The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Receptor Activation Alters Inner Surface Potential During Phagocytosis
Abstract
The surface potential of biological membranes varies according to their lipid composition. We devised genetically encoded probes to assess surface potential in intact cells. These probes revealed marked, localized alterations in the charge of the inner surface of the plasma membrane of macrophages during the course of phagocytosis. Hydrolysis of phosphoinositides and displacement of phosphatidylserine accounted for the change in surface potential at the phagosomal cup. Signaling molecules such as K-Ras, Rac1, and c-Src that are targeted to the membrane by electrostatic interactions were rapidly released from membrane subdomains where the surface charge was altered by lipid remodeling during phagocytosis.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“In addition to stage-specific v-, t-SNAREs and Rab proteins, phosphatidylinositide (PI) lipids synthesized by stage-specific phosphatidyl inositol kinases (PIK) at the cytoplasmic sheet of phagosomal membranes are specific for different phagosome stages and functionally contribute to maturation-associated vesicle fusion and actin-polymerization associated processes (16).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [16]
Citations
Cites
Hancock, J. F., Paterson, H., & Marshall, C. J. (1990) · Cell · doi:10.1016/0092-8674(90)90294-o · Cited by 1,042
Differential Localization of Rho Gtpases in Live Cells
Michaelson, D., Silletti, J., Murphy, G., D'Eustachio, P., Rush, M., & Philips, M. R. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.1.111 · Cited by 679
Self-citationThe myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions
McLaughlin, S., & Aderem, A. A. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89042-8 · Cited by 674
Cdc42, Rac1, and Rac2 Display Distinct Patterns of Activation during Phagocytosis
Hoppe, A. D., & Swanson, J. A. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-11-0847 · Cited by 365
Olivotto, M., Arcangeli, A., Carlà, M., & Wanke, E. (1996) · BioEssays · doi:10.1002/bies.950180612 · Cited by 127
McCabe, J. B., & Berthiaume, L. G. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.11.3601 · Cited by 122
Roy, M., Leventis, R., & Silvius, J. R. (2000) · Biochemistry · doi:10.1021/bi000512q · Cited by 102
Self-citationLipid-Binding Characteristics of the Polybasic Carboxy-Terminal Sequence of K-ras4B
Leventis, R., & Silvius, J. R. (1998) · Biochemistry · doi:10.1021/bi973077h · Cited by 85
Self-citationPhosphoinositide Involvement in Phagocytosis and Phagosome Maturation
Botelho, R. J., Scott, C. C., & Grinstein, S. (2004) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-18805-3_1 · Cited by 55
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- R. J. Botelho, C. C. Scott, S. Grinstein, Curr. Top. Microbiol. Immunol.282, 1 (2004).
Cited by
Sorted by citations
Items 101–200 of 328
Direct modifications of Rho proteins: deconstructing GTPase regulation
Visvikis, O., Maddugoda, M. P., & Lemichez, E. (2010) · Biology of the Cell · doi:10.1042/bc20090151 · Cited by 68
Membrane surface charge dictates the structure and function of the epithelial Na+/H+ exchanger
Alexander, R. T., Jaumouillé, V., Yeung, T., Furuya, W., Peltekova, I. T., Boucher, A., ZASLOFF, M. A., Orlowski, J., & Grinstein, S. (2011) · The EMBO Journal · doi:10.1038/emboj.2010.356 · Cited by 62
Self-citationHan, X., Yu, R., Zhen, D., Tao, S., Schmidt, M., & Han, L. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021468 · Cited by 63
Phagosome maturation in macrophages: Eat, digest, adapt, and repeat
Fountain, A., Inpanathan, S., Alves, P., Verdawala, M. B., & Botelho, R. J. (2021) · Advances in Biological Regulation · doi:10.1016/j.jbior.2021.100832 · Cited by 64
Zhou, Y., Cho, K.-J., Plowman, S. J., & Hancock, J. F. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.348490 · Cited by 61
The Structure of the Talin/Integrin Complex at a Lipid Bilayer: An NMR and MD Simulation Study
Kalli, A. C., Wegener, K. L., Goult, B. T., Anthis, N. J., Campbell, I. D., & Sansom, M. S. P. (2010) · Structure · doi:10.1016/j.str.2010.07.012 · Cited by 61
Rasmussen, M., Alexander, R. T., Darborg, B. V., Møbjerg, N., Hoffmann, E. K., Kapùs, A., & Pedersen, S. F. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00268.2007 · Cited by 59
α-Actinin-4 Is Selectively Required for Insulin-induced GLUT4 Translocation
Talior‐Volodarsky, I., Randhawa, V. K., Zaid, H., & Klip, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801750200 · Cited by 58
Khelashvili, G., Weinstein, H., & Harries, D. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.120667 · Cited by 57
Phosphatidylserine regulation of Ca2+-triggered exocytosis and fusion pores in PC12 cells.
Zhang, Z., Hui, E., Chapman, E., & Jackson, M. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-08-0691 · Cited by 56
Sengupta, P., Ruano, M. J., Tebar, F., Golebiewska, U. P., Зайцева, І., Enrich, C., McLaughlin, S., & Villalobo, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607211200 · Cited by 59
CD14 Signaling Restrains Chronic Inflammation through Induction of p38-MAPK/SOCS-Dependent Tolerance
Sahay, B., Patsey, R. L., Eggers, C. H., Salazar, J. C., Radolf, J. D., & Sellati, T. J. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000687 · Cited by 58
Dendritic Spines: The Stuff That Memories Are Made Of?
Hofer, S. B., & Bonhoeffer, T. (2010) · Current Biology · doi:10.1016/j.cub.2009.12.040 · Cited by 63
Jankowski, A., Zhu, P., & Marshall, J. G. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.05.047 · Cited by 55
Gericke, A., Leslie, N. R., Lösche, M., & Ross, A. H. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-6331-9_6 · Cited by 60
Coon, B. G., Mukherjee, D., Hanna, C. B., Riese, D. J., Lowe, M., & Aguilar, R. C. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp407 · Cited by 60
Viruses and endosome membrane dynamics
Grüenberg, J. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.03.008 · Cited by 51
Zarubica, A., Plazzo, A. P., Stöckl, M. T., Trombik, T., Hamon, Y., Müller, P. K., Pomorski, T. G., Herrmann, A., & Chimini, G. (2009) · The FASEB Journal · doi:10.1096/fj.08-122192 · Cited by 52
A FRET sensor enables quantitative measurements of membrane charges in live cells
Ma, Y., Yamamoto, Y., Nicovich, P. R., Goyette, J., Rossy, J., Gooding, J. J., & Gaus, K. (2017) · Nature Biotechnology · doi:10.1038/nbt.3828 · Cited by 52
Membrane characteristics tune activities of endosomal and autophagic human VPS34 complexes
Ohashi, Y., Tremel, S., Masson, G. R., McGinney, L., Boulanger, J., Rostislavleva, K., Johnson, C. M., Niewczas, I. S., Clark, J. P., & Williams, R. L. (2020) · eLife · doi:10.7554/elife.58281 · Cited by 62
Majonis, D., Ornatsky, O., Kinach, R., & Winnik, M. A. (2011) · Biomacromolecules · doi:10.1021/bm201011t · Cited by 52
Suicidal Membrane Repair Regulates Phosphatidylserine Externalization during Apoptosis
Mirnikjoo, B., Balasubramanian, K., & Schroit, A. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.c109.022913 · Cited by 47
Chen, C.-J., Kirshner, J., Sherman, M. A., Hu, W., Nguyen, T. T., & Shively, J. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610903200 · Cited by 50
Waheed, F., Speight, P., Kawai, G., Dan, Q., Kapùs, A., & Szászi, K. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00408.2009 · Cited by 49
Mapping the electrostatic profiles of cellular membranes
Eisenberg, S., Haimov, E., Walpole, G. F. W., Plumb, J. D., Kozlov, M. M., & Grinstein, S. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-08-0436 · Cited by 46
Self-citationCounterion release in membrane–biopolymer interactions
Harries, D., May, S., & Ben‐Shaul, A. (2013) · Soft Matter · doi:10.1039/c3sm51419f · Cited by 49
Ugolev, Y., Berdichevsky, Y., Weinbaum, C., & Pick, E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800734200 · Cited by 51
Várnai, P., & Balla, T. (2007) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-007-0270-y · Cited by 47
Levay, M. K., Settleman, J. E., & Ligeti, E. (2009) · Biochemistry · doi:10.1021/bi900667y · Cited by 52
Off the beaten paths: alternative and crosstalk regulation of Rho GTPases
Boulter, E., Estrach, S., García‐Mata, R., & Féral, C. C. (2011) · The FASEB Journal · doi:10.1096/fj.11-192252 · Cited by 49
Mu, L., Tu, Z., Miao, L., Ruan, H., Kang, N., Hei, Y., Chen, J., Wei, W., Gong, F., Wang, B., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06744-7 · Cited by 48
Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins
Pemberton, J. G., & Balla, T. (2018) · Advances in experimental medicine and biology · doi:10.1007/5584_2018_288 · Cited by 46
Beise, N., & Trimble, W. S. (2011) · Journal of Cell Science · doi:10.1242/jcs.087007 · Cited by 50
Zhong, Q., Li, G., Gvozdenovic‐Jeremic, J., & Greenberg, M. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701055200 · Cited by 45
Measles and Nipah virus assembly: Specific lipid binding drives matrix polymerization
Norris, M. J., Husby, M. L., Kiosses, W. B., Yin, J., Saxena, R., Rennick, L. J., Heiner, A., Harkins, S., Pokhrel, R., Schendel, S. L., et al. (2022) · Science Advances · doi:10.1126/sciadv.abn1440 · Cited by 44
Geissler, B., Ahrens, S., & Satchell, K. J. F. (2011) · Cellular Microbiology · doi:10.1111/j.1462-5822.2011.01718.x · Cited by 44
Cockcroft, S., & Garner, K. (2011) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.538664 · Cited by 45
Nanoscale Membrane Organization: Where Biochemistry Meets Advanced Microscopy
Cambi, A., & Lidke, D. S. (2011) · ACS Chemical Biology · doi:10.1021/cb200326g · Cited by 44
Schlam, D., Bohdanowicz, M., Chatilialoglu, A., Steinberg, B. E., Ueyama, T., Du, G., Grinstein, S., & Fairn, G. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.457606 · Cited by 45
Self-citationDecoding P4-ATPase substrate interactions
Roland, B. P., & Graham, T. R. (2016) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2016.1237934 · Cited by 42
Casbon, A.-J., Long, M. E., Dunn, K. W., Allen, L. H., & Dinauer, M. C. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0512244 · Cited by 46
Banerjee, A., Jang, H., Nussinov, R., & Gaponenko, V. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.11.010 · Cited by 42
Sequestering of Rac by the Yersinia Effector YopO Blocks Fcγ Receptor-mediated Phagocytosis
Groves, E., Rittinger, K., Amstutz, M., Berry, S., Holden, D. W., Cornelis, G. R., & Caron, E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.071035 · Cited by 41
A polybasic domain in aPKC mediates Par6-dependent control of membrane targeting and kinase activity
Dong, W., Lu, J., Zhang, X., Wu, Y. R., Lettieri, K. S., Hammond, G. R. V., & Hong, Y. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201903031 · Cited by 42
Phagocytosis of IgG‐Coated Polystyrene Beads by Macrophages Induces and Requires High Membrane Order
Magenau, A., Benzing, C., Proschogo, N. W., Don, A. S., Hejazi, L., Karunakaran, D., Jessup, W., & Gaus, K. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01272.x · Cited by 41
Grinstein, S. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00342.2010 · Cited by 39
Self-citationChanges in mitochondrial surface charge mediate recruitment of signaling molecules during apoptosis
Heit, B., Yeung, T., & Grinstein, S. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2010 · Cited by 40
Self-citationO’Neill, P., Karunarathne, A., Kalyanaraman, V., Silvius, J. R., & Gautam, N. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205345109 · Cited by 40
Self-citationInfluenza Hemagglutinin Modulates Phosphatidylinositol 4,5-Bisphosphate Membrane Clustering
Curthoys, N. M., Mlodzianoski, M. J., Parent, M. T., Butler, M. B., Raut, P., Wallace, J. N., Lilieholm, J., Mehmood, K., Maginnis, M. S., Waters, H. N., et al. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.01.017 · Cited by 38
Polyamine effects on cell function: Possible central role of plasma membrane PI(4,5)P2
Coburn, R. F. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21899 · Cited by 42
Masters, T. A., Sheetz, M. P., & Gauthier, N. C. (2016) · Cytoskeleton · doi:10.1002/cm.21287 · Cited by 40
Ultrasound-mediated spatial and temporal control of engineered cells in vivo
Ivanovski, F., Meško, M., Lebar, T., Rupnik, M., Lainšček, D., Gradišek, M., Jerala, R., & Benčina, M. (2024) · Nature Communications · doi:10.1038/s41467-024-51620-2 · Cited by 43
Small G proteins and their regulators in cellular signalling
Csépányi‐Kömi, R., Levay, M. K., & Ligeti, E. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.11.005 · Cited by 40
Burkholderia cenocepacia disrupts host cell actin cytoskeleton by inactivating Rac and Cdc42
Flannagan, R. S., Jaumouillé, V., Huynh, K. K., Plumb, J. D., Downey, G. P., Valvano, M. A., & Grinstein, S. (2011) · Cellular Microbiology · doi:10.1111/j.1462-5822.2011.01715.x · Cited by 38
Self-citationLocalized Diacylglycerol-dependent Stimulation of Ras and Rap1 during Phagocytosis
Botelho, R. J., Harrison, R. E., Stone, J. C., Hancock, J. F., Philips, M. R., Jongstra‐Bilen, J., Mason, D. Y., Plumb, J. D., Gold, M. R., & Grinstein, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.009514 · Cited by 38
Self-citationThe NADPH Oxidase and the Phagosome
Valenta, H., Erard, M., Dupré‐Crochet, S., & Nüβe, O. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-40406-2_9 · Cited by 40
Gulyás, G., Radvánszki, G., Matuska, R., Balla, A., Hunyady, L., Balla, T., & Várnai, P. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.806679 · Cited by 32
A PIP5 Kinase Essential for Efficient Chemotactic Signaling
Fets, L., Nichols, J. M. E., & Kay, R. R. (2014) · Current Biology · doi:10.1016/j.cub.2013.12.052 · Cited by 35
Phosphoinositides and Membrane Targeting in Cell PolarityPreprint
Hammond, G. R. V., & Hong, Y. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a027938 · Cited by 35
Multispecificity of Immunoglobulin M Antibodies Raised against Advanced Glycation End Products
Chikazawa, M., Otaki, N., Shibata, T., Miyashita, H., Kawai, Y., Maruyama, S., Toyokuni, S., Kitaura, Y., Matsuda, T., & Uchida, K. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.452177 · Cited by 34
Barceló, C., Paco, N., Beckett, A. J., Alvarez-Moya, B., Garrido, E., Gelabert, M., Tebar, F., Jaumot, M., Prior, I. A., & Agell, N. (2013) · Journal of Cell Science · doi:10.1242/jcs.123737 · Cited by 34
Na+–H+ exchanger-1 (NHE1) regulation in kidney proximal tubule
Parker, M. D., Myers, E. J., & Schelling, J. R. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1848-8 · Cited by 33
Eisenberg, S., Giehl, K., Henis, Y. I., & Ehrlich, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804589200 · Cited by 33
Basic Motifs Target PSGL-1, CD43, and CD44 to Plasma Membrane Sites Where HIV-1 Assembles
Grover, J. R., Veatch, S. L., & Ono, A. (2014) · Journal of Virology · doi:10.1128/jvi.02178-14 · Cited by 32
Carr, H. S., Morris, C. A., Menon, S. G., Song, E. H., & Frost, J. A. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00980-12 · Cited by 32
Investigation of the Lipid Binding Properties of the Marburg Virus Matrix Protein VP40
Wijesinghe, K. J., & Stahelin, R. V. (2015) · Journal of Virology · doi:10.1128/jvi.02607-15 · Cited by 29
Deen, A. J., Rilla, K. J., Oikari, S., Kärnä, R., Bart, G., Häyrinen, J., Bathina, A. R., Ropponen, A., Makkonen, K. M., Tammi, R., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.552133 · Cited by 31
RAS Function in cancer cells: translating membrane biology and biochemistry into new therapeutics
Kattan, W. E., & Hancock, J. F. (2020) · Biochemical Journal · doi:10.1042/bcj20190839 · Cited by 33
Influenza A M2 recruits M1 to the plasma membrane: A fluorescence fluctuation microscopy study
Petrich, A., Dunsing, V., Bobone, S., & Chiantia, S. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.11.023 · Cited by 31
Hormonal Regulation of Nuclear Permeability
O’Brien, E., Gomes, D. A., Sehgal, S., & Nathanson, M. H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606300200 · Cited by 31
Monreal, J. A., McLoughlin, F., Echevarrı́a, C., García‐Mauriño, S., & Testerink, C. S. (2009) · PLANT PHYSIOLOGY · doi:10.1104/pp.109.150326 · Cited by 31
A lipid perspective on regulated cell death
Flores‐Romero, H., Ros, U., & García‐Sáez, A. J. (2019) · International review of cytology · doi:10.1016/bs.ircmb.2019.11.004 · Cited by 32
Roles of palmitoylation and the KIKK membrane-targeting motif in leukemogenesis by oncogenic KRAS4A
Zhao, H., Liu, P., Zhang, R., Wu, M. H., Li, D., Zhao, X., Zhang, C., Jiao, B., Chen, B., Chen, Z., et al. (2015) · Journal of Hematology & Oncology · doi:10.1186/s13045-015-0226-1 · Cited by 30
Electrical properties of plasma membrane modulate subcellular distribution of K‐Ras
Gomez, G. A., & Daniotti, J. L. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05758.x · Cited by 29
Rac1 and Calmodulin Interactions Modulate Dynamics of ARF6‐Dependent Endocytosis
Vidal‐Quadras, M., Gelabert‐Baldrich, M., Soriano‐Castell, D., Lladó, A., Rentero, C., Calvo, M., Pol, A., Enrich, C., & Tebar, F. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01274.x · Cited by 28
Cailleteau, L., Estrach, S., Thyss, R., Boyer, L., Doye, A., Domange, B., Johnsson, N., Rubinstein, E., Boucheix, C., Ebrahimian, T. G., et al. (2010) · Journal of Cell Science · doi:10.1242/jcs.058875 · Cited by 28
Nakamura, A., Oki, C., Kato, K., Fujinuma, S., Maryu, G., Kuwata, K., Yoshii, T., Matsuda, M., Aoki, K., & Tsukiji, S. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00024 · Cited by 27
Nwogu, N., Ortiz, L. E., & Kwun, H. J. (2020) · Oncogenesis · doi:10.1038/s41389-020-0235-y · Cited by 28
A dynamic partitioning mechanism polarizes membrane protein distribution
Banerjee, T., Matsuoka, S., Biswas, D., Miao, Y., Pal, D. S., Kamimura, Y., Ueda, M., Devreotes, P. N., & Iglesias, P. A. (2023) · Nature Communications · doi:10.1038/s41467-023-43615-2 · Cited by 28
CaM interaction and Ser181 phosphorylation as new K-Ras signaling modulators
Alvarez-Moya, B., Barceló, C., Tebar, F., Jaumot, M., & Agell, N. (2011) · Small GTPases · doi:10.4161/sgtp.2.2.15555 · Cited by 28
Endocytosis and the internalization of pathogenic organisms: focus on phosphoinositides
Walpole, G. F. W., & Grinstein, S. (2020) · F1000Research · doi:10.12688/f1000research.22393.1 · Cited by 26
Self-citationWawrzyniak, A. M., Vermeiren, E., Zimmermann, P., & Ivarsson, Y. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.04.024 · Cited by 27
Fuzzy Association of an Intrinsically Disordered Protein with Acidic Membranes
Hicks, A., Escobar, C. A., Cross, T. A., & Zhou, H. (2020) · JACS Au · doi:10.1021/jacsau.0c00039 · Cited by 24
Macrophage reprogramming by negatively charged membrane phospholipids controls infection
Cauvi, D. M., Hawisher, D., Dores-Silva, P. R., Lizardo, R. E., & Maio, A. D. (2018) · The FASEB Journal · doi:10.1096/fj.201801579r · Cited by 25
A Network-based Analysis of Polyanion-binding Proteins Utilizing Human Protein Arrays
Salamat‐Miller, N., Fang, J., Seidel, C. W., Assenov, Y., Albrecht, M., & Middaugh, C. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610957200 · Cited by 25
CD31 delays phagocyte membrane repolarization to promote efficient binding of apoptotic cells
Vernon-Wilson, E. F., Aurade, F., Tian, L., Rowe, I. C. M., Shipston, M. J., Savill, J., & Brown, S. B. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0507283 · Cited by 25
Connolly, A., Panès, R., Tual, M., Lafortune, R., Bellemare‐Pelletier, A., & Gagnon, É. (2021) · Science Signaling · doi:10.1126/scisignal.abb5146 · Cited by 25
The promise of probiotics in honeybee health and disease management
Abdi, K., Saïd, M. B., Crotti, E., Masmoudi, A. S., & Cherif, A. (2023) · Archives of Microbiology · doi:10.1007/s00203-023-03416-z · Cited by 25
Faure, M.-C., Sulpice, J., Delattre, M., Lavielle, M., Prigent, M., Cuif, M., Melchior, C., Tschirhart, E. J., Nüße, O., & Dupré‐Crochet, S. (2013) · Biology of the Cell · doi:10.1111/boc.201300010 · Cited by 24
Electric Fields and Inflammation: May the Force be with You
Brown, S. B., & Dransfield, I. (2008) · The Scientific World JOURNAL · doi:10.1100/tsw.2008.158 · Cited by 24
Cytoskeletal confinement of CX3CL1 limits its susceptibility to proteolytic cleavage by ADAM10
Wong, H. S., Jaumouillé, V., Heit, B., Doodnauth, S. A., Patel, S., Huang, Y., Grinstein, S., & Robinson, L. A. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-11-0633 · Cited by 27
Self-citationEffects of Membrane Charge and Order on Membrane Binding of the Retroviral Structural Protein Gag
Wen, Y., Dick, R. A., Feigenson, G. W., & Vogt, V. M. (2016) · Journal of Virology · doi:10.1128/jvi.01102-16 · Cited by 23
Attractive membrane domains control lateral diffusion
Forstner, M. B., Martin, D. S., Rückerl, F., Käs, J. A., & Selle, C. (2008) · Physical Review E · doi:10.1103/physreve.77.051906 · Cited by 24
GTPases Rac1 and Ras Signaling from Endosomes
Tebar, F., Enrich, C., Rentero, C., & Grewal, T. (2018) · Progress in molecular and subcellular biology · doi:10.1007/978-3-319-96704-2_3 · Cited by 26
Wu, N., Song, H., & Veillette, A. (2021) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-00600-9 · Cited by 23
A chemogenetic platform for controlling plasma membrane signaling and synthetic signal oscillation
Suzuki, S., Nakamura, A., Hatano, Y., Yoshikawa, M., Yoshii, T., Sawada, S., Atsuta‐Tsunoda, K., Aoki, K., & Tsukiji, S. (2022) · Cell chemical biology · doi:10.1016/j.chembiol.2022.06.005 · Cited by 23
Uchida, N., Ryu, Y., Takagi, Y., Yoshizawa, K., Suzuki, K., Anraku, Y., Ajioka, I., Shimokawa, N., Takagi, M., Hoshino, N., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c12348 · Cited by 23
Yu, D.-N., Ruan, P., Meng, Z., & Zhou, J. (2015) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.24491 · Cited by 23
Al-Momany, A., Li, L., Alexander, R. T., & Ballermann, B. J. (2014) · Journal of Cell Science · doi:10.1242/jcs.147744 · Cited by 25
Han, X., Yu, R., Ji, L., Zhen, D., Tao, S., Li, S., Sun, Y., Huang, L., Feng, Z., Li, X., et al. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07726.x · Cited by 23
Metadata
- Authors
- Yeung, T., Terebiznik, M., Yu, L., Silvius, J., Abidi, W. M., Philips, M., Levine, T., Kapus, A., & Grinstein, S.
- Affiliations
- University of Toronto (CA)
- Division of Cell Biology, Hepatology, and Nutrition Department, Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada.
- Corresponding author
- Grinstein, Sergio
- ORCID
- Venue
- Science
- Published
- 2006-07-21
- Volume
- 313
- Issue
- 5785
- Pages
- 347-351
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1999972891
- Cited by
- 329
- References
- 9
- Citations by year
- 2026: 4 · 2025: 10 · 2024: 16 · 2023: 15 · 2022: 10 · 2021: 15 · 2020: 17 · 2019: 8 · 2018: 8 · 2017: 11 · 2016: 9 · 2015: 15 · 2014: 13 · 2013: 17 · 2012: 22
- FWCI
- 10.59
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
- Keywords
- membrane surface potential, phagocytosis, macrophages, plasma membrane, phosphoinositide hydrolysis, phosphatidylserine exposure, lipid remodeling, genetically encoded probes, KRAS, Rac1, Src kinase, lipid rafts, receptor activation
- MeSH terms
- Animals, Calcium, Cell Line, Cell Membrane, Fluorescent Dyes, Immunoglobulin G, Lipid Bilayers, Liposomes, Macrophages, Membrane Potentials, Neuropeptides, Opsonin Proteins, Peptides, Phagocytosis, Phagosomes, Phospholipids, Receptors, Fc, Molecular Probes, Ionomycin, ras Proteins, rac GTP-Binding Proteins, rac1 GTP-Binding Protein, Mice, Static Electricity, Hydrophobic and Hydrophilic Interactions
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review