The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras.
Open accessAbstract
Protein-tyrosine-phosphatase SHPTP2 (Syp/PTP-1D/PTP2C) is the homologue of the Drosophila corkscrew (csw) gene product, which transmits positive signals from receptor tyrosine kinases. Likewise, SHPTP2 has been implicated in positive signaling from platelet-derived growth factor receptor beta (PDGFR). Upon PDGF stimulation, SHPTP2 binds to the PDGFR and becomes tyrosine-phosphorylated. We have identified tyrosine-542 (pY542TNI) as the major in vivo site of SHPTP2 tyrosine phosphorylation. The pY542TNI sequence conforms to the consensus binding site for the SH2 domain of Grb2, which, by association with Sos1, couples some growth factor receptors to Ras. Following PDGF stimulation, Grb2 binds tyrosine-phosphorylated SHPTP2. Moreover, a mutant PDGFR lacking its SHPTP2 binding site displays markedly reduced Grb2 binding. These data indicate that phosphorylation of SHPTP2 couples Grb2 to PDGFR in vivo, providing a mechanism for Ras activation by PDGFR and for positive signaling via SHPTP2 and Csw.
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
“SHP2 is required for full activation of SOS1/2, whereas SOS1 inhibitors are inactive against SOS2.”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [142]
In the citing paper
“which is recruited to many receptor tyrosine kinases upon activation and is generally a positive regulator of Ras/MAPK signaling (Perkins et al., 1996; Bennett et al., 1994; Tang et al., 1995; Maroun et al., 2000; Oishi et al., 2006).”
From The Phosphatase SHP2 Regulates the Spacing Effect for Long-Term Memory Induction (2009) · cites this paper as Bennett et al., 1994
Citations
Cites
Signal transduction by receptors with tyrosine kinase activity
Ullrich, A., & Schlessinger, J. (1990) · Cell · doi:10.1016/0092-8674(90)90801-k · Cited by 5,435
Gene Splicing by Overlap Extension: Tailor-Made Genes Using the Polymerase Chain Reaction
Horton, R. M., Cai, Z., Ho, S. N., & Pease, L. R. (2013) · BioTechniques · doi:10.2144/000114017 · Cited by 1,292
Egan, S. E., Giddings, B. W., Brooks, M. W., Buday, L., Sizeland, A. M., & Weinberg, R. A. (1993) · Nature · doi:10.1038/363045a0 · Cited by 1,200
[42] Detection and quantification of phosphotyrosine in proteins
Cooper, J. A., Sefton, B. M., & Hunter, T. R. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)99075-4 · Cited by 1,109
Buday, L., & Downward, J. (1993) · Cell · doi:10.1016/0092-8674(93)90146-h · Cited by 1,064
The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
Rozakis-Adcock, M., Fernley, R. T., Wade, J. D., Pawson, T. J., & Bowtell, D. D. L. (1993) · Nature · doi:10.1038/363083a0 · Cited by 1,009
Phosphatidylinositol 3′‐kinase is activated by association with IRS‐1 during insulin stimulation.
Backer, J., Myers, M. G., Shoelson, S. E., Chin, D. J., Sun, X., Miralpeix, M., Hu, P. J., Margolis, B. L., Skolnik, E. Y., & Schlessinger, J. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05426.x · Cited by 1,000
Rozakis-Adcock, M., McGlade, J. C., Mbamalu, G., Pelicci, G., Daly, R. J., Li, W., Batzer, A., Thomas, S. Μ., Brugge, J. S., Pelicci, P. G., et al. (1992) · Nature · doi:10.1038/360689a0 · Cited by 973
SH2 and SH3 domains: From structure to function
Pawson, T. J., & Gish, G. D. (1992) · Cell · doi:10.1016/0092-8674(92)90504-6 · Cited by 940
Li, N., Batzer, A., Daly, R. J., Yajnik, V., Skolnik, E. Y., Chardin, P., Bar‐Sagi, D., Margolis, B. L., & Schlessinger, J. (1993) · Nature · doi:10.1038/363085a0 · Cited by 938
Cited by
Sorted by citations
Protein modules and signalling networks
Pawson, T. (1995) · Nature · doi:10.1038/373573a0 · Cited by 2,420
Hyperactive Ras in developmental disorders and cancer
Schubbert, S., Shannon, K., & Bollag, G. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2109 · Cited by 1,583
RAS-targeted therapies: is the undruggable drugged?
Moore, A. R., Rosenberg, S. C., McCormick, F., & Malek, S. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0068-6 · Cited by 1,103
Stahl, N., Farruggella, T. J., Boulton, T. G., Zhong, Z., Darnell, J. E., & Yancopoulos, G. D. (1995) · Science · doi:10.1126/science.7871433 · Cited by 979
Proteogenomic Characterization Reveals Therapeutic Vulnerabilities in Lung Adenocarcinoma
Gillette, M. A., Satpathy, S., Cao, S., Dhanasekaran, S. M., Vasaikar, S. V., Krug, K., Petralia, F., Li, Y., Liang, W.-W., Reva, B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.013 · Cited by 820
Signal transduction via platelet-derived growth factor receptors
Heldin, C., Östman, A., & Rönnstrand, L. (1998) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(98)00015-8 · Cited by 747
A family of proteins that inhibit signalling through tyrosine kinase receptors
Kharitonenkov, A., Chen, Z., Sures, I., Wang, H., Schilling, J., & Ullrich, A. (1997) · Nature · doi:10.1038/386181a0 · Cited by 662
The PD1:PD-L1/2 Pathway from Discovery to Clinical Implementation
Bardhan, K., Anagnostou, T., & Boussiotis, V. A. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00550 · Cited by 606
Suppression of SHP-2 and ERK Signalling Promotes Self-Renewal of Mouse Embryonic Stem Cells
Burdon, T., Stracey, C., Chambers, I., Nichols, J., & Smith, A. G. (1999) · Developmental Biology · doi:10.1006/dbio.1999.9265 · Cited by 585
Platelet-derived growth factor receptor signals.
Claesson, L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31591-6 · Cited by 557
Fukada, T., Hibi, M., Yamanaka, Y., Takahashi-Tezuka, M., Fujitani, Y., Yamaguchi, T., Nakajima, K., & Hirano, T. (1996) · Immunity · doi:10.1016/s1074-7613(00)80501-4 · Cited by 652
The current state of the art and future trends in RAS-targeted cancer therapies
Punekar, S. R., Velcheti, V., Neel, B. G., & Wong, K.-K. (2022) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-022-00671-9 · Cited by 549
Self-citationEstrogen Regulation of Growth Hormone Action
Leung, K., Johannsson, G., Leong, G. M., & Ho, K. K. Y. (2004) · Endocrine Reviews · doi:10.1210/er.2003-0035 · Cited by 550
Role of oncogenic KRAS in the prognosis, diagnosis and treatment of colorectal cancer
Zhu, G., Pei, L., Xia, H., Tang, Q., & Bi, F. (2021) · Molecular Cancer · doi:10.1186/s12943-021-01441-4 · Cited by 482
Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp‐2
Saxton, T. M., Henkemeyer, M. J., Gasca, S., Shen, R., Rossi, D. J., Shalaby, F., Feng, G., & Pawson, T. J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.9.2352 · Cited by 482
Biology of the Interleukin-2 Receptor
Nelson, B. H., & Willerford, D. M. (1998) · Advances in immunology · doi:10.1016/s0065-2776(08)60386-7 · Cited by 475
Mitogenic signaling via G protein-coupled receptors
van BIESEN, T., LUTTRELL, L. M., HAWES, B. E., & LEFKOWITZ, R. J. (1996) · Endocrine Reviews · doi:10.1210/edrv-17-6-698 · Cited by 361
Krøll, J., & Waltenberger, J. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32521 · Cited by 431
Signal Transduction Pathways Mediated by PECAM-1
Newman, P. J., & Newman, D. K. (2003) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000071347.69358.d9 · Cited by 399
Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials
Xie, X., Yu, T., Li, X., Zhang, N., Foster, L. J., Peng, C., Huang, W., & He, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01589-z · Cited by 396
SHP‐1 and SHP‐2 in T cells: two phosphatases functioning at many levels
Lorenz, U. M. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00760.x · Cited by 390
Divergent Roles of SHP-2 in ERK Activation by Leptin Receptors
Bjørbæk, C., Buchholz, R. M., Davis, S. M., Bates, S. H., Pierroz, D. D., Gu, H., Neel, B. G., Myers, M. G., & Flier, J. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007439200 · Cited by 364
Self-citationThe molecular functions of Shp2 in the Ras/Mitogen-activated protein kinase (ERK1/2) pathway
Dance, M., Montagner, A., Salles, J.-P., Yart, A., & Raynal, P. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2007.10.002 · Cited by 361
Coupling of Gab1 to C-Met, Grb2, and Shp2 Mediates Biological Responses
Schaeper, U., Gehring, N. H., Fuchs, K. P., Sachs, M., Kempkes, B., & Birchmeier, W. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.7.1419 · Cited by 354
SHP2 inhibition prevents adaptive resistance to MEK inhibitors in multiple cancer models
Fedele, C., Ran, H., Diskin, B., Wei, W., Jen, J., Geer, M. J., Araki, K., Ozerdem, U., Simeone, D. M., Miller, G., et al. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-0444 · Cited by 315
Self-citationDehkhoda, F., Lee, C. M. M., Medina, J., & Brooks, A. J. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00035 · Cited by 304
NOONAN SYNDROME AND RELATED DISORDERS: Genetics and Pathogenesis
Tartaglia, M., & Gelb, B. D. (2005) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.6.080604.162305 · Cited by 355
Molecular analysis of the granulocyte colony-stimulating factor receptor
Avalos, B. (1996) · Blood · doi:10.1182/blood.v88.3.761.bloodjournal883761 · Cited by 293
The Cbl family proteins: Ring leaders in regulation of cell signaling
Swaminathan, G., & Tsygankov, A. Y. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20694 · Cited by 296
Maroun, C. R., Naujokas, M. A., Holgado-Madruga, M., Wong, A. J., & Park, M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.22.8513-8525.2000 · Cited by 286
Takahashi-Tezuka, M., Yoshida, Y., Fukada, T., Ohtani, T., Yamanaka, Y., Nishida, K., Nakajima, K., Hibi, M., & Hirano, T. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.4109 · Cited by 286
Potent Stimulation of SH-PTP2 Phosphatase Activity by Simultaneous Occupancy of Both SH2 Domains
Pluskey, S., Wandless, T. J., Walsh, C. T., & Shoelson, S. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.2897 · Cited by 285
Self-citationMohi, G., Williams, I. R., Dearolf, C. R., Chan, G., Kutok, J. L., Cohen, S. L., Morgan, K. J., Boulton, C. L., Shigematsu, H., Keilhack, H., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.01.010 · Cited by 276
Self-citationDamen, J. E., Wakao, H., Miyajima, A., Krošl, J., Humphries, R. K., Cutler, R. L., & Krystal, G. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00243.x · Cited by 275
Higashi, H., Nakaya, A., Tsutsumi, R., Yokoyama, K., Fujii, Y., Ishikawa, S., Higuchi, M., Takahashi, A., Kurashima, Y., Teishikata, Y., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309964200 · Cited by 273
Lu, W., Gong, D., Bar-Sagi, D., & Cole, P. A. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00369-0 · Cited by 268
Itoh, M., Yoshida, Y., Nishida, K., Narimatsu, M., Hibi, M., & Hirano, T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.10.3695-3704.2000 · Cited by 272
Zhang, J., Zhang, F., & Niu, R. (2015) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12618 · Cited by 253
An, H., Zhao, W., Hou, J., Zhang, Y., Xie, Y., Zheng, Y., Xu, H., Qian, C., Zhou, J., Yu, Y., et al. (2006) · Immunity · doi:10.1016/j.immuni.2006.10.014 · Cited by 244
Multiple Requirements for SHPTP2 in Epidermal Growth Factor-Mediated Cell Cycle Progression
Bennett, A. M., Hausdorff, S. F., O’Reilly, A. M., Freeman, R. M., & Neel, B. G. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.3.1189 · Cited by 246
Self-citationNishida, K., Yoshida, Y., Itoh, M., Fukada, T., Ohtani, T., Shirogane, T., Atsumi, T., Takahashi-Tezuka, M., Ishihara, K., Hibi, M., et al. (1999) · Blood · doi:10.1182/blood.v93.6.1809.406k35_1809_1816 · Cited by 239
SHP2 sails from physiology to pathology
Tajan, M., de Rocca Serra, A., Valet, P., Edouard, T., & Yart, A. (2015) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2015.08.005 · Cited by 232
Araki, T., Nawa, H., & Neel, B. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306461200 · Cited by 231
Self-citationShi, Z., Yu, D.-H., Park, M., Marshall, M. S., & Feng, G. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.5.1526-1536.2000 · Cited by 231
Ahmed, T. A., Adamopoulos, C., Karoulia, Z., Wu, X., Sachidanandam, R., Aaronson, S. A., & Poulikakos, P. I. (2019) · Cell Reports · doi:10.1016/j.celrep.2018.12.013 · Cited by 214
Molecular Reactions of Protein PhosphatasesInsights from Structure and Chemistry
Jackson, M. D., & Denu, J. M. (2001) · Chemical Reviews · doi:10.1021/cr000247e · Cited by 217
Jackson, D. E., Ward, C. M., Wang, R., & Newman, P. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.11.6986 · Cited by 212
Herbst, R., Carroll, P. M., Allard, J. D., Schilling, J., Raabe, T., & Simon, M. A. (1996) · Cell · doi:10.1016/s0092-8674(00)81273-8 · Cited by 209
Signaling by IL-31 and functional consequences
Cornelissen, C., Lüscher‐Firzlaff, J., Baron, J. M., & Lüscher, B. (2011) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2011.07.006 · Cited by 207
Nonreceptor Protein-Tyrosine Phosphatases in Immune Cell Signaling
Pao, L. I., Badour, K., Siminovitch, K., & Neel, B. G. (2007) · Annual Review of Immunology · doi:10.1146/annurev.immunol.23.021704.115647 · Cited by 209
Self-citationDardaei, L., Wang, H. Q., Singh, M., Fordjour, P., Shaw, K. X., Yoda, S., Kerr, G., Yu, K., Liang, J., Cao, Y., et al. (2018) · Nature Medicine · doi:10.1038/nm.4497 · Cited by 201
Chen, H. E., Chang, S. B., Trüb, T., & Neel, B. G. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.7.3685 · Cited by 195
Self-citationSignaling Mechanisms Regulating Self-Renewal and Differentiation of Pluripotent Embryonic Stem Cells
Burdon, T., Chambers, I., Stracey, C., Niwa, H., & Smith, A. G. (1999) · Cells Tissues Organs · doi:10.1159/000016693 · Cited by 200
Liu, F., & Chernoff, J. (1997) · Biochemical Journal · doi:10.1042/bj3270139 · Cited by 179
Odai, H., Sasaki, K., Iwamatsu, A., Hanazono, Y., Tanaka, T., Mitani, K., Yazaki, Y., & Hirai, H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.18.10800 · Cited by 177
Hanafusa, H., Torii, S., Yasunaga, T., Matsumoto, K., & Nishida, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312498200 · Cited by 176
Poole, A. W., & Jones, M. L. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2005.05.016 · Cited by 174
Protein tyrosine phosphatases in signaling
Streuli, M. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80064-0 · Cited by 166
Haque, S. J., Harbor, P. C., Tabrizi, M. H., Yi, T., & Williams, B. R. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.33893 · Cited by 165
A Deletion Mutation in the SH2-N Domain of Shp-2 Severely Suppresses Hematopoietic Cell Development
Qu, C., Shi, Z., Shen, R., Tsai, F., Orkin, S. H., & Feng, G. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.9.5499 · Cited by 164
Involvement of the Src Homology 2-containing Tyrosine Phosphatase SHP-2 in Growth Hormone Signaling
Kim, S.-O., Jiang, J., Yi, W., Feng, G., & Frank, S. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.2344 · Cited by 161
Wagner, M. J., Stacey, M. M., Liu, B. A., & Pawson, T. J. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008987 · Cited by 162
The Phosphatase SHP2 Regulates the Spacing Effect for Long-Term Memory Induction
Pagani, M. R., Oishi, K., Gelb, B. D., & Zhong, Y. (2009) · Cell · doi:10.1016/j.cell.2009.08.033 · Cited by 157
Identification of a Putative Syp Substrate, the PDGFβ Receptor
Klinghoffer, R. A., & Kazlauskas, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.38.22208 · Cited by 157
Jackson, D. E., Kupcho, K. R., & Newman, P. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.40.24868 · Cited by 155
Dunn, S. L., Björnholm, M., Bates, S. H., Chen, Z., Seifert, M. M., & Myers, M. G. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0353 · Cited by 157
Newton‐Nash, D. K., & Newman, P. J. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.2.682 · Cited by 153
Functional analysis of leukemia-associated PTPN11 mutations in primary hematopoietic cells
Schubbert, S., Lieuw, K. H., Rowe, S. L., Lee, C. M., Li, X., Loh, M. L., Clapp, D. W., & Shannon, K. (2005) · Blood · doi:10.1182/blood-2004-11-4207 · Cited by 148
Tomic, S., Greiser, U., Lammers, R., Kharitonenkov, A., Имянитов, Е. Н., Ullrich, A., & Böhmer, F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.36.21277 · Cited by 144
Ihara, S., Nakajima, K., Fukada, T., Hibi, M., Nagata, S., Hirano, T., & Fukui, Y. (1997) · EMBO Journal · doi:10.1093/emboj/16.17.5345 · Cited by 157
Li, L., & Dixon, J. E. (2000) · Seminars in Immunology · doi:10.1006/smim.2000.0209 · Cited by 142
Somatostatin Activation of Mitogen-Activated Protein Kinase via Somatostatin Receptor 1 (SSTR1)
Florio, T., Yao, H. W., Carey, K. D., Dillon, T. J., & Stork, P. A. (1999) · Molecular Endocrinology · doi:10.1210/me.13.1.24 · Cited by 141
Regulation of angiotensin II-induced JAK2 tyrosine phosphorylation: roles of SHP-1 and SHP-2
Marrero, M. B., Venema, V. J., Ju, H., Eaton, D. C., & Venema, R. C. (1998) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1998.275.5.c1216 · Cited by 140
PTP1D is a positive regulator of the prolactin signal leading to beta‐casein promoter activation.
Ali, S., Chen, Z., Lebrun, J. J., Vogel, W. F., Kharitonenkov, A., Kelly, P. A., & Ullrich, A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00341.x · Cited by 140
Membrane-targeting of signalling molecules by SH2/SH3 domain-containing adaptor proteins
Buday, L. (1999) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(99)00005-2 · Cited by 139
Tauchi, T., Feng, G., Shen, R., Hoatlin, M. E., Bagby, G. C., Kabat, D., Lu, L., & Broxmeyer, H. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5631 · Cited by 139
Vitamin E: a sensor and an information transducer of the cell oxidation state
Azzi, A., Boscoboinik, D. O., Marilley, D., Özer, N. K., Stäuble, B., & Tasinato, A. (1995) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/62.6.1337s · Cited by 136
Oncogenic signaling from the hematopoietic growth factor receptors c-Kit and Flt3
Masson, K., & Rönnstrand, L. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.06.002 · Cited by 137
Protein tyrosine phosphatases: regulatory mechanisms
den Hertog, J., Östman, A., & Böhmer, F. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06247.x · Cited by 139
Klinghoffer, R. A., Duckworth, B. C., Valius, M., Cantley, L. C., & Kazlauskas, A. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.10.5905 · Cited by 136
Ivo, P. T. (2006) · Frontiers in bioscience · doi:10.2741/2103 · Cited by 130
Song, Y., Zhao, M., Zhang, H., & Yu, B. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107966 · Cited by 125
The Signaling Pathways Induced by Neutrophil-Endothelial Cell Adhesion
Wang, Q., & Doerschuk, C. M. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602753625843 · Cited by 120
Ward, A. C., Smith, L., de Koning, J. P., van Aesch, Y. M., & Touw, I. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.14956 · Cited by 120
Role of the SHP-2 tyrosine phosphatase in cytokine-induced signaling and cellular response
Qu, C. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(02)00322-1 · Cited by 120
A comprehensive review of SHP2 and its role in cancer
Asmamaw, M. D., Shi, X.-J., Zhang, L.-R., & Liu, H.-M. (2022) · Cellular Oncology · doi:10.1007/s13402-022-00698-1 · Cited by 119
Crystal Structure of the Catalytic Domain of Protein-tyrosine Phosphatase SHP-1
Yang, J. P., Liang, X., Niu, T., Meng, W., Zhao, Z. J., & Zhou, G. W. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.28199 · Cited by 118
SHP-2 and myeloid malignancies
Tartaglia, M., Niemeyer, C. M., Shannon, K., & Loh, M. L. (2003) · Current Opinion in Hematology · doi:10.1097/00062752-200401000-00007 · Cited by 118
The Role of Tyrosine Phosphorylation in Proliferation and Maturation of Erythroid Progenitor Cells
Klingmüller, U. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00637.x · Cited by 116
Structural Determinants of SHP-2 Function and Specificity in Xenopus Mesoderm Induction
O’Reilly, A. M., & Neel, B. G. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.1.161 · Cited by 116
Self-citationSymes, A., Stahl, N., Reeves, S. A., Farruggella, T., Servidei, T., Gearan, T., Yancopouloš, G., & Fink, J. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00298-3 · Cited by 133
Xu, D., Liu, X., Yu, W., Meyerson, H. J., Guo, C., Gerson, S. L., & Qu, C. (2011) · The Journal of Experimental Medicine · doi:10.1084/jem.20110450 · Cited by 115
Ito, N., Wernstedt, C., Engström, U., & Claesson, L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.36.23410 · Cited by 118
Tenev, T., Keilhack, H., Tomic, S., Stoyanov, B., Stein-Gerlach, M., Lammers, R., Krivtsov, A. V., Ullrich, A., & Böhmer, F. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.9.5966 · Cited by 105
Signal Transduction in Natural Killer Cells
Macfarlane, A. W., & Campbell, K. S. (2005) · Current topics in microbiology and immunology · doi:10.1007/3-540-27743-9_2 · Cited by 109
Sagawa, K., Kimura, T., Swieter, M., & Siraganian, R. P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.31086 · Cited by 105
Sha, F., Akçok, E. B. G., Georgeon, S., Koide, A., Yasui, N., Koide, S., & Hantschel, O. D. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303640110 · Cited by 103
Allard, J. D., Chang, H. C., Herbst, R., McNeill, H., & Simon, M. A. (1996) · Development · doi:10.1242/dev.122.4.1137 · Cited by 104
Tyrosyl phosphorylation of KRAS stalls GTPase cycle via alteration of switch I and II conformation
Kano, Y., Gebregiworgis, T., Marshall, C. B., Radulovich, N., Poon, B. P. K., St-Germain, J., Cook, J. D., Valencia-Sama, I., Grant, B. M. M., Herrera, S. G., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-08115-8 · Cited by 103
Regulation of TCR signalling by tyrosine phosphatases: from immune homeostasis to autoimmunity
Stanford, S. M., Rapini, N., & Bottini, N. (2012) · Immunology · doi:10.1111/j.1365-2567.2012.03591.x · Cited by 105
Metadata
- Authors
- Bennett, A. M., Tang, T. L., Sugimoto, S., Walsh, C. T., & Neel, B. G.
- Affiliations
- Beth Israel Deaconess Medical Center (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1994-07-19
- Volume
- 91
- Issue
- 15
- Pages
- 7335-7339
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC44394
- OpenAlex
- W2006147172
- Cited by
- 397
- References
- 43
- Citations by year
- 2026: 8 · 2025: 4 · 2024: 4 · 2023: 9 · 2022: 11 · 2021: 13 · 2020: 7 · 2019: 6 · 2018: 10 · 2017: 5 · 2016: 10 · 2015: 4 · 2014: 5 · 2013: 10 · 2012: 7
- FWCI
- 12.78
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Cancer Society
- National Institutes of Health (GM20011, CA49152)
- National Cancer Institute (CA-49152)
- National Institute of General Medical Sciences (GM 20011)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
- Keywords
- PDGFRβ, Ras activation, Grb2, SOS1, receptor tyrosine kinase signaling, tyrosine phosphorylation, SH2 domain binding
- MeSH terms
- Animals, Base Sequence, Binding Sites, Cell Line, DNA, Humans, Mice, Inbred BALB C, Molecular Sequence Data, Phosphorylation, Genes, ras, Signal Transduction, 3T3 Cells, Protein Tyrosine Phosphatases, Receptors, Platelet-Derived Growth Factor, Intracellular Signaling Peptides and Proteins, Mice, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatase, Non-Receptor Type 11, SH2 Domain-Containing Protein Tyrosine Phosphatases
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