Proteomic Analysis of Integrin-Associated Complexes Identifies RCC2 as a Dual Regulator of Rac1 and Arf6

Cluster analysis and display of genome-wide expression patterns

Eisen, M. B., Spellman, P. T., Brown, P. O., & Botstein, D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14863 · Cited by 12,617 · see citing works

Untitled work

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

Towards a proteome-scale map of the human protein–protein interaction network

Rual, J.-F. M., Venkatesan, K., Hao, T., Hirozane-Kishikawa, T., Dricot, A., Li, N., Berriz, G. F., Gibbons, F. D., Dreze, M., Ayivi-Guedehoussou, N., et al. (2005) · Nature · doi:10.1038/nature04209 · Cited by 2,937 · see citing works

A Model for Random Sampling and Estimation of Relative Protein Abundance in Shotgun Proteomics

Liu, H., Sadygov, R. G., & Yates, J. R. (2004) · Analytical Chemistry · doi:10.1021/ac0498563 · Cited by 2,486 · see citing works

A Human Protein-Protein Interaction Network: A Resource for Annotating the Proteome

Stelzl, U., Worm, U., Lalowski, M. M., Haenig, C., Brembeck, F. H., Goehler, H., Strödicke, M., Zenkner, M., Schoenherr, A., Koeppen, S., et al. (2005) · Cell · doi:10.1016/j.cell.2005.08.029 · Cited by 2,389 · see citing works

Transmembrane crosstalk between the extracellular matrix and the cytoskeleton

Geiger, B., Bershadsky, A. D., Pankov, R. G., & Yamada, K. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35099066 · Cited by 2,213 · see citing works

Integrin ligands at a glance

Humphries, J. D., Byron, A., & Humphries, M. J. (2006) · Journal of Cell Science · doi:10.1242/jcs.03098 · Cited by 1,711 · see citing works

Functional atlas of the integrin adhesome

Zaidel‐Bar, R., Itzkovitz, S., Ma’ayan, A., Iyengar, R., & Geiger, B. (2007) · Nature Cell Biology · doi:10.1038/ncb0807-858 · Cited by 1,182 · see citing works

Large‐scale mapping of human protein–protein interactions by mass spectrometry

Ewing, R. M., Chu, P. C., Elisma, F., Li, H., Taylor, P. P., Climie, S. C., McBroom, L. D. B., Robinson, M. D., O'Connor, L., Li, M. M., et al. (2007) · Molecular Systems Biology · doi:10.1038/msb4100134 · Cited by 985 · see citing works

Force Sensing by Mechanical Extension of the Src Family Kinase Substrate p130Cas

Sawada, Y., Tamada, M., Dubin‐Thaler, B. J., Cherniavskaya, O., Sakai, R., Tanaka, S., & Sheetz, M. P. (2006) · Cell · doi:10.1016/j.cell.2006.09.044 · Cited by 945 · 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

Activation of Rac and Cdc42 by Integrins Mediates Cell Spreading

Price, L., Leng, J., Schwartz, M. A., & Bokoch, G. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.7.1863 · Cited by 644 · see citing works

Integrins Regulate Rac Targeting by Internalization of Membrane Domains

del Pozo, M. Á., Alderson, N. B., Kiosses, W. B., Chiang, H.-H., Anderson, R. G. W., & Schwartz, M. A. (2004) · Science · doi:10.1126/science.1092571 · Cited by 538 · see citing works

Focal adhesion kinase is involved in mechanosensing during fibroblast migration

Wang, H.-B., Dembo, M., Hanks, S. K., & Wang, Y. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.201201198 · Cited by 503 · see citing works

A Rac switch regulates random versus directionally persistent cell migration

Pankov, R. G., Endo, Y., Even‐Ram, S., Araki, M., Clark, K., Cukierman, E., Matsumoto, K., & Yamada, K. M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200503152 · Cited by 453 · see citing works

Structure and mechanics of integrin-based cell adhesion

Arnaout, M. A., Goodman, S. L., & Xiong, J.-P. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2007.08.002 · Cited by 403 · see citing works

Integrin binding and mechanical tension induce movement of mRNA and ribosomes to focal adhesions

Chicurel, M., Singer, R. H., Meyer, C. J., & Ingber, D. E. (1998) · Nature · doi:10.1038/33719 · Cited by 374 · 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

Binding of paxillin to α4 integrins modifies integrin-dependent biological responses

Liu, S., Thomas, S. Μ., Woodside, D. G., Rose, D. M., Kiosses, W. B., Pfaff, M., & Ginsberg, M. H. (1999) · Nature · doi:10.1038/45264 · Cited by 329 · see citing works

Force activates smooth muscle α-actin promoter activity through the Rho signaling pathway

Zhao, X.-H., Laschinger, C. A., Arora, P. D., Szászi, K., Kapùs, A., & McCulloch, C. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.001586 · Cited by 325 · see citing works

Quantitative Mass Spectrometry Identifies Insulin Signaling Targets in C. elegans

Dong, M., Venable, J. D., Au, N., Xu, T., Park, S. K., Cociorva, D., Johnson, J. R., Dillin, A. G., & Yates, J. R. (2007) · Science · doi:10.1126/science.1139952 · Cited by 313 · see citing works

Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains

Chan, B. M. C., Kassner, P. D., Schiro, J. A., Byers, H. R., Kupper, T. S., & Hemler, M. E. (1992) · Cell · doi:10.1016/0092-8674(92)90077-p · Cited by 302 · see citing works

RNA and RNA Binding Proteins Participate in Early Stages of Cell Spreading through Spreading Initiation Centers

de Hoog, C. L., Foster, L. J., & Mann, M. (2004) · Cell · doi:10.1016/s0092-8674(04)00456-8 · Cited by 262 · see citing works

Integrins and the actin cytoskeleton

Delon, I., & Brown, N. H. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.12.013 · Cited by 249 · see citing works

Consolidating the set of known human protein-protein interactions in preparation for large-scale mapping of the human interactome

Ramani, A. K., Bunescu, R., Mooney, R. J., & Marcotte, E. M. (2005) · Genome biology · doi:10.1186/gb-2005-6-5-r40 · Cited by 239 · see citing works

Syndecan-4–dependent Rac1 regulation determines directional migration in response to the extracellular matrix

Bass, M. D., Roach, K. A., Morgan, M. R., Mostafavi‐Pour, Z., Schoen, T., Muramatsu, T., Mayer, U., Ballestrem, C., Spatz, J. P., & Humphries, M. J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610076 · Cited by 236 · see citing works

Integrins and cell-fate determination

Streuli, C. H. (2009) · Journal of Cell Science · doi:10.1242/jcs.018945 · Cited by 220 · see citing works

Arf6 and microtubules in adhesion-dependent trafficking of lipid rafts

Balasubramanian, N., Scott, D. W., Castle, J. D., Casanova, J. E., & Schwartz, M. A. (2007) · Nature Cell Biology · doi:10.1038/ncb1657 · Cited by 209 · see citing works

Inhibition of Rac by the GAP Activity of Centralspindlin Is Essential for Cytokinesis

Canman, J. C., Lewellyn, L., Laband, K., Smerdon, S. J., Desai, A. B., Bowerman, B. A., & Oegema, K. (2008) · Science · doi:10.1126/science.1163086 · Cited by 175 · see citing works

Rapid Induction and Isolation of Focal Adhesion Complexes

Plopper, G. E., & Ingber, D. E. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.1662 · Cited by 167 · see citing works

Centromeric Aurora-B Activation Requires TD-60, Microtubules, and Substrate Priming Phosphorylation

Rosasco, S. E., Lan, W., Khorasanizadeh, S., & Stukenberg, P. T. (2008) · Science · doi:10.1126/science.1148980 · Cited by 155 · see citing works

p619, a giant protein related to the chromosome condensation regulator RCC1, stimulates guanine nucleotide exchange on ARF1 and Rab proteins.

Rosa, J. L., Casaroli-Marano, R. P., Buckler, A., Vilaró, S., & Barbacid, M. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00801.x · Cited by 130 · see citing works

The Mammalian Passenger Protein TD-60 Is an RCC1 Family Member with an Essential Role in Prometaphase to Metaphase Progression

Mollinari, C., Reynaud, C., Martineau-Thuillier, S. X. E. P., Monier, S., Kieffer‐Jaquinod, S., Garin, J., Andreassen, P. R., Boulet, A., Goud, B., Kleman, J.-P., et al. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00205-3 · Cited by 121 · see citing works

Specialized functional properties of the integrin alpha 4 cytoplasmic domain.

Kassner, P. D., Alon, R., Springer, T. A., et al. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.6.661 · Cited by 101 · see citing works

α4 Integrin Binding Interfaces on VCAM-1 and MAdCAM-1

Newham, P., Craig, S. E., Seddon, G. N., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.31.19429 · Cited by 100 · see citing works

Perturbing integrin function inhibits microtubule growth from centrosomes, spindle assembly, and cytokinesis

Reverte, C. G., Benware, A., Jones, C. W., & LaFlamme, S. E. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200603069 · Cited by 80 · see citing works

Fibronectin controls cap-dependent translation through β1 integrin and eukaryotic initiation factors 4 and 2 coordinated pathways

Gorrini, C., Loreni, F., Gandin, V., Sala, L. A., Sonenberg, N., Marchisio, P. C., & Biffo, S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409513102 · Cited by 38 · see citing works

Dual Functionality of the Anti-β1 Integrin Antibody, 12G10, Exemplifies Agonistic Signalling from the Ligand Binding Pocket of Integrin Adhesion Receptors

Humphries, J. D., Schofield, N. R., Mostafavi‐Pour, Z., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411102200 · Cited by 34 · see citing works

Cytokinesis: the final stop for the chromosomal passengers

Carmena, M. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360367 · Cited by 27 · see citing works

Talin Concentrates to the Midbody Region During Mammalian Cell Cytokinesis

Bellissent‐Waydelich, A., Vanier, M., Albigès‐Rizo, C., et al. (1999) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215549904701102 · Cited by 19 · see citing works

Genetic meta-analysis of diagnosed Alzheimer’s disease identifies new risk loci and implicates Aβ, tau, immunity and lipid processing

Alzheimer Disease Genetics Consortium (ADGC), Kunkle, B. W., The European Alzheimer’s Disease Initiative (EADI), Cohorts for Heart and Aging Research in Genomic Epidemiology Consortium (CHARGE), Genetic and Environmental Risk in AD/Defining Genetic, P. A. E. R. F. A. D. C. (., Grenier-Boley, B., Sims, R., Bis, J. C., Damotte, V., Naj, A. C., et al. (2019) · Nature Genetics · doi:10.1038/s41588-019-0358-2 · Cited by 2,946 · see citing works

Redox chemistry and chemical biology of H2S, hydropersulfides, and derived species: Implications of their possible biological activity and utility

Ono, K., Akaike, T., Sawa, T., Kumagai, Y., Wink, D. A., Tantillo, D. J., Hobbs, A. J., Nagy, P., Xian, M., Lin, J., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.09.007 · Cited by 422 · see citing works

Targeting and transport: How microtubules control focal adhesion dynamics

Stehbens, S., & Wittmann, T. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201206050 · Cited by 244 · 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

The reaction of H2S with oxidized thiols: generation of persulfides and implications to H2S biology

Francoleon, N. E., Carrington, S. J., & Fukuto, J. M. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.09.015 · Cited by 199 · see citing works

Mammalian target of rapamycin signalling modulates amino acid uptake by regulating transporter cell surface abundance in primary human trophoblast cells

Rosario, F. J., Kanai, Y., Powell, T. L., & Jansson, T. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2012.238014 · Cited by 185 · see citing works

Scavenger receptor CD36 is essential for the cerebrovascular oxidative stress and neurovascular dysfunction induced by amyloid-β

Park, L., Wang, G., Zhou, P., Zhou, J., Pitstick, R., Previti, M. L., Younkin, L., Younkin, S. G., Van Nostrand, W. E., Cho, S., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015413108 · Cited by 156 · see citing works

Border patrol: Insights into the unique role of perlecan/heparan sulfate proteoglycan 2 at cell and tissue borders

Farach-Carson, M. C., Warren, C. R., Harrington, D. A., & Carson, D. D. (2014) · Matrix Biology · doi:10.1016/j.matbio.2013.08.004 · Cited by 155 · see citing works

The impact of nanoparticle ligand density on dendritic-cell targeted vaccines

Bandyopadhyay, A., Fine, R. L., Demento, S., Bockenstedt, L. K., & Fahmy, T. M. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2010.12.054 · Cited by 141 · see citing works

Tools used to assess the quality of peer review reports: A methodological systematic review

Superchi, C., González, J. A., Solà, I., Cobo, E., Hren, D., & Boutron, I. (2019) · BMC Medical Research Methodology · doi:10.1186/s12874-019-0688-x · Cited by 110 · see citing works

The polarity protein Scrib is essential for directed endothelial cell migration

Michaelis, U. R., Chavakis, E., Kruse, C., Jungblut, B., Kaluza, D., Wandzioch, K., Manavski, Y., Heide, H., Santoni, M.-J., Potente, M., et al. (2013) · Circulation Research · doi:10.1161/circresaha.112.300592 · Cited by 57 · see citing works

How widespread is stable protein S-nitrosylation as an end-effector of protein regulation?

Wolhuter, K., & Eaton, P. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.013 · Cited by 55 · see citing works

CD36 gene polymorphism is associated with Alzheimer's disease

Šerý, O., Janoutová, J., Ewerlingová, L., Hálová, A., Lochman, J., Janout, V., Khan, N. A., & Balcar, V. J. (2017) · Biochimie · doi:10.1016/j.biochi.2017.01.009 · Cited by 44 · see citing works

A biochemical network modeling of a whole-cell

Burke, P. E. P., Campos, C. B. D. L., Costa, L. D. F., & Quiles, M. G. (2020) · Scientific Reports · doi:10.1038/s41598-020-70145-4 · Cited by 18 · see citing works

LncSSBP1 Functions as a Negative Regulator of IL-6 Through Interaction With hnRNPK in Bronchial Epithelial Cells Infected With Talaromyces marneffei

Li, Y., Chen, H., Li, S., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02977 · Cited by 18 · see citing works

Beyond an oncogene, Lin28 is a master regulator of cancer progression.

Wang, X., Weng, M., Jin, Y., et al. (2018) · PubMed · doi:10.14670/hh-11-922 · Cited by 9 · see citing works

Master Regulator Analysis from Intratumoral Copper Modulates PD-L1 Expression and Influences Tumor Immune Evasion

Voli, F., Valli, E., Lerra, L., et al. (2023) · doi:10.1158/0008-5472.22426419

YAP controls cell migration and invasion through a Rho-GTPase switchPreprint

Shah, S. R., Ren, C., Tippens, N. D., Park, J., Mohyeldin, A., Wang, S., Vela, G., Martínez-Gutiérrez, J. C., Margolis, S. S., Schmidt, S., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/602052 · Cited by 7 · see citing works

Faculty Opinions recommendation of A bacterial type III effector targets the master regulator of salicylic acid signaling, NPR1, to subvert plant immunity.

White, F. F. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.732181228.793543673