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

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

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

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

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

A thousand and one protein kinases

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

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 997

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

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 950

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 761

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

Tonks, N. K. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2039 · Cited by 1,710

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

Roskoski, R. J. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.04.005 · Cited by 1,719

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 1,654

Serine/threonine phosphatases: mechanism through structure

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

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

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

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 1,403

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

Hydrogen Peroxide: A Signaling Messenger

Stone, J. R., & Yang, S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.243 · Cited by 1,193

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

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 905

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

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

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

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

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

Reactive oxygen and nitrogen species as signaling molecules regulating neutrophil function

Fialkow, L., Wang, Y., & Downey, G. P. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.09.030 · Cited by 723

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

Protein-tyrosine phosphatases and cancer

Östman, A., Hellberg, C. B., & Böhmer, F. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1837 · Cited by 665

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

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

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

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

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

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 558

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 551

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

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 538

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 547

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

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 502

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 502

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 470

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

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

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 445

Inhibitors of Protein Tyrosine Phosphatases: Next‐Generation Drugs?

Bialy, L., & Waldmann, H. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200461517 · Cited by 423

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 425

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

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

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 389

Protein tyrosine phosphatases and the immune response

Mustelin, T., Vang, T., & Bottini, N. (2005) · Nature reviews. Immunology · doi:10.1038/nri1530 · Cited by 361

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

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 346

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 336

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

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 339

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

Molecular basis of MAP kinase regulation

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

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 323

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

Bioconjugation via azide–Staudinger ligation: an overview

Schilling, C. I., Jung, N., Biskup, M. B., Schepers, U., & Bräse, S. (2011) · Chemical Society Reviews · doi:10.1039/c0cs00123f · Cited by 320

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 318

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 318

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 314

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

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

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

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 311

Protein tyrosine phosphatase function: the substrate perspective

Tiganis, T., & Bennett, A. M. (2007) · Biochemical Journal · doi:10.1042/bj20061548 · Cited by 303

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 300

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 295

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 292

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 301

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 280

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 286

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 282

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 279

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

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

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 277

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 271

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

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

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 256

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 260

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

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

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 246

Proteases as therapeutics

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

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 243

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

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

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 240

Protein tyrosine phosphatases and signalling

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

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 226

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 224

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 228

STAT3 in Cancer—Friend or Foe?

Zhang, H., & Lai, R. L. (2014) · Cancers · doi:10.3390/cancers6031408 · Cited by 219

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 226

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

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 219

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 215

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 216

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

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 216

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 210

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 208

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 202

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

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 311

The extended human PTP ome: a growing tyrosine phosphatase family

Alonso, A., & Pulido, R. (2015) · FEBS Journal · doi:10.1111/febs.13600 · Cited by 121

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