FAK inhibitors in Cancer, a patent review

Cell mechanics and the cytoskeleton

Fletcher, D. A., & Mullins, R. D. (2010) · Nature · doi:10.1038/nature08908 · Cited by 3,021 · see citing works

Focal adhesion kinase: in command and control of cell motility

Mitra, S. K., Hanson, D. R., & Schlaepfer, D. D. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1549 · Cited by 2,586 · see citing works

Focal adhesion kinase: the first ten years

Parsons, J. T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00373 · Cited by 1,364 · see citing works

Clinical Cancer Research

Horder, & Harnett, W. L. (1941) · BMJ · doi:10.1136/bmj.1.4186.493 · Cited by 1,319 · see citing works

Signaling through focal adhesion kinase

Schlaepfer, D. D., Hauck, C. R., & Sieg, D. J. (1999) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(98)00052-2 · Cited by 1,180 · see citing works

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 · see citing works

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 606 · see citing works

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 599 · see citing works

Nuclear FAK Controls Chemokine Transcription, Tregs, and Evasion of Anti-tumor Immunity

Serrels, A., Lund, T., Serrels, B., Byron, A., McPherson, R. C., von Kriegsheim, A., Gómez-Cuadrado, L., Canel, M., Muir, M., Ring, J. E., et al. (2015) · Cell · doi:10.1016/j.cell.2015.09.001 · Cited by 407 · see citing works

Antitumor Activity and Pharmacology of a Selective Focal Adhesion Kinase Inhibitor, PF-562,271

Roberts, W. G., Ung, E. J., Whalen, P. M., Cooper, B. A., Hulford, C. A., Autry, C., Richter, D., Emerson, E., Lin, J., Kath, J. C., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5155 · Cited by 381 · see citing works

The FERM domain: organizing the structure and function of FAK

Frame, M. C., Patel, H., Serrels, B., Lietha, D., & Eck, M. J. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2996 · Cited by 372 · see citing works

Expression of focal adhesion kinase gene and invasive cancer

Weiner, T. M., Craven, R. J., Cance, W. G., & Liu, E. T. (1993) · The Lancet · doi:10.1016/0140-6736(93)92881-s · Cited by 339 · see citing works

Increased dosage and amplification of the focal adhesion kinase gene in human cancer cells

Agochiya, M., Brunton, V. G., Owens, D. W., Parkinson, E. K., Paraskeva, C., Keith, W. N., & Frame, M. C. (1999) · Oncogene · doi:10.1038/sj.onc.1202957 · Cited by 240 · see citing works

Overexpression of focal adhesion kinase, a protein tyrosine kinase, in ovarian carcinoma

Judson, P. L., He, X., Cance, W. G., & Le, L. V. (1999) · Cancer · doi:10.1002/(sici)1097-0142(19991015)86:6 · Cited by 181 · see citing works

Focal adhesion kinase and tumour angiogenesis

Lechertier, T., & Hodivala‐Dilke, K. (2011) · The Journal of Pathology · doi:10.1002/path.3018 · Cited by 169 · see citing works

Overexpression of focal adhesion kinase in primary colorectal carcinomas and colorectal liver metastases: immunohistochemistry and real-time PCR analyses.

Lark, A. L., Livasy, C., Calvo, B. F., Caskey, L. S., Moore, D., Yang, X., & Cance, W. G. (2003) · PubMed · Cited by 169 · see citing works

Proline-rich tyrosine kinase 2 regulates osteoprogenitor cells and bone formation, and offers an anabolic treatment approach for osteoporosis

Buckbinder, L., Crawford, D. T., Qi, H., Ke, H. Z., OLSON, L. M., Long, K. R., Bonnette, P. C., Baumann, A. P., Hambor, J., GRASSER, W. A., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701421104 · Cited by 163 · see citing works

Requirement for Focal Adhesion Kinase in the Early Phase of Mammary Adenocarcinoma Lung Metastasis Formation

van Nimwegen, M. J., Verkoeijen, S., van Buren, L., Burg, D., & van de Water, B. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4126 · Cited by 131 · see citing works

Determinants of age at menarche as early life predictors of breast cancer risk

Petridou, E. T., Syrigou, E. K. I., Toupadaki, N., Zavitsanos, X., Willett, W. C., & Trichopoulos, D. (1996) · International Journal of Cancer · doi:10.1002/(sici)1097-0215(19961009)68:2 · Cited by 121 · see citing works

Overexpression of Focal Adhesion Kinase in Head and Neck Squamous Cell Carcinoma Is Independent of fak Gene Copy Number

Canel, M., Secades, P., Rodrigo, J. P., Cabanillas, R., Herrero, A., Suarez, C. M., & Chiara, M. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-1583 · Cited by 116 · see citing works

Structural Characterization of Proline-rich Tyrosine Kinase 2 (PYK2) Reveals a Unique (DFG-out) Conformation and Enables Inhibitor Design

Han, S., Mistry, A., Chang, J. S., Cunningham, D., Griffor, M., Bonnette, P. C., Wang, H., Chrunyk, B. A., Aspnes, G. E., Walker, D. P., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809038200 · Cited by 110 · see citing works

Focal Adhesion Kinase as a Cancer Therapy Target

Golubovskaya, V. (2010) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152010794728648 · Cited by 105 · see citing works

Nuclear-localized focal adhesion kinase regulates inflammatory VCAM-1 expression

Lim, S., Miller, N. L. G., Chen, X. L., Tancioni, I., Walsh, C. T., Lawson, C., Uryu, S. A., Weis, S. M., Cheresh, D. A., & Schlaepfer, D. D. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201109067 · Cited by 105 · see citing works

Targeting focal adhesion kinase signaling in tumor growth and metastasis

Schwock, J., Dhani, N. C., & Hedley, D. W. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220903460340 · Cited by 103 · see citing works

The role of FAK in tumor metabolism and therapy

Zhang, J., & Hochwald, S. N. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.12.003 · Cited by 102 · see citing works

Discovery of Clinical Candidate CEP-37440, a Selective Inhibitor of Focal Adhesion Kinase (FAK) and Anaplastic Lymphoma Kinase (ALK)

Ott, G. R., Cheng, M. M., Learn, K. S., Wagner, J., Gingrich, D. E., Lisko, J. G., Curry, M. A., Mesaros, E. F., Ghose, A. K., Quail, M. R., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00487 · Cited by 97 · see citing works

Therapeutic potential and limitations of new FAK inhibitors in the treatment of cancer

Schultze, A., & Fiedler, W. (2010) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2010.489548 · Cited by 94 · see citing works

Sulfoximine-substituted trifluoromethylpyrimidine analogs as inhibitors of proline-rich tyrosine kinase 2 (PYK2) show reduced hERG activity

Walker, D. P., Zawistoski, M. P., McGlynn, M. A., Li, J., Kung, D. W., Bonnette, P. C., Baumann, A. P., Buckbinder, L., Houser, J. A., Boer, J., et al. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.04.093 · Cited by 88 · see citing works

Focal adhesion kinase inhibitors are potent anti‐angiogenic agents

Cabrita, M. A., Jones, L., Quizi, J. L., Sabourin, L. A., McKay, B. C., & Addison, C. (2011) · Molecular Oncology · doi:10.1016/j.molonc.2011.10.004 · Cited by 86 · see citing works

Design, Synthesis, and Evaluation of Novel Imidazo[1,2- a ][1,3,5]triazines and Their Derivatives as Focal Adhesion Kinase Inhibitors with Antitumor Activity

Dao, P., Smith, N., Tomkiewicz, C., Yen‐Pon, E., Camacho‐Artacho, M., Lietha, D., Herbeuval, J.-P., Coumoul, X., Garbay, C., & Chen, H. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500784e · Cited by 62 · see citing works

Structure-based discovery of cellular-active allosteric inhibitors of FAK

Tomita, N., Hayashi, Y., Suzuki, S., Oomori, Y., Aramaki, Y., Matsushita, Y., Iwatani, M., Iwata, H., Okabe, A., Awazu, Y., et al. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.01.047 · Cited by 57 · see citing works

Trifluoromethylpyrimidine-based inhibitors of proline-rich tyrosine kinase 2 (PYK2): Structure–activity relationships and strategies for the elimination of reactive metabolite formation

Walker, D. P., Bi, F. C., Kalgutkar, A. S. S., Bauman, J. N., Zhao, S. X., Soglia, J. R., Aspnes, G. E., Kung, D. W., Klug-McLeod, J. L., Zawistoski, M. P., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.10.030 · Cited by 57 · see citing works

Discovery and characterization of novel allosteric FAK inhibitors

Iwatani, M., Iwata, H., Okabe, A., Skene, R. J., Tomita, N., Hayashi, Y., Aramaki, Y., Hosfield, D. J., Hori, A., Baba, A., et al. (2012) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2012.06.035 · Cited by 54 · see citing works

Nuclear FAK and Runx1 Cooperate to Regulate IGFBP3, Cell-Cycle Progression, and Tumor Growth

Canel, M., Byron, A., Sims, A. H., Cartier, J., Patel, H., Frame, M. C., Brunton, V. G., Serrels, B., & Serrels, A. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-0418 · Cited by 54 · see citing works

Synthesis of novel 1,2,4-triazine scaffold as FAK inhibitors with antitumor activity

Dao, P., Lietha, D., Ethève‐Quelquejeu, M., Garbay, C., & Chen, H. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.02.072 · Cited by 52 · see citing works

Scaffold mining of kinase hinge binders in crystal structure database

Xing, L., Rai, B., & Lunney, E. A. (2013) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-013-9700-4 · Cited by 42 · see citing works

Design, synthesis and biological evaluation of sulfonamide-substituted diphenylpyrimidine derivatives (Sul-DPPYs) as potent focal adhesion kinase (FAK) inhibitors with antitumor activity

Qu, M., Liu, Z., Zhao, D. Y., Wang, C., Zhang, J., Tang, Z., Liu, K., Shu, X. H., Yuan, H., & Ma, X. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.05.044 · Cited by 39 · see citing works

Ambra1 spatially regulates Src activity and Src/FAK-mediated cancer cell invasion via trafficking networks

Schoenherr, C., Byron, A., Sandilands, E., Paliashvili, K., Baillie, G. S., García-Muñoz, A., Valacca, C., Cecconi, F., Serrels, B., & Frame, M. C. (2017) · eLife · doi:10.7554/elife.23172 · Cited by 38 · see citing works

Development of Focal Adhesion Kinase Inhibitors in Cancer Therapy

Ma, W. W. (2011) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152011796817628 · Cited by 37 · see citing works

Selectivity switch between FAK and Pyk2: Macrocyclization of FAK inhibitors improves Pyk2 potency

Farand, J., Mai, N., Chandrasekhar, J., Newby, Z. E. R., Veldhuizen, J. J. V., Loyer-Drew, J., Venkataramani, C., Guerrero, J., Kwok, A., Li, N., et al. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.10.092 · Cited by 37 · see citing works

TAE226-mediated inhibition of focal adhesion kinase interferes with tumor angiogenesis and vasculogenesis

Schultze, A., Decker, S., Otten, J., Horst, A. K., Vohwinkel, G., Schuch, G., Bokemeyer, C., Loges, S., & Fiedler, W. (2009) · Investigational New Drugs · doi:10.1007/s10637-009-9326-5 · Cited by 35 · see citing works

FAK goes nuclear to control antitumor immunity—a new target in cancer immuno-therapy

Serrels, A., & Frame, M. C. (2016) · OncoImmunology · doi:10.1080/2162402x.2015.1119356 · Cited by 18 · see citing works

The Extracellular Matrix Modulates the Metastatic Journey

Kai, F., Drain, A. P., & Weaver, V. M. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.03.026 · Cited by 537 · see citing works

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 · see citing works

Epigallocatechin-3-Gallate Therapeutic Potential in Cancer: Mechanism of Action and Clinical Implications

Kciuk, M., Alam, M., Ali, N., Rashid, S., Głowacka, P., Rajamanikandan, S., Çeli̇k, İ., Yahya, E. B., Dubey, A., Zerroug, E., et al. (2023) · Molecules · doi:10.3390/molecules28135246 · Cited by 148 · see citing works

Targeting Lysyl Oxidase Family Meditated Matrix Cross-Linking as an Anti-Stromal Therapy in Solid Tumours

Setargew, Y. F. I., Wyllie, K., Grant, R. D., Chitty, J. L., & Cox, T. R. (2021) · Cancers · doi:10.3390/cancers13030491 · Cited by 112 · see citing works

Hydrogel dressing integrating FAK inhibition and ROS scavenging for mechano-chemical treatment of atopic dermatitis

Jia, Y., Hu, J., An, K., Zhao, Q., Dang, Y., Liu, H., Zhao, W., Geng, S., & Xu, F. (2023) · Nature Communications · doi:10.1038/s41467-023-38209-x · Cited by 108 · see citing works

Endogenous Control Mechanisms of FAK and PYK2 and Their Relevance to Cancer Development

Naser, R., Aldehaiman, A., Díaz‐Galicia, E., & Arold, S. T. (2018) · Cancers · doi:10.3390/cancers10060196 · Cited by 87 · see citing works

Rac1: A Regulator of Cell Migration and a Potential Target for Cancer Therapy

Ma, N., Xu, E., Luo, Q., & Song, G. (2023) · Molecules · doi:10.3390/molecules28072976 · Cited by 87 · see citing works

A FAK/HDAC5 signaling axis controls osteocyte mechanotransduction

Sato, T., Verma, S., Andrade, C. D. C., Omeara, M., Campbell, N., Wang, J. S., Cetinbas, M., Lang, A., Ausk, B. J., Brooks, D. J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17099-3 · Cited by 86 · see citing works

Focal Adhesion Kinase (FAK) Inhibition Synergizes with KRAS G12C Inhibitors in Treating Cancer through the Regulation of the FAK–YAP Signaling

Zhang, B., Zhang, Y., Zhang, J., Liu, P., Jiao, B., Wang, Z., & Ren, R. (2021) · Advanced Science · doi:10.1002/advs.202100250 · Cited by 83 · see citing works

Structural basis of Focal Adhesion Kinase activation on lipid membranes

Acebrón, I., Righetto, R. D., Schoenherr, C., de Buhr, S., Redondo, P. N., Culley, J., Rodríguez, C. F., Daday, C., Biyani, N., Llorca, Ó., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2020104743 · Cited by 78 · see citing works

Structure-kinetic relationship reveals the mechanism of selectivity of FAK inhibitors over PYK2

Berger, B., Amaral, M., Kokh, D. B., Nunes‐Alves, A., Müsil, D., Heinrich, T., Schröder, M., Neil, R., Wang, J., Navratilova, I. H., et al. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.01.003 · Cited by 78 · see citing works

The Crosstalk between FAK and Wnt Signaling Pathways in Cancer and Its Therapeutic Implication

Wörthmüller, J., & Rüegg, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239107 · Cited by 74 · see citing works

CCR9 and CCL25: A review of their roles in tumor promotion

Xu, B., Deng, C., Wu, X., Ji, T., Zhao, L., Han, Y., Yang, W., Qi, Y., Wang, Z., Yang, Z. P., et al. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29782 · Cited by 61 · see citing works

Targeting focal adhesion kinase (FAK) for cancer therapy: FAK inhibitors, FAK-based dual-target inhibitors and PROTAC degraders

Yang, M. J., Xiang, H., & Luo, G. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116246 · Cited by 56 · see citing works

Focal Adhesion Kinase Fine Tunes Multifaced Signals toward Breast Cancer Progression

Rigiracciolo, D. C., Cirillo, F., Talia, M., Muglia, L., Gutkind, J. S., Maggiolini, M., & Lappano, R. (2021) · Cancers · doi:10.3390/cancers13040645 · Cited by 53 · see citing works

Focal adhesion kinase: Insight into its roles and therapeutic potential in oesophageal cancer

Zhang, Y., Liu, S., Zhou, S. F., Yu, D., Gu, J., Qin, Q., Cheng, Y., & Sun, X. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.10.005 · Cited by 49 · see citing works

Discovery of 2,4-diarylaminopyrimidine derivatives bearing dithiocarbamate moiety as novel FAK inhibitors with antitumor and anti-angiogenesis activities

Su, Y., Li, R., Ning, X., Lin, Z., Zhao, X., Zhou, J., Liu, J., Jin, Y., & Yin, Y. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.05.048 · Cited by 48 · see citing works

Design, Synthesis, and Biological Evaluation of Covalent Inhibitors of Focal Adhesion Kinase (FAK) against Human Malignant Glioblastoma

Li, B., Li, Y., Tomkiewicz-Raulet, C., Dao, P., Lietha, D., Yen‐Pon, E., Du, Z., Coumoul, X., Garbay, C., Ethève‐Quelquejeu, M., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01059 · Cited by 48 · see citing works

Focal adhesion kinase inhibition synergizes with nab-paclitaxel to target pancreatic ductal adenocarcinoma

Large, T. Y. S. L., Bijlsma, M. F., Hassouni, B. E., Mantini, G., Lagerweij, T., Henneman, A. A., Funel, N., Kok, B., Pham, T. V., Haas, R. D. G.-D., et al. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-01892-z · Cited by 44 · see citing works

HGF-mediated elevation of ETV1 facilitates hepatocellular carcinoma metastasis through upregulating PTK2 and c-MET

Zhang, T., Wang, Y., Xie, M., Ji, X., Luo, X., Chen, X., Zhang, B., Liu, D., Feng, Y., Sun, M., et al. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02475-2 · Cited by 45 · see citing works

1,3,4-Oxadiazole Containing Compounds As Therapeutic Targets For Cancer Therapy

Ahsan, M. J. (2021) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557521666210226145837 · Cited by 43 · see citing works

SerpinB2 inhibits migration and promotes a resolution phase signature in large peritoneal macrophages

Schroder, W. A., Hirata, T. D. C., Le, T. T., Gardner, J., Boyle, G. M., Ellis, J. J., Nakayama, E., Pathirana, D., Nakaya, H. I., & Suhrbier, A. (2019) · Scientific Reports · doi:10.1038/s41598-019-48741-w · Cited by 43 · see citing works

Novel imidazo[2,1‐b]thiazole‐based anticancer agents as potential focal adhesion kinase inhibitors: Synthesis, in silico and in vitro evaluation

Başoğlu, F., Ulusoy-Güzeldemirci, N., Akalın-Çiftçi, G., Çetinkaya, S., & Ece, A. (2021) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13896 · Cited by 43 · see citing works

Focal adhesion kinase inhibitors in the treatment of solid tumors: Preclinical and clinical evidence

Quispe, P. A., Lavecchia, M. J., & León, I. E. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.11.025 · Cited by 40 · see citing works

ITK inhibition induced in vitro and in vivo anti-tumor activity through downregulating TCR signaling pathway in malignant T cell lymphoma

Liu, Y., Wang, X., Deng, L., Ping, L., Shi, Y., Zheng, W., Lin, N., Wang, X., Tu, M., Xie, Y., et al. (2019) · Cancer Cell International · doi:10.1186/s12935-019-0754-9 · Cited by 42 · see citing works

Rhodium(III)–Picolinamide Complexes Act as Anticancer and Antimetastasis Agents via Inducing Apoptosis and Autophagy

Gu, Y., Yang, K., Yang, Q., Li, H., Hu, M., Ma, M., Chen, N.-F., Liu, Y.-H., Liang, H., & Chen, Z. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00318 · Cited by 41 · see citing works

FAK is Required for Tumor Metastasis-Related Fluid Microenvironment in Triple-Negative Breast Cancer

Pan, M., Hou, M., Ou‐Yang, F., Wu, C., Chang, S., Hung, W., Yip, H., & Luo, C. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8010038 · Cited by 42 · see citing works

The dual FAK-HDAC inhibitor MY-1259 displays potent activities in gastric cancers in vitro and in vivo

Song, J., Liu, X., Zhang, Y., Tian, X.-Y., Deng, M., Huang, C., & Zhang, S. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.106328 · Cited by 40 · see citing works

The HIPPO pathway in gynecological malignancies.

Wang, D., He, J., Dong, J., Meyer, T. F., & Xu, T. (2020) · PubMed Central · Cited by 40 · see citing works

Signalling involving MET and FAK supports cell division independent of the activity of the cell cycle-regulating CDK4/6 kinases

Zhang, C., Stockwell, S. R., Elbanna, M., Ketteler, R., Freeman, J., Al‐Lazikani, B., Eccles, S. A., Brandon, A. D. H., Raynaud, F. I., Hayes, A., et al. (2019) · Oncogene · doi:10.1038/s41388-019-0850-2 · Cited by 37 · see citing works

Integrating integrins with the hallmarks of cancer

Haake, S. M., Rios, B. L., Pozzi, A., & Zent, R. (2024) · Matrix Biology · doi:10.1016/j.matbio.2024.04.003 · Cited by 37 · see citing works

S100A16 induces epithelial-mesenchymal transition in human PDAC cells and is a new therapeutic target for pancreatic cancer treatment that synergizes with gemcitabine

Li, T., Ren, T., Huang, C., Li, Y., Yang, P., Che, G., Luo, L., Chen, Y., Peng, S., Lin, Y., et al. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114396 · Cited by 37 · see citing works

Focal adhesion kinase inhibitors, a heavy punch to cancer

Wu, Y., Li, N., Ye, C., Jiang, X., Luo, H., Zhang, B., Zhang, Y., & Zhang, Q. (2021) · Discover Oncology · doi:10.1007/s12672-021-00449-y · Cited by 36 · see citing works

Targeting focal adhesion kinase (FAK) in cancer therapy: A recent update on inhibitors and PROTAC degraders

Wang, X., Li, N., Liu, Y., Wu, J., Liu, Q.-G., Niu, J.-B., Xu, Y., Huang, C., Zhang, S., & Song, J. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116678 · Cited by 33 · see citing works

A multi-kinase inhibitor APG-2449 enhances the antitumor effect of ibrutinib in esophageal squamous cell carcinoma via EGFR/FAK pathway inhibition

Luo, Q.-Y., Zhou, S.-N., Pan, W., Sun, J., Yang, L., Zhang, L., Qiu, M., & Yang, D. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114318 · Cited by 31 · see citing works

A Review of in vitro Platforms for Understanding Cardiomyocyte Mechanobiology

Chin, I. L., Hool, L. C., & Choi, Y. S. (2019) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2019.00133 · Cited by 29 · see citing works

FAK displacement from focal adhesions: a promising strategy to target processes implicated in cancer progression and metastasis

Antoniades, I., Kyriakou, M., Charalambous, A., Kalalidou, K., Christodoulou, A., Christoforou, M., & Skourides, P. A. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-020-00671-1 · Cited by 30 · see citing works

Design, synthesis and evaluation of nitric oxide releasing derivatives of 2,4-diaminopyrimidine as novel FAK inhibitors for intervention of metastatic triple-negative breast cancer

Zhang, J., Xu, K., Yang, F., Qiu, Y., Li, J., Li, J., Wang, W., Tan, G., Zou, Z., & Kang, F. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115192 · Cited by 29 · see citing works

Dual roles of FAK in tumor angiogenesis: A review focused on pericyte FAK

Zhang, J., Li, W., Wang, W., Chen, Q., Xu, Z., Deng, M., Zhou, L., & He, G. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.175694 · Cited by 28 · see citing works

Use of Antiangiogenic Therapies in Pediatric Solid Tumors

Ollauri-Ibáñez, C., & Astigarraga, I. (2021) · Cancers · doi:10.3390/cancers13020253 · Cited by 27 · see citing works

A natural xanthone suppresses lung cancer growth and metastasis by targeting STAT3 and FAK signaling pathways

Zhao, Y., Zhang, X., Li, Y., Li, Y., Zhang, H., Song, Z., Xu, J., & Guo, Y. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154118 · Cited by 27 · see citing works

New Insights on Fak and Fak Inhibitors

Brullo, C., & Tasso, B. (2020) · Current Medicinal Chemistry · doi:10.2174/0929867327666201103162239 · Cited by 24 · see citing works

A prognostic model for oral squamous cell carcinoma using 7 genes related to tumor mutational burden

Wu, F., Du, Y., Hou, X., & Cheng, W. (2022) · BMC Oral Health · doi:10.1186/s12903-022-02193-3 · Cited by 24 · see citing works

The increased adhesion of tumor cells to endothelial cells after irradiation can be reduced by FAK-inhibition

Kouam, P. N., Bühler, H., Hero, T., & Adamietz, I. U. A. (2019) · Radiation Oncology · doi:10.1186/s13014-019-1230-3 · Cited by 24 · see citing works

Targeted delivery of FAK siRNA by engineered exosomes to reverse cetuximab resistance via activating paraptosis in colon cancer

Geng, Y., Xia, W., Zheng, X., Chen, L., Zhou, Y., Feng, J., Yuan, Y., Zhang, M., Lu, J., Wei, S., et al. (2024) · APOPTOSIS · doi:10.1007/s10495-024-01986-x · Cited by 23 · see citing works

Genistein Inhibits Proliferation and Metastasis in Human Cervical Cancer Cells through the Focal Adhesion Kinase Signaling Pathway: A Network Pharmacology-Based In Vitro Study in HeLa Cells

Chen, T., Wang, J., Li, M., Wu, Q., & Cui, S. (2023) · Molecules · doi:10.3390/molecules28041919 · Cited by 21 · see citing works

Targeting of focal adhesion kinase enhances the immunogenic cell death of PEGylated liposome doxorubicin to optimize therapeutic responses of immune checkpoint blockade

Zhang, B., Li, N., Gao, J., Zhao, Y., Jiang, J., Xie, S., Zhang, C., Zhang, Q., Liu, L., Wang, Z., et al. (2024) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-024-02974-4 · Cited by 22 · see citing works

LAMC1 attenuates neuronal apoptosis via FAK/PI3K/AKT signaling pathway after subarachnoid hemorrhage

Wu, Q., Yuan, K., Yao, Y., Yao, J., Shao, J., Meng, Y., Wu, P., & Shi, H. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114776 · Cited by 21 · see citing works

miR‑142‑5p inhibits pancreatic cancer cell migration and invasion by targeting PIK3CA

Zhu, J., Zhou, L., Wei, B., Qian, Z., Wang, J., Hui, H., & Sun, Y. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11251 · Cited by 21 · see citing works

Design, synthesis and biological evaluation of novel 2,4-diaminopyrimidine cinnamyl derivatives as inhibitors of FAK with potent anti-gastric cancer activities

Liu, Y., Kong, L.-J., Li, N., Liu, Y., Jia, M.-Q., Liu, Q.-G., Zhang, S., & Song, J. H. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2023.106895 · Cited by 20 · see citing works

Design, synthesis, and biological evaluation of novel covalent inhibitors targeting focal adhesion kinase

Chen, T., Liu, Y., Shi, M., Tang, M., Si, W., Yuan, X., Wen, Y., & Chen, L. (2021) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2021.128433 · Cited by 20 · see citing works

Oncogenic mechanisms of COL10A1 in cancer and clinical challenges (Review)

Yi, Q., Zhu, G., Zhu, W., Wang, J., Ouyang, X., Yang, K., & Zhong, J. (2024) · Oncology Reports · doi:10.3892/or.2024.8821 · Cited by 19 · see citing works

Chemical biology approaches targeting the actin cytoskeleton through phenotypic screening

Bryce, N. S., Hardeman, E. C., Gunning, P. W., & Lock, J. G. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.02.013 · Cited by 19 · see citing works

Design, Synthesis, Biological Evaluation, and Molecular Docking of 2,4-Diaminopyrimidine Derivatives Targeting Focal Adhesion Kinase as Tumor Radiotracers

Qi, Y., Li, Y., Fang, Y., Gao, H., Qiang, B., Wang, S., & Zhang, H. (2021) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.0c01088 · Cited by 19 · see citing works

Combined machine learning models, docking analysis, ADMET studies and molecular dynamics simulations for the design of novel FAK inhibitors against glioblastoma

Zhao, Y., He, X., & Wan, Q. (2024) · BMC Chemistry · doi:10.1186/s13065-024-01316-x · Cited by 18 · see citing works

Focal adhesion kinase (FAK): emerging target for drug-resistant malignant tumors

Aakriti, J., Vithalkar, M. P., Maity, S., Baby, K., Nagareddy, P. R., & Nayak, Y. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-10296-7 · Cited by 20 · see citing works

Design, synthesis and biological evaluation of novel FAK inhibitors with better selectivity over IR than TAE226

Chen, T., Liu, Y., Liu, J., Tang, M., Huang, H., Bai, C., Si, W., Yang, T., Yuan, X., Wen, Y., et al. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.105790 · Cited by 17 · see citing works

Combination Treatment of Retinoic Acid Plus Focal Adhesion Kinase Inhibitor Prevents Tumor Growth and Breast Cancer Cell Metastasis

Castro-Guijarro, A. C., Mondaca, J. M., Fernandez-Muñoz, J. M., Vanderhoeven, F., Uzair, I., Redondo, A. L., Zoppino, F. C. M., Sanchez, A. M., & Flamini, M. I. (2022) · Cells · doi:10.3390/cells11192988 · Cited by 17 · see citing works

AKT2S128/CCTαS315/319/323-positive cancer-associated fibroblasts (CAFs) mediate focal adhesion kinase (FAK) inhibitors resistance via secreting phosphatidylcholines (PCs)

Chen, J., Zhang, L., Zhu, Y., Zhao, D., Zhang, J., Zhu, Y., Pang, J., Xiao, Y., Wu, Q., Wang, Y., et al. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01728-6 · Cited by 16 · see citing works

Biomimetic MOF nanoplatform for dual-targeted co-delivery of FAK inhibitor and bismuth to enhance cervical cancer radiosensitivity

Chang, Y., Huang, K., Tang, H., Yao, Y., Min, J., Quan, H., Xu, K. W., Wang, H., Zhang, J., & Zhao, Y. (2025) · Advanced Composites and Hybrid Materials · doi:10.1007/s42114-025-01242-z · Cited by 16 · see citing works

The impact of glycolysis on ischemic stroke: from molecular mechanisms to clinical applications

Liu, Y., Hu, P., Cheng, H., Xu, F., & Ye, Y. (2025) · Frontiers in Neurology · doi:10.3389/fneur.2025.1514394 · Cited by 16 · see citing works

MSC-1186, a Highly Selective Pan-SRPK Inhibitor Based on an Exceptionally Decorated Benzimidazole-Pyrimidine Core

Schröder, M., Leiendecker, M., Grädler, U., Braun, J., Blum, A., Wanior, M., Berger, B., Krämer, A., Müller, S., Esdar, C., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01705 · Cited by 14 · see citing works

Cyclin G2 Inhibits Oral Squamous Cell Carcinoma Growth and Metastasis by Binding to IGFBP3 and Regulating the FAK-SRC-STAT Signaling Pathway

Wang, D., Gao, J., Zhao, C., Li, S., Zhang, D., Hou, X., Zhuang, X., Liu, Q., & Luo, Y. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.560572 · Cited by 14 · see citing works

FAK Signaling in Rhabdomyosarcoma

Perrone, C., Pomella, S., Cassandri, M., Braghini, M. R., Pezzella, M., Locatelli, F., & Rota, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228422 · Cited by 13 · see citing works

Design, synthesis and activity evaluation of isopropylsulfonyl-substituted 2,4- diarylaminopyrimidine derivatives as FAK inhibitors for the potential treatment of pancreatic cancer

Zheng, X., Li, X., Tian, L., Wu, B., Yu, J., Wang, C., Sun, X., Ma, X., Chen, L., & Li, Y. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114607 · Cited by 13 · see citing works

FAK inhibitor PF-562271 inhibits the migration and proliferation of high-grade serous ovarian cancer cells through FAK and FAK mediated cell cycle arrest

Pan, Q., Wang, Q., Zhao, T., Zhao, X., Liang, Y., Shi, M., Chen, C., & Lin, F. (2023) · Medical Oncology · doi:10.1007/s12032-023-02092-9 · Cited by 12 · see citing works

The Psoriasis Therapeutic Potential of a Novel Short Laminin Peptide C16

Ho, T., Yeh, S., Chen, S., & Tsao, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133144 · Cited by 12 · see citing works

Activation of Autophagy Induces Monocrotaline-Induced Pulmonary Arterial Hypertension by FOXM1-Mediated FAK Phosphorylation

Zhai, C., Zhang, N., Wang, J., Cao, M., Luan, J., Liu, H., Zhang, Q., Zhu, Y., Xue, Y., & Li, S. (2022) · Lung · doi:10.1007/s00408-022-00569-4 · Cited by 12 · see citing works

siRNA-based strategies to combat drug resistance in gastric cancer

Khaleel, A. Q., Alshahrani, M. Y., Rizaev, J. A., Malathi, H., Devi, S., Pramanik, A., Mustafa, Y. F., Hjazi, A. M., Muazzamxon, I., & Husseen, B. (2024) · Medical Oncology · doi:10.1007/s12032-024-02528-w · Cited by 10 · see citing works

Targeting Focal Adhesion Kinase in Lung Diseases: Current Progress and Future Directions

Wan, Z., Zhu, Z., Wang, P., Xu, X., Ma, T., Li, H., Li, L., Qian, F., & Gu, W. (2025) · Biomolecules · doi:10.3390/biom15091233 · Cited by 10 · see citing works

SY-707, an ALK/FAK/IGF1R inhibitor, suppresses growth and metastasis of breast cancer cells

Liu, P., Sun, Y., Liu, S., Niu, J., Liu, X., Li, B., & Chu, Q. (2022) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2022008 · Cited by 11 · see citing works

Modulation of Akt vs Stat3 activity by the focal adhesion kinase in non-neoplastic mouse fibroblasts

Geletu, M., Adan, H., Niit, M., Arulanandam, R., Carefoot, E., Hoskin, V., Sina, D., Elliott, B. E., Gunning, P. T., & Raptis, L. H. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112601 · Cited by 9 · see citing works

Biochemical Discovery, Intracellular Evaluation, and Crystallographic Characterization of Synthetic and Natural Product Adenosine 3′,5′-Cyclic Monophosphate-Dependent Protein Kinase A (PKA) Inhibitors

Wilson, B. A. P., Li, N., Fiesco, J. A. M., Dalilian, M., Wang, D., Smith, E. A., Wamiru, A., Shah, R., Goncharova, E. I., Beutler, J. A., et al. (2023) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.3c00010 · Cited by 9 · see citing works

An Update on Molecular Pathways Regulating Vasculogenic Mimicry in Human Osteosarcoma and Their Role in Canine Oncology

Massimini, M., Romanucci, M., Maria, R. D., & Salda, L. D. (2021) · Frontiers in Veterinary Science · doi:10.3389/fvets.2021.722432 · Cited by 9 · see citing works

Insights of affinity-based probes for target identification in drug discovery

Wang, H., Liu, L., Zhang, Z., Li, C., Wang, K., Gao, J., Hu, Q., Wang, W., & Li, H. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117711 · Cited by 7 · see citing works

A novel selective FAK inhibitor E2 inhibits ovarian cancer metastasis and growth by inducing cytotoxic autophagy

Feng, Z., Wei, W., Wang, S., Li, X., Zhao, L., Wan, G., Hu, R., & Yu, L. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116461 · Cited by 7 · see citing works

Effect of 3-O-acetylaleuritolic acid from in vitro-cultured Drosera spatulata on cancer cells survival and migration

Totoń, E., Kędziora, I., Romaniuk-Drapała, A., Konieczna, N., Kaczmarek, M., Lisiak, N., Paszel-Jaworska, A., Rybska, A., Duszynska, W., Budzianowski, J., et al. (2020) · Pharmacological Reports · doi:10.1007/s43440-019-00008-x · Cited by 7 · see citing works

The Anti-tumor Activity and Mechanisms of rLj-RGD3 on Human Laryngeal Squamous Carcinoma Hep2 Cells

Jin, Y., Lv, L., Ning, S., Wang, J., & Xiao, R. (2019) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520619666191022160024 · Cited by 6 · see citing works

FAK inhibitors in cancer, a patent review – an update on progress

Ye, Y., Cao, Y., Xu, L., Wang, H.-C., Liu, X., & Zhu, H. (2024) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2024.2368742 · Cited by 6 · see citing works

ZINC4085554 inhibits cancer cell adhesion by interfering with the interaction of Akt1 and FAK

More, S. K., Vomhof‐DeKrey, E. E., & Basson, M. D. (2019) · Oncology Letters · doi:10.3892/ol.2019.10192 · Cited by 6 · see citing works

Ginkgetin inhibits the proliferation and migration of lung cancer cells via FAK/STAT3/AKT pathway

Sun, L., Chen, W., Yuan, W., Huang, Q., Yang, H., Zhang, W., Tang, J., & Hu, P. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-10540-0 · Cited by 5 · see citing works

Affinity probes based on small-molecule inhibitors for tumor imaging

Yi, X., Wang, Z., Hu, X., & Yu, A. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.1028493 · Cited by 4 · see citing works

Daidzein and puerarin synergistically suppress gastric cancer proliferation via STAT3/FAK pathway Inhibition

Ge, J., Liu, B., Ma, L., Su, J., & Ding, Y. (2025) · Hereditas · doi:10.1186/s41065-025-00419-2 · Cited by 4 · see citing works

Radioiodination and biological distribution of a new s‐triazine derivative for tumor uptake evaluation

Motaleb, M. A., Ibrahim, I. T., Sarhan, M. O., & Zaghary, W. A. (2018) · Journal of Labelled Compounds and Radiopharmaceuticals · doi:10.1002/jlcr.3682 · Cited by 4 · see citing works

Recognition of LD motifs by the focal adhesion targeting domains of focal adhesion kinase and proline‐rich tyrosine kinase 2‐beta: Insights from molecular dynamics simulations

Michael, E., Polydorides, S., Promponas, V. J., Skourides, P. A., & Archontis, G. (2020) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25992 · Cited by 4 · see citing works

Knockdown of RABL3 suppresses the proliferation and invasion of oral squamous cell carcinoma through inactivating the FAK/AKT pathway

Xu, Z., Huazhu, L., Lin, C., Zeng, B., Chen, Y., & Luo, Y. (2021) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-021-09871-x · Cited by 4 · see citing works

Proteomic characteristics of PM2.5 -induced differentially expressed proteins in human renal tubular epithelial cells

Li, B., Qin, S., Cai, Y., Zheng, K., Wang, B., Li, R., Huang, H., Zeng, M., Xiao, F., & Xu, X. (2021) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2021.103658 · Cited by 4 · see citing works

Expression of selected molecular factors in two types of endometrial cancer

Markowska, A., Gryboś, A., Marszałek, A., Bednarek, W., Filas, V., Gryboś, M., Markowska, J., Mądry, R., Więckowska, B., Nowalińska, D., et al. (2021) · Advances in Clinical and Experimental Medicine · doi:10.17219/acem/137383 · Cited by 4 · see citing works

Modulation of Akt vs Stat3 activity by the focal adhesion kinase in non-neoplastic mouse fibroblasts

Geletu, M., Adan, H., Niit, M., Arulanandam, R., Carefoot, E., Hoskin, V., Sina, D., Elliott, B. E., Gunning, P. T., & Raptis, L. H. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112731 · Cited by 4 · see citing works

Resibufogenin and Oxaliplatin Synergistically Inhibit Diffuse Gastric Cancer by Inactivating the FAK/AKT/GSK3β/β-Catenin Signaling Pathway

Hu, H.-H., Shang, H.-L., Ren, Y., Lv, H., Tu, S., Wang, J., Gong, Y., Li, Z., Zhang, H., Li, T., et al. (2025) · Recent Patents on Anti-Cancer Drug Discovery · doi:10.2174/0115748928320605241112094549 · Cited by 3 · see citing works

Predicting treatment outcome using kinome activity profiling in HER2+ breast cancer biopsies

Debets, D. O., de Graaf, E. L., Liefaard, M. C., Sonke, G. S., Lips, E. H., Ressa, A., & Altelaar, M. A. F. (2024) · iScience · doi:10.1016/j.isci.2024.109858 · Cited by 3 · see citing works

Mechanical network motifs as targets for mechanomedicine

Lu, M., Zhao, X., Xu, F., Yin, C., Guo, H., & Cheng, B. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.104145 · Cited by 3 · see citing works

BI 853520, a FAK-Simile of Prior FAK Inhibitors?

Lee, R. C., & Gan, H. K. (2019) · Targeted Oncology · doi:10.1007/s11523-019-00621-z · Cited by 3 · see citing works

Screening drugs of Anemoside B4 for MFAP4 expression in osteosarcoma in PDTX to increase personalized medicine

Zhang, L., Zeng, L., Zhang, J., He, Z., & Liu, X. (2025) · Discover Oncology · doi:10.1007/s12672-025-03373-7 · Cited by 2 · see citing works

Metronomic chemotherapy in pediatric neurooncology: insight the problem. A review

Dinikina, Y. V., Zheludkova, O., Ryzhova, M. V., Olkhova, L. V., Korneev, D. Y., & Belogurova, M. B. (2024) · Journal of Modern Oncology · doi:10.26442/18151434.2024.2.202637 · Cited by 1 · see citing works

Patent Highlights August–September 2018

Mucke, H. A. (2019) · Pharmaceutical Patent Analyst · doi:10.4155/ppa-2018-0033 · Cited by 1 · see citing works

[Protective effect of FAK inhibitor PF-562271 against human umbilical vein endothelial cell injury induced by aging platelets].

Bai, Y., Gang, B., Zhang, M., Wan, Z., Liu, G., & Gu, W. (2024) · PubMed · doi:10.12122/j.issn.1673-4254.2024.02.07 · Cited by 1 · see citing works

Computational Design of Peptides with Improved Recognition of the Focal Adhesion Kinase FAT Domain

Michael, E., Polydorides, S., & Archontis, G. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1855-4_18

Activation of autophagy induces monocrotaline-induced pulmonary arterial hypertension by FOXM1-mediated FAK phosphorylationPreprint

Li, S., Zhai, C., Zhang, N., Wang, J., Cao, M., Luan, J., Liu, H., zhang, Q., & Zhu, Y. (2022) · Research Square · doi:10.21203/rs.3.rs-1274598/v2

Focal adhesion kinase—An emerging viable target in cancer and development of focal adhesion kinase inhibitors

Chauhan, A., & Khan, T. A. (2020) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13808 · Cited by 52 · see citing works

Recent Advances of Small Molecule Focal Adhesion Kinase (FAK) Inhibitors as Promising Anticancer Therapeutics

Lv, P., Chen, K., & Zhu, H. (2021) · Current Medicinal Chemistry · doi:10.2174/0929867328666210331143827 · Cited by 14 · see citing works

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 221 · see citing works

FAK inhibitors in cancer, a patent review – an update on progress

Ye, Y., Cao, Y., Xu, L., Wang, H.-C., Liu, X., & Zhu, H. (2024) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2024.2368742 · Cited by 6 · see citing works

Focal adhesion kinase inhibitors in the treatment of metastatic cancer: a patent review

Shanthi, E., Krishna, M. H., Arunesh, G. M., Reddy, K. V., Kumar, J. S., & Viswanadhan, V. N. (2014) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2014.948845 · Cited by 52 · see citing works