Discovery of a Novel Series of Inhibitors of Lymphoid Tyrosine Phosphatase with Activity in Human T Cells

Development and validation of a genetic algorithm for flexible docking 1 1Edited by F. E. Cohen

Jones, G., Willett, P., Glen, R. C., Leach, A. R., & Taylor, R. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0897 · Cited by 6,763 · see citing works

Protein Tyrosine Phosphatases in the Human Genome

Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., & Mustelin, T. (2004) · Cell · doi:10.1016/j.cell.2004.05.018 · Cited by 1,886 · see citing works

Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation

Clipstone, N. A., & Crabtree, G. R. (1992) · Nature · doi:10.1038/357695a0 · Cited by 1,635 · see citing works

A Missense Single-Nucleotide Polymorphism in a Gene Encoding a Protein Tyrosine Phosphatase (PTPN22) Is Associated with Rheumatoid Arthritis

Begovich, A. B., Carlton, V. E. H., Honigberg, L. A., Schrodi, S. J., Chokkalingam, A. P., Alexander, H. C., Ardlie, K., Huang, Q., Smith, A. M., Spoerke, J. M., et al. (2004) · The American Journal of Human Genetics · doi:10.1086/422827 · Cited by 1,501 · 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

Regulatory T cells exert checks and balances on self tolerance and autoimmunity

Wing, K., & Sakaguchi, S. (2009) · Nature Immunology · doi:10.1038/ni.1818 · Cited by 1,110 · see citing works

Evaluation of enzyme inhibitors in drug discovery. A guide for medicinal chemists and pharmacologists.

Copeland, R. A. (2005) · PubMed · Cited by 1,045 · see citing works

CD45: A Critical Regulator of Signaling Thresholds in Immune Cells

Hermiston, M. L., Xu, Z., & Weiss, A. (2003) · Annual Review of Immunology · doi:10.1146/annurev.immunol.21.120601.140946 · Cited by 950 · see citing works

Altered thymic T-cell selection due to a mutation of the ZAP-70 gene causes autoimmune arthritis in mice

Sakaguchi, N., Takahashi, T., Hata, H., Nomura, T., Tagami, T., Yamazaki, S., Sakihama, T., Matsutani, T., Negishi, I., Nakatsuru, S., et al. (2003) · Nature · doi:10.1038/nature02119 · Cited by 881 · see citing works

Central Role of Defective Interleukin-2 Production in the Triggering of Islet Autoimmune Destruction

Tang, Q., Adams, J. Y., Penaranda, C., Melli, K., Piaggio, E., Sgouroudis, E., Piccirillo, C. A., Salomon, B. L., & Bluestone, J. A. (2008) · Immunity · doi:10.1016/j.immuni.2008.03.016 · Cited by 729 · see citing works

Autoimmune-associated lymphoid tyrosine phosphatase is a gain-of-function variant

Vang, T., Congia, M., Macis, M. D., Musumeci, L., Orrù, V., Zavattari, P., Nika, K., Tautz, L., Taskén, K., Cucca, F., et al. (2005) · Nature Genetics · doi:10.1038/ng1673 · Cited by 724 · see citing works

Structural and Evolutionary Relationships among Protein Tyrosine Phosphatase Domains

Andersen, J. N., Mortensen, O. H., Peters, G. H. J., Drake, P. G., Iversen, L. F., Olsen, O. H., Jansen, P. G., Andersen, H. S., Tonks, N. K., & Møller, N. P. H. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.21.7117-7136.2001 · Cited by 707 · see citing works

Evaluation of Enzyme Inhibitors in Drug Discovery

Copeland, R. A. (2013) · Wiley eBooks · doi:10.1002/9781118540398 · Cited by 689 · see citing works

Allosteric inhibition of protein tyrosine phosphatase 1B

Wiesmann, C., Barr, K. J., Kung, J., Zhu, J., Erlanson, D. A., Wang, S., Fahr, B. J., Zhong, M., Taylor, L., Randal, M., et al. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb803 · Cited by 526 · see citing works

Requirement for the coexpression of T3 and the T cell antigen receptor on a malignant human T cell line.

Weiss, A., & Stobo, J. D. (1984) · The Journal of Experimental Medicine · doi:10.1084/jem.160.5.1284 · Cited by 496 · 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

IL-2 reverses established type 1 diabetes in NOD mice by a local effect on pancreatic regulatory T cells

Grinberg‐Bleyer, Y., Baeyens, A., You, S., Elhage, R., Fourcade, G., Grégoire, S., Cagnard, N., Carpentier, W., Tang, Q., Bluestone, J. A., et al. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20100209 · Cited by 433 · see citing works

Cooperative Inhibition of T-Cell Antigen Receptor Signaling by a Complex between a Kinase and a Phosphatase

Cloutier, J., & Veillette, A. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.1.111 · Cited by 422 · 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

Interleukin-2 gene variation impairs regulatory T cell function and causes autoimmunity

Yamanouchi, J., Rainbow, D., Serra, P., Howlett, S., Hunter, K. M. D., Garner, V. E. S., González-Muñoz, A., Clark, J., Veijola, R., Cubbon, R. M., et al. (2007) · Nature Genetics · doi:10.1038/ng1958 · Cited by 367 · see citing works

Genetic Variation in PTPN22 Corresponds to Altered Function of T and B Lymphocytes

Rieck, M., Arechiga, A. F., Önengüt-Gümüşcü, S., Greenbaum, C. J., CONCANNON, P. J., & Buckner, J. H. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.7.4704 · Cited by 355 · see citing works

Role of PTPN22 in type 1 diabetes and other autoimmune diseases

Bottini, N., Vang, T., Cucca, F., & Mustelin, T. (2006) · Seminars in Immunology · doi:10.1016/j.smim.2006.03.008 · Cited by 350 · see citing works

Protein tyrosine phosphatases: prospects for therapeutics

Zhang, Z. (2001) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00223-4 · Cited by 348 · see citing works

The PTPN22 C1858T functional polymorphism and autoimmune diseases--a meta-analysis

Lee, Y. H., Rho, Y. H., Choi, S. J., Ji, J. D., Song, G. G., Nath, S. K., & Harley, J. B. (2006) · Lara D. Veeken · doi:10.1093/rheumatology/kel170 · Cited by 316 · see citing works

Identification of Substrates of Human Protein-tyrosine Phosphatase PTPN22

Wu, J., Katrekar, A., Honigberg, L. A., Smith, A. M., Conn, M. T., Tang, J., Jeffery, D. M., Mortara, K. D., Sampang, J., Williams, S. R., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600498200 · Cited by 240 · see citing works

Inhibition of PTP1B by Trodusquemine (MSI‐1436) Causes Fat‐specific Weight Loss in Diet‐induced Obese Mice

Lantz, K. A., HART, S. G. E., Planey, S. L., Roitman, M. F., Ruiz-White, I., Wolfe, H. R., & McLane, M. P. (2010) · Obesity · doi:10.1038/oby.2009.444 · Cited by 237 · see citing works

Promiscuous Aggregate-Based Inhibitors Promote Enzyme Unfolding

Coan, K. E. D., Maltby, D. A., Burlingame, A. L., & Shoichet, B. K. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm801605r · Cited by 203 · see citing works

Fragment Screening and Assembly: A Highly Efficient Approach to a Selective and Cell Active Protein Tyrosine Phosphatase 1B Inhibitor

Liu, G., Xin, Z., Pei, Z., Hajduk, P. J., Abad‐Zapatero, C., Hutchins, C. W., Zhao, H., Lubben, T. H., Ballaron, S. J., Haasch, D. L., et al. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm034122o · Cited by 164 · see citing works

Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases

Yu, X., Sun, J., He, Y., Guo, X., Liu, S., Zhou, B., Hudmon, A., & Zhang, Z. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706233104 · Cited by 145 · see citing works

Opposing Functions of the T Cell Receptor Kinase ZAP-70 in Immunity and Tolerance Differentially Titrate in Response to Nucleotide Substitutions

Siggs, O. M., Miosge, L. A., Yates, A. L., Kucharska, E. M., Sheahan, D., Brdička, T., Weiss, A., Liston, A., & Goodnow, C. C. (2007) · Immunity · doi:10.1016/j.immuni.2007.11.013 · Cited by 142 · see citing works

Crystal Structure of PTP1B Complexed with a Potent and Selective Bidentate Inhibitor

Sun, J., Fedorov, A. A., Lee, S.-Y., Guo, X. L., Shen, K., Lawrence, D. S., Almo, S. C., & Zhang, Z. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212491200 · Cited by 139 · see citing works

Targeting PTPs with small molecule inhibitors in cancer treatment

Jiang, Z., & Zhang, Z. (2008) · Cancer and Metastasis Reviews · doi:10.1007/s10555-008-9113-3 · Cited by 130 · see citing works

PTPN22 Deficiency Cooperates with the CD45 E613R Allele to Break Tolerance on a Non-Autoimmune Background

Zikherman, J., Hermiston, M. L., Steiner, D. F., Hasegawa, K., Chan, A. C., & Weiss, A. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803317 · Cited by 127 · see citing works

Gold(I)-Mediated Inhibition of Protein Tyrosine Phosphatases: A Detailed in Vitro and Cellular Study

Krishnamurthy, D., Karver, M. R., Fiorillo, E., Orrù, V., Stanford, S. M., Bottini, N., & Barrios, A. M. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800101w · Cited by 127 · see citing works

A loss-of-function variant of PTPN22 is associated with reduced risk of systemic lupus erythematosus

Orrù, V., Tsai, S., Rueda‐Medina, B., Fiorillo, E., Stanford, S. M., Dasgupta, J., Hartiala, J., Жао, Л., Ortego‐Centeno, N., D’Alfonso, S., et al. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn363 · Cited by 125 · see citing works

PEST family phosphatases in immunity, autoimmunity, and autoinflammatory disorders

Veillette, A., Rhee, I., Souza, C. M., & Davidson, D. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00747.x · Cited by 114 · see citing works

Drug Discovery and Protein Tyrosine Phosphatases

Blaskovich, M. A. T. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709788612693 · Cited by 104 · see citing works

Docking small-molecule ligands into active sites

Jones, G., & Willett, P. (1995) · Current Opinion in Biotechnology · doi:10.1016/0958-1669(95)80107-3 · Cited by 103 · see citing works

T-cell signalling and immune system disorders

Wilkinson, B., Downey, J. S., & Rudd, C. E. (2005) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399405010264 · Cited by 100 · see citing works

Molecular basis for substrate recognition by MTMR2, a myotubularin family phosphoinositide phosphatase

Begley, M. J., Taylor, G. S., Brock, M. A., Ghosh, P., Woods, V. L., & Dixon, J. E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510006103 · Cited by 93 · see citing works

Mapping Intersubunit Interactions of the Regulatory Subunit (RIα) in the Type I Holoenzyme of Protein Kinase A by Amide Hydrogen/Deuterium Exchange Mass Spectrometry (DXMS)

Hamuro, Y., Anand, G. S., Kim, J. S., Juliano, C. E., Stranz, D. D., Taylor, S. S., & Woods, V. L. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.042 · Cited by 92 · see citing works

Protein tyrosine phosphatases in T cell physiology

Mustelin, T., Alonso, A., Bottini, N., Huynh, H., Rahmouni, S., Nika, K., Louis-Dit-Sully, C., Tautz, L., Togo, S. H., Bruckner, S. R., et al. (2004) · Molecular Immunology · doi:10.1016/j.molimm.2004.04.015 · Cited by 89 · see citing works

Potent Reversible Inhibitors of the Protein Tyrosine Phosphatase CD45

Urbanek, R. A., Suchard, S. J., Steelman, G. B., Knappenberger, K. S., Sygowski, L. A., Veale, C. A., & Chapdelaine, M. J. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm000447i · Cited by 75 · see citing works

The PTPN22 R263Q polymorphism is a risk factor for rheumatoid arthritis in Caucasian case–control samples

Rodríguez‐Rodríguez, L., Taib, W. R. W., Topless, R., Steer, S. E., González‐Escribano, M. F., Balsa, A., Pascual‐Salcedo, D., González-Gay, M. Á., Raya, E., Fernández‐Gutiérrez, B., et al. (2010) · Arthritis & Rheumatism · doi:10.1002/art.30145 · Cited by 74 · see citing works

Probing the Molecular Basis for Potent and Selective Protein-tyrosine Phosphatase 1B Inhibition

Guo, X.-L., Shen, K., Wang, F., Lawrence, D. S., & Zhang, Z. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207347200 · Cited by 72 · see citing works

Location of Inhibitors Bound to Group IVA Phospholipase A2 Determined by Molecular Dynamics and Deuterium Exchange Mass Spectrometry

Burke, J. E., Babakhani, A., Gorfe, A. A., Kokotos, G., Li, S., Woods, V. L., McCammon, J. A., & Dennis, E. A. (2009) · Journal of the American Chemical Society · doi:10.1021/ja900098y · Cited by 63 · see citing works

Novel Vectors for Co-Expression of Two Proteins in E. coli

Kholod, N., & Mustelin, T. (2001) · BioTechniques · doi:10.2144/01312st03 · Cited by 62 · see citing works

Multidentate Small-Molecule Inhibitors of Vaccinia H1-Related (VHR) Phosphatase Decrease Proliferation of Cervix Cancer Cells

Wu, S., Vossius, S., Rahmouni, S., Miletic, A. V., Vang, T., Vazquez-Rodriguez, J., Cerignoli, F., Arimura, Y., Williams, S., Hayes, T., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm901016k · Cited by 60 · see citing works

Crystal Structure of the Human Lymphoid Tyrosine Phosphatase Catalytic Domain: Insights into Redox Regulation,

Tsai, S. J., Sen, U., Zhao, L., Greenleaf, W. B., Dasgupta, J., Fiorillo, E., Orrù, V., Bottini, N., & Chen, X. S. (2009) · Biochemistry · doi:10.1021/bi900166y · Cited by 55 · see citing works

T-cell anergy and altered T-cell receptor signaling: effects on autoimmune disease

Salojin, K. V., Zhang, J., Madrenas, J., & Delovitch, T. L. (1998) · Immunology Today · doi:10.1016/s0167-5699(98)01326-7 · Cited by 55 · see citing works

Methods of using click chemistry in the discovery of enzyme inhibitors

Srinivasan, R., Li, J., Ng, S. L., Kalesh, K., & Yao, S. Q. (2007) · Nature Protocols · doi:10.1038/nprot.2007.323 · Cited by 49 · see citing works

Structure of the Hematopoietic Tyrosine Phosphatase (HePTP) Catalytic Domain: Structure of a KIM Phosphatase with Phosphate Bound at the Active Site

Mustelin, T., Tautz, L., & Page, R. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.09.049 · Cited by 40 · see citing works

Structural Insights into Glucan Phosphatase Dynamics Using Amide Hydrogen−Deuterium Exchange Mass Spectrometry

Hsu, S., Kim, Y.-J., Li, S., Durrant, E. S., Pace, R. M., Woods, V. L., & Gentry, M. S. (2009) · Biochemistry · doi:10.1021/bi9008853 · Cited by 39 · see citing works

Discovery of a novel submicromolar inhibitor of the lymphoid specific tyrosine phosphatase

Xie, Y., Liu, Y., Gong, G., Rinderspacher, A., Deng, S.-X., Smith, D. H., Többen, U., Tzilianos, E., Brandén, L. J., Vidović, D., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.03.079 · Cited by 36 · see citing works

CD3 Antibody Treatment Stimulates the Functional Capability of Regulatory T Cells

Chatenoud, L. (2003) · Novartis Foundation symposium · doi:10.1002/0470871628.ch21 · Cited by 35 · see citing works

In Silico Screening for PTPN22 Inhibitors: Active Hits from an Inactive Phosphatase Conformation

Wu, S., Bottini, M., Rickert, R. C., Mustelin, T., & Tautz, L. (2009) · ChemMedChem · doi:10.1002/cmdc.200800375 · Cited by 34 · see citing works

Small molecule approach to studying protein tyrosine phosphatase

KUMAR, S., Liang, F., LAWRENCE, D., & Zhang, Z. (2004) · Methods · doi:10.1016/j.ymeth.2004.07.003 · Cited by 28 · see citing works

Nitroarylhydroxymethylphosphonic acids as inhibitors of CD45

Beers, S. A., Malloy, E. A., Wu, W., Wachter, M. P., Gunnia, U., CAVENDER, D. E., Harris, C., Davis, J. E., Brosius, R., Pellegrino-Gensey, J. L., et al. (1997) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(97)00174-0 · Cited by 23 · see citing works

A rapid oxime linker-based library approach to identification of bivalent inhibitors of the Yersinia pestis protein-tyrosine phosphatase, YopH

Liu, F., Mollaaghababa, R., Dyas, B. K., Bahta, M., Lountos, G. T., Waugh, D. S., Ulrich, R. G., & Burke, T. R. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.03.058 · Cited by 20 · see citing works

Τ Cell Signaling and Autoimmune Diabetes

Buchs, A. E., & Rapoport, M. J. (2000) · Journal of Pediatric Endocrinology and Metabolism · doi:10.1515/jpem.2000.13.9.1549 · Cited by 11 · see citing works

Acute Coronary Syndromes

Crea, F., & Libby, P. (2017) · Circulation · doi:10.1161/circulationaha.117.029870 · Cited by 488 · see citing works

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 · 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

PTPN22: the archetypal non-HLA autoimmunity gene

Stanford, S. M., & Bottini, N. (2014) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2014.109 · Cited by 242 · 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

Understanding type 1 diabetes through genetics: advances and prospects

Polychronakos, C., & Li, Q. (2011) · Nature Reviews Genetics · doi:10.1038/nrg3069 · Cited by 226 · see citing works

PTP1B: A simple enzyme for a complex world

Feldhammer, M., Uetani, N., Miranda‐Saavedra, D., & Tremblay, M. L. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.819830 · Cited by 195 · see citing works

The Autoimmunity-Associated Gene PTPN22 Potentiates Toll-like Receptor-Driven, Type 1 Interferon-Dependent Immunity

Wang, Y., Shaked, I., Stanford, S. M., Zhou, W., Curtsinger, J., Mikulski, Z., Shaheen, Z. R., Cheng, G., Sawatzke, K., Campbell, A. M., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.06.013 · Cited by 194 · see citing works

Targeting Tyrosine Phosphatases: Time to End the Stigma

Stanford, S. M., & Bottini, N. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.03.004 · Cited by 187 · see citing works

Genetic and Epigenetic Factors in Etiology of Diabetes Mellitus Type 1

Stankov, K., Benc, D., & Drašković, D. (2013) · PEDIATRICS · doi:10.1542/peds.2013-1652 · Cited by 135 · see citing works

Small molecule tools for functional interrogation of protein tyrosine phosphatases

He, R., Zeng, L., He, Y., Zhang, S., & Zhang, Z. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08718.x · Cited by 133 · see citing works

Negative regulation of TLR signaling in myeloid cells—implications for autoimmune diseases

Hamerman, J. A., Pottle, J., Ni, M., He, Y., Zhang, Z., & Buckner, J. H. (2015) · Immunological Reviews · doi:10.1111/imr.12381 · Cited by 112 · see citing works

Adaptive Immunity Dysregulation in Acute Coronary Syndromes

Flego, D., Liuzzo, G., Weyand, C. M., & Crea, F. (2016) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2016.08.036 · Cited by 86 · see citing works

Hydrogen deuterium exchange mass spectrometry in biopharmaceutical discovery and development – A review

Deng, B., Lento, C., & Wilson, D. J. (2016) · Analytica Chimica Acta · doi:10.1016/j.aca.2016.08.006 · Cited by 85 · see citing works

The role of PTPN22 in the pathogenesis of autoimmune diseases: A comprehensive review

Tizaoui, K., Terrazzino, S., Cargnin, S., Lee, K. H., Gauckler, P., Li, H. J., Shin, J. I., & Kronbichler, A. (2021) · Seminars in Arthritis and Rheumatism · doi:10.1016/j.semarthrit.2021.03.004 · Cited by 76 · see citing works

Diabetes reversal by inhibition of the low-molecular-weight tyrosine phosphatase

Stanford, S. M., Aleshin, A. E., Zhang, V., Ardecky, R., Hedrick, M. P., Zou, J., Ganji, S., Bliss, M. R., Yamamoto, F., Bobkov, A. A., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2344 · Cited by 73 · see citing works

Large-Scale Chemical Similarity Networks for Target Profiling of Compounds Identified in Cell-Based Chemical Screens

Lo, Y., Senese, S., Li, C., Hu, Q., Huang, Y., Damoiseaux, R. D., & Torres, J. Z. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004153 · Cited by 70 · see citing works

A Potent and Selective Small-Molecule Inhibitor for the Lymphoid-Specific Tyrosine Phosphatase (LYP), a Target Associated with Autoimmune Diseases

He, Y., Liu, S., Menon, A., Stanford, S. M., Oppong, E. K., Gunawan, A. M., Wu, L., Wu, D. J., Barrios, A. M., Bottini, N., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400248c · Cited by 67 · see citing works

Structure-based drug discovery for combating influenza virus by targeting the PA–PB1 interaction

Watanabe, K., Ishikawa, T., Otaki, H., Mizuta, S., Hamada, T., Nakagaki, T., Ishibashi, D., Urata, S., Yasuda, J., Tanaka, Y., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-10021-w · Cited by 39 · see citing works

Recent advances in the development of allosteric protein tyrosine phosphatase inhibitors for drug discovery

Elhassan, R. M., Hou, X., & Fang, H. (2021) · Medicinal Research Reviews · doi:10.1002/med.21871 · Cited by 39 · see citing works

Small molecule inhibitors for cancer immunotherapy and associated biomarkers – the current status

Schlicher, L., Green, L. G., Romagnani, A., & Renner, F. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1297175 · Cited by 34 · see citing works

PTPN22 Is a Critical Regulator of Fcγ Receptor–Mediated Neutrophil Activation

Vermeren, S., Miles, K., Chu, J. Y., Salter, D. M., Zamoyska, R., & Gray, M. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1600604 · Cited by 34 · see citing works

Controlled Rearrangement of Lactam‐Tethered Allenols with Brominating Reagents: A Combined Experimental and Theoretical Study on α‐ versus β‐Keto Lactam Formation

Alcaide, B., Almendros, P., Luna, A., Cembellín, S., Arnó, M., & Domingo, L. R. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201101160 · Cited by 33 · see citing works

Fast Identification of Novel Lymphoid Tyrosine Phosphatase Inhibitors Using Target–Ligand Interaction-Based Virtual Screening

Hou, X., Li, R., Li, K., Yu, X., Sun, J., & Fang, H. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500692u · Cited by 31 · see citing works

High-throughput screen using a single-cell tyrosine phosphatase assay reveals biologically active inhibitors of tyrosine phosphatase CD45

Stanford, S. M., Panchal, R. G., Walker, L. M., Wu, D. J., Falk, M. D., Mitra, S., Damle, S. S., Ruble, D., Kaltcheva, T. I., Zhang, S., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205028109 · Cited by 31 · see citing works

Protein Flexibility in Docking-Based Virtual Screening: Discovery of Novel Lymphoid-Specific Tyrosine Phosphatase Inhibitors Using Multiple Crystal Structures

Hou, X., Li, K., Yu, X., Sun, J., & Fang, H. (2015) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5b00344 · Cited by 30 · see citing works

PTPN22: structure, function, and developments in inhibitor discovery with applications for immunotherapy

Jassim, B. A., Lin, J., & Zhang, Z. (2022) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2022.2084607 · Cited by 28 · see citing works

Fragmentation hydrogen exchange mass spectrometry: A review of methodology and applications

Brock, A. (2012) · Protein Expression and Purification · doi:10.1016/j.pep.2012.04.009 · Cited by 26 · see citing works

High‐Throughput Screening (HTS) by NMR Guided Identification of Novel Agents Targeting the Protein Docking Domain of YopH

Bottini, A., Wu, B., Barile, E., De, S. K., Leone, M., & Pellecchia, M. (2015) · ChemMedChem · doi:10.1002/cmdc.201500441 · Cited by 23 · see citing works

The potential of PTPN22 as a therapeutic target for rheumatoid arthritis

Carmona, F. D., & Martin, J. J. (2018) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2018.1526924 · Cited by 22 · see citing works

NOVEL AGENTS AND EMERGING STRATEGIES FOR TARGETING THE B-CELL RECEPTOR PATHWAY IN CLL

Efremov, D. G., Wiestner, A. U., & Laurenti, L. (2012) · Mediterranean Journal of Hematology and Infectious Diseases · doi:10.4084/mjhid.2012.067 · Cited by 20 · see citing works

Identification of Small Molecule Inhibitors of PTPσ through an Integrative Virtual and Biochemical Approach

Martin, K. R., Narang, P., Xu, Y., Kauffman, A. L., Petit, J. L., Xu, H. E., Meurice, N., & MacKeigan, J. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050217 · Cited by 20 · see citing works

Exploiting novel tailored immunotherapies of type 1 diabetes: Short interfering RNA delivered by cationic liposomes enables efficient down-regulation of variant PTPN22 gene in T lymphocytes

Pellegrino, M., Ceccacci, F., Petrini, S., Scipioni, A., Santis, S. D., Cappa, M., Mancini, G., & Fierabracci, A. (2018) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2018.11.001 · Cited by 20 · see citing works

Interrogating Protein Phosphatases with Chemical Activity Probes

Casey, G. R., & Stains, C. I. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201705194 · Cited by 19 · see citing works

Identification and structure–function analyses of an allosteric inhibitor of the tyrosine phosphatase PTPN22

Li, K., Hou, X., Li, R., Bi, W., Yang, F., Chen, X., Xiao, P., Liu, T., Lu, T., Zhou, Y. M., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007129 · Cited by 17 · see citing works

Distribution patterns of variability for 18 immune system genes in Amerindians – relationship with history and epidemiology

Lindenau, J. D., Salzano, F. M., Guimaraes, L. S. P., Callegari-Jacques, S. M., Hurtado, A. M., Hill, K. R., Petzl‐Erler, M. L., Tsuneto, L. T., & Hutz, M. H. (2013) · Tissue Antigens · doi:10.1111/tan.12183 · Cited by 17 · see citing works

Synthesis, characterization and phosphatase inhibitory activity of dioxidovanadium(V) complexes with Schiff base ligands derived from pyridoxal and resorcinol

Siqueira, J. D., Menegatti, A. C. O., Terenzi, H. F., Pereira, M. B., Roman, D., Rosso, E. F., Piquini, P. C., Iglesias, B. A., & Back, D. F. (2017) · Polyhedron · doi:10.1016/j.poly.2017.04.004 · Cited by 16 · see citing works

The effect of the autoimmunity-associated gene, PTPN22, on a BXSB-derived model of lupus

Maine, C. J., Marquardt, K., Scatizzi, J. C., Pollard, K. M., Kono, D. H., & Sherman, L. A. (2014) · Clinical Immunology · doi:10.1016/j.clim.2014.11.003 · Cited by 15 · see citing works

pCAP-based peptide substrates: The new tool in the box of tyrosine phosphatase assays

Stanford, S. M., Krishnamurthy, D., Kulkarni, R. A., Karver, C. E., Bruenger, E., Walker, L. M., Ma, C.-T., Chung, T. D. Y., Sergienko, E. A., Bottini, N., et al. (2013) · Methods · doi:10.1016/j.ymeth.2013.07.022 · Cited by 11 · see citing works

C1858T Polymorphism of Protein Tyrosine Phosphatase Non-receptor Type 22 (PTPN22): an eligible target for prevention of type 1 diabetes?

Prezioso, G., Comegna, L., Giulio, C. D., Franchini, S., Chiarelli, F., & Blasetti, A. (2016) · Expert Review of Clinical Immunology · doi:10.1080/1744666x.2017.1266257 · Cited by 10 · see citing works

The protein tyrosine phosphatase Lyp/PTPN22 drives TNFα-induced priming of superoxide anions production by neutrophils and arthritis

Gardette, A., Marzaioli, V., Bedouhène, S., Hayem, G., Hurtado-Nédelec, M., He, Y., Dang, P. M., Dieudé, P., Zhang, Z., Marie, J., et al. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.12.046 · Cited by 8 · see citing works

Discovery of benzofuran-2-carboxylic acid derivatives as lymphoid tyrosine phosphatase (LYP) inhibitors for cancer immunotherapy

Liang, X., Zhao, H., Du, J., Li, X., Li, K., Zhao, Z., Bi, W., Zhang, X., Yu, D., Zhang, J., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115599 · Cited by 7 · see citing works

Substrate Selection Influences Molecular Recognition in a Screen for Lymphoid Tyrosine Phosphatase Inhibitors

Kulkarni, R. A., Vellore, N. A., Bliss, M. R., Stanford, S. M., Falk, M. D., Bottini, N., Baron, R., & Barrios, A. M. (2013) · ChemBioChem · doi:10.1002/cbic.201300273 · Cited by 7 · see citing works

Covalent Inhibition of the Lymphoid Tyrosine Phosphatase

Ahmed, V. F., Bottini, N., & Barrios, A. M. (2014) · ChemMedChem · doi:10.1002/cmdc.201300404 · Cited by 6 · see citing works

Identification of novel thiourea‐stilbene‐triazine conjugates as persuasive lymphoid tyrosine phosphatase inhibitors

Batool, I., Jabeen, F., Vellore, N. A., Shabir, G., & Saeed, A. (2020) · Journal of Heterocyclic Chemistry · doi:10.1002/jhet.4060 · Cited by 4 · see citing works

Structure-Activity Relationship Studies and Design of a Ptpn22 Inhibitor with Enhanced Isozyme Selectivity and Cellular Efficacy

Jassim, B. A., Bai, Y., Qu, Z., Sander, C. J., Lin, J., Miao, J., & Zhang, Z. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.117129 · Cited by 2 · see citing works

1H, 13C and 15N backbone resonance assignment of the catalytic domain of human PTPN22

Martin, B. T., Clarkson, M. W., Wu, P., & Lello, P. D. (2025) · Biomolecular NMR Assignments · doi:10.1007/s12104-025-10233-6 · Cited by 1 · see citing works

Targeting PTPN22 at Nonorthosteric Binding Sites─A Fragment Approach

Lello, P. D., Wells, M. M., Davis, B. J., Daniels, Z., Garner, T. P., Gazzard, L. J., Harris, R., Hubbard, R. E., Landry, M. L., Martin, B. T., et al. (2026) · ACS Omega · doi:10.1021/acsomega.5c11028 · Cited by 1 · see citing works

LYP regulates SLP76 and other adaptor proteins in T cells

Ruiz‐Martín, V., Marcos, T. K., de Pereda, J. M., Crespo, M. S., de la Fuente, M. Á., Bayón, Y., & Alonso, A. (2024) · Biological Research · doi:10.1186/s40659-024-00536-8 · Cited by 1 · see citing works

Allosteric Small Molecule Inhibitors of LMPTP

Ardecky, R., Hedrick, M. P., Stanford, S. M., Bliss, M. R., Zou, J., Gosalia, P., Yamamoto, F., Milewski, M., Barron, N., Sun, Q. Y., et al. (2015) · Europe PMC (PubMed Central) · Cited by 1 · see citing works

Chemical Dissection of the Cell Cycle for Anticancer Drug Discovery and Target Identification

Lo, Y. (2016) · eScholarship (California Digital Library) · Cited by 1 · see citing works

Protein Phosphatases in Trypanosome Growth and Development

Szöőr, B., & Matthews, K. R. (2013) · Wiley eBooks · doi:10.1002/9783527675401.ch08

Caracterización de nuevos sustratos de la fosfatasa Lyp en linfocitos T

Ruiz‐Martín, V. (2015) · doi:10.35376/10324/16244

BindingDB Entry 50043122: A potent and selective small-molecule inhibitor for the lymphoid-specific tyrosine phosphatase (LYP), a target associated with autoimmune diseases.

BindingDB (2014) · UC San Diego · doi:10.7270/q2n017xw

The Role of an Autoimmune Disease-Associated Phosphatase in Dendritic Cell Biology

Gibson, A. C. (2017) · TSpace (University of Toronto)

PRINCIPAIS EVIDÊNCIAS SOBRE DIAGNÓSTICO E INTERVENÇÕES TERAPÊUTICAS DA SÍNDROME CORONARIANA AGUDA

Nogueira, D. R., Melo, G. C. D. C., Silva, I. D. A. C. E., Moreira, L. E. P., Pedrosa, M. D. S. B., Cardinali, M. D. P., Peron, P. L. V., & Piazzi, R. G. (2024) · EPITAYA eBooks · doi:10.47879/ed.ep.2024264p41

Additional file 1 of LYP regulates SLP76 and other adaptor proteins in T cells

Ruiz‐Martín, V., Marcos, T. K., de Pereda, J. M., Crespo, M. S., de la Fuente, M. A., Bayón, Y., & Alonso, A. (2024) · DIGITAL.CSIC (Spanish National Research Council (CSIC)) · doi:10.6084/m9.figshare.27129555

A Potent and Selective Quinolone-Based PTPN22 Inhibitor with Improved Immunotherapeutic Activity

Lin, J., Jassim, B. A., Bai, Y., Qu, Z., Meke, F. N., Dong, J., Wu, L., Babalola, B. A., Yu, J., Zhang, H., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c03467

BindingDB Entry 50022736: Structure-activity relationship studies and design of a PTPN22 inhibitor with enhanced isozyme selectivity and cellular efficacy.

BindingDB (2026) · UC San Diego · doi:10.7270/q2n302sp

BindingDB Entry 50022294: Discovery of benzofuran-2-carboxylic acid derivatives as lymphoid tyrosine phosphatase (LYP) inhibitors for cancer immunotherapy.

BindingDB (2025) · UC San Diego · doi:10.7270/q23j3jps

BindingDB Entry 50044834: Fast identification of novel lymphoid tyrosine phosphatase inhibitors using target-ligand interaction-based virtual screening.

BindingDB (2016) · UC San Diego · doi:10.7270/q2zg6tvj

Identification and structure–function analyses of an allosteric inhibitor of the tyrosine phosphatase PTPN22

Li, K., Hou, X., Li, R., Bi, W., Yang, F., Chen, X., Xiao, P., Liu, T., Lu, T., Zhou, Y. M., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007129 · Cited by 17 · see citing works

Fast Identification of Novel Lymphoid Tyrosine Phosphatase Inhibitors Using Target–Ligand Interaction-Based Virtual Screening

Hou, X., Li, R., Li, K., Yu, X., Sun, J., & Fang, H. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500692u · Cited by 31 · see citing works

Inhibition of Lymphoid Tyrosine Phosphatase by Benzofuran Salicylic Acids

Vang, T., Xie, Y., Liu, W. H., Vidović, D., Liu, Y., Wu, S., Smith, D. H., Rinderspacher, A., Chung, C., Gong, G., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm101004d · Cited by 42 · see citing works

Time‐dependent inhibitors of Lymphoid Tyrosine Phosphatase

Ahmed, V. F., & Barrios, A. M. (2012) · The FASEB Journal · doi:10.1096/fasebj.26.1_supplement.964.13

Searching for lymphoid-specific phosphatase (LYP) inhibitor

Жао, Л. (2015) · University of Southern California Digital Library · doi:10.25549/usctheses-m888