1038/s41587-023-02107-w · Cited by 37 · see citing works
Current status of drugs targeting PDGF/PDGFR
Ai, J.-Y., Liu, C., Zhang, W., & Rao, G. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.103989 · Cited by 35 · see citing works
Enhanced liquidity of p62 droplets mediated by Smurf1 links Nrf2 activation and autophagy
Qin, X., Li, Y., Xu, W., Wu, C., Zheng, H., Liu, L., & Dong, L. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-00978-9 · Cited by 31 · see citing works
Proximity-Dependent Biotinylation Approaches to Explore the Dynamic Compartmentalized Proteome
Dionne, U., & Gingras, A. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.852911 · Cited by 31 · see citing works
SRC homology 3 domains: multifaceted binding modules
Dionne, U., Percival, L. J., Chartier, F. J.-M., Landry, C. R., & Bisson, N. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2022.04.005 · Cited by 31 · see citing works
EML4-ALK fusions drive lung adeno-to-squamous transition through JAK-STAT activation
Qin, Z., Yue, M., Tang, S., Wu, F., Sun, H., Li, Y., Zhang, Y., Izumi, H., Huang, H., Wang, W., et al. (2023) · The Journal of Experimental Medicine · doi:10.1084/jem.20232028 · Cited by 28 · see citing works
KRAS Hijacks the miRNA Regulatory Pathway in Cancer
Bortoletto, A. S., & Parchem, R. J. (2023) · Cancer Research · doi:10.1158/0008-5472.can-23-0296 · Cited by 29 · see citing works
A call to order: examining structured domains in biomolecular condensates
Tibble, R. W., & Gross, J. (2023) · Journal of magnetic resonance (San Diego, Calif. 1997 : Print) · doi:10.1016/j.jmr.2022.107318 · Cited by 18 · see citing works
Stress granules and organelles: coordinating cellular responses in health and disease
Liu, Y., Li, Y., & Zhang, P. (2024) · Protein & Cell · doi:10.1093/procel/pwae057 · Cited by 26 · see citing works
Ectopic biomolecular phase transitions: fusion proteins in cancer pathologies
Davis, R. B., Moosa, M. M., & Banerjee, P. R. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.03.005 · Cited by 26 · see citing works
Zhou, J., Tu, D., Peng, R., Tang, Y., Deng, Q., Su, B., Wang, S., Tang, H., Jin, S., Jiang, G., et al. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01241-x · Cited by 26 · see citing works
PI3K signaling through a biochemical systems lens
Madsen, R. R., & Toker, A. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105224 · Cited by 25 · see citing works
Phase separation-mediated biomolecular condensates and their relationship to tumor
Wang, X., Liu, J., Mao, C., & Mao, Y. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01518-9 · Cited by 25 · see citing works
Biomolecular condensates and disease pathogenesis
Ruan, K., Bai, G., Fang, Y., Li, D., Li, T., Liu, X., Lu, B., Lü, Q., Songyang, Z., Sun, S., et al. (2024) · Science China Life Sciences · doi:10.1007/s11427-024-2661-3 · Cited by 27 · see citing works
De novo designed Hsp70 activator dissolves intracellular condensates
Zhang, J. Z., Greenwood, N. F., Hernandez, J., Cuperus, J. T., Huang, B., Ryder, B. D., Queitsch, C., Gestwicki, J. E., & Baker, D. A. (2025) · Cell chemical biology · doi:10.1016/j.chembiol.2025.01.006 · Cited by 25 · see citing works
Self-citationRAS‐targeted cancer therapy: Advances in drugging specific mutations
Liu, C., Ye, D., Yang, H., Chen, X., Su, Z., Li, X., Ding, M., & Liu, Y. (2023) · MedComm · doi:10.1002/mco2.285 · Cited by 24 · see citing works
Oncogenic EML4-ALK assemblies suppress growth factor perception and modulate drug tolerance
Gonzalez-Martinez, D., Roth, L., Mumford, T. R., Guan, J., Le, A., Doebele, R. C., Huang, B., Tulpule, A., Niewiadomska–Bugaj, M., Bivona, T. G., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-53451-7 · Cited by 24 · see citing works
Self-citationBrandt, A. C., Koehn, O. J., & Williams, C. L. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.685135 · Cited by 24 · see citing works
Onco-condensates: formation, multi-component organization, and biological functions
Xu, C., Kim, A., Corbin, J. M., & Wang, G. G. (2023) · Trends in cancer · doi:10.1016/j.trecan.2023.05.006 · Cited by 24 · see citing works
The emerging role of receptor tyrosine kinase phase separation in cancer
Lin, C., Suen, K. M., Lidster, J. A., & Ladbury, J. E. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.09.002 · Cited by 24 · see citing works
Rosell, R., Aguilar, A., Pedraz‐Valdunciel, C., & CHAIB-OUKADOUR, I. (2021) · Nature Cancer · doi:10.1038/s43018-021-00289-3 · Cited by 23 · see citing works
Tortosa, E., Ghosh, A. S., Li, Q., Wong, W. R., Hinkle, T. B., Sandoval, W. N., Rose, C. M., & Hoogenraad, C. C. (2022) · The EMBO Journal · doi:10.15252/embj.2021110155 · Cited by 23 · see citing works
Phase separation underlies signaling activation of oncogenic NTRK fusions
Zhu, T., Xie, J., He, H., Li, H., Tang, X.-B., Wang, S., Li, Z., Tian, Y., Li, L., Zhu, J., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2219589120 · Cited by 22 · see citing works
CCDC6-RET fusion protein regulates Ras/MAPK signaling through the fusion- GRB2-SHC1 signal niche
Qiu, T., Kong, Y., Wei, G., Sun, K., Wang, R., Wang, Y., Chen, Y., Wang, W., Zhang, Y., Jiang, C., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2322359121 · Cited by 22 · see citing works
GUK1 activation is a metabolic liability in lung cancer
Schneider, J. L., Kurmi, K., Dai, Y., Dhiman, I., Joshi, S., Gassaway, B. M., Johnson, C. W., Jones, N., Li, Z., Joschko, C. P., et al. (2025) · Cell · doi:10.1016/j.cell.2025.01.024 · Cited by 21 · see citing works
Biophysics of endocytic vesicle formation: A focus on liquid–liquid phase separation
Lomoriello, I. S., Sigismund, S., & Day, K. J. (2022) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2022.02.002 · Cited by 21 · see citing works
Liquid–Liquid Phase Separation in Cancer Signaling, Metabolism and Anticancer Therapy
Igelmann, S., Lessard, F., & Ferbeyre, G. (2022) · Cancers · doi:10.3390/cancers14071830 · Cited by 22 · see citing works
Biomolecular Condensation: A New Phase in Cancer Research
Chakravarty, A. K., McGrail, D. J., Lozanoski, T. M., Dunn, B. S., Shih, D. J. H., Cirillo, K. M., Cetinkaya, S. H., Zheng, W. J., Mills, G. B., Yi, S. S., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-1605 · Cited by 21 · see citing works
Febres‐Aldana, C. A., Vojnic, M., Odintsov, I., Zhang, T., Cheng, R., Beach, C. Z., Lu, D., Mattar, M. S., Gazzo, A. M., Gili, L., et al. (2025) · Cancer Discovery · doi:10.1158/2159-8290.cd-24-0417 · Cited by 20 · see citing works
Progress and challenges in RET-targeted cancer therapy
Hu, X., Khatri, U., Shen, T., & Wu, J. (2023) · Frontiers of Medicine · doi:10.1007/s11684-023-0985-y · Cited by 20 · see citing works
Chemogenetic Minitool for Dissecting the Roles of Protein Phase Separation
Chung, C.-I., Yang, J., & Shu, X. (2023) · ACS Central Science · doi:10.1021/acscentsci.3c00251 · Cited by 20 · see citing works
Bremer, A., Posey, A. E., Borgia, M. B., Borcherds, W. M., Farag, M., Pappu, R. V., & Mittag, T. (2022) · Biomolecules · doi:10.3390/biom12101480 · Cited by 19 · see citing works
Phase separation in chemical and mechanical signal transduction
Cheng, X., & Case, L. B. (2023) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2023.102243 · Cited by 19 · see citing works
Mumford, T. R., Rae, D., Brackhahn, E., Idris, A., Gonzalez-Martinez, D., Pal, A. A., Chung, M. C., Guan, J., Rhoades, E. R., & Bugaj, L. J. (2024) · Cell Systems · doi:10.1016/j.cels.2024.01.005 · Cited by 19 · see citing works
Self-citationDisP-seq reveals the genome-wide functional organization of DNA-associated disordered proteins
Xing, Y., Dong, R., Lee, L., Rengarajan, S., Riggi, N., Boulay, G., & Rivera, M. N. (2023) · Nature Biotechnology · doi:10.1038/s41587-023-01737-4 · Cited by 18 · see citing works
Chakraborty, S., Mishra, J., Roy, A., Niharika, N., Manna, S., Baral, T., Nandi, P., Patra, S., & Patra, S. K. (2024) · Biochimie · doi:10.1016/j.biochi.2024.05.007 · Cited by 18 · see citing works
ERK1/2-MAPK signaling: Metabolic, organellar, and cytoskeletal interactions
Martín-Vega, A., & Cobb, M. H. (2025) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2025.102526 · Cited by 18 · see citing works
Yan, Q., Fang, X., Liu, X., Guo, S., Chen, S., Luo, M., Lan, P., & Guan, X. (2023) · Advanced Science · doi:10.1002/advs.202305653 · Cited by 17 · see citing works
Plasma membrane-associated ARAF condensates fuel RAS-related cancer drug resistance
Li, W., Shi, X., Tan, C., Jiang, Z., Li, M., Ji, Z., Zhou, J., Luo, M., Fan, Z., Ding, Z., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-024-01826-8 · Cited by 17 · see citing works
Self-citationAlternative Treatment Options to ALK Inhibitor Monotherapy for EML4-ALK-Driven Lung Cancer
Papageorgiou, S., Pashley, S. L., O’Regan, L., Khan, S., Bayliss, R. W., & Fry, A. M. (2022) · Cancers · doi:10.3390/cancers14143452 · Cited by 17 · see citing works
Endogenous YAP/TAZ partitioning in TEAD condensates orchestrates the Hippo response
Zhu, T., Li, H., Mao, S., Zhu, Y., Cao, H., Zhang, Q., Zhen, N., Zhang, H., Tian, Y., Guo, Y., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.08.014 · Cited by 16 · see citing works
Lucken, K., O’Regan, L., Choi, J., Sampson, J., Pashley, S. L., Bayliss, R. W., Khan, S., & Fry, A. M. (2022) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-21-1010 · Cited by 16 · see citing works
Abnormal phase separation of biomacromolecules in human diseases
Zhang, S., Pei, G., Li, B., Li, P., & Lin, Y. (2023) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2023139 · Cited by 16 · see citing works
Self-citationNew insights into the important roles of phase seperation in the targeted therapy of lung cancer
Zou, Y., Zheng, H., Ning, Y., Yang, Y., Wen, Q., & Fan, S. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-01101-8 · Cited by 16 · see citing works
Maruyama, K., Shimizu, Y., Nomura, Y., Oh-hara, T., Takahashi, Y., Nagayama, S., Fujita, N., & Katayama, R. (2025) · npj Precision Oncology · doi:10.1038/s41698-024-00793-6 · Cited by 16 · see citing works
GRB2 is a BECN1 interacting protein that regulates autophagy
Montero-Vergara, J., Plachetta, K., Kinch, L. N., Bernhardt, S., Kashyap, K., Levine, B., Thukral, L., Vetter, M., Thomssen, C., Wiemann, S., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-023-06387-7 · Cited by 14 · see citing works
Mechanistic patterns and clinical implications of oncogenic tyrosine kinase fusions in human cancers
Cheong, T.-C., Jang, A., Wang, Q., Leonardi, G. C., Ricciuti, B., Alessi, J. V., Federico, A. D., Awad, M. M., Lehtinen, M. K., Harris, M. H., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49499-0 · Cited by 15 · see citing works
Liquid–Liquid Phase Separation in Major Hallmarks of Cancer
Xie, C., Wang, T., Liu, X. P., Wang, Y., Dang, Q., Ding, T., Xu, J., Yu, X., Lin, H. L., Xu, X., et al. (2025) · Cell Proliferation · doi:10.1111/cpr.70122 · Cited by 13 · see citing works
Lu, X., Yu, R., Li, Z., Yang, M., Dai, J., & Liu, M. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216517 · Cited by 13 · see citing works
Concurrent inhibition of ALK and SRC kinases disrupts the ALK lung tumor cell proteome
Diaz-Jimenez, A., Ramos, M., Helm, B., Chocarro, S., Frey, D. L., Agrawal, S., Somogyi, K., Klingmüller, U., Lu, J., & Sotillo, R. (2024) · Drug Resistance Updates · doi:10.1016/j.drup.2024.101081 · Cited by 13 · see citing works
Salokas, K., Dashi, G., & Varjosalo, M. T. (2023) · Cancers · doi:10.3390/cancers15143678 · Cited by 12 · see citing works
Zhang, M.-J., Shi, M., Yu, Y., Wang, H., Ou, R., & Ge, R. (2024) · Life Sciences · doi:10.1016/j.lfs.2023.122406 · Cited by 12 · see citing works
Biomolecular condensates: A new lens on cancer biology
Jiang, L., & Kang, Y. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189245 · Cited by 12 · see citing works
De novo design of Ras isoform selective binders
Zhang, J. Z., Li, X., Batingana, A. R., Liu, C., Jiang, H., Shannon, K., Huang, B. J., Wu, K., & Baker, D. (2026) · Cell Chemical Biology · doi:10.1016/j.chembiol.2026.02.008 · Cited by 12 · see citing works
Self-citationSugiura, R. (2021) · Current Genetics · doi:10.1007/s00294-021-01192-1 · Cited by 11 · see citing works
Huang, Z., Liu, Z., Chen, L., Liu, Y., Yan, G., Ni, Y., Yan, Q., He, W., Liu, J., Luo, S., et al. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1540427 · Cited by 9 · see citing works
Identification of a EML4-ALK exon 19 fusion variant in lung adenocarcinoma and alectinib resistance
Liu, D., Xu, X., Wen, J., Zhang, C., & Fan, M. (2021) · Lung Cancer · doi:10.1016/j.lungcan.2021.07.020 · Cited by 9 · see citing works
- Authors
- Tulpule, A., Guan, J., Neel, D. S., Allegakoen, H. R., Lin, Y. P., Brown, D., Chou, Y.-T., Heslin, A., Chatterjee, N., Perati, S., Menon, S., Nguyen, T. A., Debnath, J., Ramirez, A. D., Shi, X., Yang, B., Feng, S., Makhija, S., Huang, B., & Bivona, T. G.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Huang, Bo
- Bivona, Trever G.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2021-05
- Volume
- 184
- Issue
- 10
- Pages
- 2649-2664.e18
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC8127962
- OpenAlex
- W3155633297
- Cited by
- 189
- References
- 67
- Citations by year
- 2026: 25 · 2025: 35 · 2024: 36 · 2023: 46 · 2022: 27 · 2021: 18 · 2020: 2
- FWCI
- 7.54
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell (publishedVersion, cc-by)
- SSRN Electronic Journal (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- NIH
- NCI Cancer Moonshot
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- biomolecular condensates, receptor tyrosine kinase, RAS/MAPK pathway, anaplastic lymphoma kinase, RET, fusion oncoproteins, cancer signaling
- MeSH terms
- Biomolecular Condensates, Cytoplasmic Granules, Enzyme Activation, Humans, Neoplasms, Signal Transduction, Oncogene Proteins, Fusion, ras Proteins, SOS1 Protein, Adaptor Proteins, Signal Transducing, GRB2 Adaptor Protein, HEK293 Cells
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