The final steps of integrin activation: the end game

Untitled work

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

Environmental sensing through focal adhesions

Geiger, B., Spatz, J. P., & Bershadsky, A. D. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2593 · Cited by 2,543 · 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

Integrins: Emerging Paradigms of Signal Transduction

Schwartz, M. A., Schaller, M. D., & Ginsberg, M. H. (1995) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cb.11.110195.003001 · Cited by 1,596 · 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

Talin Binding to Integrin ß Tails: A Final Common Step in Integrin Activation

Tadokoro, S., Shattil, S. J., Eto, K., Tai, V., Liddington, R., de Pereda, J. M., Ginsberg, M. H., & Calderwood, D. (2003) · Science · doi:10.1126/science.1086652 · Cited by 1,211 · 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

Structural Basis of Collagen Recognition by Integrin α2β1

Emsley, J., Knight, C. G., Farndale, R. W., Barnes, M. J., & Liddington, R. (2000) · Cell · doi:10.1016/s0092-8674(00)80622-4 · Cited by 1,007 · see citing works

Macromolecular Modeling with Rosetta

Das, R., & Baker, D. A. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.062906.171838 · Cited by 995 · see citing works

Inside Out

Ramirez, A., Fisher, G., George, E. L., Sanning, E., Forouzani, M., Allen, J., Bak, R., Halley, W., Wheeler, G., her, et al. (2003) · Cited by 960 · see citing works

Interferometric fluorescent super-resolution microscopy resolves 3D cellular ultrastructure

Shtengel, G. E., Galbraith, J. A., Galbraith, C. G., Lippincott‐Schwartz, J., Gillette, J. M., Manley, S., Sougrat, R., Waterman, C. M., Kanchanawong, P., Davidson, M. W., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813131106 · Cited by 889 · see citing works

Bidirectional Transmembrane Signaling by Cytoplasmic Domain Separation in Integrins

Kim, M., Carman, C. V., & Springer, T. A. (2003) · Science · doi:10.1126/science.1084174 · Cited by 786 · see citing works

The Tail of Integrins, Talin, and Kindlins

Moser, M., Legate, K. R., Zent, R., & Fässler, R. (2009) · Science · doi:10.1126/science.1163865 · Cited by 752 · see citing works

Mechanically Activated Integrin Switch Controls α 5 β 1 Function

Friedland, J. C., Lee, M. H., & Boettiger, D. E. (2009) · Science · doi:10.1126/science.1168441 · Cited by 717 · see citing works

Kindlin-3 is essential for integrin activation and platelet aggregation

Moser, M., Nieswandt, B., Ussar, S., Požgajová, M., & Fässler, R. (2008) · Nature Medicine · doi:10.1038/nm1722 · Cited by 700 · 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

Structural Basis of Integrin Activation by Talin

Wegener, K. L., Partridge, A. W., Han, J., Pickford, A. R., Liddington, R., Ginsberg, M. H., & Campbell, I. D. (2007) · Cell · doi:10.1016/j.cell.2006.10.048 · Cited by 677 · see citing works

Integrin cytoplasmic domains mediate inside-out signal transduction

O'Toole, T., Katagiri, Y., Faull, R., Peter, K., Tamura, R., Quaranta, V., Loftus, J., Shattil, S., & Ginsberg, M. H. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.124.6.1047 · Cited by 659 · see citing works

Integrin cytoplasmic domain-binding proteins

Liu, S., Calderwood, D., & Ginsberg, M. H. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.20.3563 · Cited by 573 · see citing works

Breaking the Integrin Hinge

Hughes, P. E., Díaz‐González, F., Leong, L., Wu, C., McDonald, J. A., Shattil, S. J., & Ginsberg, M. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.12.6571 · Cited by 571 · see citing works

A Structural Mechanism of Integrin αIIbβ3 “Inside-Out” Activation as Regulated by Its Cytoplasmic Face

Vinogradova, O., Vėlyvis, A., Velyviene, A., Hu, B., Haas, T. A., Plow, E. F., & Qin, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00906-6 · Cited by 529 · see citing works

Structural Determinants of Integrin Recognition by Talin

García‐Álvarez, B., de Pereda, J. M., Calderwood, D., Ulmer, T. S., Critchley, D. R., Campbell, I. D., Ginsberg, M. H., & Liddington, R. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00823-7 · Cited by 519 · 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

Integrin avidity regulation: are changes in affinity and conformation underemphasized?

Carman, C. V., & Springer, T. A. (2003) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2003.08.003 · Cited by 500 · see citing works

Ligands “activate” integrin αIIbβ3 (platelet GPIIb-IIIa)

Du, X., Plow, E. F., Frelinger, A. L., O’Toole, T. E., Loftus, J. C., & Ginsberg, M. H. (1991) · Cell · doi:10.1016/0092-8674(91)90458-b · Cited by 485 · see citing works

Linking Rap to cell adhesion

Bos, J. L. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.02.009 · Cited by 481 · see citing works

Suppression of Integrin Activation: A Novel Function of a Ras/Raf-Initiated MAP Kinase Pathway

Hughes, P. E., Renshaw, M. W., Pfaff, M., Forsyth, J. S., Keivens, V. M., Schwartz, M. A., & Ginsberg, M. H. (1997) · Cell · doi:10.1016/s0092-8674(00)81892-9 · Cited by 481 · see citing works

The ins and outs of fibronectin matrix assembly

Wierzbicka‐Patynowski, I., & Schwarzbauer, J. E. (2003) · Journal of Cell Science · doi:10.1242/jcs.00670 · Cited by 473 · see citing works

Ras effectors

Marshall, C. J. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80066-4 · Cited by 463 · see citing works

RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1

Katagiri, K., Maeda, A., Shimonaka, M., et al. (2003) · Nature Immunology · doi:10.1038/ni950 · Cited by 462 · see citing works

Kindlin-2 controls bidirectional signaling of integrinsPreprint

Montañez, E., Ussar, S., Schifferer, M., Bösl, M. R., Zent, R., Moser, M., & Fässler, R. (2008) · Genes & Development · doi:10.1101/gad.469408 · Cited by 452 · see citing works

Reconstructing and Deconstructing Agonist-Induced Activation of Integrin αIIbβ3

Han, J., Lim, C. J., Watanabe, N., Soriani, A., Ratnikov, B. I., Calderwood, D., Puzon-McLaughlin, W., Lafuente, E. M., Boussiotis, V. A., Shattil, S. J., et al. (2006) · Current Biology · doi:10.1016/j.cub.2006.08.035 · Cited by 447 · see citing works

The Molecular Basis of Filamin Binding to Integrins and Competition with Talin

Kiema, T., Lad, Y., Jiang, P., Oxley, C. L., Baldassarre, M., Wegener, K. L., Campbell, I. D., Ylänne, J., & Calderwood, D. A. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.011 · Cited by 434 · see citing works

Integrin β cytoplasmic domain interactions with phosphotyrosine-binding domains: A structural prototype for diversity in integrin signaling

Calderwood, D., Fujioka, Y., de Pereda, J. M., García‐Álvarez, B., Nakamoto, T., Margolis, B. L., McGlade, C. J., Liddington, R., & Ginsberg, M. H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262791999 · Cited by 427 · see citing works

RIAM, an Ena/VASP and Profilin Ligand, Interacts with Rap1-GTP and Mediates Rap1-Induced Adhesion

Lafuente, E. M., van Puijenbroek, A. A. F. L., Krause, M., Carman, C. V., Freeman, G. J., Berezovskaya, A., Constantine, E., Springer, T. A., Gertler, F. B., & Boussiotis, V. A. (2004) · Developmental Cell · doi:10.1016/j.devcel.2004.07.021 · Cited by 420 · see citing works

Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation

Svensson, L. M., Howarth, K. M., McDowall, A., Patzak, I. M., Evans, R., Ussar, S., Moser, M., Metìn, A., Fried, M., Tomlinson, I. P. M., et al. (2009) · Nature Medicine · doi:10.1038/nm.1931 · Cited by 418 · see citing works

Integrin regulation

Ginsberg, M. H., Partridge, A. W., & Shattil, S. J. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.08.010 · Cited by 415 · see citing works

The Phosphotyrosine Binding-like Domain of Talin Activates Integrins

Calderwood, D., Yan, B., de Pereda, J. M., García‐Álvarez, B., Fujioka, Y., Liddington, R., & Ginsberg, M. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111996200 · Cited by 412 · see citing works

CalDAG-GEFI integrates signaling for platelet aggregation and thrombus formation

Crittenden, J. R., Bergmeier, W., Zhang, Y., Piffath, C. L., Liang, Y., Wagner, D. D., Housman, D. E., & Graybiel, A. M. (2004) · Nature Medicine · doi:10.1038/nm1098 · Cited by 405 · see citing works

Assembly and biological role of podosomes and invadopodia

Gimona, M., Buccione, R., Courtneidge, S. A., & Linder, S. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.01.005 · Cited by 404 · see citing works

Integrin activation and structural rearrangement

Takagi, J., & Springer, T. A. (2002) · Immunological Reviews · doi:10.1034/j.1600-065x.2002.18613.x · Cited by 384 · see citing works

Migfilin and Mig-2 Link Focal Adhesions to Filamin and the Actin Cytoskeleton and Function in Cell Shape Modulation

Tu, Y., Wu, S., Shi, X., Chen, K., & Wu, C. (2003) · Cell · doi:10.1016/s0092-8674(03)00163-6 · Cited by 375 · see citing works

Kindlin-3 is required for β2 integrin–mediated leukocyte adhesion to endothelial cells

Moser, M., Bauer, M., Schmid, S., Ruppert, R., Schmidt, S., Sixt, M., Wang, H., Sperandio, M., & Fässler, R. (2009) · Nature Medicine · doi:10.1038/nm.1921 · Cited by 366 · see citing works

The GPIIb/IIIa (integrin αIIbβ3) odyssey: a technology-driven saga of a receptor with twists, turns, and even a bend

Coller, B. S., & Shattil, S. J. (2008) · Blood · doi:10.1182/blood-2008-06-077891 · Cited by 354 · see citing works

Integrin Trafficking and the Control of Cell Migration

Caswell, P. T., & Norman, J. C. (2005) · Traffic · doi:10.1111/j.1600-0854.2005.00362.x · Cited by 353 · see citing works

Kindlin-2 (Mig-2): a co-activator of β3 integrins

Ma, Y., Qin, J., Wu, C., & Plow, E. F. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200710196 · Cited by 352 · see citing works

Monoclonal antibodies to ligand-occupied conformers of integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function.

Frelinger, A. L., Du, X., Plow, E. F., & Ginsberg, M. H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47346-8 · Cited by 348 · see citing works

The structure of an integrin/talin complex reveals the basis of inside‐out signal transduction

Anthis, N. J., Wegener, K. L., Ye, F., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.287 · Cited by 344 · see citing works

The structure of the integrin αIIbβ3 transmembrane complex explains integrin transmembrane signalling

Lau, T., Kim, C., Ginsberg, M. H., & Ulmer, T. S. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.63 · Cited by 342 · see citing works

A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans

Malinin, N. L., Zhang, L., Choi, J., Ciocea, A., Razorenova, O. V., Ma, Y.-Q., Podrez, E. A., Tosi, M. F., Lennon, D. P., Caplan, A. I., et al. (2009) · Nature Medicine · doi:10.1038/nm.1917 · Cited by 339 · see citing works

Lamellipodin, an Ena/VASP Ligand, Is Implicated in the Regulation of Lamellipodial Dynamics

Krause, M., Leslie, J. D., Stewart, M. Q., Lafuente, E. M., Valderrama, F., Jagannathan, R., Strasser, G. A., Rubinson, D. A., Liu, H., Way, M., et al. (2004) · Developmental Cell · doi:10.1016/j.devcel.2004.07.024 · Cited by 335 · see citing works

Integrin cytoplasmic tyrosine motif is required for outside-in αIIbβ3 signalling and platelet function

Law, D. A., DeGuzman, F. R., Heiser, P. W., Ministri-Madrid, K., Killeen, N. P., & Phillips, D. R. (1999) · Nature · doi:10.1038/44599 · Cited by 325 · see citing works

Rap1: a key regulator in cell-cell junction formation

Kooistra, M. R. H., Dubé, N., & Bos, J. L. (2006) · Journal of Cell Science · doi:10.1242/jcs.03306 · Cited by 321 · see citing works

RIAM Activates Integrins by Linking Talin to Ras GTPase Membrane-targeting Sequences

Lee, H. S., Lim, C. J., Puzon-McLaughlin, W., Shattil, S. J., & Ginsberg, M. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807117200 · Cited by 319 · see citing works

Modulation of the Affinity of Integrin α IIb β 3 (GPIIb-IIIa) by the Cytoplasmic Domain of α IIb

O’Toole, T. E., Mandelman, D., Forsyth, J. S., et al. (1991) · Science · doi:10.1126/science.1948065 · Cited by 317 · see citing works

Rap1b is required for normal platelet function and hemostasis in mice

Chrzanowska‐Wodnicka, M., Smyth, S. S., Schoenwaelder, S. M., Fischer, T., & White, G. (2005) · Journal of Clinical Investigation · doi:10.1172/jci22973 · Cited by 315 · see citing works

Sequence and domain structure of talin

Rees, D. J. G., Ades, S. E., Singer, S. J., et al. (1990) · Nature · doi:10.1038/347685a0 · Cited by 313 · see citing works

Talin is required for integrin-mediated platelet function in hemostasis and thrombosis

Petrich, B. G., Marchese, P., Ruggeri, Z. M., Spiess, S., Weichert, R. A. M., Ye, F., Tiedt, R., Skoda, R. C., Monkley, S. J., Critchley, D. R., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20071800 · Cited by 309 · see citing works

C. elegans PAT-4/ILK Functions as an Adaptor Protein within Integrin Adhesion Complexes

Mackinnon, A. C., Qadota, H., Norman, K. R., Moerman, D. G., & Williams, B. D. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00810-2 · Cited by 309 · see citing works

Kindlin-1 and-2 directly bind the C-terminal region of β integrin cytoplasmic tails and exert integrin-specific activation effects

Harburger, D. S., Bouaouina, M., & Calderwood, D. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809233200 · Cited by 304 · see citing works

The mechanical integrin cycle

Puklin-Faucher, E., & Sheetz, M. P. (2008) · Journal of Cell Science · doi:10.1242/jcs.042127 · Cited by 295 · see citing works

Activation of Integrin αIIbß3 by Modulation of Transmembrane Helix Associations

Li, R., Mitra, N., Gratkowski, H., Vilaire, G., Игоревич, Л. Р., Nagasami, C., Weisel, J. W., Lear, J. D., DeGrado, W. F., & BENNETT, J. S. (2003) · Science · doi:10.1126/science.1079441 · Cited by 289 · see citing works

Loss of talin1 in platelets abrogates integrin activation, platelet aggregation, and thrombus formation in vitro and in vivo

Nieswandt, B., Moser, M., Pleines, I., Varga-Szabó, D., Monkley, S., Critchley, D. R., & Fässler, R. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20071827 · Cited by 273 · see citing works

Platelet GPIIb/IIIa antagonists: the first anti-integrin receptor therapeutics.

Coller, B. S. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119307 · Cited by 272 · see citing works

Control of cell adhesion dynamics by Rap1 signaling

Boettner, B., & Aelst, L. V. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.06.004 · Cited by 270 · 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

Activation of Leukocyte β2 Integrins by Conversion from Bent to Extended Conformations

Nishida, N., Xie, C., Shimaoka, M., Cheng, Y., Walz, T., & Springer, T. A. (2006) · Immunity · doi:10.1016/j.immuni.2006.07.016 · Cited by 262 · see citing works

Identification of a Novel Calcium-binding Protein That Interacts with the Integrin αIIb Cytoplasmic Domain

Naik, U. P., Patel, P. M., & Parise, L. V. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.8.4651 · Cited by 260 · see citing works

Are changes in integrin affinity and conformation overemphasized?

Bazzoni, G., & Hemler, M. E. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01141-9 · Cited by 252 · see citing works

Leukocyte adhesion deficiency type 1 (LAD-1)/variant. A novel immunodeficiency syndrome characterized by dysfunctional beta2 integrins.

Kuijpers, T. W., van Lier, R. A. W., Hamann, D., de Boer, M., Thung, L. Y., Weening, R. S., Verhoeven, A. J., & Roos, D. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119697 · Cited by 232 · see citing works

Spatial mapping of integrin interactions and dynamics during cell migration by Image Correlation Microscopy

Wiseman, P. W., Brown, C. M., Webb, D. J., et al. (2004) · Journal of Cell Science · doi:10.1242/jcs.01416 · Cited by 232 · see citing works

LAD-1/variant syndrome is caused by mutations in FERMT3

Kuijpers, T. W., van de Vijver, E., Weterman, M. A. J., de Boer, M., Tool, A. T. J., van den Berg, T. K., Moser, M., Jakobs, M. E., Seeger, K., Sanal, Ö., et al. (2008) · Blood · doi:10.1182/blood-2008-10-182154 · Cited by 230 · see citing works

Spatiotemporal regulation of the kinase Mst1 by binding protein RAPL is critical for lymphocyte polarity and adhesion

Katagiri, K., Imamura, M., & Kinashi, T. (2006) · Nature Immunology · doi:10.1038/ni1374 · Cited by 230 · see citing works

Ras GTPases: integrins' friends or foes?

Kinbara, K., Goldfinger, L. E., Hansen, M. B., Chou, F.-L., & Ginsberg, M. H. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1229 · Cited by 228 · see citing works

The primacy of affinity over clustering in regulation of adhesiveness of the integrin αLβ2

Kim, M., Carman, C. V., Yang, W. Y., Salas, A., & Springer, T. A. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200404160 · Cited by 227 · see citing works

Loss of Kindlin-1 Causes Skin Atrophy and Lethal Neonatal Intestinal Epithelial Dysfunction

Ussar, S., Moser, M., Widmaier, M., Rognoni, E., Harrer, C. J., Genzel‐Boroviczény, O., & Fässler, R. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000289 · Cited by 216 · see citing works

Outside-in Integrin Signal Transduction

Law, D. A., Nannizzi‐Alaimo, L., & Phillips, D. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.18.10811 · Cited by 206 · see citing works

Talin at a glance

Critchley, D. R., & Gingras, A. R. (2008) · Journal of Cell Science · doi:10.1242/jcs.018085 · Cited by 206 · see citing works

New insights into the structural basis of integrin activation

Xiong, J.-P., Stehle, T., Goodman, S. L., et al. (2003) · Blood · doi:10.1182/blood-2003-01-0334 · Cited by 204 · see citing works

A Specific Interface between Integrin Transmembrane Helices and Affinity for Ligand

Luo, B., Springer, T. A., & Takagi, J. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020153 · Cited by 202 · see citing works

The Conserved Membrane-proximal Region of an Integrin Cytoplasmic Domain Specifies Ligand Binding Affinity

Hughes, P. E., O’Toole, T. E., Ylänne, J., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.21.12411 · Cited by 200 · see citing works

How the headpiece hinge angle is opened: new insights into the dynamics of integrin activation

Puklin-Faucher, E., Gao, M., Schulten, K. J., & Viola Vogel, B. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200602071 · Cited by 199 · see citing works

Mice lacking the signaling molecule CalDAG-GEFI represent a model for leukocyte adhesion deficiency type III

Bergmeier, W., Goerge, T., Wang, H., Crittenden, J. R., Baldwin, A. C. W., Cifuni, S. M., Housman, D. E., Graybiel, A. M., & Wagner, D. D. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30575 · Cited by 190 · see citing works

The inner world of cell adhesion: integrin cytoplasmic domains

Williams, M. J., Hughes, P. E., O’Toole, T. E., & Ginsberg, M. H. (1994) · Trends in Cell Biology · doi:10.1016/0962-8924(94)90059-0 · Cited by 189 · see citing works

Three-dimensional EM structure of the ectodomain of integrin αVβ3 in a complex with fibronectin

Adair, B. D., Xiong, J.-P., Maddock, C., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200410068 · Cited by 187 · see citing works

Cells on the run: shear-regulated integrin activation in leukocyte rolling and arrest on endothelial cells

Alon, R., & Ley, K. F. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.04.003 · Cited by 185 · see citing works

Long range propagation of conformational changes in integrin alpha IIb beta 3.

Du, X., Gu, M., Weisel, J. W., Nagaswami, C., BENNETT, J. S., Bowditch, R. D., & Ginsberg, M. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49429-5 · Cited by 183 · see citing works

Crystal structure of the complete integrin αVβ3 ectodomain plus an α/β transmembrane fragment

Xiong, J.-P., Mahalingham, B., Alonso, J. L., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200905085 · Cited by 172 · see citing works

The Kindler syndrome protein is regulated by transforming growth factor-β and involved in integrin-mediated adhesion

Kloeker, S., Major, M. B., Calderwood, D. A., Ginsberg, M. H., Jones, D. A., & Beckerle, M. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307978200 · Cited by 163 · see citing works

Association of the Membrane Proximal Regions of the α and β Subunit Cytoplasmic Domains Constrains an Integrin in the Inactive State

Lu, C., Takagi, J., & Springer, T. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100600200 · Cited by 162 · see citing works

Three-dimensional model of the human platelet integrin α IIb β 3 based on electron cryomicroscopy and x-ray crystallography

Adair, B. D., & Yeager, M. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212498199 · Cited by 161 · see citing works

Kindlin-2 Is an Essential Component of Intercalated Discs and Is Required for Vertebrate Cardiac Structure and Function

Dowling, J. J., Gibbs, E. M., Russell, M. W. W., Goldman, D. J., Minarcik, J. C., Golden, J. A., & Feldman, E. L. (2008) · Circulation Research · doi:10.1161/circresaha.107.161489 · Cited by 161 · see citing works

The Cellular Context of T Cell Signaling

Dustin, M. L. (2009) · Immunity · doi:10.1016/j.immuni.2009.03.010 · Cited by 161 · see citing works

Oligomerization of the integrin αIIbβ3: Roles of the transmembrane and cytoplasmic domains

Li, R., Babu, C. R., Lear, J. D., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.221463098 · Cited by 159 · see citing works

Disrupting integrin transmembrane domain heterodimerization increases ligand binding affinity, not valency or clustering

Luo, B., Carman, C. V., Takagi, J., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409440102 · Cited by 159 · see citing works

Structure of an integrin αIIbβ3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation

Yang, J., Ma, Y., Page, R. C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909589106 · Cited by 158 · see citing works

Mst1 controls lymphocyte trafficking and interstitial motility within lymph nodes

Katagiri, K., Katakai, T., Ebisuno, Y., Ueda, Y., Okada, T., & Kinashi, T. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.82 · Cited by 158 · see citing works

A LAD-III syndrome is associated with defective expression of the Rap-1 activator CalDAG-GEFI in lymphocytes, neutrophils, and platelets

Pasvolsky, R., Feigelson, S. W., Kılıç, S. Ş., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070058 · Cited by 158 · see citing works

A role for the thiol isomerase protein ERP5 in platelet function

Jordan, P. A., Stevens, J. M., Hubbard, G. P., et al. (2004) · Blood · doi:10.1182/blood-2004-02-0608 · Cited by 154 · see citing works

Transmembrane Domain Helix Packing Stabilizes Integrin αIIbβ3 in the Low Affinity State

Partridge, A. W., Liu, S., Kim, S., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412701200 · Cited by 153 · see citing works

Mechanisms and consequences of agonist-induced talin recruitment to platelet integrin αIIbβ3

Watanabe, N., Bodin, L., Pandey, M., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200803094 · Cited by 152 · see citing works

Tyrosine phosphorylation of type Iγ phosphatidylinositol phosphate kinase by Src regulates an integrin–talin switch

Ling, K., Doughman, R. L., Iyer, V. V., et al. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200310067 · Cited by 150 · see citing works

The Structure of a Receptor with Two Associating Transmembrane Domains on the Cell Surface: Integrin αIIbβ3

Zhu, J., Luo, B., Barth, P., Schonbrun, J., Baker, D. A., & Springer, T. A. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.022 · Cited by 149 · see citing works

The PINCH–ILK–parvin complexes: assembly, functions and regulation

Wu, C. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.01.006 · Cited by 149 · see citing works

Dimerization of the Transmembrane Domain of Integrin αIIb Subunit in Cell Membranes

Li, R., Gorelik, R., Nanda, V., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314168200 · Cited by 147 · see citing works

The α subunit cytoplasmic domain regulates the assembly and adhesiveness of integrin lymphocyte function-associated antigen-1

Lu, C., & Springer, T. A. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.159.1.268 · Cited by 146 · see citing works

A Redox Site Involved in Integrin Activation

Yan, B., & Smith, J. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007041200 · Cited by 143 · see citing works

Kindlin-3: a new gene involved in the pathogenesis of LAD-III

Mory, A., Feigelson, S. W., Yaralı, N., et al. (2008) · Blood · doi:10.1182/blood-2008-06-163162 · Cited by 141 · see citing works

The N-terminal Domains of Talin Cooperate with the Phosphotyrosine Binding-like Domain to Activate β1 and β3 Integrins

Bouaouina, M., Lad, Y., & Calderwood, D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m709527200 · Cited by 137 · see citing works

Requirement of α and β subunit transmembrane helix separation for integrin outside-in signaling

Zhu, J., Carman, C. V., Kim, M., et al. (2007) · Blood · doi:10.1182/blood-2007-03-080077 · Cited by 127 · see citing works

Structure of the Integrin β3 Transmembrane Segment in Phospholipid Bicelles and Detergent Micelles

Lau, T., Partridge, A. W., Ginsberg, M. H., & Ulmer, T. S. (2008) · Biochemistry · doi:10.1021/bi800107a · Cited by 124 · see citing works

Direct Binding of the Platelet Integrin αIIbβ3 (GPIIb-IIIa) to Talin

Knezevic, I., Leisner, T. M., & Lam, S. C.-T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.27.16416 · Cited by 124 · see citing works

A push-pull mechanism for regulating integrin function

Li, W., Metcalf, D. G., Gorelik, R., Li, R., Mitra, N., Nanda, V., Law, P. B., Lear, J. D., DeGrado, W. F., & BENNETT, J. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409334102 · Cited by 123 · see citing works

Migfilin, a Molecular Switch in Regulation of Integrin Activation

Ithychanda, S. S., Das, M., Ma, Y., Ding, K., Wang, X., Gupta, S., Wu, C., Plow, E. F., & Qin, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807719200 · Cited by 121 · see citing works

An Integrin Phosphorylation Switch

Oxley, C. L., Anthis, N. J., Lowe, E. D., Vakonakis, I., Campbell, I. D., & Wegener, L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m709435200 · Cited by 121 · see citing works

The antithrombotic potential of selective blockade of talin-dependent integrin αIIbβ3 (platelet GPIIb–IIIa) activation

Petrich, B. G., Fogelstrand, P., Partridge, A. W., Yousefi, N., Ablooglu, A. J., Shattil, S. J., & Ginsberg, M. H. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31024 · Cited by 119 · see citing works

NMR Analysis of Structure and Dynamics of the Cytosolic Tails of Integrin αIIbβ3 in Aqueous Solution

Ulmer, T. S., Yaspan, B. L., Ginsberg, M. H., et al. (2001) · Biochemistry · doi:10.1021/bi010338l · Cited by 118 · see citing works

Kindler syndrome: a focal adhesion genodermatosis

Lai-Cheong, J. E., Tanaka, A., Hawche, G., Emanuel, P. O., Maari, C., Taşkesen, M., Akdeniz, S., Liu, L., & McGrath, J. A. (2008) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2008.08976.x · Cited by 117 · see citing works

Structural Basis of the Migfilin-Filamin Interaction and Competition with Integrin β Tails

Lad, Y., Jiang, P., Ruskamo, S., Harburger, D. S., Ylänne, J., Campbell, I. D., & Calderwood, D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802592200 · Cited by 113 · see citing works

Competition for Talin Results in Trans-dominant Inhibition of Integrin Activation

Calderwood, D., Tai, V., Paolo, G. D., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402161200 · Cited by 113 · see citing works

Redox Control of Platelet Function

Essex, D. W. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2322 · Cited by 112 · see citing works

The Platelet Integrin αIIbβ3 Has an Endogenous Thiol Isomerase Activity

O'Neill, S., Robinson, A. A., Deering, A., Ryan, M., Fitzgerald, D. J., & Moran, N. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003279200 · Cited by 109 · see citing works

Talin1 Regulates TCR-Mediated LFA-1 Function

Simonson, W. T. N., Franco, S. J., & Huttenlocher, A. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.11.7707 · Cited by 107 · see citing works

Regulation of integrin function through conformational complexity: not simply a knee-jerk reaction?

Mould, A. P., & Humphries, M. J. (2004) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2004.07.003 · Cited by 105 · see citing works

WAVE2 Regulates High-Affinity Integrin Binding by Recruiting Vinculin and Talin to the Immunological Synapse

Nolz, J. C., Medeiros, R. B., Mitchell, J. S., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00136-07 · Cited by 104 · see citing works

The Critical Cytoplasmic Regions of the αL/β2 Integrin in Rap1-induced Adhesion and Migration

Tohyama, Y., Katagiri, K., Pardi, R., et al. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-09-0615 · Cited by 101 · see citing works

Genetic analysis of β1 integrin “activation motifs” in mice

Czuchra, A., Meyer, H., Legate, K. R., Brakebusch, C., & Fässler, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604060 · Cited by 100 · see citing works

Loss of Kindlin-3 in LAD-III eliminates LFA-1 but not VLA-4 adhesiveness developed under shear flow conditions

Manevich, E., Feigelson, S. W., Pasvolsky, R., Aker, M., Grabovsky, V., Shulman, Z., Kılıç, S. Ş., Rosenthal‐Allieri, M. A., Ben‐Dor, S., Mory, A., et al. (2009) · Blood · doi:10.1182/blood-2009-04-218636 · Cited by 100 · see citing works

Cell adaptive response to extracellular matrix density is controlled by ICAP-1–dependent β1-integrin affinity

Millon‐Frémillon, A., Bouvard, D., Grichine, A., Manet, S., Block, M. R., & Albigès‐Rizo, C. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200707142 · Cited by 100 · see citing works

PINCH, N(i)ck and the ILK: network wiring at cell–matrix adhesions

Wu, C. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.07.002 · Cited by 99 · see citing works

Solution structures of the cytoplasmic tail complex from platelet integrin αIIb- and β3-subunits

Weljie, A. M., Hwang, P. M., & Vogel, H. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092515799 · Cited by 98 · see citing works

LAD-III, a novel group of leukocyte integrin activation deficiencies

Alon, R., & Etzioni, A. (2003) · Trends in Immunology · doi:10.1016/j.it.2003.08.001 · Cited by 97 · see citing works

Structure of the Integrin αIIb Transmembrane Segment

Lau, T., Dua, V., & Ulmer, T. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801748200 · Cited by 90 · see citing works

Domain-Specific Interactions of Talin with the Membrane-Proximal Region of the Integrin β3 Subunit

Ulmer, T. S., Calderwood, D., Ginsberg, M. H., & Campbell, I. D. (2003) · Biochemistry · doi:10.1021/bi034384s · Cited by 86 · see citing works

Requirement of Integrin β3 Tyrosine 747 for β3 Tyrosine Phosphorylation and Regulation of αvβ3 Avidity

Blystone, S. D., Williams, M. P., Slater, S. E., & Brown, E. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28757 · Cited by 86 · see citing works

Locking the β3 Integrin I-like Domain into High and Low Affinity Conformations with Disulfides

Luo, B., Takagi, J., & Springer, T. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312732200 · Cited by 86 · see citing works

Detection of Integrin αIIbβ3Clustering in Living Cells

Buensuceso, C. S., de Virgilio, M., & Shattil, S. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213234200 · Cited by 83 · see citing works

Role of the cytoplasmic tyrosines of β1A integrins in transformation by v-src

Sakai, T., Jove, R., Fässler, R., & Mosher, D. F. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.240456398 · Cited by 83 · see citing works

Determination of the Border between the Transmembrane and Cytoplasmic Domains of Human Integrin Subunits

Armulik, A., Nilsson, I., von HEIJNE, G., & Johansson, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37030 · Cited by 82 · see citing works

CIB1 is an endogenous inhibitor of agonist-induced integrin αIIbβ3 activation

Yuan, W., Leisner, T. M., McFadden, A. W., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200505131 · Cited by 79 · see citing works

Interactions of platelet integrin αΙΙb and β3 transmembrane domains in mammalian cell membranes and their role in integrin activation

Kim, C., Lau, T., Ulmer, T. S., et al. (2009) · Blood · doi:10.1182/blood-2008-10-186551 · Cited by 74 · see citing works

Tests of the Extension and Deadbolt Models of Integrin Activation

Zhu, J., Boylan, B., Luo, B., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700249200 · Cited by 67 · see citing works

Integrin αIIbβ3 in a Membrane Environment Remains the Same Height after Mn2+ Activation when Observed by Cryoelectron Tomography

Ye, F., Liu, J., Winkler, H., et al. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.03.014 · Cited by 62 · see citing works

Long range propagation of conformational changes in integrin αIIbβ3

Du, X., Gu, M., Weisel, J. W., et al. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)78180-0 · Cited by 62 · see citing works

A Coiled-Coil Structure of the αIIbβ3 Integrin Transmembrane and Cytoplasmic Domains in Its Resting State

Gottschalk, K. (2005) · Structure · doi:10.1016/j.str.2005.02.014 · Cited by 59 · see citing works

PEA-15 Binding to ERK1/2 MAPKs Is Required for Its Modulation of Integrin Activation

Chou, F.-L., Hill, J. M., Hsieh, J.-C., Pouysségur, J., Brunet, A., Glading, A., Überall, F., Ramos, J. W., Werner, M. H., & Ginsberg, M. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309322200 · Cited by 59 · see citing works

Rap1 controls lymphocyte adhesion cascade and interstitial migration within lymph nodes in RAPL-dependent and -independent manners

Ebisuno, Y., Katagiri, K., Katakai, T., Ueda, Y., Nemoto, T., Inada, H., Nabekura, J., Okada, T., Kannagi, R., Tanaka, T. T., et al. (2009) · Blood · doi:10.1182/blood-2009-03-211979 · Cited by 57 · see citing works

AF6 Negatively Regulates Rap1-induced Cell Adhesion

Zhang, Z., Rehmann, H., Price, L., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505057200 · Cited by 47 · see citing works

Genetic, biochemical and structural approaches to talin function

Critchley, D. R. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051308 · Cited by 45 · see citing works

In vivo β1 integrin function requires phosphorylation-independent regulation by cytoplasmic tyrosinesPreprint

Chen, H., Zou, Z., Sarratt, K. L., Zhou, D. D., Zhang, M., Sebzda, E., Hammer, D. A., & Kahn, M. L. (2006) · Genes & Development · doi:10.1101/gad.1408306 · Cited by 45 · see citing works

CIB1 deficiency results in impaired thrombosis: the potential role of CIB1 in outside‐in signaling through integrin αIIbβ3

Naik, M. U., Nigam, A., Manrai, P. A., et al. (2009) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2009.03581.x · Cited by 39 · see citing works

Genetic, biochemical and structural approaches to talin function

Critchley, D. R. (2005) · Biochemical Society Transactions · doi:10.1042/bst0331308 · Cited by 38 · see citing works

Characterization of calcium- and integrin-binding protein 1 (CIB1) knockout platelets: Potential compensation by CIB family members

Temple, B. R. S., Gentry, H. R., DeNofrio, J. C., et al. (2008) · Thrombosis and Haemostasis · doi:10.1160/th08-06-0351 · Cited by 36 · see citing works

Genetic perturbation of the putative cytoplasmic membrane-proximal salt bridge aberrantly activates α4 integrins

Imai, Y., Park, E. J., Peer, D., Peixoto, A., Cheng, G., von Andrian, U. H., Carman, C. V., & Shimaoka, M. (2008) · Blood · doi:10.1182/blood-2008-03-144543 · Cited by 31 · see citing works

Rearrangement of Integrins in Avidity Regulation by Leukocytes

Kucik, D. F. (2002) · Immunologic Research · doi:10.1385/ir:26:1-3:199 · Cited by 29 · see citing works

Multiple Approaches Converge on the Structure of the Integrin αIIb/β3 Transmembrane Heterodimer

Metcalf, D. G., Kulp, D. W., BENNETT, J. S., et al. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.06.032 · Cited by 25 · see citing works

General in Vivo Assay for the Study of Integrin Cell Membrane Receptor Microclustering

Smith, E. A., Bunch, T. A., & Brower, D. L. (2007) · Analytical Chemistry · doi:10.1021/ac062008i · Cited by 12 · see citing works

Every step of the way: integrins in cancer progression and metastasis

Hamidi, H., & Ivaska, J. (2018) · Nature Reviews Cancer · doi:10.1038/s41568-018-0038-z · Cited by 1,493 · see citing works

Targeting integrin pathways: mechanisms and advances in therapy

Pang, X., He, X., Qiu, Z., Zhang, H., Xie, R., Liu, Z., Gu, Y., Zhao, N., Xiang, Q., & Cui, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01259-6 · Cited by 1,275 · see citing works

Integrins and cancer: regulators of cancer stemness, metastasis, and drug resistance

Seguin, L., Desgrosellier, J. S., Weis, S. M., & Cheresh, D. A. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.12.006 · Cited by 685 · see citing works

Phagocytosis: Receptors, signal integration, and the cytoskeleton

Freeman, S. A., & Grinstein, S. (2014) · Immunological Reviews · doi:10.1111/imr.12212 · Cited by 548 · see citing works

Cancer-Associated Fibroblasts Build and Secure the Tumor Microenvironment

Liu, T., Zhou, L., Li, D., Andl, T., & Zhang, Y. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00060 · Cited by 446 · see citing works

Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation

Muller, M. P., Jiang, T., Sun, C., Lihan, M., Pant, S., Mahinthichaichan, P., Trifan, A., & Tajkhorshid, E. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00608 · Cited by 282 · see citing works

A macrophage-pericyte axis directs tissue restoration via amphiregulin-induced transforming growth factor beta activation

Minutti, C. M., Modak, R. V., Macdonald, F., Li, F., Smyth, D. J., Dorward, D. A., Blair, N., Husovsky, C., Muir, A., Giampazolias, E., et al. (2019) · Immunity · doi:10.1016/j.immuni.2019.01.008 · Cited by 228 · see citing works

Intrinsically disordered proteins play diverse roles in cell signaling

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

Reciprocal Interplay Between Fibrillar Collagens and Collagen‐Binding Integrins: Implications in Cancer Progression and Metastasis

Bourgot, I., Primac, I., Louis, T., Noël, A., & Maquoi, E. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01488 · Cited by 113 · see citing works

Filamentous recombinant human Tau activates primary astrocytes via an integrin receptor complex

Wang, P., & Ye, Y. (2021) · Nature Communications · doi:10.1038/s41467-020-20322-w · Cited by 93 · see citing works

Inflammasome in Platelets: Allying Coagulation and Inflammation in Infectious and Sterile Diseases?

Hottz, E. D., Monteiro, A. P. T., Bozza, F. A., & Bozza, P. T. (2015) · Mediators of Inflammation · doi:10.1155/2015/435783 · Cited by 52 · see citing works

Complementation of dominant suppression implicates CD98 in integrin activation

Fenczik, C. A., Sethi, T., Ramos, J. W., et al. (1997) · Nature · doi:10.1038/36349 · Cited by 293 · see citing works

Integrin heterodimer and receptor complexity in avian and mammalian cells.

Hynes, R. O., Marcantonio, E. E., Stepp, M. A., Urry, L. A., & Yee, G. H. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.1.409 · Cited by 150 · see citing works

N-Glycosylation of ß4 Integrin Controls the Adhesion and Motility of Keratinocytes

Kariya, Y., & Gu, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027084 · Cited by 46 · see citing works

Abstract P117: A Conserved Trans-membrane Domain Lysine in the Integrin Beta1 Subunit Regulates Renal Collecting Duct Cell Function

Mathew, S., Jiang, C., Lu, Z., et al. (2016) · Hypertension · doi:10.1161/hyp.68.suppl_1.p117

Kindlin-1 and-2 directly bind the C-terminal region of β integrin cytoplasmic tails and exert integrin-specific activation effects

Harburger, D. S., Bouaouina, M., & Calderwood, D. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809233200 · Cited by 304 · see citing works