Structural determinants of integrin β-subunit specificity for latent TGF-β

<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works

<i>Phaser</i> crystallographic software

McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612 · see citing works

Untitled work

Hynes (2002) · doi:10.1016/s0092-8674(02)00971-6 · Cited by 8,606 · see citing works

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334 · see citing works

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Davis, I., Leaver‐Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., Snoeyink, J. S., Richardson, J. S., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm216 · Cited by 3,915 · see citing works

International Tables for Crystallography

(2013) · International Tables for Crystallography · doi:10.1107/97809553602060000113 · Cited by 3,834 · see citing works

Targeted disruption of the mouse transforming growth factor-β1 gene results in multifocal inflammatory disease

Shull, M. M., Ormsby, I., Kier, A. B., Pawlowski, S., Diebold, R. J., Yin, M., Allen, R., Sidman, C., Proetzel, G., Calvin, D., et al. (1992) · Nature · doi:10.1038/359693a0 · Cited by 2,985 · see citing works

A Mechanism for Regulating Pulmonary Inflammation and Fibrosis: The Integrin αvβ6 Binds and Activates Latent TGF β1

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 · see citing works

Linking Crystallographic Model and Data Quality

Karplus, P. A., & Diederichs, K. (2012) · Science · doi:10.1126/science.1218231 · Cited by 1,781 · see citing works

Crystal Structure of the Extracellular Segment of Integrin αVβ3 in Complex with an Arg-Gly-Asp Ligand

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 · see citing works

Crystal Structure of the Extracellular Segment of Integrin αVβ3

Xiong, J.-P., Stehle, T., Diefenbach, B., Zhang, R., Dunker, R., Scott, D. L., Joachimiak, A., Goodman, S. L., & Arnaout, M. A. (2001) · Science · doi:10.1126/science.1064535 · Cited by 1,278 · see citing works

Global Conformational Rearrangements in Integrin Extracellular Domains in Outside-In and Inside-Out Signaling

Takagi, J., Petre, B. M., Walz, T., & Springer, T. A. (2002) · Cell · doi:10.1016/s0092-8674(02)00935-2 · Cited by 1,168 · see citing works

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 · see citing works

The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution

Acharya, R., Fry, E. E., Stuart, D. I., Fox, G., Rowlands, D. J., & Brown, F. (1989) · Nature · doi:10.1038/337709a0 · Cited by 866 · see citing works

Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics

Xiao, T. S., Takagi, J., Coller, B. S., Wang, J., & Springer, T. A. (2004) · Nature · doi:10.1038/nature02976 · Cited by 845 · see citing works

An Assay for Transforming Growth Factor-β Using Cells Transfected with a Plasminogen Activator Inhibitor-1 Promoter-Luciferase Construct

Abe, 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 · see citing works

The integrin αvβ8 mediates epithelial homeostasis through MT1-MMP–dependent activation of TGF-β1

Mu, D., Cambier, S., Fjellbirkeland, L., Baron, J. L., Munger, J. S., Kawakatsu, H., Sheppard, D., Broaddus, V. C., & Nishimura, S. L. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200109100 · Cited by 729 · see citing works

Cilengitide: The First Anti-Angiogenic Small Molecule Drug Candidate. Design, Synthesis and Clinical Evaluation

Mas‐Moruno, C., Rechenmacher, F., & Kessler, H. (2010) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152010794728639 · Cited by 649 · see citing works

The effect of Arg-Gly-Asp-containing peptides on fibrinogen and von Willebrand factor binding to platelets.

Plow, E. F., Pierschbacher, M. D., Ruoslahti, E. I., Marguerie, G. A., & Ginsberg, M. H. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.23.8057 · Cited by 579 · see citing works

Structure of a Complete Integrin Ectodomain in a Physiologic Resting State and Activation and Deactivation by Applied Forces

Zhu, J., Luo, B., Xiao, T. S., Zhang, C., Nishida, N., & Springer, T. A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.018 · Cited by 503 · see citing works

The pH of the Secretory Pathway: Measurement, Determinants, and Regulation

Paroutis, P., Touret, N., & Grinstein, S. (2004) · Physiology · doi:10.1152/physiol.00005.2004 · Cited by 451 · see citing works

Integrin inside-out signaling and the immunological synapse

Springer, T. A., & Dustin, M. L. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.10.004 · Cited by 392 · see citing works

Analysis of protein-ligand interactions by fluorescence polarization

Rossi, A. M., & Taylor, C. W. (2011) · Nature Protocols · doi:10.1038/nprot.2011.305 · Cited by 360 · see citing works

Absence of integrin-mediated TGFβ1 activation in vivo recapitulates the phenotype of TGFβ1-null mice

Yang, Z., Mu, Z., Dabovic, B., Jurukovski, V., Yu, D., Sung, J. J., Xiong, X., & Munger, J. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611044 · Cited by 321 · see citing works

Occupancy of an adhesive glycoprotein receptor modulates expression of an antigenic site involved in cell adhesion.

Frelinger, A. L., Lam, S. C., Plow, E. F., Smith, M. A., Loftus, J. C., & Ginsberg, M. H. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37769-x · Cited by 267 · see citing works

Crystal structure of α5β1 integrin ectodomain: Atomic details of the fibronectin receptor

Nagae, M., Re, S., Mihara, E., Nogi, T., Sugita, Y., & Takagi, J. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201111077 · Cited by 237 · see citing works

Structural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin αIIbβ3

Springer, T. A., Zhu, J., & Xiao, T. S. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200801146 · Cited by 235 · see citing works

Complete integrin headpiece opening in eight steps

Zhu, J., Zhu, J., & Springer, T. A. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201212037 · Cited by 215 · see citing works

The effect of Arg-Gry-Asp-containing peptides on tibrinogen and von Willebrand factor binding to platelets.

Plow, E. (1985) · Medical Entomology and Zoology · Cited by 181 · see citing works

GARP regulates the bioavailability and activation of TGFβ

Wang, R., Zhu, J., Dong, X., Shi, M., Lu, C., & Springer, T. A. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-12-1018 · Cited by 180 · see citing works

Regulation of integrin affinity on cell surfaces

Schürpf, T., & Springer, T. A. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.333 · Cited by 175 · see citing works

Synthetic peptides derived from fibrinogen and fibronectin change the conformation of purified platelet glycoprotein IIb-IIIa.

Parise, L. V., Helgerson, S. L., Steiner, B., Nannizzi, L., & Phillips, D. R. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45247-7 · Cited by 128 · see citing works

The integrin alphavbeta3 is a receptor for the latency-associated peptides of transforming growth factors beta1 and beta3

Ludbrook, S. B., Barry, S. T., Delves, C. J., & Horgan, C. M. T. (2003) · Biochemical Journal · doi:10.1042/bj20020809 · Cited by 126 · see citing works

Changing Ligand Specificities of αvβ1 and αvβ3 Integrins by Swapping a Short Diverse Sequence of the β Subunit

Takagi, J., Kamata, T., Meredith, J. E., Puzon-McLaughlin, W., & Takada, Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.32.19794 · Cited by 116 · see citing works

An internal ligand-bound, metastable state of a leukocyte integrin, αXβ2

Şen, M., Yuki, K., & Springer, T. A. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201308083 · Cited by 86 · see citing works

Integrin evolution: Insights from ascidian and teleost fish genomes

Huhtala, M. T., Heino, J., Casciari, D., de Luise, A., & Johnson, M. S. (2005) · Matrix Biology · doi:10.1016/j.matbio.2005.01.003 · Cited by 85 · see citing works

How Natalizumab Binds and Antagonizes α4 Integrins

Yu, Y., Schürpf, T., & Springer, T. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.501668 · Cited by 80 · see citing works

αVβ3 Integrin Crystal Structures and Their Functional Implications

Dong, X., Mi, L.-Z., Zhu, J., Wang, W., Hu, P., Luo, B., & Springer, T. A. (2012) · Biochemistry · doi:10.1021/bi300734n · Cited by 77 · see citing works

The Role of the Specificity-Determining Loop of the Integrin β Subunit I-like Domain in Autonomous Expression, Association with the α Subunit, and Ligand Binding

Takagi, J., DeBottis, D. P., Erickson, H., & Springer, T. A. (2002) · Biochemistry · doi:10.1021/bi016047u · Cited by 61 · see citing works

Fibrosis: from mechanisms to medicines

Henderson, N. C., Rieder, F., & Wynn, T. A. (2020) · Nature · doi:10.1038/s41586-020-2938-9 · Cited by 1,868 · see citing works

TGF-β1 Signaling and Tissue Fibrosis

Kim, K. K., Sheppard, D., & Chapman, H. A. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022293 · Cited by 800 · see citing works

The role of integrins in inflammation and angiogenesis

Mezu‐Ndubuisi, O. J., & Maheshwari, A. (2020) · Pediatric Research · doi:10.1038/s41390-020-01177-9 · Cited by 385 · see citing works

Overcoming TGFβ-mediated immune evasion in cancer

Tauriello, D. V. F., Sancho, E., & Batlle, E. (2022) · Nature Reviews Cancer · doi:10.1038/s41568-021-00413-6 · Cited by 377 · see citing works

Structural Biology and Evolution of the TGF-β FamilyPreprint

Hinck, A. P., Mueller, T. D., & Springer, T. A. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022103 · Cited by 364 · see citing works

TGF-β and the Tissue Microenvironment: Relevance in Fibrosis and Cancer

Caja, L., Dituri, F., Mancarella, S., Caballero‐Díaz, D., Moustakas, A., Giannelli, G., & Fabregat, I. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051294 · Cited by 353 · see citing works

The α _v β ₁ integrin plays a critical in vivo role in tissue fibrosis

Reed, N. I., Jo, H., Chen, C., Tsujino, K., Arnold, T. D., DeGrado, W. F., & Sheppard, D. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aaa5094 · Cited by 311 · see citing works

Force interacts with macromolecular structure in activation of TGF-β

Dong, X., Zhao, B., Iacob, R. E., Zhu, J., Koksal, A. C., Lu, C., Engen, J. R., & Springer, T. A. (2017) · Nature · doi:10.1038/nature21035 · Cited by 273 · see citing works

Targeting TGF-β Signaling for Therapeutic GainPreprint

Akhurst, R. J. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022301 · Cited by 243 · see citing works

Mechanical stress determines the configuration of TGFβ activation in articular cartilage

Zhen, G., Guo, Q., Li, Y., Wu, C., Zhu, S., Wang, R., Guo, X.-D. E., Kim, B. C., Huang, J., Hu, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21948-0 · Cited by 192 · see citing works

Honeybee venom and melittin suppress growth factor receptor activation in HER2-enriched and triple-negative breast cancer

Duffy, C., Sorolla, A., Wang, E., Golden, E., Woodward, E., Davern, K. M., Ho, D., Johnstone, E. K. M., Pfleger, K. D. G., Redfern, A. D., et al. (2020) · npj Precision Oncology · doi:10.1038/s41698-020-00129-0 · Cited by 186 · see citing works

Cryo-EM Reveals Integrin-Mediated TGF-β Activation without Release from Latent TGF-β

Campbell, M. G., Cormier, A., Ito, S., Seed, R., Bondesson, A. J., Lou, J., Marks, J. D., Baron, J. L., Cheng, Y., & Nishimura, S. L. (2020) · Cell · doi:10.1016/j.cell.2019.12.030 · Cited by 176 · see citing works

Conformational equilibria and intrinsic affinities define integrin activation

Li, J., Su, Y., Xia, W. T., Qin, Y., Humphries, M. J., Vestweber, D., Cabañas, C., Lu, C., & Springer, T. A. (2017) · The EMBO Journal · doi:10.15252/embj.201695803 · Cited by 149 · see citing works

An αv‐RGD Integrin Inhibitor Toolbox: Drug Discovery Insight, Challenges and Opportunities

Hatley, R. J. D., Macdonald, S. J. F., Slack, R. J., Le, J., Ludbrook, S. B., & Lukey, P. T. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201707948 · Cited by 132 · see citing works

Integrin-Mediated TGFβ Activation Modulates the Tumour Microenvironment

Brown, N. F., & Marshall, J. F. (2019) · Cancers · doi:10.3390/cancers11091221 · Cited by 116 · see citing works

TGF-β Family Signaling in Connective Tissue and Skeletal DiseasesPreprint

MacFarlane, E. G., Haupt, J., Dietz, H. C., & Shore, E. M. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022269 · Cited by 119 · see citing works

Structural mechanism of laminin recognition by integrin

Arimori, T., Miyazaki, N., Mihara, E., Takizawa, M., Taniguchi, Y., Cabañas, C., Sekiguchi, K., & Takagi, J. (2021) · Nature Communications · doi:10.1038/s41467-021-24184-8 · Cited by 110 · see citing works

Blocking immunosuppression by human Tregs in vivo with antibodies targeting integrin αVβ8

Stockis, J., Liénart, S., Colau, D., Collignon, A., Nishimura, S. L., Sheppard, D., Coulie, P. G., & Lucas, S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1710680114 · Cited by 111 · see citing works

Structural basis for Epstein–Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins

Sathiyamoorthy, K., Hu, Y. X., Möhl, B. S., Chen, J., Longnecker, R., & Jardetzky, T. S. (2016) · Nature Communications · doi:10.1038/ncomms13557 · Cited by 110 · see citing works

β1 Integrins as Therapeutic Targets to Disrupt Hallmarks of Cancer

Blandin, A.-F., Renner, G., Lehmann, M., Lelong-Rebel, I. H., Martin, S., & Dontenwill, M. (2015) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00279 · Cited by 105 · see citing works

Role of glycosylation in TGF-β signaling and epithelial-to-mesenchymal transition in cancer

Zhang, J., ten Dijke, P., Wuhrer, M., & Zhang, T. (2020) · Protein & Cell · doi:10.1007/s13238-020-00741-7 · Cited by 99 · see citing works

Rules of engagement between αvβ6 integrin and foot-and-mouth disease virus

Kotecha, A., Wang, Q., Dong, X., Ilca, S. L., Ondiviela, M., Zihe, R., Seago, J. E., Charleston, B., Fry, E. E., Abrescia, N. G. A., et al. (2017) · Nature Communications · doi:10.1038/ncomms15408 · Cited by 97 · see citing works

Transforming growth factor-β receptors: versatile mechanisms of ligand activation

Chia, Z. J., Cao, Y.-N., Little, P. J., & Kamato, D. (2024) · Acta Pharmacologica Sinica · doi:10.1038/s41401-024-01235-6 · Cited by 92 · see citing works

Stable Peptides Instead of Stapled Peptides: Highly Potent αvβ6‐Selective Integrin Ligands

Maltsev, O. V., Marelli, U. K., Kapp, T. G., Leva, F. S. D., Maro, S. D., Nieberler, M., Reuning, U., Schwaiger, M., Novellino, E., Marinelli, L., et al. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201508709 · Cited by 78 · see citing works

αIIbβ3: structure and function

Coller, B. S. (2015) · Journal of Thrombosis and Haemostasis · doi:10.1111/jth.12915 · Cited by 76 · see citing works

Discovery of a new class of integrin antibodies for fibrosis

Zhang, J., Wang, T., Saigal, A., Johnson, J., Morrisson, J., Tabrizifard, S., Hollingsworth, S. A., Eddins, M. J., Mao, W., O’Neill, K., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-81253-0 · Cited by 74 · see citing works

αvβ8 integrin adhesion and signaling pathways in development, physiology and disease

McCarty, J. H. (2020) · Journal of Cell Science · doi:10.1242/jcs.239434 · Cited by 66 · see citing works

Short linear motif candidates in the cell entry system used by SARS-CoV-2 and their potential therapeutic implications

Mészáros, B., Sámano‐Sánchez, H., Alvarado-Valverde, J., Čalyševa, J., Martínez‐Pérez, E., Alves, R., Shields, D. C., Kumar, M., Rippmann, F., Chemes, L. B., et al. (2021) · Science Signaling · doi:10.1126/scisignal.abd0334 · Cited by 66 · see citing works

Structural and Mechanistic Insights into the Tropism of Epstein-Barr Virus

Möhl, B. S., Chen, J., Sathiyamoorthy, K., Jardetzky, T. S., & Longnecker, R. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.0066 · Cited by 65 · see citing works

A general chemical principle for creating closure-stabilizing integrin inhibitors

Lin, F., Li, J., Xie, Y., Zhu, J., Nguyen, T. T. H., Zhang, Y., Zhu, J., & Springer, T. A. (2022) · Cell · doi:10.1016/j.cell.2022.08.008 · Cited by 60 · see citing works

Short linear motif candidates in the cell entry system used by SARS-CoV-2 and their potential therapeutic implications

Mészáros, B., Sámano Sánchez, H., Alvarado Valverde, J., Čalyševa, J., Martinez Perez, E., Alves, R., Shields, D. C., Kumar, M., Rippmann, F., Chemes, L. B., et al. (2021) · CONICET Digital (CONICET) · Cited by 59 · see citing works

Dynamic allostery drives autocrine and paracrine TGF-β signaling

Jin, M., Seed, R., Cai, G., Shing, T., Wang, L., Ito, S., Cormier, A., Wankowicz, S. A. M., Jespersen, J. M., Baron, J. L., et al. (2024) · Cell · doi:10.1016/j.cell.2024.08.036 · Cited by 55 · see citing works

Energy landscape differences among integrins establish the framework for understanding activation

Li, J., & Springer, T. A. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201701169 · Cited by 55 · see citing works

Distinct recognition of complement iC3b by integrins α X β 2 and α M β 2

Xu, S., Wang, J., Wang, J., & Springer, T. A. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620881114 · Cited by 54 · see citing works

Prodomain–growth factor swapping in the structure of pro-TGF-β1

Zhao, B., Xu, S., Dong, X., Lu, C., & Springer, T. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.809657 · Cited by 55 · see citing works

Matters of context guide future research in TGFβ superfamily signaling

Akhurst, R. J., & Padgett, R. W. (2015) · Science Signaling · doi:10.1126/scisignal.aad0416 · Cited by 52 · see citing works

Integrin Alpha v Beta 6 (αvβ6) and Its Implications in Cancer Treatment

Brzozowska, E., & Deshmukh, S. S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012346 · Cited by 51 · see citing works

New β-Lactam Derivatives Modulate Cell Adhesion and Signaling Mediated by RGD-Binding and Leukocyte Integrins

Baiula, M., Galletti, P., Martelli, G., Soldati, R., Belvisi, L., Civera, M., Dattoli, S. D., Spampinato, S. M., & Giacomini, D. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00576 · Cited by 51 · see citing works

Triple-hit therapeutic approach for triple negative breast cancers using docetaxel nanoparticles, EN1-iPeps and RGD peptides

Sorolla, A., Wang, E., Clemons, T. D., Evans, C. W., Plani-Lam, J. H. C., Golden, E., Dessauvagie, B., Redfern, A. D., Swaminathan-Iyer, K., & Blancafort, P. (2019) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2019.04.006 · Cited by 51 · see citing works

De novo design of highly selective miniprotein inhibitors of integrins αvβ6 and αvβ8

Roy, A., Shi, L., Chang, A., Dong, X., Fernandez, A. N., Kraft, J. C., Li, J., Le, V. Q., Winegar, R. V., Cherf, G. M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41272-z · Cited by 50 · see citing works

Alpha-v–containing integrins are host receptors for the Plasmodium falciparum sporozoite surface protein, TRAP

Dundas, K., Shears, M. J., Sun, Y. E., Hopp, C. S., Crosnier, C., Metcalf, T., Girling, G., Sinnis, P., Billker, O., & Wright, G. J. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1719660115 · Cited by 45 · see citing works

Leukocyte integrin α L β 2 headpiece structures: The αI domain, the pocket for the internal ligand, and concerted movements of its loops

Şen, M., & Springer, T. A. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1601379113 · Cited by 45 · see citing works

Fv-clasp: An Artificially Designed Small Antibody Fragment with Improved Production Compatibility, Stability, and Crystallizability

Arimori, T., Kitago, Y., Umitsu, M., Fujii, Y., Asaki, R., Tamura‐Kawakami, K., & Takagi, J. (2017) · Structure · doi:10.1016/j.str.2017.08.011 · Cited by 44 · see citing works

Selective Targeting of Integrin αvβ8 by a Highly Active Cyclic Peptide

Reichart, F., Maltsev, O. V., Kapp, T. G., Räder, A. F. B., Weinmüller, M., Marelli, U. K., Notni, J., Wurzer, A. J., Beck, R., Wester, H., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01588 · Cited by 43 · see citing works

Molecular Modeling Insights into the Structure and Behavior of Integrins: A Review

Tvaroška, I., Kozmon, S., & Kóňa, J. (2023) · Cells · doi:10.3390/cells12020324 · Cited by 42 · see citing works

Ammonium trichloro [1,2-ethanediolato-O,O′]-tellurate cures experimental visceral leishmaniasis by redox modulation of Leishmania donovani trypanothione reductase and inhibiting host integrin linked PI3K/Akt pathway

Vishwakarma, P., Parmar, N., Chandrakar, P., Sharma, T., Kathuria, M., Agnihotri, P. K., Siddiqi, M. I., Mitra, K., & Kar, S. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2653-3 · Cited by 42 · see citing works

From a Helix to a Small Cycle: Metadynamics‐Inspired αvβ6 Integrin Selective Ligands

Leva, F. S. D., Tomassi, S., Maro, S. D., Reichart, F., Notni, J., Dangi, A., Marelli, U. K., Brancaccio, D., Merlino, F., Wester, H., et al. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201803250 · Cited by 42 · see citing works

Molecular Basis of the Ligand Binding Specificity of αvβ8 Integrin

Ozawa, A., Sato, Y., Imabayashi, T., Uemura, T., Takagi, J., & Sekiguchi, K. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.719138 · Cited by 41 · see citing works

Atypical interactions of integrin α V β 8 with pro-TGF-β1

Wang, J., Dong, X., Zhao, B., Li, J., Lu, C., & Springer, T. A. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705129114 · Cited by 42 · see citing works

Discovery of (S)-3-(3-(3,5-Dimethyl-1H-pyrazol-1-yl)phenyl)-4-((R)-3-(2-(5,6,7,8-tetrahydro-1,8-naphthyridin-2-yl)ethyl)pyrrolidin-1-yl)butanoic Acid, a Nonpeptidic αvβ6 Integrin Inhibitor for the Inhaled Treatment of Idiopathic Pulmonary Fibrosis

Procopiou, P. A., Anderson, N. A., Barrett, J., Barrett, T. N., Crawford, M. H. J., Fallon, B. J., Hancock, A. P., Le, J., Lemma, S., Marshall, R. P., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00959 · Cited by 41 · see citing works

Insights into Protein–Ligand Interactions in Integrin Complexes: Advances in Structure Determinations

Zheng, Y., & Leftheris, K. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01869 · Cited by 40 · see citing works

Low-affinity integrin states have faster ligand-binding kinetics than the high-affinity state

Li, J., Yan, J., & Springer, T. A. (2021) · eLife · doi:10.7554/elife.73359 · Cited by 38 · see citing works

An engineered AAV targeting integrin alpha V beta 6 presents improved myotropism across species

Hong, A. V., Suel, L., Petat, E., Dubois, A., Brun, P., Guerchet, N., Veron, P., Poupiot, J., & Richard, I. (2024) · Nature Communications · doi:10.1038/s41467-024-52002-4 · Cited by 40 · see citing works

General structural features that regulate integrin affinity revealed by atypical αVβ8

Wang, J., Su, Y., Iacob, R. E., Engen, J. R., & Springer, T. A. (2019) · Nature Communications · doi:10.1038/s41467-019-13248-5 · Cited by 37 · see citing works

Integrin β8 prevents pericyte-myofibroblast transition and renal fibrosis through inhibiting the TGF-β1/TGFBR1/Smad3 pathway in diabetic kidney disease

Cao, Y., Su, H., Zeng, J., Xie, Y., Liu, Z., Liu, F., Qiu, Y., Yi, F., Lin, J., Hammes, H., et al. (2023) · Translational research · doi:10.1016/j.trsl.2023.10.007 · Cited by 36 · see citing works

Polymerizing laminins in development, health, and disease

Yurchenco, P. D., & Kulczyk, A. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107429 · Cited by 35 · see citing works

Cross-Talk between the TGF-β and Cell Adhesion Signaling Pathways in Cancer

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 34 · see citing works

Integrin Engagement by the Helical RGD Motif of the Helicobacter pylori CagL Protein Is Regulated by pH-induced Displacement of a Neighboring Helix

Bonsor, D. A., Pham, K. T., Beadenkopf, R., Diederichs, K., Haas, R., Beckett, D., Fischer, W. H., & Sundberg, E. J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.641829 · Cited by 33 · see citing works

Peptides, proteins and nanotechnology: a promising synergy for breast cancer targeting and treatment

Sorolla, A., Sorolla, M. A., Wang, E., & Ceña, V. (2020) · Expert Opinion on Drug Delivery · doi:10.1080/17425247.2020.1814733 · Cited by 31 · see citing works

Exploring the role of ITGB6: fibrosis, cancer, and other diseases

Zhang, Z., Wang, Z., Liu, T., Tang, J., Liu, Y., Gou, T., Chen, K., Wang, L., Zhang, J., Yang, Y., et al. (2023) · APOPTOSIS · doi:10.1007/s10495-023-01921-6 · Cited by 31 · see citing works

Exploring Integrin α5β1 as a Potential Therapeutic Target for Pulmonary Arterial Hypertension: Insights From Comprehensive Multicenter Preclinical Studies

Lemay, S.-E. S., Montesinos, M. S., Grobs, Y., Yokokawa, T., Shimauchi, T., Mougin, M., Romanet, C., Sauvaget, M., Breuils‐Bonnet, S., Bourgeois, A., et al. (2025) · Circulation · doi:10.1161/circulationaha.124.070693 · Cited by 29 · see citing works

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 30 · see citing works

Autonomous conformational regulation of β 3 integrin and the conformation-dependent property of HPA-1a alloantibodies

Thinn, A. M. M., Wang, Z., Zhou, D., Zhao, Y., Curtis, B. R., & Zhu, J. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1806205115 · Cited by 29 · see citing works

TGFβ: Signaling Blockade for Cancer Immunotherapy

Chen, S., Mamaï, O., & Akhurst, R. J. (2021) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-070620-103554 · Cited by 28 · see citing works

Molecular View on the i RGD Peptide Binding Mechanism: Implications for Integrin Activity and Selectivity Profiles

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 · see citing works

Adhesion of Several Cell Lines to Helicobacter pylori CagL Is Mediated by Integrin αVβ6 via an RGDLXXL Motif

Barden, S., & Niemann, H. H. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.01.006 · Cited by 27 · see citing works

Characterisation of a novel, high affinity and selective αvβ6 integrin RGD-mimetic radioligand

Hall, E. R., Bibby, L. I., & Slack, R. J. (2016) · Biochemical Pharmacology · doi:10.1016/j.bcp.2016.08.003 · Cited by 27 · see citing works

New Therapeutic Targets for Hepatic Fibrosis in the Integrin Family, α8β1 and α11β1, Induced Specifically on Activated Stellate Cells

Yokosaki, Y., & Nishimichi, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312794 · Cited by 24 · see citing works

Active Search for Computer‐aided Drug Design

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 · see citing works

Design, Synthesis, and Targeted Delivery of Fluorescent 1,2,4-Triazole–Peptide Conjugates to Pediatric Brain Tumor Cells

Ajmal, M., Yunus, U., Graham, R. M., & Leblanc, R. M. (2019) · ACS Omega · doi:10.1021/acsomega.9b01903 · Cited by 24 · see citing works

N -Methylation of iso DGR Peptides: Discovery of a Selective α5β1-Integrin Ligand as a Potent Tumor Imaging Agent

Kapp, T. G., Leva, F. S. D., Notni, J., Räder, A. F. B., Fottner, M., Reichart, F., Reich, D., Wurzer, A. J., Steiger, K., Novellino, E., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01752 · Cited by 24 · see citing works

The β8 integrin cytoplasmic domain activates extracellular matrix adhesion to promote brain neurovascular development

De, A., Morales, J. E., Chen, Z., Sebastian, S., & McCarty, J. H. (2022) · Development · doi:10.1242/dev.200472 · Cited by 23 · see citing works

Extracellular citrullination inhibits the function of matrix associated TGF-β

Sipilä, K. H., Ranga, V., Rappu, P., Torittu, A., Pirilä, L., Käpylä, J., Johnson, M. S., Larjava, H., & Heino, J. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.02.008 · Cited by 23 · see citing works

Investigating the Interaction of Cyclic RGD Peptidomimetics with αVβ6 Integrin by Biochemical and Molecular Docking Studies

Civera, M., Arosio, D., Bonato, F., Manzoni, L., Pignataro, L., Zanella, S., Gennari, C., Piarulli, U., & Belvisi, L. (2017) · Cancers · doi:10.3390/cancers9100128 · Cited by 23 · see citing works

Fibrillin microfibril structure identifies long-range effects of inherited pathogenic mutations affecting a key regulatory latent TGFβ-binding site

Godwin, A. R. F., Dajani, R., Zhang, X., Thomson, J., Holmes, D. F., Adamo, C. S., Sengle, G., Sherratt, M. J., Roseman, A. M., & Baldock, C. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-00950-8 · Cited by 22 · see citing works

Cryo-Electron Microscopy Structure of the αIIbβ3-Abciximab Complex

Nes̆ić, D., Zhang, Y., Spasic, A., Li, J., Provasi, D., Filizola, M., Walz, T., & Coller, B. S. (2020) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.119.313671 · Cited by 22 · see citing works

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 22 · see citing works

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 · see citing works

Specific high affinity interaction of Helicobacter pylori CagL with integrin αVβ6 promotes type IV secretion of CagA into human cells

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 · see citing works

αIIbβ3 binding to a fibrinogen fragment lacking the γ-chain dodecapeptide is activation dependent and EDTA inducible

Zafar, H., Shang, Y., Li, J., David, G., Fernandez, J., Molina, H., Filizola, M., & Coller, B. S. (2017) · Blood Advances · doi:10.1182/bloodadvances.2017004689 · Cited by 19 · see citing works

Protocol for Delivery of CRISPR/dCas9 Systems for Epigenetic Editing into Solid Tumors Using Lipid Nanoparticles Encapsulating RNA

Woodward, E., Wang, E., Wallis, C. J. D., Sharma, R. K., Tie, A. W. J., Murthy, N., & Blancafort, P. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-4051-7_14 · Cited by 18 · see citing works

The RGD-binding integrins αvβ6 and αvβ8 are receptors for mouse adenovirus-1 and -3 infection

Bieri, M., Hendrickx, R., Bauer, M., Yu, B., Jetzer, T., Dreier, B., Mittl, P. R. E., Sobek, J., Plückthun, A., Greber, U. F., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1010083 · Cited by 18 · see citing works

3D hydrogel platform with macromolecular actuators for precisely controlled mechanical forces on cancer cell migration

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 18 · see citing works

Potential of αvβ6 and αvβ1 integrin inhibition for treatment of idiopathic pulmonary fibrosis

Bellani, S., Molyneaux, P. L., Maher, T. M., & Spagnolo, P. (2024) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2024.2375375 · Cited by 15 · see citing works

Late‐Stage Functionalization by Chan–Lam Amination: Rapid Access to Potent and Selective Integrin Inhibitors

Robinson, H., Oatley, S. A., Rowedder, J. E., Slade, P., Macdonald, S. J. F., Argent, S. P., Hirst, J. D., McInally, T., & Moody, C. J. (2020) · Chemistry - A European Journal · doi:10.1002/chem.202001059 · Cited by 15 · see citing works

Targeting integrin αvβ6 with gallium-68 tris (hydroxypyridinone) based PET probes

Floresta, G., Memdouh, S., Pham, T., Ma, M., Blower, P. J., Hider, R. C., Abbate, V., & Cilibrizzi, A. (2022) · Dalton Transactions · doi:10.1039/d2dt00980c · Cited by 15 · see citing works

Discovery, recognized antigenic structures, and evolution of cross-serotype broadly neutralizing antibodies from porcine B-cell repertoires against foot-and-mouth disease virus

Li, F., Wu, S., Lv, L., Huang, S., Zhang, Z., Zerang, Z., Li, P., Cao, Y., Bao, H., Sun, P., et al. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012623 · Cited by 14 · see citing works

A Possible Action of Divalent Transition Metal Ions at the Interpentameric Interface of Inactivated Foot-and-Mouth Disease Virus Provides a Simple but Effective Approach To Enhance Stability

Lin, X., Yang, Y., Song, Y., Li, S., Zhang, X., Su, Z. G., & Zhang, S. (2021) · Journal of Virology · doi:10.1128/jvi.02431-20 · Cited by 14 · see citing works

Anti-TGF-β1 aptamer enhances therapeutic effect of tyrosine kinase inhibitor, gefitinib, on non-small cell lung cancer in xenograft model

Takahashi, M., Hashimoto, Y., & Nakamura, Y. (2022) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2022.06.001 · Cited by 13 · see citing works

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 · see citing works

Integrin-αvβ6 targeted peptide-toxin therapy in a novel αvβ6-expressing immunocompetent model of pancreatic cancer

Brown, N. F., Murray, E. R., Cutmore, L. C., Howard, P. W., Masterson, L. A., Zammarchi, F., Hartley, J. A., van Berkel, P. H., & Marshall, J. F. (2024) · Pancreatology · doi:10.1016/j.pan.2024.02.013 · Cited by 12 · see citing works

Ein Instrumentarium von αv‐RGD‐Integrin‐Inhibitoren: Wirkstoffsuche, Herausforderungen und Möglichkeiten

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 12 · see citing works

Identification, Characterization, and Optimization of Integrin αvβ6-Targeting Peptides from a One-Bead One-Compound (OBOC) Library: Towards the Development of Positron Emission Tomography (PET) Imaging Agents

Tang, Y. C., Davis, R. A., Ganguly, T., & Sutcliffe-Goulden, J. (2019) · Molecules · doi:10.3390/molecules24020309 · Cited by 12 · see citing works

Stabile Peptide statt “gestapelte Peptide”: hochaffine αvβ6‐selektive Integrinliganden

Maltsev, O. V., Marelli, U. K., Kapp, T. G., Leva, F. S. D., Maro, S. D., Nieberler, M., Reuning, U., Schwaiger, M., Novellino, E., Marinelli, L., et al. (2015) · Angewandte Chemie · doi:10.1002/ange.201508709 · Cited by 12 · see citing works

Structural 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 · see citing works

Preclinical evaluation of peptide-based radiotracers for integrin αvβ6-positive pancreatic carcinoma

Müller, M., Altmann, A., Sauter, M., Lindner, T., Jäger, D., Rathke, H. G., Herold‐Mende, C. C., Marmé, F., Babich, J. W., Mier, W., et al. (2019) · Nuklearmedizin - NuclearMedicine · doi:10.1055/a-0894-4127 · Cited by 11 · see citing works

Passing on the medicinal chemistry baton: training undergraduates to be industry-ready through research projects between the University of Nottingham and GlaxoSmithKline

Macdonald, S. J. F., Fray, M. J., & McInally, T. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.01.015 · Cited by 11 · see citing works

β6 integrinosis: a new lethal autosomal recessive ITGB6 disorder leading to impaired conformational transitions of the α V β6 integrin receptor

Weil, P. P., van den Bruck, R., Ziegenhals, T., Juranek, S., Goedde, D., Orth, V., Wirth, S., Jenke, A. C. W., & Postberg, J. (2019) · Gut · doi:10.1136/gutjnl-2019-319015 · Cited by 11 · see citing works

Synthetic integrin antibodies discovered by yeast display reveal αV subunit pairing preferences with β subunits

Hao, Y., Yan, J., Fraser, C., Jiang, A., Anuganti, M., Zhang, R., Lloyd, K., Jardine, J. G., Coppola, J. D., Meijers, R., et al. (2024) · mAbs · doi:10.1080/19420862.2024.2365891 · Cited by 9 · see citing works

Activation of transforming growth factor beta 1 through integrin alpha V beta 6 and its molecular insights into cancer progression, and future directions

Deb, V. K., & Jain, U. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.147121 · Cited by 11 · see citing works

Identification of a Region in the Integrin β3 Subunit That Confers Ligand Binding Specificity

Lin, E. C. K., Ratnikov, B. I., Tsai, P. M., Carron, C. P., Myers, D. M., Barbas, C. F., & Smith, J. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23912 · Cited by 48 · see citing works

Molecular Basis of the Ligand Binding Specificity of αvβ8 Integrin

Ozawa, A., Sato, Y., Imabayashi, T., Uemura, T., Takagi, J., & Sekiguchi, K. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.719138 · Cited by 41 · see citing works

Structural basis for the molecular recognition of various RGD-containing ligands by integrin αVβ3: The role of the specificity-determining loop (SDL)

Mariasoosai, C., Bose, S., & Senthil, N. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2022.11.1841

Synthetic integrin antibodies discovered by yeast display reveal αV subunit pairing preferences with β subunits

Hao, Y., Yan, J., Fraser, C., Jiang, A., Anuganti, M., Zhang, R., Lloyd, K., Jardine, J. G., Coppola, J. D., Meijers, R., et al. (2024) · mAbs · doi:10.1080/19420862.2024.2365891 · Cited by 9 · see citing works

Structural insights into the molecular recognition of integrin αVβ3 by RGD-containing ligands: The role of the specificity-determining loop (SDL)Preprint

Mariasoosai, C., Bose, S., & Natesan, S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.23.614545 · Cited by 2 · see citing works