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Force interacts with macromolecular structure in activation of TGF-β
Open accessAbstract
Integrins are adhesion receptors that transmit force across the plasma membrane between extracellular ligands and the actin cytoskeleton. In activation of the transforming growth factor-β1 precursor (pro-TGF-β1), integrins bind to the prodomain, apply force, and release the TGF-β growth factor. However, we know little about how integrins bind macromolecular ligands in the extracellular matrix or transmit force to them. Here we show how integrin α V β 6 binds pro-TGF-β1 in an orientation biologically relevant for force-dependent release of TGF-β from latency. The conformation of the prodomain integrin-binding motif differs in the presence and absence of integrin binding; differences extend well outside the interface and illustrate how integrins can remodel extracellular matrix. Remodelled residues outside the interface stabilize the integrin-bound conformation, adopt a conformation similar to earlier-evolving family members, and show how macromolecular components outside the binding motif contribute to integrin recognition. Regions in and outside the highly interdigitated interface stabilize a specific integrin/pro-TGF-β orientation that defines the pathway through these macromolecules which actin-cytoskeleton-generated tensile force takes when applied through the integrin β-subunit. Simulations of force-dependent activation of TGF-β demonstrate evolutionary specializations for force application through the TGF-β prodomain and through the β- and not α-subunit of the integrin.
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“mice genetically engineered to replace murine β8 with its human ortholog demonstrated that a blocking antibody against human αvβ8 blocks TGF-β1 activation and protects against allergic airway inflammation and remodeling induced by cigarette smoke106”
From Fibrosis: from mechanisms to medicines (2020) · cites this paper as [106]
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Cites
Svergun, D. I., Barberato, C., & Koch, M. (1995) · Journal of Applied Crystallography · doi:10.1107/s0021889895007047 · Cited by 3,388
PRIMUS: a Windows PC-based system for small-angle scattering data analysis
Konarev, P. V., Волков, В. В., Sokolova, A. V., Koch, M. H. J., & Svergun, D. I. (2003) · Journal of Applied Crystallography · doi:10.1107/s0021889803012779 · Cited by 2,850
Xiong, J.-P., Stehle, T., Zhang, R., Joachimiak, A., Frech, M., Goodman, S. L., & Arnaout, M. A. (2002) · Science · doi:10.1126/science.1069040 · Cited by 1,617
Latent TGF-β structure and activation
Shi, M., Zhu, J., Wang, R., Chen, X., Mi, L., Walz, T., & Springer, T. A. (2011) · Nature · doi:10.1038/nature10152 · Cited by 1,013
Self-citationHydrogen exchange mass spectrometry for the analysis of protein dynamics
Wales, T. E., & Engen, J. R. (2005) · Mass Spectrometry Reviews · doi:10.1002/mas.20064 · Cited by 864
Self-citationAbe, M., Harpel, J. G., Metz, C. N., Nunes, I., Loskutoff, D. J., & Rifkin, D. B. (1994) · Analytical Biochemistry · doi:10.1006/abio.1994.1042 · Cited by 757
TGF-β Superfamily Signaling in Embryonic Development and Homeostasis
Wu, M., & Hill, C. S. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.02.012 · Cited by 743
Fibronectins, Their Fibrillogenesis, and In Vivo FunctionsPreprint
Schwarzbauer, J. E., & DeSimone, D. W. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005041 · Cited by 445
Strength of a Weak Bond Connecting Flexible Polymer Chains
Evans, E. A., & Ritchie, K. P. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77399-6 · Cited by 429
Regulation of the Bioavailability of TGF-β and TGF-β-Related Proteins
Robertson, I. B., & Rifkin, D. B. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021907 · Cited by 403
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Lockhart‐Cairns, M. P., Cain, S. A., Dajani, R., Steer, R., Thomson, J., Alanazi, Y. F., Kielty, C. M., & Baldock, C. (2022) · Matrix Biology · doi:10.1016/j.matbio.2022.01.005 · Cited by 38
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Wang, W., Gao, Y., Chen, Y., Cheng, M., Sang, Y., Wei, L., Dai, R., Wang, Y., & Zhang, L. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1583616 · Cited by 37
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Liao, J., Chen, R., Lin, B., Deng, R., Liang, Y., Zeng, J., Ma, S., & Qiu, X. (2024) · International Journal of Medical Sciences · doi:10.7150/ijms.96274 · Cited by 38
Mechanical loading and the control of stem cell behavior
Manokawinchoke, J., Pavasant, P., Limjeerajarus, C. N., Limjeerajarus, N., Osathanon, T., & Egusa, H. (2021) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2021.105092 · Cited by 34
Ion channel mediated mechanotransduction in immune cells
Atcha, H., Jairaman, A., Evans, E. L., Pathak, M. M., Cahalan, M. D., & Liu, W. F. (2021) · Current Opinion in Solid State and Materials Science · doi:10.1016/j.cossms.2021.100951 · Cited by 34
Tolloid cleavage activates latent GDF8 by priming the pro‐complex for dissociation
Le, V. Q., Iacob, R. E., Tian, Y., McConaughy, W., Jackson, J., Su, Y., Zhao, B., Engen, J. R., Pirruccello, M., & Springer, T. A. (2018) · The EMBO Journal · doi:10.15252/embj.201797931 · Cited by 33
Self-citationZheng, B., Xiao, Y., Tong, B., Mao, Y., Ge, R., Tian, F., Dong, X., & Zheng, P. (2023) · JACS Au · doi:10.1021/jacsau.3c00142 · Cited by 30
Self-citationDas, S. S., Ahlawat, S., Thakral, P., Malik, D., Šimeček, J., Virupakshappa, C. B., Koley, M., Gupta, J., & Sen, I. B. (2024) · Clinical Nuclear Medicine · doi:10.1097/rlu.0000000000005278 · Cited by 32
New insights into the pathogenesis of Peyronie's disease: A narrative review
Krakhotkin, D. V., Chernylovskyi, V. A., Mottrie, A., Greco, F., & Bugaev, R. A. (2020) · Chronic Diseases and Translational Medicine · doi:10.1016/j.cdtm.2020.06.001 · Cited by 33
Gori, I., George, R., Purkiss, A. G., Strohbuecker, S., Randall, R. A., Ogrodowicz, R. W., Carmignac, V., Faivre, L. O., Joshi, D., Kjær, S., et al. (2021) · eLife · doi:10.7554/elife.63545 · Cited by 32
Wang, S., Niu, Y., Jia, P., Liao, Z.-T., Guo, W., Chaves, R. C., Tran‐Ba, K., He, L., Bai, H., Sia, S., et al. (2021) · Bioactive Materials · doi:10.1016/j.bioactmat.2021.12.015 · Cited by 33
Anderson, J. M., Li, J., & Springer, T. A. (2022) · Molecular Biology of the Cell · doi:10.1091/mbc.e21-11-0536 · Cited by 32
Self-citationTargeting cluster of differentiation 26 / dipeptidyl peptidase 4 (CD26/DPP4) in organ fibrosis
Ohm, B., Moneke, I., & Jungraithmayr, W. (2022) · British Journal of Pharmacology · doi:10.1111/bph.15967 · Cited by 35
Zhang, Q., Ye, W., Liu, Y., Decao, N., Zhao, X., Li, G., Qu, Y., & Zhao, Z. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.114018 · Cited by 32
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Cai, K., Zhang, X., & Bai, X. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c01035 · Cited by 31
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Matsuoka, T., & Yashiro, M. (2023) · Biomolecules · doi:10.3390/biom13101551 · Cited by 32
68Ga-Trivehexin PET/CT: a promising novel tracer for primary hyperparathyroidism
Kuyumcu, S., Denizmen, D., Şimşek, D. H., Poyanlı, A., Üzüm, A. K., Büyükkaya, F., Işık, E. G., Önder, S. Y., Aksakal, N., Özkan, Z. G., et al. (2024) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-024-06846-z · Cited by 31
Kim, D., Sung, M., Park, M., Sun, E. G., Yoon, S., Yoo, K. H., Radhakrishnan, K., Jung, S. Y., Bae, W., Cho, S., et al. (2024) · 癌症：英文版 · doi:10.1002/cac2.12600 · Cited by 31
Del-1, an Endogenous Inhibitor of TGF-β Activation, Attenuates Fibrosis
Kim, D.-Y., Lee, S. H., Fu, Y., Jing, F., Kim, W., Hong, S., Song, J.-A., Choe, H., Ryu, H. J., Kim, M.-J., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00068 · Cited by 31
A tumor-specific mechanism of T reg enrichment mediated by the integrin αvβ8
Seed, R., Kobayashi, K., Ito, S., Takasaka, N., Cormier, A., Jespersen, J. M., Publicover, J., Trilok, S., Combes, A. J., Chew, N. W., et al. (2021) · Science Immunology · doi:10.1126/sciimmunol.abf0558 · Cited by 31
Specificity of TGF-β1 signal designated by LRRC33 and integrin αVβ8
Duan, Z., Lin, X., Wang, L., Zhen, Q., Jiang, Y., Chen, C., Yang, J. H., Lee, C., Qin, Y., Li, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32655-9 · Cited by 31
Self-citationMechanotransduction for therapeutic approaches: Cellular aging and rejuvenation
Han, H.-M., Kim, S.-Y., & Kim, D. (2025) · APL Bioengineering · doi:10.1063/5.0263236 · Cited by 30
Dagbay, K. B., Treece, E. R., Streich, F. C., Jackson, J., Faucette, R., Nikiforov, A., Lin, S. C., Boston, C., Nicholls, S. B., Capili, A. D., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012293 · Cited by 32
Jackson, J., Streich, F. C., Pal, A., Coricor, G., Boston, C., Brueckner, C., Canonico, K., Chapron, C., Cote, S. M., Dagbay, K. B., et al. (2024) · Science Signaling · doi:10.1126/scisignal.adn6052 · Cited by 30
D’Amore, V. M., Donati, G., Lenci, E., Ludwig, B. S., Kossatz, S., Baiula, M., Trabocchi, A., Kessler, H., Leva, F. S. D., & Marinelli, L. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c01071 · Cited by 27
The Role of Mechanotransduction in Contact Inhibition of Locomotion and Proliferation
Nakamura, F. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25042135 · Cited by 30
Kossatz, S., Beer, A. J., & Notni, J. (2021) · Cancers · doi:10.3390/cancers13235958 · Cited by 28
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Santus, W., Barresi, S., Mingozzi, F., Broggi, A., Orlandi, I., Stamerra, G., Vai, M., Martorana, A. M., Polissi, A., Köhler, J. R., et al. (2017) · Science Immunology · doi:10.1126/sciimmunol.aan2725 · Cited by 27
Huang, Y.-J., Sun, M., Lu, Z., Zhong, Q., Tan, M., Wei, Q., & Li, Z. (2024) · Regenerative Biomaterials · doi:10.1093/rb/rbae017 · Cited by 26
Welsh, B. T., Faucette, R., Bilic, S., Martin, C. J., Schürpf, T., Chen, D. J., Nicholls, S. B., Lansita, J. A., & Kalra, A. V. (2021) · International Journal of Toxicology · doi:10.1177/1091581821998945 · Cited by 28
Zakrzewski, P. K. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10173900 · Cited by 27
Higgins, C. E., Tang, J., Higgins, S. P., Gifford, C. C., Mian, B. M., Jones, D., Zhang, W., Costello, A., Conti, D. J., Samarakoon, R., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.678524 · Cited by 25
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Yamashiro, Y., & Yanagisawa, H. (2017) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat.rv17015 · Cited by 25
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Shen, L., Jiang, S., Zhang, Q., Jin, B. R., Lv, D., Li, W., Zhao, M., Jiang, C., Dai, C., & Liu, Z. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.733831 · Cited by 27
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Schwarz, E. (2017) · Biological Chemistry · doi:10.1515/hsz-2017-0163 · Cited by 24
Yokosaki, Y., & Nishimichi, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312794 · Cited by 24
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Oglić, D., Oatley, S. A., Macdonald, S. J. F., Mcinally, T., Garnett, R., Hirst, J. D., & Gärtner, T. (2018) · Molecular Informatics · doi:10.1002/minf.201700130 · Cited by 24
Does protein unfolding play a functional role in vivo?
Sharma, S., Subramani, S., & Popa, I. (2020) · FEBS Journal · doi:10.1111/febs.15508 · Cited by 22
Song, X., Shi, J., Liu, J., Liu, Y., Yu, Y., Qiu, Y., Cao, Z., Pan, Y., Yuan, X., Chu, Y., et al. (2022) · Molecular Medicine · doi:10.1186/s10020-022-00508-2 · Cited by 22
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Tan, M., Ge, Y., Wang, X., Wang, Y., Liu, Y., He, F., & Teng, H. (2023) · Technology in Cancer Research & Treatment · doi:10.1177/15330338231171463 · Cited by 22
A specialized integrin-binding motif enables proTGF-β2 activation by integrin αVβ6 but not αVβ8
Le, V. Q., Zhao, B., Ramesh, S., Toohey, C., DeCosta, A., Mintseris, J., Liu, X., Gygi, S. P., & Springer, T. A. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2304874120 · Cited by 23
Self-citationMattson, N. M., Chan, A., Miyashita, K., Mukhaleva, E., Chang, W.-H., Yang, L., Ma, N., Wang, Y., Pokharel, S. P., Li, M., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01211-y · Cited by 22
High integrin α V β 6 affinity reached by hybrid domain deletion slows ligand-binding on-rate
Dong, X., Zhao, B., Lin, F., Lu, C., Rogers, B. N., & Springer, T. A. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718662115 · Cited by 22
Self-citationSpatiotemporal regulation of PEDF signaling by type I collagen remodeling
Kawahara, K., Yoshida, T., Maruno, T., Oki, H., Ohkubo, T., Koide, T., & Kobayashi, Y. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2004034117 · Cited by 22
Systemic inhibition of BMP1-3 decreases progression of CCl4-induced liver fibrosis in rats
Grgurević, L., Erjavec, I., Grgurević, I., Dumić-Čule, I., Brkljačić, J. M., Verbanac, D., Matijašić, M., Paljetak, H. Č., Novak, R., Plečko, M., et al. (2017) · Growth Factors · doi:10.1080/08977194.2018.1428966 · Cited by 21
Quigley, N. G., Steiger, K., Richter, F., Weichert, W., Hoberück, S., Kotzerke, J., & Notni, J. (2020) · EJNMMI Research · doi:10.1186/s13550-020-00706-1 · Cited by 21
Nakamura, Y., & Shimizu, Y. (2023) · Cells · doi:10.3390/cells12040548 · Cited by 20
Zhang, H., Wang, Z., Nguyen, H. T. T., Watson, A. J., Lao, Q., Li, A., & Zhu, J. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2311913120 · Cited by 20
Self-citationLi, S., Yang, Q., Chen, F., Tian, L., Huo, J., Meng, Y., Tang, Q., & Wang, W. (2021) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2021.114901 · Cited by 20
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Buß, M., Tegtmeyer, N., Schnieder, J., Dong, X., Li, J., Springer, T. A., Backert, S., & Niemann, H. H. (2019) · FEBS Journal · doi:10.1111/febs.14962 · Cited by 20
Self-citationCao, J., Gong, Z., Liu, X., Meng, F., Sun, X., Yuan, X., Li, A., Huang, H., Wang, Y., Lu, C., et al. (2023) · ACS Materials Letters · doi:10.1021/acsmaterialslett.3c00357 · Cited by 19
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Ha, T. (2017) · Nature · doi:10.1038/nature21119 · Cited by 19
He, J., Jiang, Y., Wang, Y., Tian, X., & Sun, S. (2020) · Chinese Medical Journal · doi:10.1097/cm9.0000000000000720 · Cited by 19
Li, B., Fu, Q., Lu, Y. Z., Chen, C., Zhao, Y., Zhao, Y., Cao, M., Zhou, W., Fan, X., Jiang, X., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60062-3 · Cited by 19
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Liu, Q., Hsu, C., Li, J., & Shyr, Y. (2022) · Bioinformatics · doi:10.1093/bioinformatics/btac294 · Cited by 20
Li, X., Zhu, G., Li, Y., Huang, H., Wu, D., 曹佩军, Shi, R., Chen, C., Su, L., Zhang, R., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1096818 · Cited by 18
Cui, S., Fu, Y., Yu, M., Zhang, L., Zhao, W., Zhang, T., Qiu, L.-X., Gu, Y., Zhou, Y.-H., & Liu, Y. (2021) · Chemical Engineering Journal · doi:10.1016/j.cej.2021.133220 · Cited by 18
Theory of frequency response of mechanically driven cardiomyocytes
Cohen, O., & Safran, S. A. (2018) · Scientific Reports · doi:10.1038/s41598-018-20307-2 · Cited by 18
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Rahaman, S. G., Khan, M. I., Sankaran, K. R., & Rahaman, S. O. (2025) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00595.2025 · Cited by 18
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Zhu, W., Fan, C., Zhao, Y., Li, W., Niu, J., Dong, S., Yang, Z., & Zhou, W. (2025) · Cancer Cell International · doi:10.1186/s12935-025-03980-y · Cited by 17
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Singh, K., Sachan, N., Ene, T., Dabovic, B., & Rifkin, D. B. (2022) · Matrix Biology · doi:10.1016/j.matbio.2022.08.001 · Cited by 16
Tomassi, S., D’Amore, V. M., Leva, F. S. D., Vannini, A., Quilici, G., Weinmüller, M., Reichart, F., Amato, J., Romano, B., Izzo, A. A., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00533 · Cited by 15
Song, D., Tang, L., Huang, J., Wang, L., Zeng, T., & Wang, X. (2019) · Journal of Translational Medicine · doi:10.1186/s12967-019-02181-2 · Cited by 15
Mendoza, F. A., & Jiménez, S. A. (2021) · Rheumatology · doi:10.1093/rheumatology/keab762 · Cited by 14
Immune Checkpoints and the Immunology of Liver Fibrosis
Tsomidis, I., Voumvouraki, A., & Kouroumalis, E. (2025) · Livers · doi:10.3390/livers5010005 · Cited by 14
Sodium Salicylate Inhibits Urokinase Activity in MDA MB-231 Breast Cancer Cells
Madunić, J., Horvat, L., Majstorović, I., Jodłowska, I., Antica, M., & Matulić, M. (2017) · Clinical Breast Cancer · doi:10.1016/j.clbc.2017.03.015 · Cited by 13
Family-wide analysis of integrin structures predicted by AlphaFold2
Zhang, H., Zhu, D. S., & Zhu, J. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.09.022 · Cited by 12
Self-citationStructural analysis of peptide binding to integrins for cancer detection and treatment
Urquiza, M., Benavides-Rubio, D., & Jimenez-Camacho, S. (2023) · Biophysical Reviews · doi:10.1007/s12551-023-01084-3 · Cited by 12
Huang, S., Lin, Y., Deng, Q., Zhang, Y., Peng, S., Qiu, Y., Huang, W., Wang, Z., & Lai, X. (2024) · Matrix Biology · doi:10.1016/j.matbio.2024.07.001 · Cited by 14
Integrins in cancer stem cells
Gou, S., Wu, A., & Luo, Z. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1434378 · Cited by 12
Human ITGAV variants are associated with immune dysregulation, brain abnormalities, and colitis
Ghasempour, S., Warner, N. E., Guan, R., Rodari, M. M., Ivanochko, D., Hawkins, R. W., Marwaha, A., Nowak, J. K., Liang, Y., Mulder, D. J., et al. (2024) · The Journal of Experimental Medicine · doi:10.1084/jem.20240546 · Cited by 13
Advanced In Vitro Modeling to Study the Paradox of Mechanically Induced Cardiac Fibrosis
Gartner, T. C. L. B., Stein, J. M., Muylaert, D. E. P., Bouten, C. V. C., Doevendans, P. A., Khademhosseini, A., Suyker, W. J. L., Sluijter, J. P. G., & Hjortnaes, J. (2021) · Tissue Engineering Part C Methods · doi:10.1089/ten.tec.2020.0298 · Cited by 12
Deb, V. K., & Jain, U. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.147121 · Cited by 11
Characterization of tolloid-mediated cleavage of the GDF8 procomplex
McCoy, J. C., Goebel, E. J., & Thompson, T. B. (2021) · Biochemical Journal · doi:10.1042/bcj20210054 · Cited by 11
Zhu, X., Li, Q., George, V., Spanoudis, C. M., Gilkes, C., Shrestha, N., Liu, B., Kong, L., You, L., Echeverri, C. A., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1114802 · Cited by 11
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Popa, I., & Gutzman, J. H. (2018) · Emerging Topics in Life Sciences · doi:10.1042/etls20180043 · Cited by 11
Maldonado, H., Dreger, M., Bedgood, L. D., Kyriakou, T., Wolanska, K. I., Rigby, M. E., Marotta, V., Webster, J. M., Wang, J., Rusilowicz-Jones, E. V., et al. (2024) · Science Advances · doi:10.1126/sciadv.adk9944 · Cited by 10
Han, X., Zhang, C., Lei, Q., Xu, J. H., & Zhou, Y. (2025) · Biomaterials Advances · doi:10.1016/j.bioadv.2025.214240 · Cited by 10
Bugatti, K., Andreucci, E., Monaco, N., Battistini, L., Peppicelli, S., Ruzzolini, J., Curti, C., Zanardi, F., Bianchini, F., & Sartori, A. M. (2022) · ACS Omega · doi:10.1021/acsomega.2c00535 · Cited by 11
Lee, H., Han, J.-H., Kang, Y. J., Hwangbo, H., Yoon, A., Kim, H., Lee, D., Lee, S. Y., Choi, B. H., Kim, J., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.991056 · Cited by 10
Stachowski, T. R., Grant, T. D., & Snell, E. H. (2019) · Journal of Synchrotron Radiation · doi:10.1107/s1600577519005113 · Cited by 10
Wang, Y., Rattner, A., Li, Z., Smallwood, P. M., & Nathans, J. (2025) · eLife · doi:10.7554/elife.107018 · Cited by 12
Lechner, A., Jordan, P. A., da Cruz, G. C. M., Lamson, J. S., Gordon, J., Okada, B. K., Anderson, K., Chaudhari, R. R., Rosario, C. J., Mikesell, J., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c06142 · Cited by 9
Wu, H., Li, C., Li, L. J., Tian, Y., Xiao, Z., Huang, Y., Zhong, J., Huang, J., Chen, Q., & He, Y. (2025) · Advanced Science · doi:10.1002/advs.202508225 · Cited by 9
Mechanobiology and Resolution of Lung Fibrosis
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Ma, F., Zhang, Y., Yang, G., Mo, L., Liu, D., Yang, L., Liu, Z., Ning, Y., & Yang, P. (2020) · Immunology Letters · doi:10.1016/j.imlet.2020.12.011 · Cited by 8
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Self-citation
Metadata
- Authors
- Dong, X., Zhao, B., Iacob, R. E., Zhu, J., Koksal, A. C., Lu, C., Engen, J. R., & Springer, T. A.
- Affiliations
- Boston Children's Hospital (US)
- Northeastern University (US)
- Corresponding author
- Springer, Timothy A.
- ORCID
- Venue
- Nature
- Published
- 2017-01-25
- Volume
- 542
- Issue
- 7639
- Pages
- 55-59
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC5586147
- OpenAlex
- W2582355481
- Cited by
- 273
- References
- 30
- Citations by year
- 2026: 13 · 2025: 34 · 2024: 30 · 2023: 24 · 2022: 28 · 2021: 37 · 2020: 34 · 2019: 21 · 2018: 27 · 2017: 23
- FWCI
- 23.58
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Charles A. King Trust
- National Institutes of Health
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR067288)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Keywords
- TGF-beta activation, integrin αvβ6, latent TGF-beta, integrin binding, co-crystal structure, extracellular matrix remodeling, integrin beta subunit, conformational change
- MeSH terms
- Amino Acid Sequence, Antigens, Neoplasm, Binding Sites, Humans, Models, Molecular, Protein Binding, Protein Conformation, Integrins, Crystallography, X-Ray, Evolution, Molecular, Transforming Growth Factor beta1
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