Bidirectional Transmembrane Signaling by Cytoplasmic Domain Separation in Integrins

Partitioning of Lipid-Modified Monomeric GFPs into Membrane Microdomains of Live Cells

Zacharias, D. A., Violin, J. D., Newton, A. C., & Tsien, R. Y. (2002) · Science · doi:10.1126/science.1068539 · Cited by 2,242 · see citing works

Leukocytes roll on a selectin at physiologic flow rates: Distinction from and prerequisite for adhesion through integrins

Lawrence, M. B., & Springer, T. A. (1991) · Cell · doi:10.1016/0092-8674(91)90393-d · Cited by 2,157 · see citing works

The molecular structure of green fluorescent protein

Yang, F., Moss, L. G., & Phillips, G. N. (1996) · Nature Biotechnology · doi:10.1038/nbt1096-1246 · Cited by 1,580 · see citing works

T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1

Dustin, M. L., & Springer, T. A. (1989) · Nature · doi:10.1038/341619a0 · Cited by 1,547 · 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

Chemokines and the Arrest of Lymphocytes Rolling Under Flow Conditions

Campbell, J. J., Hedrick, J. A., Zlotnik, A., Siani, M. A., Thompson, D. A., & Butcher, E. C. (1998) · Science · doi:10.1126/science.279.5349.381 · Cited by 994 · see citing works

The Talin Head Domain Binds to Integrin β Subunit Cytoplasmic Tails and Regulates Integrin Activation

Calderwood, D. A., Zent, R., Grant, R., Rees, D. J. G., Hynes, R. O., & Ginsberg, M. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28071 · Cited by 720 · 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

Conformational Regulation of Integrin Structure and Function

Shimaoka, M., Takagi, J., & Springer, T. A. (2002) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.31.101101.140922 · Cited by 538 · 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

Chemokines Trigger Immediate β2 Integrin Affinity and Mobility Changes

Constantin, G., Majeed, M., Giagulli, C., Piccio, L. M., Kim, J. Y., Butcher, E. C., & Laudanna, C. (2000) · Immunity · doi:10.1016/s1074-7613(00)00074-1 · Cited by 519 · see citing works

Divalent cation regulation of the function of the leukocyte integrin LFA-1.

Dransfield, I., Cabañas, C., Craig, A. G., et al. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.116.1.219 · Cited by 492 · 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

Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation

Beglova, N., Blacklow, S. C., Takagi, J., & Springer, T. A. (2002) · Nature Structural Biology · doi:10.1038/nsb779 · Cited by 314 · 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

A Zinc Clasp Structure Tethers Lck to T Cell Coreceptors CD4 and CD8

Kim, P. W., Sun, Z.-Y. J., Blacklow, S. C., Wagner, G., & Eck, M. J. (2003) · Science · doi:10.1126/science.1085643 · Cited by 275 · see citing works

C-terminal opening mimics 'inside-out' activation of integrin alpha5beta1.

Takagi, J., Erickson, H., & Springer, T. A. (2001) · Nature Structural Biology · doi:10.1038/87569 · Cited by 264 · see citing works

Reversibly locking a protein fold in an active conformation with a disulfide bond: Integrin αL I domains with high affinity and antagonist activity in vivo

Shimaoka, M., Lu, C., Palframan, R. T., von Andrian, U. H., McCormack, A., Takagi, J., & Springer, T. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.101130498 · Cited by 209 · see citing works

Locking in alternate conformations of the integrin αLβ2 I domain with disulfide bonds reveals functional relationships among integrin domains

Lu, C., Shimaoka, M., Zang, Q. S., Takagi, J., & Springer, T. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041618598 · Cited by 192 · see citing works

Epitope Mapping of Antibodies to the C-Terminal Region of the Integrin β2 Subunit Reveals Regions that Become Exposed Upon Receptor Activation

Lu, C., Ferzly, M., Takagi, J., et al. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.9.5629 · Cited by 165 · 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

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

The regulation of integrin function by Ca2+

Leitinger, B., McDowall, A., Stanley, P., & Hogg, N. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(00)00086-0 · Cited by 154 · 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

An isolated, surface-expressed I domain of the integrin αLβ2 is sufficient for strong adhesive function when locked in the open conformation with a disulfide bond

Lu, C., Shimaoka, M., Ferzly, M., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041606398 · Cited by 125 · 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

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

Cytoplasmic tails of beta 1, beta 2, and beta 7 integrins differentially regulate LFA-1 function in K562 cells.

Lub, M., van Vliet, S. J., Oomen, S. P. M. A., et al. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.4.719 · Cited by 53 · see citing works

Progesterone triggers rapid transmembrane calcium influx and/or calcium mobilization from endoplasmic reticulum, via a pertussis-insensitive G-protein in granulosa cells in relation to luteinization process

Machelon, V., Mercier‐Nomé, F., Grosse, B., & Lieberherr, M. (1996) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19960616)61:4 · Cited by 52 · see citing works

The final steps of integrin activation: the end game

Shattil, S. J., Kim, C., & Ginsberg, M. H. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2871 · Cited by 1,086 · see citing works

Mechanisms that regulate adaptor binding to β-integrin cytoplasmic tails

Legate, K. R., & Fässler, R. (2009) · Journal of Cell Science · doi:10.1242/jcs.041624 · Cited by 370 · see citing works

From inflammation to cancer

Korniluk, A., Koper, O., Kemona, H., & Dymicka-Piekarska, V. (2017) · Irish Journal of Medical Science (1971 -) · doi:10.1007/s11845-016-1464-0 · Cited by 282 · see citing works

Tie1 controls angiopoietin function in vascular remodeling and inflammation

Korhonen, E. A., Lampinen, A., Giri, H., Anisimov, A., Kim, M., Allen, B., Fang, S., D’Amico, G., Sipilä, T. J., Lohela, M., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci84923 · Cited by 283 · see citing works

Repeated Social Defeat, Neuroinflammation, and Behavior: Monocytes Carry the Signal

Weber, M. D., Godbout, J. P., & Sheridan, J. F. (2017) · Neuropsychopharmacology · doi:10.1038/npp.2016.102 · Cited by 283 · see citing works

Kindlins: essential regulators of integrin signalling and cell-matrix adhesion

Larjava, H., Plow, E. F., & Wu, C. (2008) · The EMBO Reports · doi:10.1038/embor.2008.202 · Cited by 268 · see citing works

Integrin modulation and signaling in leukocyte adhesion and migration

Rose, D. M., Alon, R., & Ginsberg, M. H. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00536.x · Cited by 243 · see citing works

Mechanisms of leukocyte migration across the blood-retina barrier

Crane, I. J., & Liversidge, J. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0106-7 · Cited by 152 · see citing works

Allosteric β1 Integrin Antibodies That Stabilize the Low Affinity State by Preventing the Swing-out of the Hybrid Domain

Luo, B.-H., Strokovich, K., Walz, T., Springer, T. A., & Takagi, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404354200 · Cited by 73 · see citing works

Sequence of the SARS-CoV-2 spike transmembrane domain makes it inherently dynamicPreprint

Lall, S., Balaram, P., Mathew, M. K., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.07.447334 · Cited by 1 · see citing works

A mutational study of transmembrane helix–helix interactions

Prodöhl, A., Weber, M., Dreher, C., et al. (2007) · Biochimie · doi:10.1016/j.biochi.2007.06.006 · Cited by 20 · see citing works

Isolated Toll-like Receptor Transmembrane Domains Are Capable of Oligomerization

Godfroy, J. I., Roostan, M., Moroz, Y. S., Korendovych, I. V., & Yin, H. H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048875 · Cited by 81 · see citing works

3‐D Structure of G Protein‐coupled Receptors

Pardo, L., Deupí, X., Govaerts, C., et al. (2006) · Methods and principles in medicinal chemistry · doi:10.1002/3527608249.ch10 · Cited by 2 · see citing works

Structure, transmembrane topology and helix packing of P‐type ion pumps

Stokes, D. L., Taylor, W. R., & Green, N. M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00297-5 · Cited by 66 · see citing works