ARF1 regulates adhesion of MDA-MB-231 invasive breast cancer cells through formation of focal adhesions

Integrins in cancer: biological implications and therapeutic opportunities

Desgrosellier, J. S., & Cheresh, D. A. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2748 · Cited by 3,721 · 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

FAK integrates growth-factor and integrin signals to promote cell migration

Sieg, D. J., Hauck, C. R., Ilić, D., Klingbeil, C. K., SCHAEFER, E. M., Damsky, C. H., & Schlaepfer, D. D. (2000) · Nature Cell Biology · doi:10.1038/35010517 · Cited by 1,240 · see citing works

Functional atlas of the integrin adhesome

Zaidel‐Bar, R., Itzkovitz, S., Ma’ayan, A., Iyengar, R., & Geiger, B. (2007) · Nature Cell Biology · doi:10.1038/ncb0807-858 · Cited by 1,182 · see citing works

Tyrosine Phosphorylation of Focal Adhesion Kinase at Sites in the Catalytic Domain Regulates Kinase Activity: a Role for Src Family Kinases

Calalb, M. B., Polte, T. R., & Hanks, S. K. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.2.954 · Cited by 987 · see citing works

Paxillin and focal adhesion signalling

Turner, C. E. (2000) · Nature Cell Biology · doi:10.1038/35046659 · Cited by 839 · see citing works

Integrins in Cell MigrationPreprint

Anna Huttenlocher, A., & Horwitz, A. R. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005074 · Cited by 762 · see citing works

Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration

Sieg, D. J., Hauck, C. R., & Schlaepfer, D. D. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.16.2677 · Cited by 688 · see citing works

Src in cancer: deregulation and consequences for cell behaviour

Frame, M. C. (2002) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(02)00040-9 · Cited by 682 · see citing works

The Clinical Significance of Epidermal Growth Factor Receptor (EGF-R) in Human Breast Cancer: A Review on 5232 Patients*

Klijn, J. G. M., Berns, P. M. J. J., Schmitz, P. I. M., & Foekens, J. A. (1992) · Endocrine Reviews · doi:10.1210/edrv-13-1-3 · Cited by 596 · see citing works

Biochemical signals and biological responses elicited by the focal adhesion kinase

Schaller, M. D. (2001) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(01)00123-9 · Cited by 583 · see citing works

Paxillin: a focal adhesion-associated adaptor protein

Schaller, M. D. (2001) · Oncogene · doi:10.1038/sj.onc.1204786 · Cited by 542 · see citing works

Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa.

Linstedt, A. D., & Hauri, H.-P. (1993) · Molecular Biology of the Cell · doi:10.1091/mbc.4.7.679 · Cited by 417 · see citing works

A new protein of adhesion plaques and ruffling membranes.

Burridge, K., & Connell, L. B. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.97.2.359 · Cited by 410 · see citing works

Coupling of PAK-Interacting Exchange Factor PIX to GIT1 Promotes Focal Complex Disassembly

Zhao, Z.-S., Manser, E. J., Loo, T.-H., & Lim, L. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.17.6354-6363.2000 · Cited by 364 · see citing works

Regulation of Arf Activation: the Sec7 Family of Guanine Nucleotide Exchange Factors

Casanova, J. E. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00634.x · Cited by 349 · see citing works

The Role of Src in Solid Tumors

Wheeler, D. L., Iida, M., & Dunn, E. F. (2009) · The Oncologist · doi:10.1634/theoncologist.2009-0009 · Cited by 346 · see citing works

Stimulation‐Dependent Recycling of Integrin β1 Regulated by ARF6 and Rab11

Powelka, A. M., Sun, J., Li, J., Gao, M., Shaw, L. M., Sonnenberg, A., & Hsu, V. W. (2003) · Traffic · doi:10.1111/j.1600-0854.2004.00150.x · Cited by 331 · see citing works

Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells.

Hauck, C. R., Sieg, D. J., Hsia, D. A., Loftus, J. C., Gaarde, W. A., Monia, B. P., & Schlaepfer, D. D. (2001) · PubMed · Cited by 249 · see citing works

Epidermal growth factor promotes MDA-MB-231 breast cancer cell migration through a phosphatidylinositol 3'-kinase and phospholipase C-dependent mechanism.

Price, J. T., Tiganis, T., Agarwal, A., Djakiew, D., & Thompson, E. W. (1999) · PubMed · Cited by 236 · see citing works

GEP100 links epidermal growth factor receptor signalling to Arf6 activation to induce breast cancer invasion

Morishige, M., Hashimoto, S., Ogawa, E., Toda, Y., Kotani, H., Hirose, M., Wei, S., Hashimoto, A., Yamada, A., Yano, H., et al. (2007) · Nature Cell Biology · doi:10.1038/ncb1672 · Cited by 220 · see citing works

The Arf GTPase-activating protein ASAP1 regulates the actin cytoskeleton

Randazzo, P. A., Andrade, J., Miura, K., Brown, M. T., Long, Y.-Q., Stauffer, S., Roller, P., & Cooper, J. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.070552297 · Cited by 210 · see citing works

Active Arf6 Recruits ARNO/Cytohesin GEFs to the PM by Binding Their PH Domains

Cohen, L. A., Honda, A., Várnai, P., Brown, F. D., Balla, T., & Donaldson, J. G. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-11-0998 · Cited by 207 · see citing works

Epidermal growth factor receptor expression in breast cancer: Association with response to endocrine therapy

Nicholson, R. I., McClelland, R. A., Gee, J. M. W., Manning, D. L., Cannon, P., Robertson, J. F. R., Ellis, I. O., & Blamey, R. W. (1994) · Breast Cancer Research and Treatment · doi:10.1007/bf00666187 · Cited by 190 · see citing works

Cortactin phosphorylation sites mapped by mass spectrometry

Martin, K. H., Jeffery, E. D., Grigera, P. R., Shabanowitz, J., Hunt, D. F., & Parsons, J. T. (2006) · Journal of Cell Science · doi:10.1242/jcs.03034 · Cited by 182 · see citing works

The RhoA-dependent assembly of focal adhesions in Swiss 3T3 cells is associated with increased tyrosine phosphorylation and the recruitment of both pp125FAK and protein kinase C-δ to focal adhesions

Barry, S. T., & Critchley, D. R. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.7.2033 · Cited by 170 · see citing works

Localization and function of Arf family GTPases

Donaldson, J. G., & Honda, A. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330639 · Cited by 170 · see citing works

The Association of ASAP1, an ADP Ribosylation Factor-GTPase Activating Protein, with Focal Adhesion Kinase Contributes to the Process of Focal Adhesion Assembly

Liu, Y., Loijens, J. C., Martin, K. H., Karginov, A. V., & Parsons, J. T. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-01-0018 · Cited by 169 · see citing works

ADP-ribosylation factor 6 regulates tumor cell invasion through the activation of the MEK/ERK signaling pathway

Tague, S. E., Muralidharan-Chari, V., & D’Souza‐Schorey, C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403531101 · Cited by 168 · see citing works

Regulated Exocytosis in Chromaffin Cells

Galas, M., Helms, J. B., Vitale, N., Thiersé, D., Aunis, D., & Bader, M. F. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.5.2788 · Cited by 150 · see citing works

ARF1 regulates the Rho/MLC pathway to control EGF-dependent breast cancer cell invasion

Schlienger, S., Campbell, S. L., & Claing, A. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-06-0335 · Cited by 141 · see citing works

ARF1 Mediates Paxillin Recruitment to Focal Adhesions and Potentiates Rho-stimulated Stress Fiber Formation in Intact and Permeabilized Swiss 3T3 Fibroblasts

Norman, J. C., Jones, D., Barry, S. T., Holt, M., Cockcroft, S., & Critchley, D. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1981 · Cited by 139 · see citing works

Requirement for Rho in Integrin Signalling

Barry, S. T., Flinn, H. M., Humphries, M. J., Critchley, D. R., & Ridley, A. J. (1997) · Cell Communication & Adhesion · doi:10.3109/15419069709004456 · Cited by 125 · see citing works

Structure-based discovery of an inhibitor of Arf activation by Sec7 domains through targeting of protein–protein complexes

Viaud, J., Zeghouf, M., Barelli, H., Zeeh, J., Padilla, A., Guibert, B., Chardin, P., Royer, C. A., Cherfils, J., & Chavanieu, A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700773104 · Cited by 98 · see citing works

ADP-ribosylation Factor 1 Controls the Activation of the Phosphatidylinositol 3-Kinase Pathway to Regulate Epidermal Growth Factor-dependent Growth and Migration of Breast Cancer Cells

Boulay, P.-L., Cotton, M., Melançon, P., & Claing, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803603200 · Cited by 98 · see citing works

The Ras Signaling Pathway in Mammary Tumorigenesis and Metastasis

Malaney, S., & Daly, R. J. (2001) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1023/a:1009572700317 · Cited by 83 · see citing works

ADP-ribosylation Factor 4 Small GTPase Mediates Epidermal Growth Factor Receptor-dependent Phospholipase D2 Activation

Kim, S.-W., Hayashi, M., Lo, J., Yang, Y. C., Yoo, J.-S., & Lee, J.-D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m205819200 · Cited by 64 · see citing works

Endogenous ARF6 Interacts with Rac1 upon Angiotensin II Stimulation to Regulate Membrane Ruffling and Cell Migration

Cotton, M., Boulay, P.-L., Houndolo, T., Vitale, N., Pitcher, J. A., & Claing, A. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-06-0567 · Cited by 62 · see citing works

ARF1 controls proliferation of breast cancer cells by regulating the retinoblastoma protein

Boulay, P.-L., Schlienger, S., Lewis-Saravalli, S., Vitale, N., Ferbeyre, G., & Claing, A. (2011) · Oncogene · doi:10.1038/onc.2011.100 · Cited by 61 · see citing works

Focal Adhesion Kinase Is Not Essential for in Vitro and in Vivo Differentiation of ES Cells

Ilić, D., Furuta, Y., Suda, T., Atsumi, T., Fujimoto, J., Ikawa, Y., Yamamoto, T., & Aizawa, S. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.1503 · Cited by 57 · see citing works

The role of focal adhesion kinase in the regulation of cellular mechanical properties

Mierke, C. T. (2013) · Physical Biology · doi:10.1088/1478-3975/10/6/065005 · Cited by 56 · see citing works

The Adaptor Proteins p66Shc and Grb2 Regulate the Activation of the GTPases ARF1 and ARF6 in Invasive Breast Cancer Cells

Haines, E., Saucier, C., & Claing, A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.516047 · Cited by 51 · see citing works

FAK phosphorylation sites mapped by mass spectrometry

Grigera, P. R., Jeffery, E. D., Martin, K. H., Shabanowitz, J., Hunt, D. F., & Parsons, J. T. (2005) · Journal of Cell Science · doi:10.1242/jcs.02696 · Cited by 50 · see citing works

ARF1 controls Rac1 signaling to regulate migration of MDA-MB-231 invasive breast cancer cells

Lewis-Saravalli, S., Campbell, S. L., & Claing, A. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.05.011 · Cited by 47 · see citing works

Endothelin-1 promotes migration of endothelial cells through the activation of ARF6 and the regulation of FAK activity

Daher, Z., Noël, J., & Claing, A. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.08.021 · Cited by 38 · see citing works

Src as a Therapeutic Target in Breast Cancer

Morgan, L. D., Nicholson, R. I., & Hiscox, S. (2008) · Endocrine Metabolic & Immune Disorders - Drug Targets · doi:10.2174/187153008786848295 · Cited by 18 · see citing works

Endocytosis in cancer and cancer therapy

Banushi, B., Joseph, S. R., Lum, B., Lee, J. J., & Simpson, F. (2023) · Nature reviews. Cancer · doi:10.1038/s41568-023-00574-6 · Cited by 245 · see citing works

Integrins in cancer: Emerging mechanisms and therapeutic opportunities

Liu, F., Wu, Q., Dong, Z., & Liu, K. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108458 · Cited by 191 · see citing works

Endocytosis: a pivotal pathway for regulating metastasis

Khan, I., & Steeg, P. S. (2021) · British Journal of Cancer · doi:10.1038/s41416-020-01179-8 · Cited by 178 · see citing works

Drugging the Small GTPase Pathways in Cancer Treatment: Promises and Challenges

Prieto‐Domínguez, N., Parnell, C., & Teng, Y. (2019) · Cells · doi:10.3390/cells8030255 · Cited by 85 · see citing works

The Role of ARF Family Proteins and Their Regulators and Effectors in Cancer Progression: A Therapeutic Perspective

Casalou, C., Ferreira, A., & Barral, D. C. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00217 · Cited by 73 · see citing works

Arf proteins in cancer cell migration

Casalou, C., Faustino, A., & Barral, D. C. (2016) · Small GTPases · doi:10.1080/21541248.2016.1228792 · Cited by 76 · see citing works

A New Look at the Functional Organization of the Golgi Ribbon

Saraste, J., & Prydz, K. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00171 · Cited by 71 · see citing works

Conversion of nanoscale topographical information of cluster-assembled zirconia surfaces into mechanotransductive events promotes neuronal differentiation

Schulte, C., Rodighiero, S., Cappelluti, M. A., Puricelli, L., Maffioli, E., Borghi, F., Negri, A. L., Sogne, E., Galluzzi, M., Piazzoni, C., et al. (2016) · Journal of Nanobiotechnology · doi:10.1186/s12951-016-0171-3 · Cited by 70 · see citing works

Cargo-specific recruitment in clathrin- and dynamin-independent endocytosis

Moreno‐Layseca, P., Jäntti, N. Z., Godbole, R. K., Sommer, C., Jacquemet, G., Al‐Akhrass, H., Conway, J. R. W., Kronqvist, P., Kallionpää, R., Oliveira‐Ferrer, L., et al. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00767-x · Cited by 66 · see citing works

Insights of Endocytosis Signaling in Health and Disease

Pathak, C., Vaidya, F. U., Waghela, B. N., Jaiswara, P. K., Gupta, V. K., Kumar, A., Rajendran, B. K., & Ranjan, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032971 · Cited by 59 · see citing works

Arf GAPs as Regulators of the Actin Cytoskeleton—An Update

Tanna, C. E., Goss, L. B., Ludwig, C., & Chen, P.-W. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20020442 · Cited by 61 · see citing works

Anti-allergic drug azelastine suppresses colon tumorigenesis by directly targeting ARF1 to inhibit IQGAP1-ERK-Drp1-mediated mitochondrial fission

Hu, H., Xu, W. W., Li, Y., He, Y., Zhang, W., Liao, L., Zhang, Q., Han, L., Yin, X., Xiao-xu, Z., et al. (2020) · Theranostics · doi:10.7150/thno.48698 · Cited by 60 · see citing works

Suppression of breast cancer metastasis through the inactivation of ADP-ribosylation factor 1

Xie, X., Tang, S.-C., Cai, Y., Pi, W., Deng, L., Wu, G., Chavanieu, A., & Teng, Y. (2016) · Oncotarget · doi:10.18632/oncotarget.11185 · Cited by 50 · see citing works

Anterior gradient 2 is induced in cutaneous wound and promotes wound healing through its adhesion domain

Zhu, Q., Mangukiya, H. B., Mashausi, D. S., Guo, H., Negi, H., Merugu, S. B., Wu, Z., & Li, D. (2017) · FEBS Journal · doi:10.1111/febs.14155 · Cited by 47 · see citing works

FOXM1 transcriptionally regulates expression of integrin β1 in triple-negative breast cancer

Hamurcu, Z., Kahraman, N., Ashour, A. A., & Özpolat, B. (2017) · Breast Cancer Research and Treatment · doi:10.1007/s10549-017-4207-7 · Cited by 41 · see citing works

Functional disruption of the Golgi apparatus protein ARF1 sensitizes MDA-MB-231 breast cancer cells to the antitumor drugs Actinomycin D and Vinblastine through ERK and AKT signaling

Luchsinger, C., Aguilar, M. N., Burgos, P. V., Ehrenfeld, P., & Mardones, G. A. (2018) · PLoS ONE · doi:10.1371/journal.pone.0195401 · Cited by 40 · see citing works

Golgi Complex: A Signaling Hub in Cancer

Spano, D., & Colanzi, A. (2022) · Cells · doi:10.3390/cells11131990 · Cited by 40 · see citing works

Family-wide Analysis of the Inhibition of Arf Guanine Nucleotide Exchange Factors with Small Molecules: Evidence of Unique Inhibitory Profiles

Benabdi, S., Peurois, F., Nawrotek, A., Chikireddy, J., Cañeque, T., Yamori, T., Shiina, I., Ohashi, Y., Dan, S., Rodriguez, R., et al. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00706 · Cited by 35 · see citing works

Overexpression of ARF1 is associated with cell proliferation and migration through PI3K signal pathway in ovarian cancer

Gu, G.-F., Chen, Y., Duan, C., Zhou, L., Chen, C., Chen, J., Cheng, J., Shi, N., Jin, Y., Xi, Q., et al. (2017) · Oncology Reports · doi:10.3892/or.2017.5388 · Cited by 34 · see citing works

Systematic drug sensitivity testing reveals synergistic growth inhibition by dasatinib or mTOR inhibitors with paclitaxel in ovarian granulosa cell tumor cells

Haltia, U., Andersson, N., Yadav, B., Färkkilä, A., Kulesskiy, E., Kankainen, M., Tang, J. P., Bützow, R. C., Riska, A., Leminen, A., et al. (2017) · Gynecologic Oncology · doi:10.1016/j.ygyno.2016.12.016 · Cited by 32 · see citing works

ADP-ribosylation factor 1 expression regulates epithelial-mesenchymal transition and predicts poor clinical outcome in triple-negative breast cancer

Schlienger, S., Campbell, S., Pasquin, S., Gaboury, L., & Claing, A. (2016) · Oncotarget · doi:10.18632/oncotarget.7515 · Cited by 26 · see citing works

β1-Integrin plays a major role in resveratrol-mediated anti-invasion effects in the CRC microenvironment

Brockmueller, A., Mueller, A., Shayan, P., & Shakibaei, M. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.978625 · Cited by 22 · see citing works

Targeting ARF1-IQGAP1 interaction to suppress colorectal cancer metastasis and vemurafenib resistance

Hu, H., Gao, G., He, X., Li, Y., Li, Y., Li, B., Pan, Y.-L., Wang, Y., & He, Q. (2022) · Journal of Advanced Research · doi:10.1016/j.jare.2022.11.006 · Cited by 21 · see citing works

Endogenous and Exogenous Regulatory Signaling in the Secretory Pathway: Role of Golgi Signaling Molecules in Cancer

Giudice, S. D., Luca, V. D., Parizadeh, S., Russo, D., Luini, A., & Martino, R. D. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.833663 · Cited by 19 · see citing works

Chlortetracycline, a Novel Arf Inhibitor That Decreases the Arf6-Dependent Invasive Properties of Breast Cancer Cells

Macia, E., Rojas, M. V., Robiolo, A., Fayad, R., Abélanet, S., Mus‐Veteau, I., Fontaine‐Vive, F., Mehiri, M., Luton, F., & Franco, M. (2021) · Molecules · doi:10.3390/molecules26040969 · Cited by 18 · see citing works

Recombinant protein ofHaemonchus contortussmall GTPase ADP-ribosylation factor 1 (HcARF1) modulate the cell mediated immune responsein vitro

Gadahi, J. A., Ehsan, M., Wang, S., Zhang, Z., Yan, R., Song, X., Xu, L., & Li, X. (2017) · Oncotarget · doi:10.18632/oncotarget.22662 · Cited by 16 · see citing works

Unraveling the Relevance of ARL GTPases in Cutaneous Melanoma Prognosis through Integrated Bioinformatics Analysis

Brito, C., Costa‐Silva, B., Barral, D. C., & Pojo, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179260 · Cited by 15 · see citing works

Inhibition of growth and metastasis of triple-negative breast cancer targeted by Traditional Chinese Medicine Tubeimu in orthotopic mice models

Wang, J., Yang, X., Han, H., Wang, L., Bao, W., Wang, S., Hoffman, R. M., Yang, M., Qi, H., An, C., et al. (2018) · Chinese Journal of Cancer Research · doi:10.21147/j.issn.1000-9604.2018.01.12 · Cited by 15 · see citing works

Comprehensive circular RNA profiling reveals the�regulatory role of the hsa_circ_0137606/miR‑1231 pathway in bladder cancer progression

Li, W., Li, Y., Sun, Z., Zhou, J., Cao, Y., Ma, W., Xie, K., & Yan, X. (2019) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2019.4340 · Cited by 13 · see citing works

Identification of a prognostic long noncoding RNA signature in lung squamous cell carcinoma: a population-based study with a mean follow-up of 3.5 years

Zheng, R., Zheng, M., Wang, M., Lu, F., & Hu, M. (2021) · Archives of Public Health · doi:10.1186/s13690-021-00588-2 · Cited by 12 · see citing works

Membrane trafficking alterations in breast cancer progression

Ferreira, A., Castanheira, P., Escrevente, C., Barral, D. C., & Barona, T. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1350097 · Cited by 8 · see citing works

The small GTPase ARF3 controls invasion modality and metastasis by regulating N-cadherin levels

Sandilands, E., Freckmann, E. C., Cumming, E. M., Román‐Fernández, Á., McGarry, L., Anand, J., Galbraith, L. C. A., Mason, S. M., Patel, R., Nixon, C., et al. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202206115 · Cited by 11 · see citing works

Nanoparticles (PLGA and Chitosan)-Entrapped ADP-Ribosylation Factor 1 of Haemonchus contortus Enhances the Immune Responses in ICR Mice

Hasan, M. W., Haseeb, M., Ehsan, M., Gadahi, J. A., Naqvi, M. A., Wang, Q. Q., Liu, X., Lakho, S. A., Yan, R., Xu, L., et al. (2020) · Vaccines · doi:10.3390/vaccines8040726 · Cited by 11 · see citing works

Shear stress triggered circular dorsal ruffles formation to facilitate cancer cell migration

Qin, X., Zhang, Y., He, Y., Chen, K., Zhang, Y., Li, P., Jiang, Y., Li, S., Li, T., Yang, H., et al. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108967 · Cited by 11 · see citing works

Role of the Mosaic Cisternal Maturation Machinery in Glycan Synthesis and Oncogenesis

Sahu, P., Balakrishnan, A., Martino, R. D., Luini, A., & Russo, D. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.842448 · Cited by 10 · see citing works

ARF GTPases control phenotypic switching of vascular smooth muscle cells through the regulation of actin function and actin dependent gene expression

Charles, R., Bourmoum, M., & Claing, A. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.02.012 · Cited by 9 · see citing works

Myelination by signaling through Arf guanine nucleotide exchange factor

Torii, T., Miyamoto, Y., & Yamauchi, J. (2024) · Journal of Neurochemistry · doi:10.1111/jnc.16141 · Cited by 7 · see citing works

The role of cell cycle-related genes in the tumorigenesis of adrenal and thyroid neuroendocrine tumors

Просандеева, Е. С., Gorodkova, E., Shcherbakova, A. S., Asaad, W., Popov, S. V., Mel'nichenko, G. A., Mokrysheva, N. G., & Utkina, M. V. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e41457 · Cited by 7 · see citing works

Catharanthus roseus L. extract downregulates the expression profile of motility-related genes in highly invasive human breast cancer cell line MDA-MB-231

Eltayeb, N. M., Al‐Amin, M., Yousif, A. M., Balakrishnan, V., & Salhimi, S. M. (2020) · Biologia · doi:10.2478/s11756-020-00641-5 · Cited by 5 · see citing works

Cytoskeletal dynamics in breast cancer: mechanistic insights and therapeutic opportunities

Malla, R. R., Tumbali, A., Chode, P., Manda, K., Samudrala, A. S., Nuthalapati, Y., Mangam, C., Bhamidipati, P., Srilatha, M., & Nagaraju, G. P. (2025) · Journal of the National Cancer Center · doi:10.1016/j.jncc.2025.09.006 · Cited by 3 · see citing works

Differential AXL expression and Arf1 regulation control stiffness-dependent Golgi organization in breast cancer cells

Saha, A., Sherkhane, T., & Balasubramanian, N. (2026) · Journal of Cell Science · doi:10.1242/jcs.263956 · Cited by 3 · see citing works

Golgi localized Arl15 regulates cargo transport, cell adhesion and motilityPreprint

Sharma, P., Venkatesh, P. H., Paddillaya, N., Shah, N., Rajeshwari, B. R., Dakua, A., Penmatsa, A., Balasubramanian, N., Gundiah, N., & Setty, S. R. G. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.18.504432 · Cited by 2 · see citing works

Golgi Localized Arl15 Regulates Cargo Transport and Cell Adhesion

Sharma, P., Venkatesh, P. H., Samal, S., Paddillaya, N., Shah, N., Rajeshwari, B. R., Bhat, A., Nair, D. K., Dakua, A., Penmatsa, A., et al. (2025) · Traffic · doi:10.1111/tra.70004 · Cited by 1 · see citing works

The Impact of Golgi Organization on Cell Cycle and Cancer Development

Colanzi, A., & Ayala, I. (2025) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-032-06936-8_6 · Cited by 1 · see citing works

Role of EFA6B, Exchange Factor of Arf6, in epithelial morphogenesis and collective invasion of human mammary cells

Fayad, R. (2019) · theses.fr (ABES) · doi:10.70675/d65209ffz508cz4e76zae65zee1960b4e819 · Cited by 1 · see citing works

Identification of a prognostic three-long noncoding RNA signature in lung squamous cell carcinoma via bioinformatic analysisPreprint

Zheng, R., Zheng, M., Wang, M., & Hu, M. (2020) · doi:10.21203/rs.3.rs-60427/v1

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Xie, X., Tang, S., Cai, Y., Pi, W., Deng, L., Wu, G., Chavanieu, A., & Teng, Y. (2020) · Vide Leaf, Hyderabad eBooks · doi:10.37247/pacr.1.2020.16

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Zheng, R., Zheng, M., Wang, M., Lu, F., & Hu, M. (2021) · Figshare · doi:10.6084/m9.figshare.14509492

Exploration of traditional medicines as source of bioactive compounds : from ethnobotany to pharmacomodulation

Ortíz, S. (2019) · doi:10.70675/57d4e95czd255z4610z858fza39d5c488623

EFA6B regulates a stop signal for collective invasion in breast cancer

Rojas, M. V. (2020) · doi:10.70675/78f3db3dzf275z41f3zb818z9ad4d5770845

ARF1 controls Rac1 signaling to regulate migration of MDA-MB-231 invasive breast cancer cells

Lewis-Saravalli, S., Campbell, S. L., & Claing, A. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.05.011 · Cited by 47 · see citing works

ADP-ribosylation Factor 1 Controls the Activation of the Phosphatidylinositol 3-Kinase Pathway to Regulate Epidermal Growth Factor-dependent Growth and Migration of Breast Cancer Cells

Boulay, P.-L., Cotton, M., Melançon, P., & Claing, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803603200 · Cited by 98 · see citing works

Paxillin-Associated Arf GAPs

Sabe, H. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/1-4020-2593-9_9 · Cited by 3 · see citing works

Arf proteins in cancer cell migration

Casalou, C., Faustino, A., & Barral, D. C. (2016) · Small GTPases · doi:10.1080/21541248.2016.1228792 · Cited by 76 · see citing works

ARF1 regulates the Rho/MLC pathway to control EGF-dependent breast cancer cell invasion

Schlienger, S., Campbell, S. L., & Claing, A. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-06-0335 · Cited by 141 · see citing works