The DOI matches its Crossref record; 61 of the 62 references it cites were found in a registry or an index.
Sprouty, an Intracellular Inhibitor of Ras Signaling
Open accessAbstract
Sprouty was identified in a genetic screen as an inhibitor of Drosophila EGF receptor signaling. The Egfr triggers cell recruitment in the eye, and sprouty- eyes have excess photoreceptors, cone cells, and pigment cells. Sprouty's function is, however, more widespread. We show that it also interacts genetically with the receptor tyrosine kinases Torso and Sevenless, and it was first discovered through its effect on FGF receptor signaling. In contrast to an earlier proposal that Sprouty is extracellular, we show by biochemical analysis that Sprouty is an intracellular protein, associated with the inner surface of the plasma membrane. Sprouty binds to two intracellular components of the Ras pathway, Drk and Gap1. Our results indicate that Sprouty is a widespread inhibitor of Ras pathway signal transduction.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Four of the validated miR-21 target genes are known negative regulators of the Ras/MEK/ERK pathway: sprouty 1 (Spry1), sprouty 2 (Spry2), B-cell translocation gene 2 (Btg2), and programmed cell death 4 (Pdcd4).”
From Modulation of K-Ras-Dependent Lung Tumorigenesis by MicroRNA-21 (2010) · cites this paper as Casci et al., 1999
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
Brand, A. H., & Perrimon, N. (1993) · Development · doi:10.1242/dev.118.2.401 · Cited by 9,510
Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
Nielsen, H., Engelbrecht, J., Brunak, S., & von HEIJNE, G. (1997) · Protein Engineering Design and Selection · doi:10.1093/protein/10.1.1 · Cited by 5,343
Analysis of genetic mosaics in developing and adult Drosophila tissues
Xu, T., & Rubin, G. M. (1993) · Development · doi:10.1242/dev.117.4.1223 · Cited by 2,066
The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
Lowenstein, E. J., Daly, R. J., Batzer, A., Li, W., Margolis, B. L., Lammers, R., Ullrich, A., Skolnik, E. Y., Bar‐Sagi, D., & Schlessinger, J. (1992) · Cell · doi:10.1016/0092-8674(92)90167-b · Cited by 1,632
A new member of the frizzled family from Drosophila functions as a Wingless receptor
Bhanot, P., van den Brink, M. R. M., Samos, C. H., Hsieh, J.-C., Wang, Y., Macke, J. P., Andrew, D. J., Nathans, J., & Nusse, R. (1996) · Nature · doi:10.1038/382225a0 · Cited by 1,504
Buday, L., & Downward, J. (1993) · Cell · doi:10.1016/0092-8674(93)90146-h · Cited by 1,064
Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
Leevers, S. J., Paterson, H. F., & Marshall, C. J. (1994) · Nature · doi:10.1038/369411a0 · Cited by 1,011
Activation of Raf as a Result of Recruitment to the Plasma Membrane
Stokoe, D., Macdonald, S. G., Cadwallader, K. A., Symons, M. H., & Hancock, J. F. (1994) · Science · doi:10.1126/science.7811320 · Cited by 976
Reiterative Use of the EGF Receptor Triggers Differentiation of All Cell Types in the Drosophila Eye
Freeman, M. (1996) · Cell · doi:10.1016/s0092-8674(00)81385-9 · Cited by 877
Self-citationSimon, M. A., Bowtell, D. D. L., Dodson, G. S., Laverty, T., & Rubin, G. M. (1991) · Cell · doi:10.1016/0092-8674(91)90065-7 · Cited by 860
Cited by
Sorted by citations
Items 301–400 of 468
A Functional Domain of Dof That Is Required for Fibroblast Growth Factor Signaling
Wilson, R. J., Battersby, A., Csiszár, Á., Vogelsang, E., & Leptin, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.6.2263-2276.2004 · Cited by 21
Wang, Y., Werz, C., Xu, D., Chen, Z., Li, Y., Hafen, E., & Bergmann, A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001447 · Cited by 20
Sprouty gain of function disrupts lens cellular processes and growth by restricting RTK signaling
Shin, E. H. H., Zhao, G., Wang, Q., & Lovicu, F. J. (2015) · Developmental Biology · doi:10.1016/j.ydbio.2015.09.005 · Cited by 19
Regulation of EGFR and Notch signaling by distinct isoforms of D-cbl during Drosophila development
Wang, Y., Chen, Z., & Bergmann, A. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.03.005 · Cited by 19
Yang, X., Gong, Y., & Friesel, R. E. (2012) · PLoS ONE · doi:10.1371/annotation/eb3485a7-612b-4244-8d2a-43a80cdd15eb · Cited by 19
Activation of Unfolded Protein Response in Transgenic Mouse Lenses
Reneker, L. W., Chen, H., & Overbeek, P. A. (2011) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.10-5650 · Cited by 17
Arafeh, R., Flores, K., Keren‐Paz, A., Maik-Rachline, G., Gutkind, N. E., Rosenberg, S. A., Seger, R., & Samuels, Y. (2017) · Scientific Reports · doi:10.1038/s41598-017-16558-0 · Cited by 18
Recruitment of Sprouty1 to Immune Synapse Regulates T Cell Receptor Signaling
Lee, J. S., Lee, J., Oh, Y. M., Park, J. B., Choi, H., Choi, C. Y., Kim, I.-H., Lee, S. H., & Choi, K. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803799 · Cited by 18
Incidence of P53 and K‐ras alterations in ovarian mucinous and serous tumors
Morita, K., Ono, Y., Fukui, H., Tomita, S., Ueda, Y., Terano, A., & Fujimori, T. (2000) · Pathology International · doi:10.1046/j.1440-1827.2000.01028.x · Cited by 18
A fly's eye view of EGF receptor signalling
Freeman, M. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf679 · Cited by 18
Self-citationForbes, A. J., & Lehmannt, R. (1999) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(99)80072-0 · Cited by 18
Role of SPRY4 in health and disease
Pan, H., Xu, R., & Zhang, Y. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1376873 · Cited by 17
Astroglial transcriptome dysregulation in early disease of an ALS mutant SOD1 mouse model
Miller, S., Zhang, P.-W., Glatzer, J. C., & Rothstein, J. D. (2016) · Journal of Neurogenetics · doi:10.1080/01677063.2016.1260128 · Cited by 18
Eve-3: A liver enriched suppressor of Ras/MAPK signaling
King, J. A. J., Corcoran, N. M., D’Abaco, G. M., Straffon, A. F. L., Smith, C. T., Poon, C. L. C., Büchert, M., Stacey, I., Hall, N. E., Lock, P., et al. (2005) · Journal of Hepatology · doi:10.1016/j.jhep.2005.10.031 · Cited by 17
Firth, L. C., Manchester, J., Lorenzen, J. A., Baron, M., & Perkins, L. A. (2000) · Genetics · doi:10.1093/genetics/156.2.733 · Cited by 17
Airway patterning: A paradigm for restricted signalling
Placzek, M., & Skaer, H. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80322-4 · Cited by 17
Genetic analysis of vein function in the Drosophila embryonic nervous system
Lanoue, B. R., Gordon, M. D., Battye, R., & Jacobs, J. R. (2000) · Genome · doi:10.1139/g00-014 · Cited by 17
FGF signaling acts on different levels of mesoderm development within Spiralia
Andrikou, C., & Hejnol, A. (2021) · Development · doi:10.1242/dev.196089 · Cited by 15
Mood, K., Friesel, R. E., & Daar, I. O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203894200 · Cited by 16
Abrell, S., Carrera, P., & Jäckle, H. (2000) · Chromosoma · doi:10.1007/s004120000092 · Cited by 16
Signaling by the Drosophila epidermal growth factor receptor pathway during development
Shilo, B. (2003) · Elsevier eBooks · doi:10.1016/b978-012160281-9/50013-x · Cited by 16
Functional and Comparative Genomic Analysis of the Piebald Deletion Region of Mouse Chromosome 14
Peterson, K. A., King, B. L., Hagge-Greenberg, A., Roix, J. J., Bult, C. J., & O’Brien, T. P. (2002) · Genomics · doi:10.1006/geno.2002.6818 · Cited by 16
Human Sprouty1 suppresses growth, migration, and invasion in human breast cancer cells
Mekkawy, A. H., Pourgholami, M. H., & Morris, D. L. (2014) · Tumor Biology · doi:10.1007/s13277-014-1665-y · Cited by 15
Sprouty2 regulates positioning of retinal progenitors through suppressing the Ras/Raf/MAPK pathway
Sun, J., Yoon, J., Lee, M., Hwang, Y., & Daar, I. O. (2020) · Scientific Reports · doi:10.1038/s41598-020-70670-2 · Cited by 15
Susanto, A., Zhao, G., Wazin, F., Feng, Y., Rasko, J. E. J., Bailey, C. G., & Lovicu, F. J. (2018) · Experimental Eye Research · doi:10.1016/j.exer.2018.09.019 · Cited by 15
Sprouty2 Interacts with Protein Kinase Cδ and Disrupts Phosphorylation of Protein Kinase D1
Chow, S. Y., Yu, C. Y., & Guy, G. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.021600 · Cited by 15
Generation of distinct signaling modes via diversification of the Egfr ligand-processing cassette
Rousso, T., Lynch, J., Yogev, S., Roth, S., Schejter, E. D., & Shilo, B. (2010) · Development · doi:10.1242/dev.049858 · Cited by 15
Davidson, B. P., Cheng, L. Y., Kinder, S. J., & Tam, P. (2000) · Developmental Biology · doi:10.1006/dbio.2000.9663 · Cited by 15
SPRED proteins provide a NF-ty link to Ras suppressionPreprint
McClatchey, A. I., & Cichowski, K. M. (2012) · Genes & Development · doi:10.1101/gad.197434.112 · Cited by 15
Liu, Z., Liu, X., Cao, W., & Hua, Z. (2015) · Europe PMC (PubMed Central) · Cited by 14
How Genetics Has Helped Piece Together the MAPK Signaling Pathway
Ashton‐Beaucage, D., & Therrien, M. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6424-6_1 · Cited by 15
Martin-Bermudo, M. D., Bardet, P., Bellaı̈che, Y., & Malartre, M. (2015) · Development · doi:10.1242/dev.110585 · Cited by 14
Targeted gain-of-function screening inDrosophilausingGAL4-UASand random transposon insertions
Zhong, J., & Yedvobnick, B. (2009) · Genetics Research · doi:10.1017/s0016672309990152 · Cited by 14
Cell‐type specific utilization of multiple negative feedback loops generates developmental constancy
Iwanami, M., Hiromi, Y., & Okabe, M. (2005) · Genes to Cells · doi:10.1111/j.1365-2443.2005.00871.x · Cited by 14
Sprouty keeps bowel kinases regular in colon cancer, while miR-21 targets Sprouty
Frey, M. R., Carraro, G., Batra, R. K., Polk, D. B., & Warburton, D. (2011) · Cancer Biology & Therapy · doi:10.4161/cbt.11.1.14176 · Cited by 13
In non‐small cell lung cancer mitogenic signaling leaves Sprouty1 protein levels unaffected
Kral, R. M., Mayer, C., Vanas, V., Gsur, A., & Sutterlüty, H. (2013) · Cell Biochemistry and Function · doi:10.1002/cbf.2976 · Cited by 13
Taketomi, T., Onimura, T., Yoshiga, D., Muratsu, D., Sanui, T., Fukuda, T., Kusukawa, J., & Nakamura, S. (2017) · Cell Biology International · doi:10.1002/cbin.10876 · Cited by 13
Komisarczuk, A. Z., Topp, S., Stigloher, C., Kapsimali, M., Bally‐Cuif, L., & Becker, T. S. (2008) · Developmental Dynamics · doi:10.1002/dvdy.21689 · Cited by 13
Spry1 as a novel regulator of erythropoiesis, EPO/EPOR target, and suppressor of JAK2
Sathyanarayana, P., Dev, A., Pradeep, A., Ufkin, M. L., Licht, J. D., & Wojchowski, D. M. (2012) · Blood · doi:10.1182/blood-2011-11-392571 · Cited by 13
Frazzetto, G., Klingbeil, P., & Bouwmeester, T. (2002) · Mechanisms of Development · doi:10.1016/s0925-4773(01)00664-5 · Cited by 13
Transport and gradient formation of Wnt and Fgf in the early zebrafish gastrula
Cooper, E. J., & Scholpp, S. (2023) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2023.12.003 · Cited by 12
Negative regulation of lens fiber cell differentiation by RTK antagonists Spry and Spred
Zhao, G., Bailey, C. G., Feng, Y., Rasko, J. E. J., & Lovicu, F. J. (2018) · Experimental Eye Research · doi:10.1016/j.exer.2018.02.025 · Cited by 12
Developmental roles of Rhomboid proteases
Shilo, B. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.07.014 · Cited by 12
Li-Villarreal, N., Wong, R. L. Y., Garcia, M. D., Udan, R. S., Poché, R. A., Rasmussen, T. L., Rhyner, A. M., Wythe, J. D., & Dickinson, M. E. (2022) · Development · doi:10.1242/dev.200131 · Cited by 11
Sprouty2 Regulates PI(4,5)P2/Ca2+ Signaling and HIV-1 Gag Release
Ehrlich, L. S., Medina, G. N., & Carter, C. A. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.069 · Cited by 11
So, W., Cheng, J., Fan, Q., Wong, A. S. T., Huntsman, D. D., Gilks, C. B., & Leung, P. C. K. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.12.012 · Cited by 11
siRNA mediated down-regulation of Sprouty2/4 diminishes ischemic brain injury
Klimaschewski, L. P., Sueiro, B. P., & Millán, L. M. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.11.050 · Cited by 11
Sprouty2 expression controls endothelial monolayer integrity and quiescence
Peier, M., Walpen, T., Christofori, G., Battegay, E., & Humar, R. (2012) · Angiogenesis · doi:10.1007/s10456-012-9330-9 · Cited by 11
Gao, X., Hicks, K. C., Neumann, P. H., & Patel, T. B. (2017) · PLoS ONE · doi:10.1371/journal.pone.0171616 · Cited by 11
Leevers, S. J. (1999) · Nature Cell Biology · doi:10.1038/8960 · Cited by 11
Hashimoto, S., Nakano, H., Suguta, Y., Irie, S., Jianhua, L., & Katyal, S. L. (2012) · Pathobiology · doi:10.1159/000334839 · Cited by 10
Molecular mechanisms underlying cellular effects of human MEK1 mutations
Marmion, R. A., Yang, L., Goyal, Y., Jindal, G. A., Wetzel, J. L., Singh, M., Schüpbach, T., & Shvartsman, S. Y. (2021) · Molecular Biology of the Cell · doi:10.1091/mbc.e20-10-0625 · Cited by 10
Brock, E. J., Jackson, R. M., Boerner, J. L., Li, Q., Tennis, M. A., Sloane, B. F., & Mattingly, R. R. (2021) · PLoS ONE · doi:10.1371/journal.pone.0252314 · Cited by 10
Yang, X., Gong, Y. Q., & Friesel, R. E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018374 · Cited by 10
Ding, W., & Warburton, D. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.08.037 · Cited by 10
Yawut, N., Kaewpiboon, C., Budluang, P., Cho, I.-R., Kaowinn, S., Koh, S. S., & Chung, Y.-H. (2020) · Cancer Management and Research · doi:10.2147/cmar.s271109 · Cited by 9
Chitra, E., Lin, Y., Davamani, F. A., Hsiao, K.-N., Sia, C., Hsieh, S.-Y., Wei, O. L., Chen, J., & Chow, Y. (2010) · Retrovirology · doi:10.1186/1742-4690-7-62 · Cited by 9
Sesé, M., Corominas, M., Stocker, H., Heino, T. I., Hafen, E., & Serras, F. (2006) · Journal of Cell Science · doi:10.1242/jcs.03294 · Cited by 9
Sheng, Z., & Du, W. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1008863 · Cited by 8
Li, S., Zhao, S., Liang, N., Zhang, S., Zhang, L., Zhou, L., Liu, A., Cao, X., Tian, J., Yu, Y., et al. (2023) · Gastric Cancer · doi:10.1007/s10120-023-01402-4 · Cited by 8
Sex specific gene expression is present prior to metamorphosis in the sea urchin
Pieplow, C. A., Furze, A. R., Gregory, P., Oulhen, N., & Wessel, G. M. (2024) · Developmental Biology · doi:10.1016/j.ydbio.2024.10.003 · Cited by 8
Rojas, J. M., & Santos, E. (2006) · Springer eBooks · doi:10.1007/1-4020-4708-8_2 · Cited by 8
SUKHANOVA, M. J., Steele, L. J., Zhang, T., Gordon, G. M., & Du, W. (2011) · Developmental Biology · doi:10.1016/j.ydbio.2011.08.018 · Cited by 8
Future Aspects of Tumor Suppressor Gene
Cheng, Y. (2013) · InTech eBooks · doi:10.5772/56471 · Cited by 8
Rapacioli, M., Palma, V., & Flores, V. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00067 · Cited by 8
Selland, L. G., Koch, S., Laraque, M., & Waskiewicz, A. J. (2018) · Mechanisms of Development · doi:10.1016/j.mod.2018.02.005 · Cited by 8
Modulation of Mosquito Immune Defenses as a Control Strategy
Rhodes, V. L. M., & Michel, K. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805350-8.00004-0 · Cited by 8
Argos Mutants Define an Affinity Threshold for Spitz Inhibition in Vivo
Alvarado, D., Evans, T. A., Sharma, R., Lemmon, M. A., & Duffy, J. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603782200 · Cited by 8
Namini, M. T., Bhagya, G., & Sharma, M. (2025) · Aspects of Molecular Medicine · doi:10.1016/j.amolm.2025.100073 · Cited by 7
Assinder, S. J., Beniamen, D., & Lovicu, F. J. (2015) · BioMed Research International · doi:10.1155/2015/827462 · Cited by 7
The negative regulatory Spred1 and Spred2 proteins are required for lens and eye morphogenesis
Wazin, F., & Lovicu, F. J. (2020) · Experimental Eye Research · doi:10.1016/j.exer.2020.107917 · Cited by 7
Current challenges to underpinning the genetic basis for cholangiocarcinoma
Cigliano, A., Chen, X., & Calvisi, D. F. (2021) · Expert Review of Gastroenterology & Hepatology · doi:10.1080/17474124.2021.1915128 · Cited by 9
Regulator of Epidermal Growth Factor Signaling: Sprouty
Wong, E. S. M., & Guy, G. R. (2006) · Humana Press eBooks · doi:10.1385/1-59745-012-x:61 · Cited by 7
Mutations Modulating the Argos-Regulated Signaling Pathway in Drosophila Eye Development
Taguchi, A., Sawamoto, K., & Okano, H. (2000) · Genetics · doi:10.1093/genetics/154.4.1639 · Cited by 7
Zhang, Y., & Woude, G. F. V. (2013) · InTech eBooks · doi:10.5772/54393 · Cited by 8
Human Sprouty1 Suppresses Urokinase Receptor-Stimulated Cell Migration and Invasion
Mekkawy, A. H., & Morris, D. L. (2013) · ISRN Biochemistry · doi:10.1155/2013/598251 · Cited by 6
Beatty, J. S., Molnar, C., Luque, C. M., de Celis, J. F., & Martin-Bermudo, M. D. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009738 · Cited by 6
Li, N., Chen, Y., Wang, H., Li, J., & Zhao, R. C. (2022) · Adipocyte · doi:10.1080/21623945.2022.2123097 · Cited by 6
Cui, Y.-Z., Xu, F., Zhou, Y., Wang, Z., Yang, X.-Y., Fu, N.-C., Chen, X., Zheng, Y., Chen, X., Ye, L., et al. (2024) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2024.02.018 · Cited by 6
García-Domínguez, C. A., Martinez, N. J., Gragera, T., Pérez-Rodríguez, A., Retana, D., León‐Espinosa, G., Sánchez, A., Oliva, J. L., Pérez‐Sala, D., & Rojas, J. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016787 · Cited by 6
Zaremba, A., Schmuecker, U., & Esche, H. (2011) · Virology Journal · doi:10.1186/1743-422x-8-192 · Cited by 6
Wu, H., Wu, H., Li, H., Wu, H., Li, H., & Guo, J. (2008) · Brain Injury · doi:10.1080/02699050801911295 · Cited by 6
Wazin, F., & Lovicu, F. J. (2024) · Cells · doi:10.3390/cells13040290 · Cited by 5
Hausott, B., Pircher, L., Kind, M., Park, J., Claus, P., Obexer, P., & Klimaschewski, L. P. (2024) · Cells · doi:10.3390/cells13231967 · Cited by 5
Immunolocalization of Sprouty-1 and Sprouty-2 in Developing Rat Lung
Hashimoto, S., Nakano, H., Suguta, Y., Singh, G., & Katyal, S. L. (2012) · Pathobiology · doi:10.1159/000332215 · Cited by 5
Lievens, P., Zanolli, E., Garofalo, S., & Liboi, E. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.09.021 · Cited by 5
Gao, C., & Woude, G. F. V. (2015) · Springer eBooks · doi:10.1007/978-3-319-11888-8_8 · Cited by 5
Cardiovascular Genomics: A Current Overview of In Vivo and In Vitro Studies
Mariappan, D., Winkler, J., Hescheler, J., & Sachinidis, A. (2006) · Stem Cell Reviews and Reports · doi:10.1007/s12015-006-0010-2 · Cited by 5
Pasnuri, N., Jaiswal, M., Ray, K., & Mazumder, A. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1010622 · Cited by 3
Regulation of EGF Receptor Signaling in the Fruitfly D. melanogaster and the Nematode C. elegans
Lacenere, C. J., & Sternberg, P. W. (2000) · Breast Disease · doi:10.3233/bd-1999-11103 · Cited by 4
McKay, J. P., Nightingale, B. S., & Pollock, J. A. (2008) · Journal of Neurogenetics · doi:10.1080/01677060801893276 · Cited by 4
Dansereau, D. A., Mckearin, D. M., & Lasko, P. F. (2005) · Elsevier eBooks · doi:10.1016/b0-44-451924-6/00013-2 · Cited by 4
Signal Transduction Pathway for Anterior-Posterior Development in Drosophila
Baek, K., & Lee, K. (1999) · Journal of Biomedical Science · doi:10.1007/bf02253520 · Cited by 4
EGF Receptor Signaling: A Prickly Proposition
Firth, L. C., & Baker, N. E. (2003) · Current Biology · doi:10.1016/j.cub.2003.09.020 · Cited by 4
Sprouty and Cerberus proteins in urogenital system development
Chi, L. (2007) · Cited by 4
Genolet, O., Monaco, A. A., Dunkel, I., Boettcher, M., & Schulz, E. G. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.09.983544 · Cited by 4
Barraud, P., He, X., Zhao, C., Caldwell, M. A., & Franklin, R. J. M. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.03.001 · Cited by 3
EGFR signaling modulates synaptic connectivity via Gurken
Naylor, S. A., & DiAntonio, A. (2011) · Developmental Neurobiology · doi:10.1002/dneu.20992 · Cited by 3
CrkL is a novel target of Sprouty2 in fibroblast growth factor signaling
Satoh, T., Torii, S., Nakayama, K., & Nishida, E. (2010) · Genes to Cells · doi:10.1111/j.1365-2443.2009.01373.x · Cited by 3
Tracheal System Development and Morphogenesis
Uv, A., & Samakovlis, C. (2005) · Elsevier eBooks · doi:10.1016/b0-44-451924-6/00020-x · Cited by 3
Metadata
- Authors
- Casci, T., Vinós, J., & Freeman, M.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Freeman, Matthew
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1999-03
- Volume
- 96
- Issue
- 5
- Pages
- 655-665
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2082773871
- Cited by
- 467
- References
- 62
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 5 · 2023: 8 · 2022: 8 · 2021: 13 · 2020: 13 · 2019: 4 · 2018: 10 · 2017: 11 · 2016: 19 · 2015: 16 · 2014: 12 · 2013: 15 · 2012: 17
- FWCI
- 10.93
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Keywords
- Sprouty, Ras signaling, EGF receptor signaling, Drosophila, Torso receptor, FGF receptor signaling, DRK, GAP1, receptor tyrosine kinase, pigment cells, plasma membrane
- MeSH terms
- Animals, Cells, Cultured, Cysteine, Depression, Chemical, Drosophila melanogaster, Eye, Eye Abnormalities, Eye Proteins, Membrane Glycoproteins, Membrane Proteins, Morphogenesis, Proteins, Signal Transduction, ras Proteins, Insect Proteins, ras GTPase-Activating Proteins, Receptor Protein-Tyrosine Kinases, Drosophila Proteins, Macromolecular Substances, ErbB Receptors
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