The DOI matches its Crossref record; 81 of the 81 references it cites were found in a registry or an index.
Integrin–TGF‐β crosstalk in fibrosis, cancer and wound healing
Open accessAbstract
Accumulating evidence indicates that there is extensive crosstalk between integrins and TGF-beta signalling. TGF-beta affects integrin-mediated cell adhesion and migration by regulating the expression of integrins, their ligands and integrin-associated proteins. Conversely, several integrins directly control TGF-beta activation. In addition, a number of integrins can interfere with both Smad-dependent and Smad-independent TGF-beta signalling in different ways, including the regulation of the expression of TGF-beta signalling pathway components, the physical association of integrins with TGF-beta receptors and the modulation of downstream effectors. Reciprocal TGF-beta-integrin signalling is implicated in normal physiology, as well as in a variety of pathological processes including systemic sclerosis, idiopathic pulmonary fibrosis, chronic obstructive pulmonary disease and cancer; thus, integrins could provide attractive therapeutic targets to interfere with TGF-beta signalling in these processes.
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
“By disrupting mechanical force transmission between cells and the ECM, integrin inhibitors not only attenuate TGF-b activation but also modulate immune cell adhesion and migration, effectively dampening pro-fibrotic inflammation at its source (129).”
From The mechanotransduction-immune axis in organ fibrosis: dual regulatory mechanisms and translational therapeutic perspectives (2025) · cites this paper as [129]
In the citing paper
“integrins are known to activate TGF-β”
From Integrin Beta 3 Regulates Cellular Senescence by Activating the TGF-β Pathway (2017) · cites this paper as Margadant and Sonnenberg, 2010
In the citing paper
“Accumulating evidence indicates that a cross-talk between integrins and TGF-β exists, in particular to regulate fibrosis, wound healing, and cancer (Asano et al., 2005, Margadant and Sonnenberg, 2010).”
From Integrin Beta 3 Regulates Cellular Senescence by Activating the TGF-β Pathway (2017) · cites this paper as Margadant and Sonnenberg, 2010
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
Hynes (2002) · doi:10.1016/s0092-8674(02)00971-6 · Cited by 8,606
Singer, A. J., & Clark, R. A. F. (1999) · New England Journal of Medicine · doi:10.1056/nejm199909023411006 · Cited by 6,106
Massagué, J. (2008) · Cell · doi:10.1016/j.cell.2008.07.001 · Cited by 3,907
Regulation of Wound Healing by Growth Factors and Cytokines
WERNER, S., & GROSE, R. (2003) · Physiological Reviews · doi:10.1152/physrev.2003.83.3.835 · Cited by 3,629
Munger, J. S., Huang, X., Kawakatsu, H., Griffiths, M. J. D., Dalton, S. L., Wu, J., Pittet, J.-F., Kaminski, N., Garat, C., Matthay, M. A., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80545-0 · Cited by 2,076
Controlling TGF-beta signaling.
Massagué, J., & Chen, Y. (2000) · PubMed · Cited by 1,780
Controlling TGF-β signalingPreprint
Massagué, J., & Chen, Y. (2000) · Genes & Development · doi:10.1101/gad.14.6.627 · Cited by 1,589
Brooks, P. C., Strömblad, S., Sanders, L. C., Schalscha, T. V., Aimes, R. T., Stetler‐Stevenson, W. G., Quigley, J. P., & Cheresh, D. A. (1996) · Cell · doi:10.1016/s0092-8674(00)81235-0 · Cited by 1,566
Myofibroblast contraction activates latent TGF-β1 from the extracellular matrix
Wipff, P.-J., Rifkin, D. B., Meister, J.-J., & Hinz, B. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704042 · Cited by 1,346
TGFβ: the molecular Jekyll and Hyde of cancer
Bierie, B., & Moses, H. L. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1926 · Cited by 1,291
Flagged first, then by citations
Cited by
Sorted by citations
Items 401–500 of 654
TMPRSS11a is a novel age‐altered, tissue specific regulator of migration and wound healing
Fernández, C., Burgos, A., Morales, D., Rosales‐Rojas, R., Canelo, J., Vergara‐Jaque, A., Vieira, G. V., da Silva, R. A. A., Sales, K. U., Conboy, M. J., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202002253rrr · Cited by 15
Li, W., Liu, X., Muhammad, S., Shi, J., Meng, Y., & Wang, J. (2018) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2018.07.002 · Cited by 14
Rabelo, L. F. G., Ferreira, B. A., Deconte, S. R., Tomiosso, T. C., dos Santos, P. K., Andrade, S. P., Selistre-de-Araújo, H. S., & Araújo, F. D. A. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.08.171 · Cited by 14
Toh, B., Toh, B., Abastado, J., & Abastado, J. (2012) · OncoImmunology · doi:10.4161/onci.22196 · Cited by 15
The role of Rho kinase (Rock) in re-epithelialization of adult zebrafish skin wounds
Richardson, R. J., & Hammerschmidt, M. (2016) · Small GTPases · doi:10.1080/21541248.2016.1219208 · Cited by 14
Liu, S., Wang, Q., Min, J., Zhang, Y., Zhang, Y., Yang, J., Tan, Y., Tan, L., Yin, M., Zhang, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64211-6 · Cited by 15
Djafarzadeh, R., Notohamiprodjo, S., Rieth, N., Hofstetter, M., Noeßner, E., & Nelson, P. J. (2012) · Journal of Investigative Dermatology · doi:10.1038/jid.2012.375 · Cited by 13
“The cytokines connective tissue growth factor and TGF-b1 also have important roles in wound healing (Singer and Clark, 1999; Leask and Abraham, 2004; Margadant and Sonnenberg, 2010).”
BackgroundIntegrin β1 activation induces an anti-melanoma host response
Ritsma, L., Dey‐Guha, I., Talele, N. P., Solé, X., Salony, Chowdhury, J., Ross, K. N., & Ramaswamy, S. (2017) · PLoS ONE · doi:10.1371/journal.pone.0175300 · Cited by 12
Titus, A. S., Venugopal, H., Ushakumary, M. G., Wang, M., Cowling, R. T., Lakatta, E. G., & Kailasam, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179343 · Cited by 15
“Our findings on the role of Integrin-β1 as an ‘effector molecule’ in a complex regulatory cascade are consistent with an earlier report that ECM-mediated mechanical stress activates TGFβ and triggers the expression of Integrins and the pro-fibrotic gene program in cardiac fibroblasts [44].”
ResultSilver, F. H., Deshmukh, T., Ryan, N., Romm, A., & Nadiminti, H. (2022) · Biomolecules · doi:10.3390/biom12101332 · Cited by 15
“ECM remodeling is primarily mediated by matrix metalloproteinases (MMPs) [8] and transforming growth factor (TGF)-β–integrin signaling is implicated in normal physiology.”
BackgroundLiver Fibrosis, Liver Cancer, and Advances in Therapeutic Approaches
Rajapaksha, I. G. (2022) · Livers · doi:10.3390/livers2040028 · Cited by 14
Deng, M., Liu, P., Xiao, H., Zhang, Y., Wang, Y., Zhao, J., & Xu, J. (2015) · Cell and Tissue Research · doi:10.1007/s00441-015-2154-3 · Cited by 13
“Furthermore, integrins, as the mechanical response elements of the mechanotransduction process, could also crosstalk to the BMP signaling pathway (Margadant and Sonnenberg 2010; Papachroni et al. 2009).”
BackgroundTGF β1 Mediates Epithelial Mesenchymal Transition via β6 Integrin Signaling Pathway in Breast Cancer
Li, W., Zhang, B., Li, H., Zhao, C., zhong, Y., Sun, J., & Lv, S. (2014) · Cancer Investigation · doi:10.3109/07357907.2014.933235 · Cited by 13
Chen, S.-Y. (2019) · International Journal of Ophthalmology · doi:10.18240/ijo.2020.01.03 · Cited by 14
Tomasovic, A., Kurrle, N., Wempe, F., De-Zolt, S., Scheibe, S., Koli, K. M., Serchinger, M., Schnütgen, F., Sürün, D., Sterner‐Kock, A., et al. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.09.006 · Cited by 13
Granulation Tissue Formation and Remodeling
Häkkinen, L., Larjava, H., & Koivisto, L. (2012) · Wiley eBooks · doi:10.1002/9781118704509.ch6 · Cited by 13
Canet-Jourdan, C., Pagès, D.-L., Nguyen-Vigouroux, C., Cartry, J., Zajac, O., Desterke, C., Lopez, J.-B., Gutierrez-Mateyron, E., Signolle, N., Adam, J., et al. (2022) · Journal of Cell Science · doi:10.1242/jcs.259256 · Cited by 17
Integrin-based adhesion compartmentalizes ALK3 of the BMPRII to control cell adhesion and migration
Guevara-Garcia, A., Fourel, L., Bourrin‐Reynard, I., Sales, A., Oddou, C. I., Pezet, M., Rossier, O., Machillot, P., Chaar, L., Bouin, A., et al. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202107110 · Cited by 12
“Several studies have reported synergistic effects between integrin mechanoreceptors and growth factor – receptor signaling pathways (Comoglio et al., 2003; Margadant and Sonnenberg, 2010; Ivaska and Heino, 2011).”
Ohshio, Y., Teramoto, K., Hashimoto, M., KITAMURA, S., Hanaoka, J., & Kontani, K. (2013) · Oncology Reports · doi:10.3892/or.2013.2505 · Cited by 12
“TGF-β induces the de novo expression of several types of integrins, such as α5β1, αvβ3, αvβ5 and αvβ6, in epithelial cells (26).”
Hatley, R. J. D., Macdonald, S. J. F., Slack, R. J., Le, J., Ludbrook, S. B., & Lukey, P. T. (2017) · Angewandte Chemie · doi:10.1002/ange.201707948 · Cited by 13
Pei, Z., Ji, J., Gao, Y., Wang, H., Wu, Y., Yang, J., Yang, Q., & Zhang, L. (2023) · Scientific Reports · doi:10.1038/s41598-023-36145-w · Cited by 12
“Emerging evidence has demonstrated that the transforming growth factor-β (TGF-β)/Smad signaling pathway plays a critical role in cardiac fibrosis 39 .”
β1 Integrins restrict the growth of foci and spheroids
Gupta, R. K., & Johansson, S. (2012) · Histochemistry and Cell Biology · doi:10.1007/s00418-012-1003-7 · Cited by 12
“cytokines deposited in the ECM (Hynes 2009; Margadant and Sonnenberg 2010; Parsons et al. 2010; Shi et al. 2011; Singh et al. 2010; Wickstrom et al. 2011).”
Bianchini, F., Peppicelli, S., Fabbrizzi, P., Biagioni, A., Mazzanti, B., Menchi, G., Calorini, L., Pupi, A., & Trabocchi, A. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2847-2 · Cited by 12
Sakata, T., Hana, K., Mikami, T., Yoshida, T., Endou, H., & Okayasu, I. (2020) · Pathology - Research and Practice · doi:10.1016/j.prp.2020.152972 · Cited by 12
Mao, Q., Liu, J., Yan, Y., Wang, G., Zhang, M., Wang, Z., Wen, X., Jiang, Z., Li, H., Li, J., et al. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.156545 · Cited by 14
A primer on cancer-associated fibroblast mechanics and immunosuppressive ability
Talayero, V. C., & Vicente‐Manzanares, M. (2023) · Exploration of Targeted Anti-tumor Therapy · doi:10.37349/etat.2023.00120 · Cited by 11
“Signaling downstream of integrins have multiple effects in this context, mainly TGF-β activation [51] and matrix reorganization in a myosin II-dependent manner [52].”
BackgroundKim, M., Renert‐Yuval, Y., Stepensky, P., Even‐Or, E., Zaidman, I., Fachler, T., Neumark, M., Zamir, M., NandyMazumdar, M., Gour, D. S., et al. (2023) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2023.08.026 · Cited by 11
Miskin, R. P., & DiPersio, C. M. (2024) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00128.2024 · Cited by 11
Schoberleitner, I., Lackner, M., Coraça-Huber, D. C., Augustin, A., Imsirovic, A., Sigl, S., & Wolfram, D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111675 · Cited by 11
“The contractile activity of myofibroblasts, driven by sustained TGF-β signaling [40,79], contributes significantly to capsule contraction and rigidity [23,29,86].”
BackgroundAmphiregulin in Fibrotic Diseases and Cancer
Kim, T. R., Son, B., Lee, C. G., & Park, H.-O. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146945 · Cited by 11
“Additionally, AREG sustains a feedforward loop involving integrin-α v and TGF-β signaling, perpetuating fibroblast activation and ECM remodeling [15,16,88,89].”
Brooks, D. L. P., Zimmer, A. S., Wakefield, L. M., Lyle, L. T., Difilippantonio, S., Tucci, F. C., Illiano, S., Annunziata, C. M., & Steeg, P. S. (2018) · Oncotarget · doi:10.18632/oncotarget.25231 · Cited by 13
Tanaka, S., Hamada, Y., Yokoyama, Y., Yamamoto, H., & Kogo, M. (2021) · Japanese Dental Science Review · doi:10.1016/j.jdsr.2021.09.002 · Cited by 10
Sani, F., Sani, M., Moayedfard, Z., Darayee, M., Tayebi, L., & Azarpira, N. (2023) · Stem Cell Research & Therapy · doi:10.1186/s13287-023-03364-x · Cited by 11
“TGF-β ligands stimulate the Smad-2/3 pathway and the expression of several profibrotic genes, including various types of collagens [95, 96], plasminogen activator inhibitor-1 (PAI-1) [97, 98], integrins [99], some proteoglycans [100, 101], MMPs [102], and connective tissue growth factor [103].”
Backgroundthe PBC Study Group in NHOSLJ, Inamine, T., Nakamura, M., Kawauchi, A., Shirakawa, Y., Hashiguchi, H., Aiba, Y., Taketomi, A., Shirabe, K., Nakamuta, M., et al. (2010) · Journal of Gastroenterology · doi:10.1007/s00535-010-0351-0 · Cited by 11
Sun, Y., Moriya, T., Zhao, C., Kirk, R. L., Chikenji, T., Passe, S. M., An, K., & Amadio, P. C. (2011) · Journal of Orthopaedic Research® · doi:10.1002/jor.21565 · Cited by 11
Retinal biomarkers and pharmacological targets for Hermansky-Pudlak syndrome 7
Romano, G. L., Platania, C. B. M., Leggio, G. M., Torrisi, S. A., Giunta, S., Salomone, S., Purrello, M., Ragusa, M., Barbagallo, C., Giblin, F. J., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-60931-5 · Cited by 10
Iwatate, Y., Yokota, H., Hoshino, I., Ishige, F., Kuwayama, N., Itami, M., Mori, Y., Chiba, S., Arimitsu, H., Yanagibashi, H., et al. (2022) · International Journal of Oncology · doi:10.3892/ijo.2022.5350 · Cited by 11
Translational control of the fibroblast-extracellular matrix association
Nho, R. S., & Polunovsky, V. A. (2013) · Translation · doi:10.4161/trla.23934 · Cited by 11
Recent proteomic advances in developmental, regeneration, and cancer governing signaling pathways
Franco, C., & Hess, S. Y. (2014) · PROTEOMICS · doi:10.1002/pmic.201400368 · Cited by 11
Geniposide alleviates pressure overload in cardiac fibrosis with suppressed TGF-β1 pathway
Yao, Y., Lin, L., Tang, W., Shen, Y., Chen, F., & Li, N. (2023) · Acta Histochemica · doi:10.1016/j.acthis.2023.152044 · Cited by 10
Zheng, X., Du, Y., Liu, M., & Wang, C. (2023) · Functional & Integrative Genomics · doi:10.1007/s10142-023-01122-z · Cited by 10
RetractedMolecular genetics of Dupuytren’s contracture
Aissvarya, S., Ling, K., Arumugam, M., & Thilakavathy, K. (2024) · EFORT Open Reviews · doi:10.1530/eor-23-0056 · Cited by 10
“The integrin pathway controls the regulation of cell adhesion, spreading of cells and migration, proliferation, differentiation and ECM remodelling ( 46).”
Laskaratos, F., Levi, A., Schwach, G., Pfragner, R., Hall, A. R., Xia, D., von Stempel, C. B., Bretherton, J., Thanapirom, K., Alexander, S., et al. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.629665 · Cited by 10
“In addition, there is extensive crosstalk between integrins and TGFb signaling, which is important in both cancer progression and fibrosis development (47).”
BackgroundTenascins and osteopontin in biological response in cornea
Sumioka, T., Matsumoto, K., Reinach, P. S., & Saika, S. (2023) · The Ocular Surface · doi:10.1016/j.jtos.2023.05.005 · Cited by 10
Regulation of TGFβ superfamily signaling by two separable domains of glypican LON-2 inC. elegans
Taneja‐Bageshwar, S., & Gumienny, T. L. (2013) · Worm · doi:10.4161/worm.23843 · Cited by 9
Involvement of transcription factor E ts‐1 in the expression of the α3 integrin subunit gene
Kamoshida, G., Matsuda, A., Katabami, K., Kato, T., Mizuno, H., Sekine, W., Oku, T., Itoh, S., Tsuiji, M., Hattori, Y., et al. (2012) · FEBS Journal · doi:10.1111/febs.12040 · Cited by 10
Microenvironmental factors involved in human amnion mesenchymal stem cells fate decisions
Syva, S. H., Ampon, K. H., Lasimbang, H. B., & Fatimah, S. S. (2015) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1002/term.2043 · Cited by 10
“…regulate signalling pathways corresponding to soluble properties, such as growth factors and cytokines, the specific actions of protein receptors in the ECM can be set for particular stem cell niche (Legate et al., 2009; Uberti et al., 2010; Margadant and Sonnenberg, 2010; Ivaska and Heino, 2011).”
BackgroundDjafarzadeh, R., Conrad, C. H., Notohamiprodjo, S., Hipp, S., Nieß, H., Bruns, C. J., & Nelson, P. J. (2014) · Wound Repair and Regeneration · doi:10.1111/wrr.12132 · Cited by 9
Letsoalo, K., Nortjé, E., Patrick, S. M., Nyakudya, T. T., & Hlophe, Y. N. (2024) · Cell Biochemistry and Function · doi:10.1002/cbf.3950 · Cited by 9
Pashaei, M., Farhadi, E., Kavosi, H., Madreseh, E., Enayati, S., Mahmoudi, M., & Amirzargar, A. (2024) · Inflammopharmacology · doi:10.1007/s10787-024-01536-6 · Cited by 9
Advances in applications of low-dimensional piezoelectric materials in musculoskeletal system
Liu, L., Li, Z., Zhu, T., Sun, Y., & Xu, J. L. (2025) · Materials Today Bio · doi:10.1016/j.mtbio.2025.102065 · Cited by 11
“Similar to the Wnt pathway, the TGF-β /SMAD pathway can also be regulated by integrins, in this way providing opportunities for electromechanical synergy [68].”
Mardhian, D. F., Pednekar, K. P., Hemdan, A. G., Kuninty, P. R., Karim, S. A., de Winter, S., Metselaar, J. M., Morton, J. P., & Prakash, J. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.10.022 · Cited by 11
Mechanism and research progress of MAPK signaling pathway in myocardial fibrosis
Wu, J., Chen, M., Peng, Z., Sun, Y., & Jin, J. (2025) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2025.1667568 · Cited by 14
Sun, Q., Hu, J., Yu, P., Zhu, Z., Yu, R., Ge, C., Li, C., Wu, G., Lin, B., Liu, G., et al. (2019) · Experimental Lung Research · doi:10.1080/01902148.2019.1614696 · Cited by 9
Chang, C. W.-J., Cheng, N., Bai, Y., Skidgel, R. A., & Du, X. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2001385 · Cited by 8
Shifting Towards αVβ6 Integrin Ligands Using Novel Aminoproline‐Based Cyclic Peptidomimetics
Bugatti, K., Bruno, A., Arosio, D., Sartori, A. M., Curti, C., Augustijn, L., Zanardi, F., & Battistini, L. (2020) · Chemistry - A European Journal · doi:10.1002/chem.202002554 · Cited by 9
Mygind, K. J., Nikodemus, D., Gnosa, S. P., Kweder, R., Albrechtsen, N. J. W., Kveiborg, M., Erler, J. T., & Albrechtsen, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25115871 · Cited by 9
Shi, J., Qin, X., Sha, H., Wang, R., Shen, H., Chen, Y., & Chen, X. (2025) · Renal Failure · doi:10.1080/0886022x.2024.2449195 · Cited by 8
Tunable Synthetic Hydrogel Modulates Hepatic Lineage Specification of Human Liver Organoid
Wang, L., Riediger, L., Rao, Q., Xu, X., Nie, Y., Zhou, Y., Zhang, J., Tang, P., Wang, W., Tacke, F., et al. (2025) · Advanced Functional Materials · doi:10.1002/adfm.202508430 · Cited by 11
Antifibrotic mechanism of avitinib in bleomycin-induced pulmonary fibrosis in mice
Miao, Y., Wang, Y., Bi, Z., Huang, K., Gao, J., Li, X., Li, S., Wei, L., Zhou, H., & Yang, C. (2023) · BMC Pulmonary Medicine · doi:10.1186/s12890-023-02385-9 · Cited by 8
Basic Science for the Clinician 57
Sigal, L. H. (2012) · JCR Journal of Clinical Rheumatology · doi:10.1097/rhu.0b013e318262232c · Cited by 8
Ahmad, A., Askari, S., Befekadu, R., & Hahn‐Strömberg, V. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2014.3083 · Cited by 8
Chang, Z., Chen, C.-C., Liu, H.-M., Yeh, Y.-C., Lin, T.-Y., Lee, T.-Y., & Huang, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20174181 · Cited by 9
Alzoghaibi, M. A., & Zubaidi, A. M. (2013) · Asian Journal of Surgery · doi:10.1016/j.asjsur.2013.07.016 · Cited by 8
Lu, Y., Lin, Y., Kao, Y., Chung, C., Yeh, Y., Chen, S., & Chen, Y. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.5635 · Cited by 8
Chong, K., Kwon, W., Kim, J. H., Park, Y., Yoon, W. K., Kim, J. H., Kwon, T. H., & Moon, H. J. (2018) · Journal of Orthopaedic Research® · doi:10.1002/jor.24207 · Cited by 8
Fu, Y., Sun, X., Gu, Z., & Zhuang, Z. (2020) · OncoTargets and Therapy · doi:10.2147/ott.s229076 · Cited by 8
Wound healing mechanism in Mongolian gerbil skin
Lee, M.-J., Lee, D., & Jung, H.-S. (2018) · Histochemistry and Cell Biology · doi:10.1007/s00418-018-1752-z · Cited by 8
Growth Factors in the Gastrointestinal Tract
Kuemmerle, J. F., Barnard, J. A., & McHugh, K. M. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-382026-6.00008-7 · Cited by 8
Re‐Epithelialization of Wounds
Larjava, H., Häkkinen, L., & Koivisto, L. (2012) · Wiley eBooks · doi:10.1002/9781118704509.ch5 · Cited by 8
Schoberleitner, I., Faserl, K., Lackner, M., Coraça-Huber, D. C., Augustin, A., Imsirovic, A., Sigl, S., & Wolfram, D. (2024) · Biomolecules · doi:10.3390/biom14111433 · Cited by 7
Yu, L., Wang, R., Hou, Q., Yang, F., Liu, Y., Peng, M., Dong, Y., Liu, Y., & Cheng, Z. (2025) · Scientific Reports · doi:10.1038/s41598-025-09318-y · Cited by 10
NIPPER, M. J., Xu, Y., Liu, J., Yin, X., Liu, Z., Ye, Z., Zhang, J., Chen, Y., & Wang, P. (2024) · Cells · doi:10.3390/cells13020186 · Cited by 8
“…between YAP1 and SMAD4 in inducing ADM-associated transcriptional changes adds a new dimension to our understanding of Hippo and TGF β pathways in human ADM. TGF-β is well-known for its role in wound healing and tissue repair and has been shown to induce fibrosis in various organs [51].”
BackgroundFioretto, B. S., Rosa, I., Tani, A., Andreucci, E., Romano, E., Sgambati, E., & Manetti, M. (2024) · Cells · doi:10.3390/cells13121067 · Cited by 7
Fu, Y., Sun, X., He, Q., Gu, Z., Jia, X., & Zhuang, Z. (2024) · SLAS TECHNOLOGY · doi:10.1016/j.slast.2024.100190 · Cited by 7
Activation of integrin-ERBB2 signaling in undifferentiated thyroid cancer.
Zhu, X., Zhu, Y. J., Kim, D. W., Meltzer, P. S., & Cheng, S.-Y. (2014) · Europe PMC (PubMed Central) · Cited by 7
Pan, X. L., Li, J., He, X., Deng, J., Dong, F., Wang, K., & Yu, S. (2019) · BioMetals · doi:10.1007/s10534-019-00205-4 · Cited by 7
Shibui, T., Yajima, T., Irie, K., Ochi, M., & Sakakura, Y. (2020) · Anatomical Science International · doi:10.1007/s12565-020-00526-2 · Cited by 7
Role of β1 integrin in thrombocytopoiesis
Mazzarini, M., Verachi, P., Martelli, F., & Migliaccio, A. R. (2021) · Faculty Reviews · doi:10.12703/r/10-68 · Cited by 7
Engineering Multivalent and Multispecific Protein Therapeutics
Liu, C. J., & Cochran, J. R. (2013) · Springer eBooks · doi:10.1007/978-1-4471-4372-7_14 · Cited by 7
“15), occurs in both healthy and diseased states [56–59].”
BackgroundLiu, J., Xu, D., Li, J., Gao, N., Liao, C., Jing, R., Wu, B., Ma, B., Shao, Y., & Pei, C. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3912 · Cited by 9
Silencing of p53 reduces cell migration in human Tenon's fibroblasts induced by TGF-β
Li, N., & Zhang, R. (2020) · International Ophthalmology · doi:10.1007/s10792-020-01320-9 · Cited by 7
Klungsaeng, S., Hongsrichan, N., Chaidee, A., Intuyod, K., Pinlaor, P., Roytrakul, S., Vaeteewoottacharn, K., Charoenlappanit, S., Dangtakot, R., Mahaamnad, N., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-99980-z · Cited by 6
Xiao, H., Zhang, W., Liu, J., Ma, Y., Liu, D., Li, M., Xin, R., He, L., & Liu, S. (2026) · Advanced Healthcare Materials · doi:10.1002/adhm.202503560 · Cited by 6
“Studies have shown that FAK is closely related to the occurrence of fibrosis-related diseases [62, 63].”
Nanoapproach targeting TGFβ1-Smad pathway and modulating lung microenvironment
Kulshrestha, R., Singh, A. K., Kumar, P., Nair, D. S., Batra, J., Mishra, A., & Dinda, A. K. (2022) · Process Biochemistry · doi:10.1016/j.procbio.2022.06.027 · Cited by 6
Hara, M., Matsuura, T., & Kojima, S. (2015) · Springer eBooks · doi:10.1007/978-4-431-55651-0_26 · Cited by 6
Su, J., Gan‐Schreier, H., Goeppert, B. F., Chamulitrat, W., Stremmel, W., & Pathil, A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103254 · Cited by 6
“Furthermore, integrins have been reported to be involved in HSC activation and migration [2] and found to be upregulated during liver fibrosis [3].”
BackgroundDonnelly, H., Kurjan, A., Yong, L., Xiao, Y., Lemgruber, L., West, C. C., Salmerón‐Sánchez, M., & Dalby, M. J. (2023) · Biomaterials Advances · doi:10.1016/j.bioadv.2023.213370 · Cited by 6
“SMADs (small mothers against decapentaplegic) are intracellular mediators activated by phosphorylation upon TGF β 1/SMAD signalling [48,49].”
BackgroundFeatures of intestinal lesions in the clinical course of Inflammatory Bowel Diseases
Vetuschi, A., Latella, G., Pompili, S., Gaudio, E., & Sferra, R. (2015) · Italian Journal of Anatomy and Embryology · doi:10.13128/ijae-15562 · Cited by 8
Tunable Microfibers Suppress Fibrotic Encapsulation via Inhibition of TGFβ Signaling
Allen, J., Ryu, J., Maggi, A., Flores, B., Greer, J. R., & Desai, T. A. (2015) · Tissue Engineering Part A · doi:10.1089/ten.tea.2015.0087 · Cited by 6
Zhu, L., Xie, L., Zhi, Y., Huang, Y., Chen, H., Chen, Z., Hong, J., Guo, Y., & Chen, C. (2025) · Regenerative Biomaterials · doi:10.1093/rb/rbaf057 · Cited by 5
The immunoregulatory role of integrins in pulmonary diseases
Xu, Q., Yang, C., Li, W., Qian, W., Chen, S., & Yang, L. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1716118 · Cited by 5
Smad2 overexpression enhances adhesion of gingival epithelial cells
Hongo, S., Yamamoto, T., Yamashiro, K., Shimoe, M., Tomikawa, K., Ugawa, Y., Kochi, S., Ideguchi, H., Maeda, H. A., & Takashiba, S. (2016) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2016.06.025 · Cited by 5
Integrin activating molecule-talin1 promotes skin fibrosis in systemic sclerosis
Xu, D., Yuan, X., Zhao, L., & Mu, R. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1400819 · Cited by 8
Network-based analysis of genotype–phenotype correlations between different inheritance modes
Hao, D., Li, C., Zhang, S., Lu, J., Jiang, Y., Wang, S., & Zhou, M. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu482 · Cited by 5
“Previous studies on human disease highlight the importance of bottleneck genes that mediate the communication between functional modules (Margadant and Sonnenberg, 2010; Shao et al ., 2012; Taylor et al ., 2009; Xu et al ., 2011), for which the node degree might be small but with important protein…”
BackgroundGolinelli, G., Talami, R., Frabetti, S., Candini, O., Grisendi, G., Spano, C., Chiavelli, C., Arnaud, G., Mari, G., & Dominici, M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.767253 · Cited by 5
Arg-Gly-Asp-binding integrins activate hepatic stellate cells via the hippo signaling pathway
Kitsugi, K., Noritake, H., Matsumoto, M., Hanaoka, T., Umemura, M., Yamashita, M., Takatori, S., Ito, J., Ohta, K., Chida, T., et al. (2022) · Cellular Signalling · doi:10.1016/j.cellsig.2022.110437 · Cited by 5
Baghmisheh, S. T., Wu, Y.-Y., Wu, J., Hsu, K., Chen, Y., & Hong, T.-M. (2023) · PubMed Central · Cited by 5
Recently reported cell migration inhibitors: Opportunities and challenges for antimetastatic agents
Akompong, S. K., Li, Y., Gong, W., Ye, L., & Liu, J. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.103906 · Cited by 5
Reassessing the Role of Tissue Factor Pathway Inhibitor 2 in Neoplastic and Non-Neoplastic Lesions
Kobayashi, H., Shigetomi, H., & Imanaka, S. (2025) · Cancers · doi:10.3390/cancers17091447 · Cited by 5
Metadata
- Authors
- Margadant, C., & Sonnenberg, A.
- Affiliations
- The Netherlands Cancer Institute (NL)
- Corresponding author
- Sonnenberg, Arnoud
- Venue
- The EMBO Reports
- Published
- 2010-01-15
- Volume
- 11
- Issue
- 2
- Pages
- 97-105
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC2828749
- OpenAlex
- W2112195516
- Cited by
- 653
- References
- 81
- Citations by year
- 2026: 28 · 2025: 50 · 2024: 32 · 2023: 41 · 2022: 30 · 2021: 38 · 2020: 41 · 2019: 34 · 2018: 45 · 2017: 38 · 2016: 45 · 2015: 43 · 2014: 49 · 2013: 36 · 2012: 51
- FWCI
- 3.90
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- EMBO Reports (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Molecular Biology Organization
- Dystrophic Epidermolysis Bullosa Research Association
- KWF Kankerbestrijding
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- TGF-beta signaling, integrins, Smad signaling, TGF-beta receptor, cell adhesion, cell migration, fibrosis, systemic sclerosis, idiopathic pulmonary fibrosis, chronic obstructive pulmonary disease, cancer, wound healing, therapeutic target
- MeSH terms
- Animals, Fibrosis, Humans, Models, Biological, Neoplasms, Wound Healing, Integrins, Transforming Growth Factor beta, Disease Progression, Receptor Cross-Talk
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