Protein Tyrosine Phosphatases in the Human Genome

The protein kinase complement of the human genome

Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145 · see citing works

Increased Insulin Sensitivity and Obesity Resistance in Mice Lacking the Protein Tyrosine Phosphatase-1B Gene

Elchebly, M., Payette, P., Michaliszyn, E., Cromlish, W., Collins, S., Loy, A. L., Normandin, D., Cheng, A., Himms-Hagen, J., Chan, C.-C., et al. (1999) · Science · doi:10.1126/science.283.5407.1544 · Cited by 2,210 · see citing works

Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome

Liaw, D., Marsh, D. J., Li, J., Dahia, P. L. M., Wang, S. I., Zheng, Z., Bose, S., Call, K. M., Tsou, H. C., Peacoke, M., et al. (1997) · Nature Genetics · doi:10.1038/ng0597-64 · Cited by 2,067 · see citing works

Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome

Tartaglia, M., Mehler, E. L., Goldberg, R. B., Zampino, G., Brunner, H. G., Kremer, H., van der Burgt, I., Crosby, A. H., Ion, A., Jeffery, S., et al. (2001) · Nature Genetics · doi:10.1038/ng772 · Cited by 1,736 · see citing works

A functional variant of lymphoid tyrosine phosphatase is associated with type I diabetes

Bottini, N., Musumeci, L., Alonso, A., Rahmouni, S., Nika, K., Rostamkhani, M., MacMurray, J. P., Meloni, T., Lucarelli, P., Pellecchia, M., et al. (2004) · Nature Genetics · doi:10.1038/ng1323 · Cited by 1,419 · see citing works

A thousand and one protein kinases

Hunter, T. R. (1987) · Cell · doi:10.1016/0092-8674(87)90509-5 · Cited by 1,057 · see citing works

Crystal Structure of the Tyrosine Phosphatase SHP-2

Hof, P., Pluskey, S., Dhe‐Paganon, S., Eck, M. J., & Shoelson, S. E. (1998) · Cell · doi:10.1016/s0092-8674(00)80938-1 · Cited by 996 · see citing works

Protein Tyrosine Phosphatases: A Diverse Family of Intracellular and Transmembrane Enzymes

Fischer, E. H., Charbonneau, H., & Tonks, N. K. (1991) · Science · doi:10.1126/science.1650499 · Cited by 969 · see citing works

Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate

Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T.-C., Hinks, J. A., Tonks, N. K., & Barford, D. (2003) · Nature · doi:10.1038/nature01680 · Cited by 951 · see citing works

CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B

Barford, D., Flint, A. J., & Tonks, N. K. (1994) · Science · doi:10.1126/science.8128219 · Cited by 762 · see citing works

The Phosphatase Cdc14 Triggers Mitotic Exit by Reversal of Cdk-Dependent Phosphorylation

Visintin, R., Craig, K. L., Hwang, E. S., Prinz, S., Tyers, M., & Amon, A. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80286-5 · Cited by 735 · see citing works

Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B

van Montfort, R. L. M., Congreve, M., Tisi, D., Carr, R. A. E., & Jhoti, H. (2003) · Nature · doi:10.1038/nature01681 · Cited by 642 · see citing works

A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast

Laporte, J., Hu, L. J., Kretz, C., Mandel, J.-L., Kioschis, P., Coy, J. F., Klauck, S. M., Poustka, A., & Dahl, N. (1996) · Nature Genetics · doi:10.1038/ng0696-175 · Cited by 639 · see citing works

Eya protein phosphatase activity regulates Six1–Dach–Eya transcriptional effects in mammalian organogenesis

Li, X., Ohgi, K. A., Zhang, J., Krones, A., Bush, K. T., Glass, C. K., Nigám, S. K., Aggarwal, A. K., Maas, R. L., Rose, D. W., et al. (2003) · Nature · doi:10.1038/nature02083 · Cited by 636 · see citing works

From Form to Function: Signaling by Protein Tyrosine Phosphatases

Tonks, N. K., & Neel, B. G. (1996) · Cell · doi:10.1016/s0092-8674(00)81357-4 · Cited by 537 · see citing works

PROTEIN TYROSINE PHOSPHATASES

Walton, K. M., & Dixon, J. E. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.000533 · Cited by 529 · see citing works

Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy

Minassian, B. A., Lee, J. R., Herbrick, J.-A., Huizenga, J. J., Soder, S., Mungall, A. J. J., Dunham, I., Gardner, R. J., Fong, C.-Y. G., Carpenter, S., et al. (1998) · Nature Genetics · doi:10.1038/2470 · Cited by 488 · see citing works

Molecular Basis for the Dephosphorylation of the Activation Segment of the Insulin Receptor by Protein Tyrosine Phosphatase 1B

Salmeen, A. E., Andersen, J. N., Myers, M. P., Tonks, N. K., & Barford, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00137-4 · Cited by 470 · see citing works

Charcot-Marie-Tooth type 4B is caused by mutations in the gene encoding myotubularin-related protein-2

Bolino, A., Muglia, M., Conforti, F. L., Leguern, É., Salih, M. A. M., Georgiou, D.-M., Christodoulou, K., Hausmanowa-Petrusewicz, I., Mandich, P., Schenone, A. E., et al. (2000) · Nature Genetics · doi:10.1038/75542 · Cited by 466 · see citing works

Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate.

Guan, K., & Dixon, J. E. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47335-3 · Cited by 460 · see citing works

Protein Tyrosine Phosphatases: Structure and Function, Substrate Specificity, and Inhibitor Development

Zhang, Z. (2002) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.42.083001.144616 · Cited by 435 · see citing works

Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: A paradigm for inhibitor design

Puius, Y. A., Zhao, Y. C., Sullivan, M., Lawrence, D. S., Almo, S. C., & Zhang, Z. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.25.13420 · Cited by 407 · see citing works

A Tyr/Ser protein phosphatase encoded by vaccinia virus

Guan, K., Broyles, S. S., & Dixon, J. E. (1991) · Nature · doi:10.1038/350359a0 · Cited by 399 · see citing works

Activation of the tumour suppressor kinase LKB1 by the STE20‐like pseudokinase STRAD

Baas, A. F., Boudeau, J., Sapkota, G. P., Smit, L., Medema, R. H., Morrice, N. A., Alessi, D. R., & Clevers, H. C. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg292 · Cited by 385 · see citing works

PEST Domain-Enriched Tyrosine Phosphatase (PEP) Regulation of Effector/Memory T Cells

Hasegawa, K., Martin, F., Huang, G., Tumas, D., Diehl, L. J., & Chan, A. C. (2004) · Science · doi:10.1126/science.1092138 · Cited by 379 · see citing works

Crystal Structure of the Dual Specificity Protein Phosphatase VHR

Yuvaniyama, J., Denu, J. M., Dixon, J. E., & Saper, M. A. (1996) · Science · doi:10.1126/science.272.5266.1328 · Cited by 344 · see citing works

The rhodanese/Cdc25 phosphatase superfamily

Bordo, D., & Peer Bork, B. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf150 · Cited by 327 · see citing works

Nucleotide sequence of an avian sarcoma virus oncogene (src) and proposed amino acid sequence for gene product

Czernilofsky, A. P., Levinson, A. D., VARMUS, H. E., Bishop, J. M., Tischer, E., & Goodman, H. M. (1980) · Nature · doi:10.1038/287198a0 · Cited by 321 · see citing works

Mutations in MTMR13, a New Pseudophosphatase Homologue of MTMR2 and Sbf1, in Two Families with an Autosomal Recessive Demyelinating Form of Charcot-Marie-Tooth Disease Associated with Early-Onset Glaucoma

Azzedine, H., Bolino, A., Taïeb, T., Birouk, N., Duca, M. D., Bouhouche, A., Benamou, S., Mrabet, A., Hamadouche, T., Chkili, T., et al. (2003) · The American Journal of Human Genetics · doi:10.1086/375034 · Cited by 313 · see citing works

A genomic perspective on protein tyrosine phosphatases: gene structure, pseudogenes, and genetic disease linkage

Andersen, J. N., Jansen, P. G., Echwald, S. M., Mortensen, O. H., Fukada, T., Vecchio, R. D., Tonks, N. K., & M⊘ller, N. P. H. (2004) · The FASEB Journal · doi:10.1096/fj.02-1212rev · Cited by 303 · see citing works

Structure and function of the WW domain

Sudol, M. (1996) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(96)00008-9 · Cited by 296 · see citing works

Crystal Structure of the Catalytic Domain of the Human Cell Cycle Control Phosphatase, Cdc25A

Fauman, E. B., Cogswell, J. P., Lovejoy, B., Rocque, W. J., Holmes, W. D., Montana, V. G., Piwnica-Worms, H. M., Rink, M. J., & Saper, M. A. (1998) · Cell · doi:10.1016/s0092-8674(00)81190-3 · Cited by 286 · see citing works

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 · see citing works

Positive and negative regulation of T-cell activation through kinases and phosphatases

Mustelin, T., & Taskén, K. (2003) · Biochemical Journal · doi:10.1042/bj20021637 · Cited by 275 · see citing works

Human placenta protein-tyrosine-phosphatase: amino acid sequence and relationship to a family of receptor-like proteins.

Charbonneau, H., Tonks, N. K., Kumar, S., Diltz, C. D., Harrylock, M., Cool, D. E., Krebs, E. G., Fischer, E. H., & Walsh, K. A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.14.5252 · Cited by 274 · see citing works

ICA 512, an autoantigen of type I diabetes, is an intrinsic membrane protein of neurosecretory granules.

Solimena, M., Dirkx, R. A., Hermel, J., Pleasic‐Williams, S., Shapiro, J., Caron, L. A., & Rabin, D. U. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00564.x · Cited by 258 · see citing works

The transcription factor Eyes absent is a protein tyrosine phosphatase

Tootle, T. L., Silver, S. J., Davies, E. L., Newman, V., Latek, R. R., Mills-Henry, I., Selengut, J., Parlikar, B. E. W., & Rebay, I. (2003) · Nature · doi:10.1038/nature02097 · Cited by 254 · see citing works

Eyes absent represents a class of protein tyrosine phosphatases

Rayapureddi, J. P., Kattamuri, C., Steinmetz, B. D., Frankfort, B. J., Ostrin, E. J., Mardon, G., & Hegde, R. S. (2003) · Nature · doi:10.1038/nature02093 · Cited by 240 · see citing works

A novel complex of membrane proteins required for formation of a spherical nucleus

Siniossoglou, S., Santos‐Rosa, H., Rappsilber, J., Mann, M., & Hurt, E. (1998) · The EMBO Journal · doi:10.1093/emboj/17.22.6449 · Cited by 212 · see citing works

Cloning and expression of a protein-tyrosine-phosphatase.

Guan, K., Haun, R. S., Watson, S. J., Geahlen, R. L., & Dixon, J. E. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1501 · Cited by 212 · see citing works

The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase

Su, X., Taddei, N., Stefani, M., Ramponi, G., & Nordlund, P. (1994) · Nature · doi:10.1038/370575a0 · Cited by 204 · see citing works

Intramolecular Regulation of Protein Tyrosine Phosphatase SH-PTP1: A New Function for Src Homology 2 Domains

Pei, D., Lorenz, U. M., Klingmüller, U., Neel, B. G., & Walsh, C. T. (1994) · Biochemistry · doi:10.1021/bi00255a030 · Cited by 198 · see citing works

A point mutation in PTPRC is associated with the development of multiple sclerosis

Jacobsen, M., Schweer, D., Ziegler, A., Gaber, R., Schock, S., Schwinzer, R., Wonigeit, K., Lindert, R.-B., Kantarci, O. H., Schaefer-Klein, J. L., et al. (2000) · Nature Genetics · doi:10.1038/82659 · Cited by 196 · see citing works

Vaccinia Virus Blocks Gamma Interferon Signal Transduction: Viral VH1 Phosphatase Reverses Stat1 Activation

Najarro, P., Traktman, P., & Lewis, J. A. (2001) · Journal of Virology · doi:10.1128/jvi.75.7.3185-3196.2001 · Cited by 189 · see citing works

Expression cloning of a human dual-specificity phosphatase.

Ishibashi, T., Bottaro, D. P., Chan, A. M.-L., Miki, T., & Aaronson, S. A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.12170 · Cited by 184 · see citing works

PTEN and myotubularin phosphatases: from 3-phosphoinositide dephosphorylation to disease

Wishart, M. J., & Dixon, J. E. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(02)02412-1 · Cited by 182 · see citing works

A Deletion in the Gene Encoding the CD45 Antigen in a Patient with SCID

Tchilian, E. Z., Wallace, D. L., Wells, R. S., Flower, D. R., Morgan, G., & Beverley, P. C. L. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.2.1308 · Cited by 175 · see citing works

A Unique Carbohydrate Binding Domain Targets the Lafora Disease Phosphatase to Glycogen

Wang, J., Stuckey, J. A., Wishart, M. J., & Dixon, J. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c100686200 · Cited by 168 · see citing works

Extracellular Regulated Kinases (ERK) 1 and ERK2 Are Authentic Substrates for the Dual-specificity Protein-tyrosine Phosphatase VHR

Todd, J. L., Tanner, K. G., & Denu, J. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13271 · Cited by 156 · see citing works

Protein phosphatases and the regulation of MAP kinase activity

Keyse, S. M. (1998) · Seminars in Cell and Developmental Biology · doi:10.1006/scdb.1997.0219 · Cited by 153 · see citing works

Inhibitory Role for Dual Specificity Phosphatase VHR in T Cell Antigen Receptor and CD28-induced Erk and Jnk Activation

Alonso, A., Saxena, M., Williams, S., & Mustelin, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006497200 · Cited by 149 · see citing works

Crystal Structure of a Phosphoinositide Phosphatase, MTMR2

Begley, M. J., Taylor, G. S., Kim, S., Veine, D. M., Dixon, J. E., & Stuckey, J. A. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00486-6 · Cited by 148 · see citing works

Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains

Wishart, M. J., & Dixon, J. E. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01241-9 · Cited by 138 · see citing works

Extracellular signals and scores of phosphatases: All roads lead to MAP kinase

Saxena, M., & Mustelin, T. (2000) · Seminars in Immunology · doi:10.1006/smim.2000.0219 · Cited by 128 · see citing works

Spatio‐temporal analysis of gene expression during aging in Drosophila melanogaster

Seroude, L., Brummel, T., Kapahi, P., & Benzer, S. (2002) · Aging Cell · doi:10.1046/j.1474-9728.2002.00007.x · Cited by 128 · see citing works

Protein tyrosine phosphatases

Mustelin, T. (2002) · Frontiers in bioscience · doi:10.2741/a770 · Cited by 121 · see citing works

A Single Mutation Converts a Novel Phosphotyrosine Binding Domain into a Dual-specificity Phosphatase

Wishart, M. J., Denu, J. M., Williams, J. A., & Dixon, J. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26782 · Cited by 119 · see citing works

Tyrosine phosphorylation of VHR phosphatase by ZAP-70

Alonso, A., Rahmouni, S., Williams, S., van Stipdonk, M. J. B., Jaroszewski, L., Godzik, A., Abraham, R. T., Schoenberger, S. P., & Mustelin, T. (2002) · Nature Immunology · doi:10.1038/ni856 · Cited by 103 · see citing works

Dephosphorylation of human p34cdc2 kinase on both Thr‐14 and Tyr‐15 by human cdc25B phosphatase

Honda, R., Ohba, Y., Nagata, A., Okayama, H., & Yasuda, H. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80540-b · Cited by 103 · see citing works

Protein tyrosine phosphorylation in T cell signaling

Mustelin, T. (2002) · Frontiers in bioscience · doi:10.2741/a821 · Cited by 88 · see citing works

Human PIR1 of the Protein-tyrosine Phosphatase Superfamily Has RNA 5′-Triphosphatase and Diphosphatase Activities

Deshpande, T., Takagi, T., Hao, L., Buratowski, S., & Charbonneau, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.23.16590 · Cited by 74 · see citing works

STEP: a family of brain-enriched PTPs. Alternative splicing produces transmembrane, cytosolic and truncated isoforms.

Bult, A., Zhao, F., Dirkx, R. A., Raghunathan, A., Solimena, M., & Lombroso, P. J. (1997) · PubMed · Cited by 71 · see citing works

Psr1p/Psr2p, Two Plasma Membrane Phosphatases with an Essential DXDX(T/V) Motif Required for Sodium Stress Response in Yeast

Siniossoglou, S., Hurt, E., & Pelham, H. R. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001314200 · Cited by 66 · see citing works

The Second Domain of the CD45 Protein Tyrosine Phosphatase Is Critical for Interleukin-2 Secretion and Substrate Recruitment of TCR-ζ in Vivo

Kashio, N., Matsumoto, W., Parker, S. A., & Rothstein, D. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.50.33856 · Cited by 53 · see citing works

Molecular Cloning and Characterization of the Human Transmembrane Protein Tyrosine Phosphatase Homologue, Phogrin, an Autoantigen of Type 1 Diabetes

Kawasaki, E., Hutton, J. C., & Eisenbarth, G. S. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1526 · Cited by 52 · see citing works

The dual-specific protein tyrosine phosphatase family

Alonso, A., Rojas, A. M., Godzik, A., & Mustelin, T. (2003) · Topics in current genetics · doi:10.1007/978-3-540-40035-6_16 · Cited by 49 · see citing works

Protein tyrosine phosphorylation in T cell signaling

Mustelin, T. (2002) · Frontiers in bioscience · doi:10.2741/musteli1 · Cited by 48 · see citing works

Gene Structure, Sequence, and Chromosomal Localization of the Human Red Cell-Type Low-Molecular-Weight Acid Phosphotyrosyl Phosphatase Gene, ACP1

Bryson, G. L. M., Massa, H. F., Trask, B. J., & Etten, R. L. V. (1995) · Genomics · doi:10.1006/geno.1995.9893 · Cited by 47 · see citing works

Homotypic Secretory Vesicle Fusion Induced by the Protein Tyrosine Phosphatase MEG2 Depends on Polyphosphoinositides in T Cells

Huynh, H., Wang, X., Li, W., Bottini, N., Williams, S., Nika, K., Ishihara, H., Godzik, A., & Mustelin, T. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.12.6661 · Cited by 45 · see citing works

Molecular cloning and characterization of dullard: a novel gene required for neural development

Satow, R., Chan, T.-C., & Asashima, M. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00641-1 · Cited by 44 · see citing works

Protein tyrosine phosphatases

Mustelin, T. (2002) · Frontiers in bioscience · doi:10.2741/mustelin · Cited by 40 · see citing works

A novel isoform of the low molecular weight phosphotyrosine phosphatase, LMPTP‐C, arising from alternative mRNA splicing

Tailor, P., Gilman, J., Williams, S., & Mustelin, T. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00353.x · Cited by 28 · see citing works

Meeting at Mitosis: Cell Cycle-Specific Regulation of c-Src by RPTPα

Mustelin, T., & Hunter, T. R. (2002) · Science s STKE · doi:10.1126/stke.2002.115.pe3 · Cited by 21 · see citing works

A novel egg‐derived tyrosine phosphatase, EDTP, that participates in the embryogenesis of Sarcophaga peregrina (flesh fly)

Yamaguchi, S., Homma, K., & Natori, S. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00143.x · Cited by 16 · see citing works

Protein Tyrosine Phosphatases

Pagliarini, D. J., Robinson, F. L., & Dixon, J. E. (2004) · Encyclopedia of Biological Chemistry · doi:10.1016/b0-12-443710-9/00696-7 · Cited by 11 · see citing works

Protein Tyrosine Phosphatases

Stauffacher, C. V., & Charbonneau, H. (2000) · Humana Press eBooks · doi:10.1007/978-1-59259-032-2_19 · Cited by 8 · see citing works

Untitled work

Jonnal (2000) · doi:10.1002/1096-8628(20001204)96:6

Protein tyrosine phosphatases: from genes, to function, to disease

Tonks, N. K. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2039 · Cited by 1,685 · see citing works

ERK1/2 MAP kinases: Structure, function, and regulation

Roskoski, R. J. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.04.005 · Cited by 1,642 · see citing works

Protein Posttranslational Modifications: The Chemistry of Proteome Diversifications

Walsh, C. T., Garneau‐Tsodikova, S., & Gatto, G. J. J. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200501023 · Cited by 1,609 · see citing works

Serine/threonine phosphatases: mechanism through structure

Shi, Y. (2009) · Cell · doi:10.1016/j.cell.2009.10.006 · Cited by 1,488 · see citing works

Mechanisms of specificity in protein phosphorylation

Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451 · see citing works

Differential regulation and properties of MAPKs

Raman, M., Chen, W., & Cobb, M. H. (2007) · Oncogene · doi:10.1038/sj.onc.1210392 · Cited by 1,430 · see citing works

The ErbB/HER family of protein-tyrosine kinases and cancer

Roskoski, R. J. (2013) · Pharmacological Research · doi:10.1016/j.phrs.2013.11.002 · Cited by 1,365 · see citing works

The crucial role of protein phosphorylation in cell signaling and its use as targeted therapy (Review)

Ardito, F., Giuliani, M., PERRONE, D., Troiano, G., & Muzio, L. L. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.3036 · Cited by 1,349 · see citing works

Hydrogen Peroxide: A Signaling Messenger

Stone, J. R., & Yang, S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.243 · Cited by 1,175 · see citing works

The role of JAK/STAT signaling pathway and its inhibitors in diseases.

Xin, P., Xu, X., Deng, C., Liu, S., Wang, Y., Zhou, X., Ma, H., Wei, D., & Sun, S. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.106210 · Cited by 1,010 · see citing works

Structure and dynamics of molecular networks: A novel paradigm of drug discovery

Csermely, P., Korcsmáros, T., Kiss, H., London, G., & Nussinov, R. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.01.016 · Cited by 889 · see citing works

A Proteome-wide, Quantitative Survey of In Vivo Ubiquitylation Sites Reveals Widespread Regulatory Roles

Wagner, S., Beli, P., Weinert, B. T., Nielsen, M. L., Cox, J., Mann, M., & Choudhary, C. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.013284 · Cited by 889 · see citing works

Classification of small molecule protein kinase inhibitors based upon the structures of their drug-enzyme complexes

Roskoski, R. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2015.10.021 · Cited by 886 · see citing works

Phosphatase‐mediated crosstalk between MAPK signaling pathways in the regulation of cell survival

Junttila, M. R., Li, S., & Westermarck, J. (2008) · The FASEB Journal · doi:10.1096/fj.06-7859rev · Cited by 826 · see citing works

SIRT1 Improves Insulin Sensitivity under Insulin-Resistant Conditions by Repressing PTP1B

Sun, C., Zhang, F., Ge, X., Yan, T., Chen, X., Shi, X., & Zhai, Q. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.08.014 · Cited by 766 · see citing works

Dual-specificity phosphatases: critical regulators with diverse cellular targets

Patterson, K. I., Brummer, T., O'brien, P. M., & Daly, R. J. (2009) · Biochemical Journal · doi:10.1042/bj20082234 · Cited by 744 · see citing works

Reactive oxygen and nitrogen species as signaling molecules regulating neutrophil function.

Fialkow, L., Wang, Y.-C., & Downey, G. (2007) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2006.09.030 · Cited by 722 · see citing works

Tyrosine phosphorylation: thirty years and counting

Hunter, T. R. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.01.028 · Cited by 664 · see citing works

Protein-tyrosine phosphatases and cancer

Östman, A., Hellberg, C. B., & Böhmer, F. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1837 · Cited by 657 · see citing works

Identification of an Acquired JAK2 Mutation in Polycythemia Vera

Zhao, R., Xing, S., Li, Z., Fu, X., Li, Q., Krantz, S. B., & Zhao, Z. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500138200 · Cited by 616 · see citing works

Src protein-tyrosine kinase structure, mechanism, and small molecule inhibitors

Roskoski, R. J. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.01.003 · Cited by 611 · see citing works

Src kinase regulation by phosphorylation and dephosphorylation

Roskoski, R. J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.012 · Cited by 577 · see citing works

PTP1B as a drug target: recent developments in PTP1B inhibitor discovery

Zhang, S., & Zhang, Z. (2007) · Drug Discovery Today · doi:10.1016/j.drudis.2007.03.011 · Cited by 566 · see citing works

The kinetic-segregation model: TCR triggering and beyond

Davis, S. J., & van der Merwe, P. A. (2006) · Nature Immunology · doi:10.1038/ni1369 · Cited by 562 · see citing works

Targeting dual-specificity phosphatases: Manipulating MAP kinase signalling and immune responses

Jeffrey, K. L., Camps, M., Rommel, C., & Mackay, C. R. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2289 · Cited by 533 · see citing works

Mitogen-Activated Protein (MAP) Kinase/MAP Kinase Phosphatase Regulation: Roles in Cell Growth, Death, and Cancer

Boutros, T., Chevet, É., & Metrakos, P. P. (2008) · Pharmacological Reviews · doi:10.1124/pr.107.00106 · Cited by 545 · see citing works

Ephrin-B2 regulates VEGFR2 function in developmental and tumour angiogenesis

Sawamiphak, S., Seidel, S., Essmann, C. L., Wilkinson, G. A., Pitulescu, M. E., Acker, T., & Acker‐Palmer, A. (2010) · Nature · doi:10.1038/nature08995 · Cited by 532 · see citing works

Reconstruction of cellular signalling networks and analysis of their properties

Papin, J. A., Hunter, T. R., Palsson, B. Ø., & Subramaniam, S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1570 · Cited by 531 · see citing works

A historical overview of protein kinases and their targeted small molecule inhibitors

Roskoski, R. J. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.07.010 · Cited by 527 · see citing works

Inside the human cancer tyrosine phosphatome

Julien, S. G., Dubé, N., Hardy, S., & Tremblay, M. L. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2980 · Cited by 498 · see citing works

Small molecule inhibitors targeting the EGFR/ErbB family of protein-tyrosine kinases in human cancers

Roskoski, R. J. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.11.014 · Cited by 495 · see citing works

Phosphatase: PP2A structural importance, regulation and its aberrant expression in cancer

Seshacharyulu, P., Pandey, P., Datta, K., & Batra, S. K. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.02.036 · Cited by 479 · see citing works

Large-Scale Structural Analysis of the Classical Human Protein Tyrosine Phosphatome

Barr, A., Ugochukwu, E., Lee, W. H., King, O. N. F., Filippakopoulos, P., Alfano, I., Savitsky, P. A., Burgess-Brown, N., Müller, S., & Knapp, S. (2009) · Cell · doi:10.1016/j.cell.2008.11.038 · Cited by 468 · see citing works

Multiple Functions of Peroxiredoxins: Peroxidases, Sensors and Regulators of the Intracellular Messenger H ₂ O ₂ , and Protein Chaperones

Rhee, S. G., & Woo, H. A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3393 · Cited by 463 · see citing works

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442 · see citing works

Protein tyrosine phosphatases – from housekeeping enzymes to master regulators of signal transduction

Tonks, N. K. (2012) · FEBS Journal · doi:10.1111/febs.12077 · Cited by 438 · see citing works

Inhibitors of Protein Tyrosine Phosphatases: Next‐Generation Drugs?

Bialy, L., & Waldmann, H. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200461517 · Cited by 420 · see citing works

Phosphoinositide 3-Kinase/Akt Signaling and Redox Metabolism in Cancer

Koundouros, N., & Poulogiannis, G. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00160 · Cited by 420 · see citing works

Thiol-based redox switches in eukaryotic proteins

Brandes, N., Schmitt, S., & Jakob, U. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2285 · Cited by 373 · see citing works

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 370 · see citing works

Emerging roles of nuclear protein phosphatases

Moorhead, G. B. G., Trinkle‐Mulcahy, L., & Ulke‐Lemée, A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2126 · Cited by 365 · see citing works

Protein tyrosine phosphatases and the immune response

Mustelin, T., Vang, T., & Bottini, N. (2005) · Nature reviews. Immunology · doi:10.1038/nri1530 · Cited by 354 · see citing works

Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins

Xing, Y., Xu, Y., Chen, Y., Jeffrey, P. D., Chao, Y., Lin, Z., Li, Z., Strack, S., Stock, J. B., & Shi, Y. (2006) · Cell · doi:10.1016/j.cell.2006.09.025 · Cited by 334 · see citing works

Phosphotyrosine Signaling: Evolving a New Cellular Communication System

Lim, W. A., & Pawson, T. J. (2010) · Cell · doi:10.1016/j.cell.2010.08.023 · Cited by 344 · see citing works

Protein tyrosine phosphatases as potential therapeutic targets

He, R., Yu, Z.-H., Zhang, R., & Zhang, Z. (2014) · Acta Pharmacologica Sinica · doi:10.1038/aps.2014.80 · Cited by 334 · see citing works

DUSP Meet Immunology: Dual Specificity MAPK Phosphatases in Control of the Inflammatory Response

Lang, R., Hammer, M., & Mages, J. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.11.7497 · Cited by 332 · see citing works

The role of cysteine residues as redox-sensitive regulatory switches

Barford, D. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.09.012 · Cited by 331 · see citing works

Diverse physiological functions for dual-specificity MAP kinase phosphatases

Dickinson, R. J., & Keyse, S. M. (2006) · Journal of Cell Science · doi:10.1242/jcs.03266 · Cited by 329 · see citing works

Molecular basis of MAP kinase regulation

Peti, W., & Page, R. (2013) · Protein Science · doi:10.1002/pro.2374 · Cited by 302 · see citing works

High-resolution aCGH and expression profiling identifies a novel genomic subtype of ER negative breast cancer

Chin, S., Teschendorff, A. E., Marioni, J. C., Wang, Y., Barbosa‐Morais, N. L., Thorne, N., Costa, J. L., Pinder, S. E., van de Wiel, M. A., Green, A. R., et al. (2007) · Genome biology · doi:10.1186/gb-2007-8-10-r215 · Cited by 320 · see citing works

Recent Advances in the Discovery of Competitive Protein Tyrosine Phosphatase 1B Inhibitors for the Treatment of Diabetes, Obesity, and Cancer

Combs, A. P. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm901090b · Cited by 321 · see citing works

Bioconjugation via azide-Staudinger ligation: an overview.

Schilling, C. I., Jung, N., Biskup, M., Schepers, U., & Bräse, S. (2011) · Chemical Society Reviews · doi:10.1039/c0cs00123f · Cited by 263 · see citing works

Functions and Mechanisms of Redox Regulation of Cysteine-Based Phosphatases

Salmeen, A. E., & Barford, D. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.560 · Cited by 312 · see citing works

Hydrogen Peroxide as a Cell-Survival Signaling Molecule

Groeger, G., Quiney, C., & Cotter, T. G. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2728 · Cited by 312 · see citing works

Targeting ERK1/2 protein-serine/threonine kinases in human cancers

Roskoski, R. J. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.01.039 · Cited by 309 · see citing works

Association of a functional single‐nucleotide polymorphism of PTPN22 , encoding lymphoid protein phosphatase, with rheumatoid arthritis and systemic lupus erythematosus

Orozco, G., Sánchez, E., González-Gay, M. Á., López‐Nevot, M. Á., Torres, B., Cáliz, R., Ortego‐Centeno, N., Jiménez-Alonso, J. F., Pascual‐Salcedo, D., Balsa, A., et al. (2005) · Arthritis & Rheumatism · doi:10.1002/art.20771 · Cited by 310 · see citing works

Genomics and evolution of protein phosphatases

Chen, M. J., Dixon, J. E., & Manning, G. (2017) · Science Signaling · doi:10.1126/scisignal.aag1796 · Cited by 299 · see citing works

Discovery of protein phosphatase inhibitor classes by biology-oriented synthesis

Nören‐Müller, A., Junior, I. R. C., Prinz, H., Rosenbaum, C., Saxena, K., Schwalbe, H., Vestweber, D., Cagna, G., Schunk, S. J., Schwarz, O., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601490103 · Cited by 304 · see citing works

Anaplastic lymphoma kinase (ALK): Structure, oncogenic activation, and pharmacological inhibition

Roskoski, R. J. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.11.007 · Cited by 301 · see citing works

Protein tyrosine phosphatase function: the substrate perspective

Tiganis, T., & Bennett, A. M. (2007) · Biochemical Journal · doi:10.1042/bj20061548 · Cited by 299 · see citing works

The Human and Mouse Complement of SH2 Domain Proteins—Establishing the Boundaries of Phosphotyrosine Signaling

Liu, B. A., Jablonowski, K. D., Raina, M., Arcé, M., Pawson, T. J., & Nash, P. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.001 · Cited by 294 · see citing works

Synthesis, biology and clinical significance of pentacyclic triterpenes: a multi-target approach to prevention and treatment of metabolic and vascular diseases

Sheng, H., & Sun, H. (2011) · Natural Product Reports · doi:10.1039/c0np00059k · Cited by 290 · see citing works

Regulation of protein tyrosine phosphatases by reversible oxidation

Östman, A., Frijhoff, J., Sandin, Å., & Böhmer, F. (2011) · The Journal of Biochemistry · doi:10.1093/jb/mvr104 · Cited by 288 · see citing works

MnSOD in Oxidative Stress Response-Potential Regulation via Mitochondrial Protein Influx

Candas, D., & Li, J. J. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5305 · Cited by 287 · see citing works

Discovery of a Novel Shp2 Protein Tyrosine Phosphatase Inhibitor

Chen, L., Sung, S., Yip, M. L. R., Lawrence, H. R., Ren, Y., Guida, W. C., Sebti, S. M., Lawrence, N. J., & Wu, J. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.025536 · Cited by 282 · see citing works

Cancer-Associated PTEN Mutants Act in a Dominant-Negative Manner to Suppress PTEN Protein Function

Papa, A., Wan, L., Bonora, M., Salmena, L., Song, M. S., Hobbs, R. M., Lunardi, A., Webster, K. A., Ng, C., Newton, R. H., et al. (2014) · Cell · doi:10.1016/j.cell.2014.03.027 · Cited by 277 · see citing works

The role of Shp2 (PTPN11) in cancer

Mohi, G., & Neel, B. G. (2007) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2006.12.011 · Cited by 277 · see citing works

MicroRNA dysregulation in gastric cancer: a new player enters the game

Wu, W. K. K., Lee, C., Cho, C. H., Fan, D., Wu, K., Yu, J. Q., & Sung, J. J. �. (2010) · Oncogene · doi:10.1038/onc.2010.352 · Cited by 278 · see citing works

Control of autophagy initiation by phosphoinositide 3‐phosphatase jumpy

Vergne, I., Roberts, E., Elmaoued, R. A., Tosch, V., Delgado, M. A., Proikas‐Cezanne, T., Laporte, J., & Deretic, V. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.159 · Cited by 270 · see citing works

Dusp6 (Mkp3) is a negative feedback regulator of FGF-stimulated ERK signaling during mouse development

Li, C., Scott, D., Hatch, E., Tian, X.-Y., & Mansour, S. (2007) · Development · doi:10.1242/dev.02701 · Cited by 298 · see citing works

A Mechanism for the Evolution of Phosphorylation Sites

Pearlman, S. M., Serber, Z., & Ferrell, J. E. (2011) · Cell · doi:10.1016/j.cell.2011.08.052 · Cited by 271 · see citing works

Protein Tyrosine Phosphatases as Drug Targets: Strategies and Challenges of Inhibitor Development

Barr, A. (2010) · Future Medicinal Chemistry · doi:10.4155/fmc.10.241 · Cited by 268 · see citing works

Human protein factory for converting the transcriptome into an in vitro–expressed proteome

Goshima, N., Kawamura, Y., Fukumoto, A., Miura, A., Honma, R., Satoh, R., Wakamatsu, A., Yamamoto, J., Kimura, K., Nishikawa, T., et al. (2008) · Nature Methods · doi:10.1038/nmeth.1273 · Cited by 262 · see citing works

Inhibition of the protein tyrosine phosphatase PTP1B: potential therapy for obesity, insulin resistance and type-2 diabetes mellitus

Koren, S., & Fantus, I. G. (2007) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2007.08.004 · Cited by 266 · see citing works

Structural and Evolutionary Division of Phosphotyrosine Binding (PTB) Domains

Uhlik, M. T., Temple, B., Bencharit, S., Kimple, A. J., Siderovski, D. P., & Johnson, G. L. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.038 · Cited by 261 · see citing works

Evolution of protein phosphatases in plants and animals

Moorhead, G. B. G., Wever, V. D., Templeton, G. W., & Kerk, D. (2008) · Biochemical Journal · doi:10.1042/bj20081986 · Cited by 254 · see citing works

Targeting mycobacterium protein tyrosine phosphatase B for antituberculosis agents

Zhou, B., He, Y., Zhang, X., Xu, J., Luo, Y., Wang, Y., Franzblau, S. G., Yang, Z., Chan, R. J., Liu, Y., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909133107 · Cited by 250 · see citing works

STARCH-EXCESS4 Is a Laforin-Like Phosphoglucan Phosphatase Required for Starch Degradation in Arabidopsis thaliana

Kötting, O., Santelia, D., Edner, C., Eicke, S., Marthaler, T., Gentry, M. S., Comparot-Moss, S., Chen, J., Smith, A. M., Steup, M., et al. (2009) · The Plant Cell · doi:10.1105/tpc.108.064360 · Cited by 246 · see citing works

Cytoplasmic protein tyrosine phosphatases, regulation and function: the roles of PTP1B and TC-PTP

Bourdeau, A., Dubé, N., & Tremblay, M. L. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.02.001 · Cited by 244 · see citing works

Proteases as therapeutics

Craik, C. S., Page, M. J., & Madison, E. L. (2011) · Biochemical Journal · doi:10.1042/bj20100965 · Cited by 238 · see citing works

NADPH oxidases in fungi: Diverse roles of reactive oxygen species in fungal cellular differentiation

Takemoto, D., Tanaka, A., & Scott, B. (2007) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2007.04.011 · Cited by 238 · see citing works

The Chemical Biology of Protein Phosphorylation

Tarrant, M. K., & Cole, P. A. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.070907.103047 · Cited by 238 · see citing works

The human phosphatase interactome: An intricate family portrait

Sacco, F., Perfetto, L., Castagnoli, L., & Cesareni, G. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.05.008 · Cited by 235 · see citing works

Tyrosine Phosphatase PTPN22: Multifunctional Regulator of Immune Signaling, Development, and Disease

Bottini, N., & Peterson, E. J. (2013) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032713-120249 · Cited by 234 · see citing works

Protein tyrosine phosphatases and signalling

Stoker, A. W. (2005) · Journal of Endocrinology · doi:10.1677/joe.1.06069 · Cited by 233 · see citing works

The Src homology 2 domain tyrosine phosphatases SHP-1 and SHP-2: diversified control of cell growth, inflammation, and injury.

Chong, Z. Z., & Maiese, K. (2007) · PubMed · doi:10.14670/hh-22.1251 · Cited by 228 · see citing works

Cracking the O-GlcNAc code in metabolism

Ruan, H., Singh, J. P., Li, M., Wu, J., & Yang, X. (2013) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.02.002 · Cited by 226 · see citing works

Mitochondrial modulation: reversible phosphorylation takes center stage?

Pagliarini, D. J., & Dixon, J. E. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.11.005 · Cited by 223 · see citing works

STAT3 in Cancer—Friend or Foe?

Zhang, H., & Lai, R. L. (2014) · Cancers · doi:10.3390/cancers6031408 · Cited by 223 · see citing works

ErbB/HER protein-tyrosine kinases: Structures and small molecule inhibitors

Roskoski, R. J. (2014) · Pharmacological Research · doi:10.1016/j.phrs.2014.06.001 · Cited by 217 · see citing works

Mitochondrial Phosphatase PTPMT1 Is Essential for Cardiolipin Biosynthesis

Zhang, J., Guan, Z., Murphy, A. N., Wiley, S. E., Perkins, G. A., Worby, C. A., Engel, J. D., Heacock, P. N., Nguyen, O. K., Wang, J. H., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.04.007 · Cited by 216 · see citing works

D-SCRIPT translates genome to phenome with sequence-based, structure-aware, genome-scale predictions of protein-protein interactions

Sledzieski, S., Singh, R., Cowen, L., & Berger, B. (2021) · Cell Systems · doi:10.1016/j.cels.2021.08.010 · Cited by 208 · see citing works

Specificity in reactive oxidant signaling: think globally, act locally

Terada, L. S. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605036 · Cited by 214 · see citing works

Human Protein Reference Database and Human Proteinpedia as resources for phosphoproteome analysis

Goel, R., Gowda, H., Pandey, A., & Prasad, T. S. K. (2011) · Molecular BioSystems · doi:10.1039/c1mb05340j · Cited by 212 · see citing works

Applications of Nonenzymatic Catalysts to the Alteration of Natural Products

Shugrue, C. R., & Miller, S. J. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00022 · Cited by 212 · see citing works

The protist, Monosiga brevicollis , has a tyrosine kinase signaling network more elaborate and diverse than found in any known metazoan

Manning, G., Young, S. L., Miller, W. T., & Zhai, Y. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801314105 · Cited by 211 · see citing works

The regulation of cell-cell adhesion during epithelial-mesenchymal transition, motility and tumor progression

Bras, G. F. L., Taubenslag, K. J., & Andl, C. D. (2012) · Cell Adhesion & Migration · doi:10.4161/cam.21326 · Cited by 204 · see citing works

Natural products possessing protein tyrosine phosphatase 1B (PTP1B) inhibitory activity found in the last decades

Jiang, C., Liang, L., & Guo, Y. (2012) · Acta Pharmacologica Sinica · doi:10.1038/aps.2012.90 · Cited by 205 · see citing works

NADPH oxidases in lung biology and pathology: Host defense enzymes, and more

van der Vliet, A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.11.016 · Cited by 201 · see citing works

Negative regulation of EGFR signalling through integrin-α1β1-mediated activation of protein tyrosine phosphatase TCPTP

Mattila, E., Pellinen, T. S., Nevo, J., Vuoriluoto, K., Arjonen, A., & Ivaska, J. (2004) · Nature Cell Biology · doi:10.1038/ncb1209 · Cited by 203 · see citing works

Protein Tyrosine Phosphatases

Östman, A., & Kappert, K. (2007) · Cambridge University Press eBooks · doi:10.1017/cbo9780511546198.085

Kinases/Phosphatases | Protein Tyrosine Phosphatases

Pagliarini, D. J., Robinson, F. L., Worby, C. A., & Dixon, J. E. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00615-0

A genomic perspective on protein tyrosine phosphatases: gene structure, pseudogenes, and genetic disease linkage

Andersen, J. N., Jansen, P. G., Echwald, S. M., Mortensen, O. H., Fukada, T., Vecchio, R. D., Tonks, N. K., & M⊘ller, N. P. H. (2004) · The FASEB Journal · doi:10.1096/fj.02-1212rev · Cited by 303 · see citing works

The extended human PTP ome: a growing tyrosine phosphatase family

Alonso, A., & Pulido, R. (2015) · FEBS Journal · doi:10.1111/febs.13600 · Cited by 122 · see citing works

Novel putative protein tyrosine phosphatases identified by the polymerase chain reaction

Nishi, M., Ohagi, S., & Steiner, D. F. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80400-d · Cited by 20 · see citing works