Protein Tyrosine Phosphatases in the Human Genome

The protein kinase complement of the human genome

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

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

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

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

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A thousand and one protein kinases

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Crystal Structure of the Tyrosine Phosphatase SHP-2

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

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

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CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B

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Resting and Active States of the ERK2:HePTP Complex

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Redox Regulation of the Human Dual Specificity Phosphatase YVH1 through Disulfide Bond Formation

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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

Cellular prostatic acid phosphatase, a PTEN-functional homologue in prostate epithelia, functions as a prostate-specific tumor suppressor

Muniyan, S., Ingersoll, M. A., Batra, S. K., & Lin, M. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.04.006 · Cited by 32

PTPN3 suppresses lung cancer cell invasiveness by counteracting Src-mediated DAAM1 activation and actin polymerization

Li, M.-Y., Peng, W.-H., Wu, C., Chang, Y.-M., Lin, Y., Chang, G., Wu, H., & Chen, G. (2019) · Oncogene · doi:10.1038/s41388-019-0948-6 · Cited by 32

Role of Receptor Protein Tyrosine Phosphatases (RPTPs) in Insulin Signaling and Secretion

Sevillano, J., Sánchez‐Alonso, M. G., Pizarro‐Delgado, J., & Ramos, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115812 · Cited by 31

Protein kinases: Role of their dysregulation in carcinogenesis, identification and inhibition

Sarkar, N., Singh, A. K., Kumar, P., & Kaushik, M. (2023) · Drug Research · doi:10.1055/a-1989-1856 · Cited by 32

Bidentate Inhibitors of Protein Tyrosine Phosphatases

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Protein phosphatase modulation of the intercellular junctional communication: Importance in cardiac myocytes

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PTPRR Protein Tyrosine Phosphatase Isoforms and Locomotion of Vesicles and Mice

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Deregulation of protein phosphatase expression in acute myeloid leukemia

Kabir, N. N., Rönnstrand, L., & Kazi, J. U. (2013) · Medical Oncology · doi:10.1007/s12032-013-0517-8 · Cited by 32

Phylogenetic and genetic linkage between novel atypical dual-specificity phosphatases from non-metazoan organisms

Mateo, C. R., Sacristán-Reviriego, A., Beresford, N. J., Caparros-Martin, J. A., Culiáñez‐Macià, F. A., Martı́n, H., Molina, M., Tabernero, L., & Pulido, R. (2011) · Molecular Genetics and Genomics · doi:10.1007/s00438-011-0611-6 · Cited by 31

Dual-Specificity Phosphatase 10 Controls Brown Adipocyte Differentiation by Modulating the Phosphorylation of P38 Mitogen-Activated Protein Kinase

Choi, H., Kim, W. K., Kim, E. Y., Han, B., Min, J., Chi, S., Park, S. G., Bae, K., & Lee, S. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072340 · Cited by 32

DUSP26 negatively affects the proliferation of epithelial cells, an effect not mediated by dephosphorylation of MAPKs

Patterson, K., Brummer, T., Daly, R. J., & O’Brien, P. M. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.03.014 · Cited by 31

Seleninate in Place of Phosphate: Irreversible Inhibition of Protein Tyrosine Phosphatases

Abdo, M., Liu, S., Zhou, B., Walls, C. D., Wu, L., Knapp, S., & Zhang, Z. (2008) · Journal of the American Chemical Society · doi:10.1021/ja804489m · Cited by 31

Dual Specificity Phosphatases: From Molecular Mechanisms to Biological Function

Pulido, R., & Lang, R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184372 · Cited by 31

Self-Sorting of Amphiphilic Block-Pendant Homopolymers into Sphere or Rod Micelles in Water

Kimura, Y., Takenaka, M., Ouchi, M., & Terashima, T. (2020) · Macromolecules · doi:10.1021/acs.macromol.0c00620 · Cited by 31

Protein arginine phosphorylation in organisms

Huang, B., Zhao, Z., Zhao, Y., & Huang, S. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.01.015 · Cited by 31

A case study of proline isomerization in cell signaling

Min, L. (2005) · Frontiers in bioscience · doi:10.2741/1536 · Cited by 31

Normal TCR Signal Transduction in Mice That Lack Catalytically Active PTPN3 Protein Tyrosine Phosphatase

Bauler, T. J., Hughes, E. D., Arimura, Y., Mustelin, T., Saunders, T. L., & King, P. D. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.6.3680 · Cited by 31

Cantharidin impedes the activity of protein serine/threonine phosphatase in Plutella xylostella

Chen, X., Liu, J., & Zhang, Y. (2013) · Molecular BioSystems · doi:10.1039/c3mb70410f · Cited by 31

Capillary microfluidic electrophoretic mobility shift assays: application to enzymatic assays in drug discovery

Perrin, D., Frémaux, C., & Shutes, A. (2009) · Expert Opinion on Drug Discovery · doi:10.1517/17460440903493431 · Cited by 31

NRAMP-1 Expression Modulates Protein-tyrosine Phosphatase Activity in Macrophages

Gómez, M. A., Li, S., Tremblay, M. L., & Olivier, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703140200 · Cited by 31

Involvement of the N-terminal unique domain of Chk tyrosine kinase in Chk-induced tyrosine phosphorylation in the nucleus

Nakayama, Y., Kawana, A., Igarashi, A., & Yamaguchi, N. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.03.021 · Cited by 31

Protein tyrosine and serine–threonine phosphatases in the sea urchin, Strongylocentrotus purpuratus: Identification and potential functions

Byrum, C. A., Walton, K. D., Robertson, A., Carbonneau, S., Thomason, R. T., Coffman, J. A., & McClay, D. R. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.08.050 · Cited by 31

Sodium orthovanadate overcomes sorafenib resistance of hepatocellular carcinoma cells by inhibiting Na+/K+-ATPase activity and hypoxia-inducible pathways

Jiang, W., Li, G., Li, W., Wang, P., Xiu, P., Jiang, X. L., Liu, B., Sun, X., & Jiang, H. (2018) · Scientific Reports · doi:10.1038/s41598-018-28010-y · Cited by 31

Redox regulation of dimerization of the receptor protein‐tyrosine phosphatases RPTPα, LAR, RPTPμ and CD45

Groen, A. J., Overvoorde, J., van der Wijk, T., & den Hertog, J. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06407.x · Cited by 31

Pseudophosphatases: Methods of analysis and physiological functions

Kharitidi, D., Manteghi, S., & Pause, A. (2013) · Methods · doi:10.1016/j.ymeth.2013.09.009 · Cited by 28

Oxidative Inactivation of the Lipid Phosphatase Phosphatase and Tensin Homolog on Chromosome Ten (PTEN) as a Novel Mechanism of Acquired Long QT Syndrome

Wan, X., Dennis, A. T., Obejero‐Paz, C. A., Overholt, J. L., Heredia‐Moya, J., Kirk, K. L., & Ficker, E. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.125526 · Cited by 30

Dimerization of tyrosine phosphatase PTPRO decreases its activity and ability to inactivate TrkC

Hower, A. E., Beltran, P. J., & Bixby, J. L. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06261.x · Cited by 30

Fullerene derivatives as a new class of inhibitors of protein tyrosine phosphatases

Kobzar, O. L., Trush, V. V., Tanchuk, V. Y., Zhilenkov, A. V., Troshin, P. A., & Vovk, A. I. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.04.110 · Cited by 30

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

Protein Tyrosine Phosphatase-1B Negatively Impacts Host Defense against Pseudomonas aeruginosa Infection

Yue, L., Xie, Z., Li, H., Pang, Z., Junkins, R. D., Tremblay, M. L., Chen, X., & Lin, T. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.01.005 · Cited by 30

Protein tyrosine phosphatases in skeletal development and diseases

Yang, H., Wang, L., Shigley, C., & Yang, W. (2022) · Bone Research · doi:10.1038/s41413-021-00181-x · Cited by 32

Tyrosine Phosphatase SHP-1 in Oxidative Stress and Development of Allergic Airway Inflammation

Cho, Y. S., Oh, S. Y., & Zhu, Z. (2008) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2007-0229oc · Cited by 30

Tyrosine phosphatases as regulators of skeletal development and metabolism

Schiller, K. R., & Mauro, L. J. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20515 · Cited by 30

Illudalic acid as a potential LAR inhibitor: Synthesis, SAR, and preliminary studies on the mechanism of action

Ling, Q., Huang, Y., Zhou, Y., Cai, Z.-L., Xiong, B., Zhang, Y., Ma, L., Wang, X., Li, X., Li, J. X., et al. (2008) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2008.06.014 · Cited by 30

Protein Tyrosine Phosphatases Are Regulated by Mononuclear Iron Dicitrate

Gómez, M. A., Alisaraie, L., Shio, M. T., Berghuis, A. M., Lebrun, C., Gautier‐Luneau, I., & Olivier, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.107037 · Cited by 30

Dynamic Substrate Enhancement for the Identification of Specific, Second‐Site‐Binding Fragments Targeting a Set of Protein Tyrosine Phosphatases

Schmidt, M. F., Groves, M. R., & Rademann, J. (2011) · ChemBioChem · doi:10.1002/cbic.201100414 · Cited by 30

A deletion mutation of the protein tyrosine phosphatase kappa (Ptprk) gene is responsible for T-helper immunodeficiency (thid) in the LEC rat

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Tyrosine Phosphatases ε and α Perform Specific and Overlapping Functions in Regulation of Voltage-gated Potassium Channels in Schwann Cells

Tiran, Z., Peretz, A. S., Sines, T., Shinder, V., Sap, J., Attali, B., & Elson, A. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-02-0151 · Cited by 30

Function and regulatory mechanisms of the candidate tumor suppressor receptor protein tyrosine phosphatase gamma (PTPRG) in breast cancer cells.

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Deficiency in VHR/DUSP3, a suppressor of focal adhesion kinase, reveals its role in regulating cell adhesion and migration

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Reversible Tyrosine Protein Phosphorylation Regulates Large Conductance Voltage- and Calcium-activated Potassium Channels via Cortactin

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Insights into the Catalytic Mechanism of Human sEH Phosphatase by Site-Directed Mutagenesis and LC–MS/MS Analysis

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Nanocomputed Tomography Imaging of Bacterial Alkaline Phosphatase Activity with an Iodinated Hydrogelator

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Protein phosphatase 2ACα gene knock-out results in cortical atrophy through activating hippo cascade in neuronal progenitor cells

Liu, B., Sun, L.-H., Huang, Y.-F., Guo, L.-J., & Luo, L.-S. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.12.015 · Cited by 29

PTPRO-related CD8+ T-cell signatures predict prognosis and immunotherapy response in patients with breast cancer

Dong, H., Xie, C., Yao, Z., Zhao, R., Lin, Y., Luo, Y., Chen, S., Qin, Y., Chen, Y., & Zhang, H. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.947841 · Cited by 30

Multifunctional PTCA/GO for a Glucose-Driven Electrochemiluminescence Biosensor

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Chapter 1 Protein Phosphorylation by Semisynthesis

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Inhibition of Low Molecular Weight Protein Tyrosine Phosphatase by an Induced-Fit Mechanism

He, R., Wang, J., Yu, Z.-H., Zhang, R., Liu, S., Wu, L., & Zhang, Z. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00993 · Cited by 29

Cooperative dynamics across distinct structural elements regulate PTP1B activity

Torgeson, K. R., Clarkson, M. W., Kumar, G. S., Page, R., & Peti, W. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014652 · Cited by 30

A Review of DUSP26: Structure, Regulation and Relevance in Human Disease

Thompson, E. M., & Stoker, A. W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020776 · Cited by 29

Aberrant Expression of proPTPRN2 in Cancer Cells Confers Resistance to Apoptosis

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Dynamic Active-Site Protection by the M. tuberculosis Protein Tyrosine Phosphatase PtpB Lid Domain

Flynn, E. M., Hanson, J., Alber, T., & Yang, H. (2010) · Journal of the American Chemical Society · doi:10.1021/ja909968n · Cited by 30

Gold(I) phosphine mediated selective inhibition of lymphoid tyrosine phosphatase

Karver, M. R., Krishnamurthy, D., Bottini, N., & Barrios, A. M. (2009) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2009.12.012 · Cited by 29

The role of protein tyrosine phosphatases in prostate cancer biology

Nunes‐Xavier, C. E., Mingo, J., Lopez, J. I., & Pulido, R. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.06.016 · Cited by 29

Structural Basis of Substrate Recognition by Hematopoietic Tyrosine Phosphatase,

Critton, D. A., Tortajada, A., Stetson, G., Peti, W., & Page, R. (2008) · Biochemistry · doi:10.1021/bi801724n · Cited by 28

A facile strategy for the construction of a phage display cyclic peptide library for the selection of functional macrocycles

Xiang, H., Bai, L., Zhang, X., Dan, T., Cheng, P., Yang, X., Ai, H., Li, K., & Lei, X. (2024) · Chemical Science · doi:10.1039/d4sc03207a · Cited by 28

Identification and Expression of the Family of Classical Protein-Tyrosine Phosphatases in Zebrafish

van Eekelen, M., Overvoorde, J., van Rooijen, C., & den Hertog, J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012573 · Cited by 27

High Expression of PRL-3 can Promote Growth of Gastric Cancer and Exhibits a Poor Prognostic Impact on Patients

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Triomics Analysis of Imatinib-Treated Myeloma Cells Connects Kinase Inhibition to RNA Processing and Decreased Lipid Biosynthesis

Breitkopf, S. B., Yuan, M., Helenius, K., Lyssiotis, C. A., & Asara, J. M. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b03040 · Cited by 27

Role of Protein Phosphatase 2A in Osteoblast Differentiation and Function

Okamura, H., Yoshida, K., Morimoto, H., Teramachi, J., Ochiai, K., Haneji, T., & Yamamoto, A. (2017) · Journal of Clinical Medicine · doi:10.3390/jcm6030023 · Cited by 28

Temporal Sampling of Enzymes from Live Cells by Localized Electroporation and Quantification of Activity by SAMDI Mass Spectrometry

Mukherjee, P., Berns, E. J., Patino, C. A., Moully, E. H., Chang, L., Nathamgari, S. S. P., Kessler, J. A., Mrksich, M., & Espinosa, H. D. (2020) · Small · doi:10.1002/smll.202000584 · Cited by 28

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 29

Engineering the catalytic domain of human protein tyrosine phosphatase β for structure-based drug discovery

Evdokimov, A. G., Pokross, M. E., WALTER, R. D., Mekel, M. J., Cox, B., Li, C., Bechard, R. T., Genbauffe, F. S., Andrews, R. P., Diven, C. F., et al. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906037784 · Cited by 28

Expression and Prognostic Value of PRL-3 in Human Intrahepatic Cholangiocarcinoma

Xu, Y., Zhu, M., Zhang, S., Liu, H., Li, T., & Qin, C. (2009) · Pathology & Oncology Research · doi:10.1007/s12253-009-9200-y · Cited by 28

Development of Accessible Peptidic Tool Compounds To Study the Phosphatase PTP1B in Intact Cells

Meyer, C., Hoeger, B., Temmerman, K., Tatarek‐Nossol, M., Pogenberg, V., Bernhagen, J., Wilmanns, M., Kapurniotu, A., & Köhn, M. (2014) · ACS Chemical Biology · doi:10.1021/cb400903u · Cited by 28

Perspective: Tyrosine phosphatases as novel targets for antiplatelet therapy

Tautz, L., Senis, Y. A., Oury, C., & Rahmouni, S. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.03.075 · Cited by 30

Identifying Selective Protein Tyrosine Phosphatase Substrates and Inhibitors from a Fluorogenic, Combinatorial Peptide Library

Mitra, S., & Barrios, A. M. (2008) · ChemBioChem · doi:10.1002/cbic.200800046 · Cited by 28

Protein tyrosine phosphatase σ targets apical junction complex proteins in the intestine and regulates epithelial permeability

Murchie, R., Guo, C., Persaud, A. K., Muise, A. M., & Rotin, D. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315017111 · Cited by 27

Protein tyrosine phosphatases: promising targets in pancreatic ductal adenocarcinoma

Ruckert, M. T., de Andrade, P. V., Santos, V. S., & Silveira, V. S. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03095-4 · Cited by 26

PTPL1 suppresses lung cancer cell migration via inhibiting TGF-β1-induced activation of p38 MAPK and Smad 2/3 pathways and EMT

Zhu, N., Zhang, X., Zou, H., Zhang, Y., Xia, J., Zhang, P., Zhang, Y., Li, J., Dong, L., Wumaier, G., et al. (2021) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-00596-y · Cited by 27

Emerging Role of ERBB2 in Targeted Therapy for Metastatic Colorectal Cancer: Signaling Pathways to Therapeutic Strategies

Wang, N., Cao, Y., Si, C., Shao, P., Su, G., Wang, X., Bao, J., & Liu, Y. (2022) · Cancers · doi:10.3390/cancers14205160 · Cited by 29

Muscle Glycogen Remodeling and Glycogen Phosphate Metabolism following Exhaustive Exercise of Wild Type and Laforin Knockout Mice

Irimia, J. M., Tagliabracci, V. S., Meyer, C. M., Segvich, D. M., DePaoli-Roach, A. A., & Roach, P. J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.673897 · Cited by 28

Protein-tyrosine Phosphatase ϵ Regulates Shc Signaling in a Kinase-specific Manner

Kraut‐Cohen, J., Muller, W. J., & Elson, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708822200 · Cited by 27

Receptor Protein Tyrosine Phosphatase From Stem Cells to Mature Glial Cells of the Central Nervous System

Lamprianou, S., & Harroch, S. (2006) · Journal of Molecular Neuroscience · doi:10.1385/jmn:29:3:241 · Cited by 27

Tyrosine Residues at the Carboxyl Terminus of Vav1 Play an Important Role in Regulation of Its Biological Activity

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Potent and selective inhibition of T-cell proteintyrosine phosphatase (TCPTP) by a dinuclear copper( ii ) complex

Yuan, C., Zhu, M., Wang, Q., Lu, L., Xing, S., Fu, X., Jiang, Z. R., Zhang, S., Li, Z., Li, Z., et al. (2011) · Chemical Communications · doi:10.1039/c2cc16818a · Cited by 27

Prioritizing Potentially Druggable Mutations with dGene: An Annotation Tool for Cancer Genome Sequencing Data

Kumar, R. D., Chang, L., Ellis, M. J., & Bose, R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067980 · Cited by 27

Reactive oxygen species induce the association of SHP-1 with c-Src and the oxidation of both to enhance osteoclast survival

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Protein tyrosine phosphatase inhibitors: a patent review (2002 – 2011)

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Protein tyrosine phosphatases in osteoclast differentiation, adhesion, and bone resorption

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Chapter 6 Cell and Molecular Biology of the Novel Protein Tyrosine‐Phosphatase‐Interacting Protein 51

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Protein Tyrosine Phosphatases

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