An ensemble of flexible conformations underlies mechanotransduction by the cadherin–catenin adhesion complex
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Significance: Adherens junctions are specialized cell–cell adhesion complexes found in epithelial, endothelial, and neuronal tissues of multicellular organism. The cadherin–catenin complex is the core component of the adherens junction and transmits mechanical stress from cell to cell. This study reveals that the cadherin–catenin complex displays a wide spectrum of flexible structures, which suggests a dynamic mechanism for this complex in mechanotransduction for cell–cell adhesion.
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Mechanical stress is transmitted between cells via cell-cell adhesion adherens junctions composed of the ABE complex (alpha-catenin, beta-catenin, and epithelial cadherin cytoplasmic domain).
“Mechanical stress is transmitted between cells via cell–cell adhesion adherens junctions composed of the ABE complex (alpha-catenin, beta-catenin, and epithelial cadherin cytoplasmic domain) [223].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [223]
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UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works
Protein Identification and Analysis Tools on the ExPASy Server
Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M. R., Appel, R. D., & Bairoch, A. (2005) · Humana Press eBooks · doi:10.1385/1-59259-890-0:571 · Cited by 10,133 · see citing works
Epithelial–mesenchymal transitions in tumour progression
Thiery, J. P. (2002) · Nature reviews. Cancer · doi:10.1038/nrc822 · Cited by 6,632 · see citing works
The I-TASSER Suite: protein structure and function prediction
Yang, J., Yan, R., Roy, A., Xu, D., Poisson, J., & Zhang, Y. (2015) · Nature Methods · doi:10.1038/nmeth.3213 · Cited by 5,596 · see citing works
Irreversibility and heat generation in the computing process
Landauer, R. (1961) · IBM Journal of Research and Development · doi:10.1147/rd.53.0183 · Cited by 4,980 · see citing works
Mechanics of Motor Proteins and the Cytoskeleton
Howard, & Clark (2002) · Applied Mechanics Reviews · doi:10.1115/1.1451234 · Cited by 2,909 · see citing works
Irreversibility and heat generation in the computing process
Landauer, R. W. (2000) · IBM Journal of Research and Development · doi:10.1147/rd.441.0261 · Cited by 2,617 · see citing works
Svergun, D. I. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77443-6 · Cited by 2,229 · see citing works
<i>DAMMIF</i> , a program for rapid <i>ab-initio</i> shape determination in small-angle scattering
Franke, D., & Svergun, D. I. (2009) · Journal of Applied Crystallography · doi:10.1107/s0021889809000338 · Cited by 2,021 · see citing works
The role of dynamic conformational ensembles in biomolecular recognition
Boehr, D. D., Nussinov, R., & Wright, P. E. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.232 · Cited by 2,008 · see citing works
Single myosin molecule mechanics: piconewton forces and nanometre steps
Finer, J. T., Simmons, R. M., & Spudich, J. A. (1994) · Nature · doi:10.1038/368113a0 · Cited by 1,900 · see citing works
Mantid—Data analysis and visualization package for neutron scattering and μ SR experiments
Arnold, O., Bilheux, J.-C., Borreguero, J. M., Buts, A., Campbell, S. I., Chapon, L. C., Doucet, M., Draper, N., Leal, R. F., Gigg, M., et al. (2014) · Nuclear Instruments and Methods in Physics Research Section A Accelerators Spectrometers Detectors and Associated Equipment · doi:10.1016/j.nima.2014.07.029 · Cited by 1,812 · see citing works
Regulation of cadherin-mediated adhesion in morphogenesis
Gumbiner, B. M. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1699 · Cited by 1,523 · see citing works
Determination of Domain Structure of Proteins from X-Ray Solution Scattering
Svergun, D. I., Petoukhov, M. V., & Koch, M. H. J. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)76260-1 · Cited by 1,425 · see citing works
The ensemble nature of allostery
Motlagh, H. N., Wrabl, J. O., Li, J., & Hilser, V. J. (2014) · Nature · doi:10.1038/nature13001 · Cited by 1,247 · see citing works
Deconstructing the Cadherin-Catenin-Actin Complex
Yamada, S., Pokutta, S., Drees, F., Weis, W. I., & Nelson, W. J. (2005) · Cell · doi:10.1016/j.cell.2005.09.020 · Cited by 1,022 · see citing works
α-Catenin as a tension transducer that induces adherens junction development
Yonemura, S., Wada, Y., Watanabe, T., Nagafuchi, A., & Shibata, M. (2010) · Nature Cell Biology · doi:10.1038/ncb2055 · Cited by 972 · see citing works
Dynamic molecular processes mediate cellular mechanotransduction
Hoffman, B. D., Grashoff, C., & Schwartz, M. A. (2011) · Nature · doi:10.1038/nature10316 · Cited by 956 · see citing works
The front and rear of collective cell migration
Mayor, R., & Etienne‐Manneville, S. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.14 · Cited by 879 · see citing works
Cell binding function of E‐cadherin is regulated by the cytoplasmic domain.
Nagafuchi, A., & Takeichi, M. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03249.x · Cited by 805 · see citing works
Huber, A. H., & Weis, W. I. (2001) · Cell · doi:10.1016/s0092-8674(01)00330-0 · Cited by 777 · see citing works
Cadherins and cancer: how does cadherin dysfunction promote tumor progression?
Jeanes, A., Gottardi, C. J., & Yap, A. S. (2008) · Oncogene · doi:10.1038/onc.2008.343 · Cited by 764 · see citing works
Absolute calibration of small-angle neutron scattering data
Wignall, G. D., & Bates, F. S. (1987) · Journal of Applied Crystallography · doi:10.1107/s0021889887087181 · Cited by 737 · see citing works
Three-Dimensional Structure of the Armadillo Repeat Region of β-Catenin
Huber, A. H., Nelson, W. J., & Weis, W. I. (1997) · Cell · doi:10.1016/s0092-8674(00)80352-9 · Cited by 706 · see citing works
E-cadherin mediates contact inhibition of proliferation through Hippo signaling-pathway components
Kim, N.-G., Koh, E., Chen, X., & Gumbiner, B. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103345108 · Cited by 698 · see citing works
Negative staining and image classification — powerful tools in modern electron microscopy
Ohi, M. D., Li, Y., Cheng, Y., & Walz, T. (2004) · Biological Procedures Online · doi:10.1251/bpo70 · Cited by 685 · see citing works
Self-citationGNOM – a program package for small-angle scattering data processing
Semenyuk, A. V., & Svergun, D. I. (1991) · Journal of Applied Crystallography · doi:10.1107/s002188989100081x · Cited by 647 · see citing works
The minimal cadherin-catenin complex binds to actin filaments under force
Buckley, C. D., Tan, J., Anderson, K., Hanein, D., Volkmann, N., Weis, W. I., Nelson, W. J., & Dunn, A. R. (2014) · Science · doi:10.1126/science.1254211 · Cited by 629 · see citing works
Dynamic contacts: rearranging adherens junctions to drive epithelial remodelling
Takeichi, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3802 · Cited by 605 · see citing works
Advanced ensemble modelling of flexible macromolecules using X-ray solution scattering
Tria, G., Mertens, H. D. T., Kachala, M., & Svergun, D. I. (2015) · IUCrJ · doi:10.1107/s205225251500202x · Cited by 597 · see citing works
Borghi, N., Sorokina, M., Shcherbakova, O. G., Weis, W. I., Pruitt, B. L., Nelson, W. J., & Dunn, A. R. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204390109 · Cited by 596 · see citing works
E-cadherin junctions as active mechanical integrators in tissue dynamics
Lecuit, T., & Yap, A. S. (2015) · Nature Cell Biology · doi:10.1038/ncb3136 · Cited by 550 · see citing works
E-cadherin in contact inhibition and cancer
Mendonsa, A. M., Na, T.-Y., & Gumbiner, B. M. (2018) · Oncogene · doi:10.1038/s41388-018-0304-2 · Cited by 528 · see citing works
Cell–Cell Junctions Organize Structural and Signaling NetworksPreprint
García, M. Á., Nelson, W. J., & Chavez, N. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a029181 · Cited by 506 · see citing works
Notes on Landauer's principle, reversible computation, and Maxwell's Demon
Bennett, C. H. (2003) · Studies in History and Philosophy of Science Part B Studies in History and Philosophy of Modern Physics · doi:10.1016/s1355-2198(03)00039-x · Cited by 493 · see citing works
Structure and Biochemistry of Cadherins and CateninsPreprint
Shapiro, L. S., & Weis, W. I. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003053 · Cited by 460 · see citing works
Force-dependent conformational switch of α-catenin controls vinculin binding
Yao, M., Qiu, W., Liu, R., Efremov, A. K., Cong, P., Seddiki, R., Payre, M., Lim, C. T., Ladoux, B., Mège, R., et al. (2014) · Nature Communications · doi:10.1038/ncomms5525 · Cited by 456 · see citing works
ATSAS 2.1 – towards automated and web-supported small-angle scattering data analysis
Petoukhov, M. V., Konarev, P. V., Kikhney, A., & Svergun, D. I. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807002853 · Cited by 452 · see citing works
Cadherin Adhesion and Mechanotransduction
Leckband, D. E., & de Rooij, J. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013212 · Cited by 394 · see citing works
SPARX, a new environment for Cryo-EM image processing
Hohn, M. H., Tang, G., Goodyear, G., Baldwin, P. R., Huang, Z. X., Penczek, P. A., Yang, C., Glaeser, R. M., Adams, P. D., & Ludtke, S. J. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.07.003 · Cited by 364 · see citing works
How Random are Intrinsically Disordered Proteins? A Small Angle Scattering Perspective
Receveur‐Brechot, V., & Christiane, D. D. (2012) · Current Protein and Peptide Science · doi:10.2174/138920312799277901 · Cited by 357 · see citing works
Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering
Bernadó, P., & Svergun, D. I. (2011) · Molecular BioSystems · doi:10.1039/c1mb05275f · Cited by 347 · see citing works
Thomas, W. E., Vogel, V., & Sokurenko, E. V. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125804 · Cited by 340 · see citing works
Christiane, D. D., Vivès, C., Cannella, D., Pérez, J., Pebay‐Peyroula, E., Vachette, P., & Fieschi, F. (2009) · Journal of Structural Biology · doi:10.1016/j.jsb.2009.08.009 · Cited by 312 · see citing works
A Complete Mapping of the Proteins in the Small Ribosomal Subunit of Escherichia coli
Capel, M. S., Engelman, D. M., Freeborn, B., Kjeldgaard, M., Langer, J. A., Ramakrishnan, V., Schindler, D. G., Schneider, D. K., SCHOENBORN, B. P., Sillers, I.-Y., et al. (1987) · Science · doi:10.1126/science.3317832 · Cited by 272 · see citing works
Mechanistic insights from structural studies of β-catenin and its binding partners
Xu, W., & Kimelman, D. (2007) · Journal of Cell Science · doi:10.1242/jcs.013771 · Cited by 246 · see citing works
Structure of the Dimerization and β-Catenin- Binding Region of α-Catenin
Pokutta, S., & Weis, W. I. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80447-5 · Cited by 242 · see citing works
Iterative Stable Alignment and Clustering of 2D Transmission Electron Microscope Images
Yang, Z., Fang, J., Chittuluru, J. R., Asturias, F. J., & Penczek, P. A. (2012) · Structure · doi:10.1016/j.str.2011.12.007 · Cited by 241 · see citing works
Veigel, C., Bartoo, M. L., White, D. C. S., Sparrow, J. C., & Molloy, J. E. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)74061-5 · Cited by 234 · see citing works
Crystal Structure of a Full-Length β-Catenin
Xing, Y., Takemaru, K., Liu, J., Berndt, J. D., Zheng, J., Moon, R. T., & Xu, W. (2008) · Structure · doi:10.1016/j.str.2007.12.021 · Cited by 214 · see citing works
Endothelial adherens junctions at a glance
Dejana, E., & Orsenigo, F. (2013) · Journal of Cell Science · doi:10.1242/jcs.124529 · Cited by 206 · see citing works
Small Angle Neutron Scattering
Zaccai, G., & Jacrot, B. (1983) · Annual Review of Biophysics and Bioengineering · doi:10.1146/annurev.bb.12.060183.001035 · Cited by 201 · see citing works
The extended Q -range small-angle neutron scattering diffractometer at the SNS
Zhao, J., Gao, C. Y., & Liu, D. (2010) · Journal of Applied Crystallography · doi:10.1107/s002188981002217x · Cited by 198 · see citing works
Catch-Bond Model Derived from Allostery Explains Force-Activated Bacterial Adhesion
Thomas, W. E., Forero-Shelton, M., Yakovenko, O., Nilsson, L. M., Vicini, P., Sokurenko, E. V., & Viola Vogel, B. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.066548 · Cited by 196 · see citing works
The suite of small-angle neutron scattering instruments at Oak Ridge National Laboratory
Heller, W. T., Cuneo, M. J., DeBeer‐Schmitt, L., Do, C., He, L., Heroux, L., Littrell, K. C., Pingali, S. V., Qian, S., Stanley, C. B., et al. (2018) · Journal of Applied Crystallography · doi:10.1107/s1600576718001231 · Cited by 190 · see citing works
Self-citationMonomeric α-catenin links cadherin to the actin cytoskeleton
Desai, R., Sarpal, R., Ishiyama, N., Pellikka, M., Ikura, M., & Tepaß, U. (2013) · Nature Cell Biology · doi:10.1038/ncb2685 · Cited by 188 · see citing works
Whitten, A. E., Cai, S., & Trewhella, J. (2008) · Journal of Applied Crystallography · doi:10.1107/s0021889807055136 · Cited by 182 · see citing works
Nanoscale architecture of cadherin-based cell adhesions
Bertocchi, C., Wang, Y., Ravasio, A., Hara, Y., Wu, Y., Sailov, T., Baird, M. A., Davidson, M. W., Zaidel‐Bar, R., Toyama, Y., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3456 · Cited by 179 · see citing works
αE-catenin is an autoinhibited molecule that coactivates vinculin
Choi, H., Pokutta, S., Cadwell, G. W., Bobkov, A. A., Bankston, L. A., Liddington, R., & Weis, W. I. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203906109 · Cited by 156 · see citing works
Shibata, T., Chuma, M., Kokubu, A., Sakamoto, M., & Hirohashi, S. (2003) · Hepatology · doi:10.1053/jhep.2003.50270 · Cited by 155 · see citing works
Steinhusen, U., Badock, V., Bauer, A., Behrens, J., Wittman-Liebold, B., Dörken, B., & Bommert, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001458200 · Cited by 147 · see citing works
Curtis, J. E., Raghunandan, S., Nanda, H., & Krueger, S. (2011) · Computer Physics Communications · doi:10.1016/j.cpc.2011.09.010 · Cited by 141 · see citing works
The mechanotransduction machinery at work atadherensjunctions
Ladoux, B., Nelson, W. J., Yan, J., & Mège, R. (2015) · Integrative Biology · doi:10.1039/c5ib00070j · Cited by 133 · see citing works
Ishiyama, N., Tanaka, N., Abe, K., Yang, Y. J., Abbas, Y. M., Umitsu, M., Nagar, B., Bueler, S. A., Rubinstein, J. L., Takeichi, M., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.453928 · Cited by 118 · see citing works
Dimer asymmetry defines α-catenin interactions
Rangarajan, E. S., & Izard, T. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2479 · Cited by 111 · see citing works
The Cytoskeletal Protein α-Catenin Unfurls upon Binding to Vinculin
Rangarajan, E. S., & Izard, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.351023 · Cited by 94 · see citing works
Perkins, S. J., Wright, D. W., Zhang, H., Brookes, E., Chen, J., Irving, T. C., Krueger, S., Barlow, D. J., Edler, K. J., Scott, D. J., et al. (2016) · Journal of Applied Crystallography · doi:10.1107/s160057671601517x · Cited by 81 · see citing works
Architectures of Whole-Module and Bimodular Proteins from the 6-Deoxyerythronolide B Synthase
Edwards, A. L., Matsui, T., Weiss, T. M., & Khosla, C. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.03.015 · Cited by 60 · see citing works
Self-citationSmall-Angle Scattering and Neutron Contrast Variation for Studying Bio-Molecular Complexes
Whitten, A. E., & Trewhella, J. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-483-4_20 · Cited by 50 · see citing works
Improving Protein Template Recognition by Using Small-Angle X-Ray Scattering Profiles
dos Reis, M. A., Aparício, R., & Zhang, Y. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.10.046 · Cited by 39 · see citing works
Mo, R., Chew, T., Maher, M. T., Bellipanni, G., Weinberg, E. S., & Gottardi, C. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.045039 · Cited by 31 · see citing works
α-Catenin Structure and Nanoscale Dynamics in Solution and in Complex with F-Actin
Nicholl, I. D., Matsui, T., Weiss, T. M., Stanley, C. B., Heller, W. T., Martel, A., Farago, B., Callaway, D. J. E., & Bu, Z. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.07.005 · Cited by 21 · see citing works
Self-citationHirano, Y., Amano, Y., Yonemura, S., & Hakoshima, T. (2018) · Genes to Cells · doi:10.1111/gtc.12578 · Cited by 19 · see citing works
Structure of the free form of the N‐terminal VH1 domain of monomeric α‐catenin
Shibahara, T., Hirano, Y., & Hakoshima, T. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.05.053 · Cited by 6 · see citing works
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Bondos, S. E., Dunker, A. K., & Uversky, V. N. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00821-7 · Cited by 222 · see citing works
Cell-cell junctions as sensors and transducers of mechanical forces
Angulo‐Urarte, A., van der Wal, T., & Huveneers, S. (2020) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2020.183316 · Cited by 152 · see citing works
Fu, F., Bao, R., Yao, S., Zhou, C., Luo, H., Zhang, Z., Zhang, H., Li, Y., Yan, S., Yu, H., et al. (2021) · Scientific Reports · doi:10.1038/s41598-020-80756-6 · Cited by 83 · see citing works
Draper, E. R., Dietrich, B., McAulay, K., Brasnett, C., Abdizadeh, H., Patmanidis, I., Marrink, . J., Su, H., Cui, H., Schweins, R., et al. (2020) · Matter · doi:10.1016/j.matt.2019.12.028 · Cited by 70 · see citing works
Molecular Mobility-Mediated Regulation of E-Cadherin Adhesion
Biswas, K. H. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.10.012 · Cited by 62 · see citing works
Krueger, S. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102375 · Cited by 52 · see citing works
Horikoshi, N., Hwang, S., Gati, C., Matsui, T., Castillo-Orellana, C., Raub, A. G., Garcia, A. A., Jabbarpour, F., Batyuk, A., Broweleit, J., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2022790118 · Cited by 37 · see citing works
Self-citationThe α-Catenin mechanosensing M region is required for cell adhesion during tissue morphogenesis
Sheppard, L., Green, D. G., Lerchbaumer, G., Rothenberg, K. E., Fernández‐González, R., & Tepaß, U. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202108091 · Cited by 29 · see citing works
N-cadherin crosstalk with integrin weakens the molecular clutch in response to surface viscosity
Barcelona‐Estaje, E., Gonzalez‐Oliva, M. A., Cunniffe, F., Rodrigo‐Navarro, A., Genever, P. G., Dalby, M. J., Roca‐Cusachs, P., Cantini, M., & Salmerón‐Sánchez, M. (2024) · Nature Communications · doi:10.1038/s41467-024-53107-6 · Cited by 27 · see citing works
Sorting of cadherin–catenin-associated proteins into individual clusters
Troyanovsky, R. B., Sergeeva, A. P., Indra, I., Chen, C.-S., Kato, R., Shapiro, L. S., Honig, B. H., & Troyanovsky, S. M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2105550118 · Cited by 27 · see citing works
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Kluger, C., Braun, L., Sedlak, S. M., Pippig, D. A., Bauer, M. S., Miller, K., Milles, L. F., Gaub, H. E., & Viola Vogel, B. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2019.12.042 · Cited by 27 · see citing works
Qian, S., Heller, W. T., Chen, W., Christianson, A. D., Do, C., Wang, Y., Lin, J., Huegle, T., Jiang, C., Boone, C., et al. (2022) · Review of Scientific Instruments · doi:10.1063/5.0090527 · Cited by 25 · see citing works
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Farago, B., Nicholl, I. D., Wang, S., Cheng, X., Callaway, D. J. E., & Bu, Z. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2025012118 · Cited by 16 · see citing works
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Chen, S. H., Weiss, K. L., Stanley, C. B., & Bhowmik, D. (2023) · Protein Science · doi:10.1002/pro.4772 · Cited by 12 · see citing works
Self-citationAzumah, R., Hummitzsch, K., Hartanti, M. D., John, J. C. S., Anderson, R. A., & Rodgers, R. J. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2021.762177 · Cited by 11 · see citing works
Concato, V. M., Silva, T. F., Detoni, M. B., Cruz, E. M. S., Gonçalves, M. D., Bortoleti, B. T. D. S., Tomiotto‐Pellissier, F., Carloto, A. C. M., Madureira, M. B., Rodrigues, A. C. J., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115979 · Cited by 10 · see citing works
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Recent progress of mechanosensitive mechanism on breast cancer
Chai, X., Liu, J., Yu, T., Zhang, G., Sun, W., Zhou, Y., Ren, L., Cao, H.-L., Yin, D., & Zhang, C. (2023) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2023.09.003 · Cited by 9 · see citing works
Sumner, J., & Qian, S. (2022) · BBA Advances · doi:10.1016/j.bbadva.2022.100063 · Cited by 8 · see citing works
Self-citationAn ensemble of cadherin-catenin-vinculin complex employs vinculin as the major F-actin binding mode
Shi, B., Matsui, T., Qian, S., Weiss, T. M., Nicholl, I. D., Callaway, D. J. E., & Bu, Z. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2023.04.026 · Cited by 7 · see citing works
Self-citationMonster, J. L., Manzato, C., van der Beek, J., Pannekoek, W., Hummelink, J. A., Hadders, M. A., de Heus, C., Klumperman, J., Schuijers, J., & Gloerich, M. (2025) · Nature Communications · doi:10.1038/s41467-025-66984-2 · Cited by 6 · see citing works
Rangarajan, E. S., Smith, E. W., & Izard, T. (2023) · Communications Biology · doi:10.1038/s42003-023-04610-x · Cited by 6 · see citing works
Paths to stability – actin regulation of adherens junction mechanics
James, J., Winn, L. B. A., Mottram-Epson, P., & Köster, D. V. (2025) · Journal of Cell Science · doi:10.1242/jcs.264055 · Cited by 5 · see citing works
Callaway, D. J. E., Nicholl, I. D., Shi, B., Reyes, G., Farago, B., & Bu, Z. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2408459121 · Cited by 5 · see citing works
Self-citationKodama, T. S., Furuita, K., & Kojima, C. (2025) · Molecules · doi:10.3390/molecules30061220 · Cited by 5 · see citing works
The nematode α-catenin ortholog, HMP1, has an extended α-helix when bound to actin filaments
Rangarajan, E. S., Smith, E. W., & Izard, T. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102817 · Cited by 5 · see citing works
A microfluidic model to study the effects of arrhythmic flows on endothelial cells
Lai, A., Hawke, A., Mohammed, M. M., Thurgood, P., Concilia, G., Peter, K., Khoshmanesh, K., & Baratchi, S. (2024) · Lab on a Chip · doi:10.1039/d3lc00834g · Cited by 5 · see citing works
Effects of actuation of nanoporous gold on cell orientation in a fibroblast sheet
Wu, P., Sawaki, S., Hakamada, M., & Mabuchi, M. (2021) · Journal of Materials Science Materials in Medicine · doi:10.1007/s10856-021-06584-w · Cited by 4 · see citing works
Zhang, M., Xiong, S., Gao, D., Liu, C., & Xiao, L. (2024) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.18133 · Cited by 1 · see citing works
Hui, B., Bu, Z., & Cheng, X. (2025) · Protein Science · doi:10.1002/pro.70259 · Cited by 1 · see citing works
Self-citationTawani, A., Qian, S., Sparks, S., Sashi, P., Cahill, S. M., Rout, M. P., & Cowburn, D. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.20.599953 · Cited by 1 · see citing works
Self-citationHung, Y.-F., Chen, Q., Pires, I., Rosenthal, P. B., & Kursula, I. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.09.519741 · Cited by 1 · see citing works
A platform for dissecting force sensitivity and multivalency in actin networksPreprint
Levin, J. T., Pan, A., Barrett, M. T., & Alushin, G. M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.15.553463
Wildgruber, C., Qian, S., Chen, S. H., Herwig, K. W., Urban, V. S., & O’Neill, H. (2024) · Journal of Applied Crystallography · doi:10.1107/s1600576724004254
Self-citationLong, H., Xiong, X., Zhou, C., Yu, J., Liang, T., & Shao, W. (2025) · Journal of Orthopaedics · doi:10.1016/j.jor.2025.05.015
Retractedα-Catenin phosphorylation is tension-sensitive and supports epithelial barrier functions via afadin
Quinn, J. M., Le, P. M., Weng, A., Flozak, A. S., Folmsbee, S. S., Arroyo-Colon, E., Aillon, R. P., Jain, S. I., Pokutta, S., Weis, W. I., et al. (2026) · The Journal of Cell Biology · doi:10.1083/jcb.202508188
- Authors
- Bush, M., Alhanshali, B. M., Qian, S., Stanley, C. B., Heller, W. T., Matsui, T., Weiss, T. M., Nicholl, I. D., Walz, T., Callaway, D. J. E., & Bu, Z.
- Affiliations
- Rockefeller University (US)
- The Graduate Center, CUNY (US)
- Oak Ridge National Laboratory (US)
- Stanford Synchrotron Radiation Lightsource (US)
- University of Wolverhampton (GB)
- City College of New York (US)
- Corresponding author
- Callaway, David J. E.
- Bu, Zimei
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2019-10-07
- Volume
- 116
- Issue
- 43
- Pages
- 21545-21555
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC6815173
- OpenAlex
- W2979505241
- Cited by
- 42
- References
- 74
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 7 · 2023: 7 · 2022: 11 · 2021: 6 · 2020: 3 · 2019: 1
- FWCI
- 1.74
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- CUNY Academic Works (City University of New York) (submittedVersion, cc-by-nc-nd)
- Wolverhampton Intellectual Repository and E-Theses (University of Wolverhampton) (submittedVersion, cc-by-nc-nd)
- Funders
- National Science Foundation (MCB-1817684)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Wnt/β-catenin signaling in development and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- mechanotransduction, adherens junctions, alpha-catenin, β-catenin, E-cadherin, protein flexibility, intrinsically disordered regions, conformational ensembles, nanostructures, mechanical tension, catch bonds, cell-cell adhesion
- MeSH terms
- Protein Domains, Humans, Molecular Conformation, Protein Binding, Cadherins, Amino Acid Motifs, Adherens Junctions, Mechanotransduction, Cellular, beta Catenin, alpha Catenin, Scattering, Small Angle
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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.
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