The DOI matches its Crossref record; 143 of the 143 references it cites were found in a registry or an index.
FAK in cancer: mechanistic findings and clinical applications
Open accessAbstract
Focal adhesion kinase (FAK) is a cytoplasmic protein tyrosine kinase that is overexpressed and activated in several advanced-stage solid cancers. FAK promotes tumour progression and metastasis through effects on cancer cells, as well as stromal cells of the tumour microenvironment. The kinase-dependent and kinase-independent functions of FAK control cell movement, invasion, survival, gene expression and cancer stem cell self-renewal. Small molecule FAK inhibitors decrease tumour growth and metastasis in several preclinical models and have initial clinical activity in patients with limited adverse events. In this Review, we discuss FAK signalling effects on both tumour and stromal cell biology that provide rationale and support for future therapeutic opportunities.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
In the citing paper
“Interestingly, multiple previous studies have implicated FAK activation in the development of resistance against various chemotherapy agents through its regulation of the tumor microenvironment.[ 11, 15, 44 ]”
From Focal Adhesion Kinase (FAK) Inhibition Synergizes with KRAS G12C Inhibitors in Treating Cancer through the Regulation of the FAK–YAP Signaling (2021) · cites this paper as [11]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Comprehensive molecular portraits of human breast tumours
The Cancer Genome Atlas Network (2012) · Nature · doi:10.1038/nature11412 · Cited by 12,129
The protein kinase complement of the human genome
Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145
Integrated genomic analyses of ovarian carcinoma
Perou, C. M. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/hvp3-wg08 · Cited by 7,927
Matrix Crosslinking Forces Tumor Progression by Enhancing Integrin Signaling
Levental, K. R., Yu, H., Kass, L., Lakins, J. N., Egeblad, M., Erler, J. T., Fong, S. F. T., Csiszar, K., Giaccia, A., Weninger, W., et al. (2009) · Cell · doi:10.1016/j.cell.2009.10.027 · Cited by 4,101
Focal adhesion kinase: in command and control of cell motility
Mitra, S. K., Hanson, D. A., & Schlaepfer, D. D. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1549 · Cited by 2,657
Self-citationFocal adhesion kinase: the first ten years
Parsons, J. T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00373 · Cited by 1,389
The role of focal-adhesion kinase in cancer — a new therapeutic opportunity
McLean, G. W., Carragher, N. O., Avizienyte, E., EVANS, J., Brunton, V. G., & Frame, M. C. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1647 · Cited by 1,049
E-cadherin–integrin crosstalk in cancer invasion and metastasis
Canel, M., Serrels, A., Frame, M. C., & Brunton, V. G. (2013) · Journal of Cell Science · doi:10.1242/jcs.100115 · Cited by 651
Cellular functions of FAK kinases: insight into molecular mechanisms and novel functions
Schaller, M. D. (2010) · Journal of Cell Science · doi:10.1242/jcs.045112 · Cited by 613
Signal transduction by focal adhesion kinase in cancer
Zhao, J., & Guan, J. (2009) · Cancer and Metastasis Reviews · doi:10.1007/s10555-008-9165-4 · Cited by 608
Flagged first, then by citations
Cited by
Sorted by citations
Macrophages as regulators of tumour immunity and immunotherapy
DeNardo, D. G., & Ruffell, B. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0127-6 · Cited by 2,591
Targeting focal adhesion kinase renders pancreatic cancers responsive to checkpoint immunotherapy
Jiang, H., Hegde, S., Knolhoff, B. L., Zhu, Y., Herndon, J. M., Meyer, M. A., Nywening, T. M., Hawkins, W. G., Shapiro, I. M., Weaver, D. T., et al. (2016) · Nature Medicine · doi:10.1038/nm.4123 · Cited by 1,060
Nia, H. T., Munn, L. L., & Jain, R. K. (2020) · Science · doi:10.1126/science.aaz0868 · Cited by 882
The delivery of therapeutic oligonucleotides
Juliano, R. L. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw236 · Cited by 882
Yang, X., Lin, Y., Shi, Y., Li, B., Liu, W., Yin, W., Dang, Y., Chu, Y., Fan, J., & He, R. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2973 · Cited by 748
Permeability of the Endothelial Barrier: Identifying and Reconciling Controversies
Claesson, L., Dejana, E., & McDonald, D. M. (2020) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2020.11.006 · Cited by 657
Organization, dynamics and mechanoregulation of integrin-mediated cell–ECM adhesions
Kanchanawong, P., & Calderwood, D. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00531-5 · Cited by 630
Hirata, E., Girotti, M. R., Viros, A., Hooper, S., Spencer-Dene, B., Matsuda, M., Larkin, J., Marais, R., & Sahai, E. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.03.008 · Cited by 593
Lampi, M. C., & Reinhart-King, C. A. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aao0475 · Cited by 551
FAK signaling in human cancer as a target for therapeutics
Lee, B. Y., Timpson, P., Horvath, L. G., & Daly, R. J. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.10.001 · Cited by 439
Tumor Microenvironment and Differential Responses to Therapy
Hirata, E., & Sahai, E. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026781 · Cited by 422
Targeting FAK in anticancer combination therapies
Dawson, J. C., Serrels, A., Stupack, D. G., Schlaepfer, D. D., & Frame, M. C. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00340-6 · Cited by 407
Self-citationFrom state-of-the-art treatments to novel therapies for advanced-stage pancreatic cancer
Nevala-Plagemann, C., Hidalgo, M. M., & Garrido‐Laguna, I. (2019) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-019-0281-6 · Cited by 403
Alteration of the Antitumor Immune Response by Cancer-Associated Fibroblasts
Ziani, L., Chouaïb, S., & Thiery, J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00414 · Cited by 391
Proteolysis-targeting chimeras (PROTACs) in cancer therapy
Li, X., Pu, W., Zheng, Q., Ai, M., Chen, S., & Peng, Y. (2022) · Molecular Cancer · doi:10.1186/s12943-021-01434-3 · Cited by 389
Epithelial–mesenchymal transition: a new target in anticancer drug discovery
Marcucci, F., Stassi, G., & Maria, R. D. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2015.13 · Cited by 345
Lukjanenko, L., Jung, M. J., Hegde, N., Perruisseau-Carrier, C., Migliavacca, E., Rozo, M., Karaz, S., Jacot, G. E., Schmidt, M., Li, L., et al. (2016) · Nature Medicine · doi:10.1038/nm.4126 · Cited by 347
Cancer cell behaviors mediated by dysregulated pH dynamics at a glance
White, K. A., Grillo‐Hill, B. K., & Barber, D. L. (2017) · Journal of Cell Science · doi:10.1242/jcs.195297 · Cited by 330
Trial Watch: Immunogenic cell death inducers for anticancer chemotherapy
Pol, J. G., Vacchelli, E., Aranda, F., Castoldi, F., Eggermont, A. M. M., Cremer, I., Sautès‐Fridman, C., Fucikova, J. P., Galon, J., Špíšek, R., et al. (2015) · OncoImmunology · doi:10.1080/2162402x.2015.1008866 · Cited by 320
Addressing Kinase-Independent Functions of Fak via PROTAC-Mediated Degradation
Cromm, P. M., Samarasinghe, K. T. G., Hines, J., & Crews, C. M. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b08008 · Cited by 293
Targeted protein degradation: A promise for undruggable proteins
Samarasinghe, K. T. G., & Crews, C. M. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.011 · Cited by 297
PROTACs: great opportunities for academia and industry (an update from 2020 to 2021)
He, M., Cao, C., Ni, Z., Liu, Y., Song, P., Hao, S., He, Y., Sun, X., & Rao, Y. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00999-9 · Cited by 283
Theodosiou, M., Widmaier, M., Böttcher, R. T., Rognoni, E., Veelders, M., Bharadwaj, M., Lambacher, A., Austen, K., Müller, D. J., Zent, R., et al. (2016) · eLife · doi:10.7554/elife.10130 · Cited by 279
Extracellular matrix stiffness: Mechanisms in tumor progression and therapeutic potential in cancer
Zhang, M., & Zhang, B. (2025) · Experimental Hematology & Oncology · doi:10.1186/s40164-025-00647-2 · Cited by 269
“Changes in matrix composition or stiffness, cytokines, growth factors, integrins, and pH trigger FAK activity through the αvβ5/FAK/PI3K/Akt signaling pathway [146] to prevent anoikis and other types of cell death.”
Tetraspanins Function as Regulators of Cellular Signaling
Termini, C. M., & Gillette, J. M. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00034 · Cited by 267
Diehl, C. J., & Ciulli, A. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00387b · Cited by 269
Current treatment options for meningioma
Apra, C., Peyre, M., & Kalamarides, M. (2018) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2018.1429920 · Cited by 254
Small molecule immunomodulation: the tumor microenvironment and overcoming immune escape
Osipov, A., Saung, M. T., Zheng, L., & Murphy, A. G. (2019) · Journal for ImmunoTherapy of Cancer · doi:10.1186/s40425-019-0667-0 · Cited by 252
Tumor-associated fibrosis as a regulator of tumor immunity and response to immunotherapy
Jiang, H., Hegde, S., & DeNardo, D. G. (2017) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-017-2003-1 · Cited by 246
Feng, X., Arang, N., Rigiracciolo, D. C., Lee, J. S., Yeerna, H., Wang, Z., Lubrano, S., Kishore, A., Pachter, J. A., König, G. M., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.01.009 · Cited by 237
Self-citationAdvances on Natural Polyphenols as Anticancer Agents for Skin Cancer
Sajadimajd, S., Bahramsoltani, R., Iranpanah, A., Patra, J. K., Das, G., Gouda, S., Rahimi, R., Rezaeiamiri, E., Cao, H., Giampieri, F., et al. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104584 · Cited by 238
Targeting KRAS mutant cancers: from druggable therapy to drug resistance
Zhu, C., Guan, X., Zhang, X., Luan, X., Song, Z., Cheng, X., Zhang, W., & Qin, J.-J. (2022) · Molecular Cancer · doi:10.1186/s12943-022-01629-2 · Cited by 231
CircPTK2 (hsa_circ_0005273) as a novel therapeutic target for metastatic colorectal cancer
Yang, H., Li, X., Meng, Q., Sun, H., Wu, S., Hu, W., Liu, G., Li, X., Yang, Y., & Chen, R. (2020) · Molecular Cancer · doi:10.1186/s12943-020-1139-3 · Cited by 234
Jiang, J., Wang, K., Chen, Y., Chen, H., Nice, E. C., & Huang, C. (2017) · Signal Transduction and Targeted Therapy · doi:10.1038/sigtrans.2017.36 · Cited by 233
Emerging Roles of Focal Adhesion Kinase in Cancer
Tai, Y.-L., Chen, L., & Shen, T. (2015) · BioMed Research International · doi:10.1155/2015/690690 · Cited by 233
Understanding the Roles of FAK in Cancer
Yoon, H., Dehart, J. P., Murphy, J. M., & Lim, S. (2014) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155414561498 · Cited by 228
Focal adhesion kinase signaling in unexpected places
Kleinschmidt, E. G., & Schlaepfer, D. D. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.01.003 · Cited by 219
Self-citationTargeting focal adhesion kinase in cancer cells and the tumor microenvironment
Murphy, J. M., Rodriguez, Y. A. R., Jeong, K., Ahn, E.-Y. E., & Lim, S. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-0447-4 · Cited by 226
Prognostic biomarkers in oral squamous cell carcinoma: A systematic review
Rivera, C., Oliveira, A. K., Costa, R. A. P. E., Rossi, T. D., & Leme, A. F. P. (2017) · Oral Oncology · doi:10.1016/j.oraloncology.2017.07.003 · Cited by 218
FAK Structure and Regulation by Membrane Interactions and Force in Focal Adhesions
Tapial Martínez, P., López Navajas, P., & Lietha, D. (2020) · Biomolecules · doi:10.3390/biom10020179 · Cited by 206
“The importance of FAK in cell motility is also reflected in disease where FAK plays major roles in tumour invasion and metastasis [11].”
BackgroundChamcheu, J. C., Roy, T., Uddin, M. B., Banang‐Mbeumi, S., Chamcheu, R. N., Walker, A. L., Liu, Y., & Huang, S. (2019) · Cells · doi:10.3390/cells8080803 · Cited by 212
Mechanisms of Selective Autophagy in Normal Physiology and Cancer
Mancias, J. D., & Kimmelman, A. C. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.02.027 · Cited by 196
PI3K therapy reprograms mitochondrial trafficking to fuel tumor cell invasion
Caino, M. C., Ghosh, J. C., Chae, Y. C., Vaira, V., Rivadeneira, D. B., Faversani, A., Rampini, P. M., Kossenkov, A. V., Aird, K. M., Zhang, R., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1500722112 · Cited by 204
Extracellular Matrices and Cancer-Associated Fibroblasts: Targets for Cancer Diagnosis and Therapy?
Belhabib, I., Zaghdoudi, S., Lac, C., Bousquet, C., & Jean, C. (2021) · Cancers · doi:10.3390/cancers13143466 · Cited by 210
Self-citationAutophagy and epithelial–mesenchymal transition: an intricate interplay in cancer
Gugnoni, M., Sancisi, V., Manzotti, G., Gandolfi, G., & Ciarrocchi, A. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.415 · Cited by 205
Mechanisms and context underlying the role of autophagy in cancer metastasis
Dower, C. M., Wills, C. A., Frisch, S. M., & Wang, H. (2018) · Autophagy · doi:10.1080/15548627.2018.1450020 · Cited by 196
Shen, M., Jiang, Y., Wei, Y., Ell, B. J., Sheng, X., Esposito, M., Kang, J., Hang, X., Zheng, H., Rowicki, M., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2018.11.016 · Cited by 203
Yuzhalin, A. E., Gordon-Weeks, A. N., Tognoli, M. L., Jones, K. I., Markelc, B., Konietzny, R., Fischer, R., Muth, A., O’Neill, E. E., Thompson, P. R., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07306-7 · Cited by 195
Dynamic interplay between tumour, stroma and immune system can drive or prevent tumour progression
Seager, R. J., Hajal, C., Spill, F., Kamm, R. D., & Zaman, M. H. (2017) · Convergent Science Physical Oncology · doi:10.1088/2057-1739/aa7e86 · Cited by 192
Thakur, R. K., Trivedi, R., Rastogi, N., Singh, M., & Mishra, D. P. (2015) · Scientific Reports · doi:10.1038/srep10194 · Cited by 187
FAK in Cancer: From Mechanisms to Therapeutic Strategies
Chuang, H.-H., Zhen, Y., Tsai, Y.-C., Chuang, C., Hsiao, M., Huang, M., & Yang, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031726 · Cited by 193
EZH2 engages TGFβ signaling to promote breast cancer bone metastasis via integrin β1-FAK activation
Zhang, L., Qu, J., Qi, Y., Duan, Y., Huang, Y.-W., Zhou, Z., Li, P., Yao, J., Huang, B., Zhang, S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30105-0 · Cited by 182
Izumi, D., Ishimoto, T., Miyake, K., Sugihara, H., Eto, K., Sawayama, H., Yasuda, T., Kiyozumi, Y., Kaida, T., Kurashige, J., et al. (2015) · International Journal of Cancer · doi:10.1002/ijc.29864 · Cited by 188
Matrix Stiffness: the Conductor of Organ Fibrosis
Santos, A., & Lagares, D. (2018) · Current Rheumatology Reports · doi:10.1007/s11926-018-0710-z · Cited by 183
ECM stiffness-tuned exosomes drive breast cancer motility through thrombospondin-1
Patwardhan, S., Mahadik, P., Shetty, O. A., & Sen, S. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.121185 · Cited by 183
FAK controls the mechanical activation of YAP, a transcriptional regulator required for durotaxis
Lachowski, D., Cortes, E., Robinson, B., Rice, A., Rombouts, K., & Del Río Hernández, A. E. (2018) · The FASEB Journal · doi:10.1096/fj.201700721r · Cited by 175
Zhang, H., Schaefer, A., Wang, Y., Hodge, R. G., Blake, D. R., Diehl, J. N., Papageorge, A. G., Stachler, M. D., Liao, J., Zhou, J. R., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-0811 · Cited by 170
Recent Advances in Pyrimidine-Based Drugs
Nammalwar, B., & Bunce, R. A. (2024) · Pharmaceuticals · doi:10.3390/ph17010104 · Cited by 171
RUNX2 and the PI3K/AKT axis reciprocal activation as a driving force for tumor progression
Cohen-Solal, K., Boregowda, R. K., & Lasfar, A. (2015) · Molecular Cancer · doi:10.1186/s12943-015-0404-3 · Cited by 170
Wu, C. Y.-J., Chen, C., Lin, C., Feng, L.-Y., Lin, Y., Wei, K., Huang, C.-Y., Fang, J., & Chen, P. (2019) · Neuro-Oncology · doi:10.1093/neuonc/noz189 · Cited by 165
Angiopoietin-2 exacerbates cardiac hypoxia and inflammation after myocardial infarction
Lee, S.-J., Lee, C.-K., Kang, S., Park, I., Kim, Y. H., Kim, S. K., Hong, S. P., Bae, H., He, Y., Kubota, Y., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci99659 · Cited by 164
Glycogen synthase kinase‐3β is a pivotal mediator of cancer invasion and resistance to therapy
Domoto, T., Pyko, I. V., Furuta, T., Miyashita, K., Uehara, M., Shimasaki, T., Nakada, M., & Minamoto, T. (2016) · Cancer Science · doi:10.1111/cas.13028 · Cited by 161
Focal adhesion kinase: from biological functions to therapeutic strategies
Tan, X., Yan, Y., Song, B., Zhu, S., Mei, Q., & Wu, K. (2023) · Experimental Hematology & Oncology · doi:10.1186/s40164-023-00446-7 · Cited by 158
Cancer associated fibroblast FAK regulates malignant cell metabolism
Demircioglu, F., Wang, J., Candido, J. B., Costa, A. S. H., Casado, P., de Luxán‐Delgado, B., Reynolds, L. E., Gómez-Escudero, J., Newport, E., Rajeeve, V., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15104-3 · Cited by 158
Decoding leader cells in collective cancer invasion
Mercedes, S. A. V., Bocci, F., Levine, H., Onuchic, J. N., Jolly, M. K., & Wong, P. K. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00376-8 · Cited by 153
MMP proteolytic activity regulates cancer invasiveness by modulating integrins
Das, A., Monteiro, M., Barai, A., Kumar, S., & Sen, S. (2017) · Scientific Reports · doi:10.1038/s41598-017-14340-w · Cited by 156
Du, H., Zhang, X., Zeng, Y., Huang, X., Chen, H., Wang, S., Wu, J., Li, Q., Zhu, W., Li, H., et al. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01620 · Cited by 150
Soria, J., Gan, H. K., Blagden, S. P., Plummer, R., Arkenau, H., Ranson, M., Evans, T. R. J., Zalcman, G., Bahleda, R., Hollebecque, A., et al. (2016) · Annals of Oncology · doi:10.1093/annonc/mdw427 · Cited by 148
Annexin A2 and cancer: A systematic review
Christensen, M., Høgdall, C. K., Jochumsen, K. M., & Høgdall, E. V. S. (2017) · International Journal of Oncology · doi:10.3892/ijo.2017.4197 · Cited by 148
FAK activity sustains intrinsic and acquired ovarian cancer resistance to platinum chemotherapy
Diaz Osterman, C. J., Ozmadenci, D., Kleinschmidt, E. G., Taylor, K. N., Barrie, A. M., Jiang, S., Bean, L. M., Sulzmaier, F. J., Jean, C., Tancioni, I., et al. (2019) · eLife · doi:10.7554/elife.47327 · Cited by 145
Self-citationDynamic matrisome: ECM remodeling factors licensing cancer progression and metastasis
Yuzhalin, A. E., Lim, S. Y., Kutikhin, A. G., & Gordon-Weeks, A. N. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.09.002 · Cited by 147
Mechano-therapeutics: Targeting Mechanical Signaling in Fibrosis and Tumor Stroma
Tschumperlin, D. J., & Lagares, D. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107575 · Cited by 146
Small Molecule Kinase Inhibitors for the Treatment of Brain Cancer
Heffron, T. P. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00618 · Cited by 144
Popow, J., Arnhof, H., Bader, G., Berger, H., Ciulli, A., Covini, D., Dank, C., Gmaschitz, T., Greb, P., Karolyi-Özguer, J., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01826 · Cited by 138
Complementary Alu sequences mediate enhancer–promoter selectivity
Liang, L., Cao, C., Ji, L., Cai, Z., Wang, D., Ye, R., Chen, J., Yu, X., Zhou, J., Bai, Z., et al. (2023) · Nature · doi:10.1038/s41586-023-06323-x · Cited by 147
Kamarajan, P., Ateia, I., Shin, J. M., Fenno, J. C., Le, C., Zhan, L., Chang, A., Darveau, R., & Kapila, Y. L. (2020) · PLOS Pathogens · doi:10.1371/journal.ppat.1008881 · Cited by 134
Apoptosis induced by luteolin in breast cancer: Mechanistic and therapeutic perspectives
Ahmed, S., Khan, H. Z., Fratantonio, D., Hasan, M. M., Sharifi, S., Fathi, N., Ullah, H., & Rastrelli, L. (2019) · Phytomedicine · doi:10.1016/j.phymed.2019.152883 · Cited by 134
Mekhdjian, A. H., Kai, F., Rubashkin, M. G., Prahl, L. S., Przybyla, L., McGregor, A., Bell, E. S., Barnes, J. M., DuFort, C. C., Ou, G., et al. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-09-0654 · Cited by 140
Siu, M. K. Y., Jiang, Y., Wang, J., Leung, T., Han, C. Y., Tsang, B. K., Cheung, A., Ngan, H., & Chan, K. K. L. (2019) · Cancers · doi:10.3390/cancers11060813 · Cited by 135
Development of resistance to FAK inhibition in pancreatic cancer is linked to stromal depletion
Jiang, H., Liu, X., Knolhoff, B. L., Hegde, S., Lee, K. B., Jiang, H., Fields, R. C., Pachter, J. A., Lim, K.-H., & DeNardo, D. G. (2020) · Gut · doi:10.1136/gutjnl-2018-317424 · Cited by 130
Angiogenesis biomarkers and their targeting ligands as potential targets for tumor angiogenesis
Mashreghi, M., Azarpara, H., Bazaz, M. R., Jafari, A., Masoudifar, A., Mirzaei, H., & Jaafari, M. R. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26049 · Cited by 129
Cowan, A. D., & Ciulli, A. (2022) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-032620-104421 · Cited by 136
Chan, K. K. L., Siu, M. K. Y., Jiang, Y., Wang, J., Leung, T. H. Y., & Ngan, H. (2018) · Cancer Cell International · doi:10.1186/s12935-018-0559-2 · Cited by 126
Immune therapies in pancreatic ductal adenocarcinoma: Where are we now?
Hilmi, M., Bartholin, L., & Neuzillet, C. (2018) · World Journal of Gastroenterology · doi:10.3748/wjg.v24.i20.2137 · Cited by 126
PD-L1 on invasive fibroblasts drives fibrosis in a humanized model of idiopathic pulmonary fibrosis
Geng, Y., Liu, X., Liang, J., Habiel, D. M., Kulur, V., Coelho, A. L., Deng, N., Xie, T., Wang, Y., Liu, N., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.125326 · Cited by 127
CXCL8 in Tumor Biology and Its Implications for Clinical Translation
Xiong, X., Liao, X., Qiu, S., Xu, H., Zhang, S., Wang, S., Ai, J., & Yang, L. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.723846 · Cited by 129
An Experimenter’s Guide to Glioblastoma Invasion Pathways
de Gooijer, M. C., Navarro, M. G., Bernards, R., Würdinger, T., & van Tellingen, O. (2018) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2018.07.003 · Cited by 129
Discovery and Characterisation of Highly Cooperative FAK‐Degrading PROTACs
Law, R. P., Nunes, J., Chung, C., Bantscheff, M., Buda, K., Dai, H., Evans, J. P., Flinders, A., Klimaszewska, D., Lewis, A. J., et al. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202109237 · Cited by 122
Targeting of proangiogenic signalling pathways in chronic inflammation
Tas, S. W., Maracle, C. X., Balogh, E., & Szekanecz, Z. (2015) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2015.164 · Cited by 123
Glioblastoma: Current Status, Emerging Targets, and Recent Advances
Thakur, A., Faujdar, C., Sharma, R., Sharma, S., Malik, B., Nepali, K., & Liou, J. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01946 · Cited by 122
Cancer Metastasis: A Reappraisal of Its Underlying Mechanisms and Their Relevance to Treatment
Riggi, N., Aguet, M., & Stamenkovic, I. (2017) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-020117-044127 · Cited by 121
FAK/PYK2 promotes the Wnt/β-catenin pathway and intestinal tumorigenesis by phosphorylating GSK3β
Gao, C., Chen, G., Kuan, S., Zhang, D. H., Schlaepfer, D. D., & Hu, J. (2015) · eLife · doi:10.7554/elife.10072 · Cited by 118
Self-citationExtracellular Matrix Components and Mechanosensing Pathways in Health and Disease
Berdiaki, A., Neagu, M. T., Tzanakakis, P., Spyridaki, I., Pérez, S., & Nikitovic, D. (2024) · Biomolecules · doi:10.3390/biom14091186 · Cited by 117
Song, X., Xu, H., Wang, P., Wang, J., Affò, S., Wang, H., Xu, M. M., Liang, B.-Y., Che, L., Qiu, W., et al. (2021) · Journal of Hepatology · doi:10.1016/j.jhep.2021.05.018 · Cited by 117
Lander, V. E., Belle, J. I., Kingston, N. L., Herndon, J. M., Hogg, G. D., Liu, X., Kang, L.-I., Knolhoff, B. L., Bogner, S. J., Baer, J. M., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-22-0192 · Cited by 114
FAK and paxillin, two potential targets in pancreatic cancer
Kanteti, R., Batra, S. K., Lennon, F. E., & Salgia, R. (2016) · Oncotarget · doi:10.18632/oncotarget.8040 · Cited by 121
Li, Z., Zheng, Z., Wei, Z.-H., Zhang, L., Li, F., Lin, L., Liu, R., Huang, X., Lv, J., Chen, F., et al. (2019) · Theranostics · doi:10.7150/thno.36585 · Cited by 114
Miller, A. E., Hu, P., & Barker, T. H. (2020) · Advanced Healthcare Materials · doi:10.1002/adhm.201901445 · Cited by 119
Bourgot, I., Primac, I., Louis, T., Noël, A., & Maquoi, E. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01488 · Cited by 113
Balsas, P., Palomero, J., Eguileor, Á., Rodríguez, M. L., Vegliante, M. C., Planas‐Rigol, E., Sureda-Gómez, M., Cid, M. C., Campo, E., & Amador, V. (2017) · Blood · doi:10.1182/blood-2017-04-776740 · Cited by 112
Metadata
- Authors
- Sulzmaier, F. J., Jean, C., & Schlaepfer, D. D.
- Affiliations
- University of California San Diego (US)
- Corresponding author
- Schlaepfer, David D.
- Venue
- Nature Reviews Cancer
- Published
- 2014-08-07
- Volume
- 14
- Issue
- 9
- Pages
- 598-610
- ISSN
- 1474-175X (ISSN-L)
- 1474-1768
- PMC
- PMC4365862
- OpenAlex
- W2044423100
- Cited by
- 1,381
- References
- 142
- Citations by year
- 2026: 92 · 2025: 85 · 2024: 131 · 2023: 111 · 2022: 147 · 2021: 154 · 2020: 144 · 2019: 122 · 2018: 105 · 2017: 128 · 2016: 91 · 2015: 63 · 2014: 6
- FWCI
- 12.73
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature reviews. Cancer (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- HAL (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- American Heart Association
- Verastem Oncology
- National Institutes of Health
- National Cancer Institute (R01CA102310, CA102310, R01CA180769, CA180769, T32CA121938)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Oncology › Cancer Cells and Metastasis
- Keywords
- focal adhesion kinase, FAK inhibitors, tumor microenvironment, tumor stromal cells, metastasis, tumor progression, cancer stem cells, cell invasion, cell migration, small molecule inhibitors, clinical development
- MeSH terms
- Animals, Humans, Neoplasm Invasiveness, Neoplasms, Signal Transduction, Stromal Cells, Protein Kinase Inhibitors, Focal Adhesion Kinase 1, Small Molecule Libraries, Molecular Targeted Therapy, Tumor Microenvironment
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