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

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

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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

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

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Sodium orthovanadate inhibits proliferation and triggers apoptosis in oral squamous cell carcinoma in vitro

Khalil, A. A., & Jameson, M. J. (2017) · Biochemistry (Moscow) · doi:10.1134/s0006297917020067 · Cited by 26

Design, Synthesis, and Biological Evaluation of Novel 7H-[1,2,4]Triazolo[3,4-b][1,3,4]thiadiazine Inhibitors as Antitumor Agents

Ismail, M. I., Mohamady, S., Samir, N., & Abouzid, K. A. M. (2020) · ACS Omega · doi:10.1021/acsomega.0c01829 · Cited by 26

Curcumin and Its New Derivatives: Correlation between Cytotoxicity against Breast Cancer Cell Lines, Degradation of PTP1B Phosphatase and ROS Generation

Kostrzewa, T., Wołosewicz, K., Jamrozik, M., Drzeżdżon, J., Siemińska, J., Jacewicz, D., Górska‐Ponikowska, M., Kołaczkowski, M., Łaźny, R., & Kuban‐Jankowska, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910368 · Cited by 26

Overview of the Generation, Validation, and Application of Phosphosite-Specific Antibodies

Brumbaugh, K., Johnson, W. M., Liao, W., Lin, M.-S., Houchins, J. P., Cooper, J., Stoesz, S. P., & Campos‐González, R. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-024-9_1 · Cited by 26

Receptor-type Protein Tyrosine Phosphatase β (RPTP-β) Directly Dephosphorylates and Regulates Hepatocyte Growth Factor Receptor (HGFR/Met) Function

Xu, Y., Xia, W., Baker, D. K., Zhou, J., Cha, H. C., Voorhees, J. J., & Fisher, G. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.212597 · Cited by 26

Involvement of SHP2 in focal adhesion, migration and differentiation of neural stem cells

Huang, Y., Cheng, C., Chueh, S., Hueng, D., Huang, Y.-F., Chu, C., Wu, S., Tai, M., Liang, C., Liao, M.-H., et al. (2011) · Brain and Development · doi:10.1016/j.braindev.2011.10.011 · Cited by 26

Identification of cancer genes by mutational profiling of tumor genomes

Benvenuti, S., Arena, S., & Bardelli, A. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.02.015 · Cited by 26

Assemblies of salen-type oxidovanadium( iv ) complexes: substituent effects and in vitro protein tyrosine phosphatase inhibition

Zabierowski, P., Szklarzewicz, J., Gryboś, R., Mordyl, B., & Nitek, W. (2014) · Dalton Transactions · doi:10.1039/c4dt02344g · Cited by 26

Paladin is an antiphosphatase that regulates neural crest cell formation and migration

Roffers‐Agarwal, J., Hutt, K. J., & Gammill, L. S. (2012) · Developmental Biology · doi:10.1016/j.ydbio.2012.08.007 · Cited by 25

Dual Specificity Phosphatases 18 and 21 Target to Opposing Sides of the Mitochondrial Inner Membrane

Rardin, M. J., Wiley, S. E., Murphy, A. N., Pagliarini, D. J., & Dixon, J. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709547200 · Cited by 26

Crystal structure of human TMDP, a testis‐specific dual specificity protein phosphatase: Implications for substrate specificity

Kim, S. J., Jeong, D. G., Yoon, T., Son, J. H., Cho, S. K., Ryu, S. E., & Kim, J. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21197 · Cited by 26

Novel Ser/Thr Protein Phosphatases in Cell Death Regulation

Sun, H., & Wang, Y. (2012) · Physiology · doi:10.1152/physiol.00034.2011 · Cited by 28

Atomic Structure of Dual-Specificity Phosphatase 26, a Novel p53 Phosphatase

Lokareddy, R. K., Bhardwaj, A., & Cingolani, G. (2013) · Biochemistry · doi:10.1021/bi301476m · Cited by 25

Small Molecule Gated Split-Tyrosine Phosphatases and Orthogonal Split-Tyrosine Kinases

Camacho-Soto, K., Castillo‐Montoya, J., Tye, B., Ogunleye, L. O., & Ghosh, I. (2014) · Journal of the American Chemical Society · doi:10.1021/ja5080745 · Cited by 25

miR-26a desensitizes non-small cell lung cancer cells to tyrosine kinase inhibitors by targeting PTPN13

Xu, S., Wang, T., Yang, Z., Li, Y., Li, W., Wang, S., Zhang, S., Jia, L., Zhang, S., & Li, S. (2016) · Oncotarget · doi:10.18632/oncotarget.9920 · Cited by 26

A cellular target engagement assay for the characterization of SHP2 (PTPN11) phosphatase inhibitors

Romero, C., Lambert, L. J., Sheffler, D. J., Backer, L. J. S. D., Dhanya, R.-P., Celeridad, M., Grotegut, S., Rodiles, S., Holleran, J. P., Sergienko, E. A., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010838 · Cited by 27

Tyrosine phosphorylation of R3 subtype receptor‐type protein tyrosine phosphatases and their complex formations with Grb2 or Fyn

Murata, Y., Mori, M., Kotani, T., Supriatna, Y., Okazawa, H., Kusakari, S., Saito, Y., Ohnishi, H., & Matozaki, T. (2010) · Genes to Cells · doi:10.1111/j.1365-2443.2010.01398.x · Cited by 26

Role of Tyrosine Kinases and Phosphatases in Polycythemia Vera

Zhao, Z. J., Vainchenker, W., Krantz, S. B., Casadevall, N., & Constantinescu, S. N. (2005) · Seminars in Hematology · doi:10.1053/j.seminhematol.2005.05.019 · Cited by 26

Phosphatidylinositol Phosphate Kinase Type Iγ Directly Associates with and Regulates Shp-1 Tyrosine Phosphatase

Bairstow, S. F., Ling, K., & Anderson, R. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500576200 · Cited by 26

Tick vitellin is dephosphorylated by a protein tyrosine phosphatase during egg development: Effect of dephosphorylation on VT proteolysis

da Silveira, A. B., Castro-Santos, J., Senna, R., Logullo, C., Fialho, E., & Silva-Neto, M. A. C. (2006) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2006.01.015 · Cited by 26

Expression of protein tyrosine phosphatases and Bombyx embryonic development

Gu, S., Chen, C., & Lin, P. (2021) · Journal of Insect Physiology · doi:10.1016/j.jinsphys.2021.104198 · Cited by 25

Advances in SHP2 tunnel allosteric inhibitors and bifunctional molecules

Guo, Z., Duan, Y., Sun, K., Zheng, T., Liu, J., Xu, S., & Xu, J. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116579 · Cited by 26

Global Analysis of Phosphoproteome Regulation by the Ser/Thr Phosphatase Ppt1 in Saccharomyces cerevisiae

Schreiber, T. B., Mäusbacher, N., Soroka, J., Wandinger, S. K., Büchner, J., & Daub, H. (2012) · Journal of Proteome Research · doi:10.1021/pr201134p · Cited by 25

Loss of PTPN4 activates STAT3 to promote the tumor growth in rectal cancer

Zhang, B. L., Li, Y., Ding, L., Wang, Y., Liu, H., & Jia, B. (2019) · Cancer Science · doi:10.1111/cas.14031 · Cited by 25

Peptide-templated gold nanoparticle nanosensor for simultaneous detection of multiple posttranslational modification enzymes

Zhang, D., Meng, Y.-R., & Zhang, C. (2019) · Chemical Communications · doi:10.1039/c9cc09019c · Cited by 25

Influence of dual‐specificity protein phosphatase 5 on mechanical properties of rat cerebral and renal arterioles

Zhang, H., Zhang, C., Liu, Y., Gao, W., Wang, S., Fang, X., Guo, Y., Li, M., Liu, R., Roman, R. J., et al. (2020) · Physiological Reports · doi:10.14814/phy2.14345 · Cited by 22

Inhibition of protein tyrosine phosphatase receptor type F suppresses Wnt signaling in colorectal cancer

Gan, T., Stevens, A. T., Xiong, X., Wen, Y., Farmer, T. N., Li, A. T., Stevens, P. D., Golshani, S., Weiss, H. L., Evers, B. M., et al. (2020) · Oncogene · doi:10.1038/s41388-020-01472-z · Cited by 25

A Comprehensive Review of Receptor-Type Tyrosine-Protein Phosphatase Gamma (PTPRG) Role in Health and Non-Neoplastic Disease

Boni, C., Laudanna, C., & Sorio, C. (2022) · Biomolecules · doi:10.3390/biom12010084 · Cited by 25

Cancer plasticity: Investigating the causes for this agility

Saha, S., Pradhan, N., Neha, B., Mahadevappa, R., Minocha, S., & Kumar, S. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2022.12.005 · Cited by 27

Mass Spectrometry-Based Loss of Heterozygosity Analysis of Single-Nucleotide Polymorphism Loci in Paraffin Embedded Tumors Using the MassEXTEND Assay

van Puijenbroek, M., Dierssen, J. W. F., Stanssens, P. E., van Eijk, R., Cleton-Jansen, A., van Wezel, T., & Morreau, H. M. (2005) · Journal of Molecular Diagnostics · doi:10.1016/s1525-1578(10)60596-x · Cited by 25

Synthesis and evaluation of turn-on fluorescent probes for imaging steroid sulfatase activities in cells

Tai, C., Lu, C., Wu, S., & Lo, L. (2014) · Chemical Communications · doi:10.1039/c4cc01282h · Cited by 25

A Drosophila ‐centric view of protein tyrosine phosphatases

Hatzihristidis, T., Desai, N., Hutchins, A. P., Meng, T., Tremblay, M. L., & Miranda‐Saavedra, D. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.03.005 · Cited by 23

Reversible phosphorylation in haematological malignancies: Potential role for protein tyrosine phosphatases in treatment?

Ruela-de-Sousa, R. R., Queiroz, K. C. S., Peppelenbosch, M. P., & Fuhler, G. M. (2010) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2010.07.007 · Cited by 28

Myotubularin-related Proteins 3 and 4 Interact with Polo-like Kinase 1 and Centrosomal Protein of 55 kDa to Ensure Proper Abscission

St‐Denis, N., Gupta, G. D., Lin, Z. Y., Gonzalez-Badillo, B., Pelletier, L., & Gingras, A. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.046086 · Cited by 25

New Aspects of the Phosphatase VHZ Revealed by a High-Resolution Structure with Vanadate and Substrate Screening

Kuznetsov, V. I., Hengge, A. C., & Johnson, S. (2012) · Biochemistry · doi:10.1021/bi300908y · Cited by 25

Structure and catalytic mechanism of human protein tyrosine phosphatome

Kim, S. J., & Ryu, S. E. (2012) · BMB Reports · doi:10.5483/bmbrep.2012.45.12.240 · Cited by 25

Receptor protein tyrosine phosphatases and cancer

Nikolaienko, R. M., Agyekum, B., & Bouyain, S. (2012) · Cell Adhesion & Migration · doi:10.4161/cam.21242 · Cited by 25

Toward the discovery of small molecule PTP1B inhibitors for the treatment of metabolic diseases

Nichols, A. J., Mashal, R. D., & Balkan, B. (2006) · Drug Development Research · doi:10.1002/ddr.20122 · Cited by 25

Protein Tyrosine Phosphatase σ in Proteoglycan-Mediated Neural Regeneration Regulation

Chien, P. N., & Ryu, S. E. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8346-x · Cited by 26

Investigation of POPX2 phosphatase functions by comparative phosphoproteomic analysis

Singh, P., Gan, C. S., Guo, T., Phang, H., Sze, S. K., & Koh, C.-G. (2011) · PROTEOMICS · doi:10.1002/pmic.201100044 · Cited by 25

Activation of maxi-anion channel by protein tyrosine dephosphorylation

Toychiev, A. H., Sabirov, R. Z., Takahashi, N., Ando‐Akatsuka, Y., Liu, H., Shintani, T., Noda, M., & Okada, Y. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00131.2009 · Cited by 25

Association of Tyrosine Phosphatase Epsilon with Microtubules Inhibits Phosphatase Activity and Is Regulated by the Epidermal Growth Factor Receptor

Sines, T., Granot-Attas, S., Weisman-Welcher, S., & Elson, A. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02096-06 · Cited by 25

The tyrosine phosphatase, SHP-1, is involved in bronchial mucin production during oxidative stress

Jang, M. K., Kim, S., Lee, K., Kim, T., Moon, K. A., Park, C. S., Bae, Y. J., Zhu, Z., Moon, H., & Cho, Y. S. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.01.102 · Cited by 25

Is Cdc25 a Druggable Target?

Lazo, J. S., & Wipf, P. (2008) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152008786847738 · Cited by 26

Lipid Raft Targeting of Hematopoietic Protein Tyrosine Phosphatase by Protein Kinase C θ-Mediated Phosphorylation

Nika, K., Charvet, C., Williams, S., Tautz, L., Bruckner, S. R., Rahmouni, S., Bottini, N., Schoenberger, S. P., Baier, G., Altman, A., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.5.1806-1816.2006 · Cited by 25

ERK2 Shows a Restrictive and Locally Selective Mechanism of Recognition by Its Tyrosine Phosphatase Inactivators Not Shared by Its Activator MEK1

Tárrega, C., Ríos, P., Cejudo-Marín, R., Blanco‐Aparicio, C., van den Berk, L., Schepens, J. T. G., Hendriks, W. J. A. J., Tabernero, L., & Pulido, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504366200 · Cited by 25

PHACTR1 Gene Polymorphism Is Associated with Increased Risk of Developing Premature Coronary Artery Disease in Mexican Population

Pérez‐Hernández, N., Vargas‐Alarcón, G., Posadas‐Sánchez, R., Martínez‐Rodríguez, N., Tovilla‐Zárate, C. A., Rodríguez-Cortés, A. A., Pérez-Méndez, O. A., Blachman-Braun, R., & Rodrı́guez-Pérez, J. M. (2016) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph13080803 · Cited by 24

Prognostic Value of Phosphotyrosine Phosphatases in Hepatocellular Carcinoma

Zhangyuan, G., Yin, Y., Zhang, W., Yu, W., Jin, K., Wang, F., Huang, R., Shen, H., Wang, X., & Sun, B. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000489625 · Cited by 24

The mechanisms of colorectal cancer cell mesenchymal-epithelial transition induced by hepatocyte exosome-derived miR-203a-3p

Xu, H., Lan, Q., Huang, Y., Zhang, Y., Zeng, Y., Su, P., Chu, Z., Wei, L., & Chu, Z. (2021) · BMC Cancer · doi:10.1186/s12885-021-08419-x · Cited by 24

Ratiometric fluorescent sensor based on MoS2 QDs and AuNCs for determination and bioimaging of alkaline phosphatase

Liu, Y., Zhang, Y., Zhang, W., Wang, X., Sun, Y. X., Yi, H., Ma, P., Ding, J., & Song, D. (2021) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2021.120087 · Cited by 24

The Role of the Tumor Suppressor Gene Protein Tyrosine Phosphatase Gamma in Cancer

Boni, C., & Sorio, C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.768969 · Cited by 24

Role of PTEN-Akt-CREB Signaling Pathway in Nervous System impairment of Rats with Chronic Arsenite Exposure

Qu, L., Gao, Y., Sun, H., Wang, H., Liu, X., & Sun, D. (2015) · Biological Trace Element Research · doi:10.1007/s12011-015-0478-1 · Cited by 24

Regulation of the catalytic activity of the human phosphatase PTPN 4 by its PDZ domain

Maisonneuve, P., Caillet‐Saguy, C., Raynal, B. D. E., Gilquin, B., Chaffotte, A. F., Pérez, J., Zinn‐Justin, S., Delepierre, M., BUC, H. C., Cordier, F., et al. (2014) · FEBS Journal · doi:10.1111/febs.13024 · Cited by 24

Targeted analysis of tyrosine phosphorylation by immuno-affinity enrichment of tyrosine phosphorylated peptides prior to mass spectrometric analysis

Zoumaro-Djayoon, A. D., Heck, A. J. R., & Muñoz, J. (2011) · Methods · doi:10.1016/j.ymeth.2011.09.003 · Cited by 24

New potential eukaryotic substrates of the mycobacterial protein tyrosine phosphatase PtpA: hints of a bacterial modulation of macrophage bioenergetics state

Margenat, M., Labandera, A., Gil, M., Carrión, F., Purificação, M., Razzera, G., Portela, M. M., Obal, G., Terenzi, H. F., Pritsch, O., et al. (2015) · Scientific Reports · doi:10.1038/srep08819 · Cited by 24

MAP kinase phosphatase activity sets the threshold for thymocyte positive selection

Bettini, M. L., & Kersh, G. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705321104 · Cited by 24

Phosphatase of regenerating liver-3 is regulated by signal transducer and activator of transcription 3 in acute myeloid leukemia

Zhou, J., Chong, P. S. Y., Lu, X., Cheong, L.-L., Bi, C., Liu, S.-C., Zhou, Y., Tan, T. Z., Yang, H. H., Chung, T., et al. (2014) · Experimental Hematology · doi:10.1016/j.exphem.2014.08.001 · Cited by 24

Positive regulation of apoptosis signal-regulating kinase 1 by dual-specificity phosphatase 13A

Park, J. E., Park, B. C., Kim, H.-A., Song, M.-N., Park, S. G., Lee, D. H., Kim, H., Choi, H., Kim, J., & Cho, S. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0353-3 · Cited by 24

GLEPP1/Protein-tyrosine Phosphatase ϕ Inhibitors Block Chemotaxis in Vitro and in Vivo and Improve Murine Ulcerative Colitis

Gobert, R. P., van den Eijnden, M., Szyndralewiez, C., Jorand‐Lebrun, C., Swinnen, D., Chen, L., Gilliéron, C., Pixley, F. J., Juillard, P., Gerber, P., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807241200 · Cited by 24

VHZ is a novel centrosomal phosphatase associated with cell growth and human primary cancers

Tang, J. P., Tan, C. P. B., Li, J., Siddique, M. M., Guo, K., Chan, S. W., Park, J. E., Tay, W. N., Huang, Z. Y., Li, W. C., et al. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-128 · Cited by 24

Dephosphorylation by Default, a Potential Mechanism for Regulation of Insulin Receptor Substrate-1/2, Akt, and ERK1/2

Zhande, R., Zhang, W., Zheng, Y., Pendleton, E., Li, Y., Polakiewicz, R. D., & Sun, X. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605251200 · Cited by 24

Testis-specific serine/threonine protein kinase 4 (Tssk4) phosphorylates Odf2 at Ser-76

Wang, X., Li, H., Fu, G., Wang, Y., Du, S., Yu, L., Wei, Y., & Chen, S. (2016) · Scientific Reports · doi:10.1038/srep22861 · Cited by 24

Photoaffinity-engineered protein scaffold for systematically exploring native phosphotyrosine signaling complexes in tumor samples

Chu, B., He, A., Tian, Y., He, W., Chen, P., Hu, J., Xu, R., Zhou, W., Zhang, M., Yang, P., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1805633115 · Cited by 24

Tea contains potent inhibitors of tyrosine phosphatase PTP1B

Ma, J., Li, Z., Xing, S., Ho, W., Fu, X., & Zhao, Z. J. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.02.116 · Cited by 25

Oxidative inactivation of protein tyrosine phosphatase 1B by organic hydroperoxides

Bhattacharya, S., LaButti, J. N., Seiner, D. R., & Gates, K. S. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.06.029 · Cited by 25

The R3 receptor-like protein tyrosine phosphatase subfamily inhibits insulin signalling by dephosphorylating the insulin receptor at specific sites

Shintani, T., Higashi, S., Takeuchi, Y., Gaudio, E., Trapasso, F., Fusco, A., & Noda, M. (2015) · The Journal of Biochemistry · doi:10.1093/jb/mvv045 · Cited by 24

The KIM-family protein-tyrosine phosphatases use distinct reversible oxidation intermediates: Intramolecular or intermolecular disulfide bond formation

Machado, L. E. S. F., Shen, T., Page, R., & Peti, W. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.774174 · Cited by 23

Technological advances for interrogating the human kinome

Baharani, A., Trost, B., KUSALIK, A. J., & Napper, S. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160163 · Cited by 22

RPTPα phosphatase activity is allosterically regulated by the membrane-distal catalytic domain

Wen, Y., Yang, S. K., Wakabayashi, K., Svensson, M. N. D., Stanford, S. M., Santelli, E., & Bottini, N. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011808 · Cited by 23

SYNTHESIS AND SAR STRATEGY OF THIAZOLIDINEDIONE: A NOVEL APPROACH FOR CANCER TREATMENT

Rashid, M., Shrivastava, N., & Husain, A. (2020) · Journal of the Chilean Chemical Society · doi:10.4067/s0717-97072020000204817 · Cited by 23

Importance of Tyrosine Phosphorylation in Hormone-Regulated Plant Growth and Development

Song, W.-M., Li, H., Ma, Z., Yang, L., & Li, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126603 · Cited by 23

Profiling protein tyrosine phosphatase activity with mechanistic probes

Krishnamurthy, D., & Barrios, A. M. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.07.017 · Cited by 23

Dual specificity phosphatases in prostate cancer

Arnoldussen, Y. J., & Saatcioglu, F. (2009) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.05.019 · Cited by 23

Inhibition of protein tyrosine phosphatases in spinal dorsal horn attenuated inflammatory pain by repressing Src signaling

Suo, Z., Yang, X. Z., Li, L., Liu, Y.-N., Shi, L., & Hu, X. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.01.015 · Cited by 23

Systems biology‐embedded target validation: improving efficacy in drug discovery

Vandamme, D., Minke, B., Fitzmaurice, W., Kholodenko, B. Ν., & Kölch, W. (2013) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1253 · Cited by 24

Using Magnetic Resonance Imaging to Study Enzymatic Hydrogelation

Wang, W., Qian, J., Tang, A., An, L., Zhong, K., & Liang, G. (2014) · Analytical Chemistry · doi:10.1021/ac500967x · Cited by 23

Palmitoylated SCP1 is targeted to the plasma membrane and negatively regulates angiogenesis

Liao, P., Wang, W., Li, Y., Wang, R., Jin, J., Pang, W., Chen, Y., Shen, M., Wang, X., Jiang, D., et al. (2017) · eLife · doi:10.7554/elife.22058 · Cited by 23

PRL2 links magnesium flux and sex-dependent circadian metabolic rhythms

Uetani, N., Hardy, S., Gravel, S., Kießling, S., Pietrobon, A., Wong, N. N., Chénard, V., Cermakian, N., St‐Pierre, J., & Tremblay, M. L. (2017) · JCI Insight · doi:10.1172/jci.insight.91722 · Cited by 30

A Human Tyrosine Phosphatase Interactome Mapped by Proteomic Profiling

Kumar, P., Munnangi, P., Chowdary, K. R., Shah, V. J., Shinde, S. R., Kolli, N. R., Halehalli, R. R., Nagarajaram, H. A., & Maddika, S. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00065 · Cited by 23

In silico-prediction of protein–protein interactions network about MAPKs and PP2Cs reveals a novel docking site variants in Brachypodium distachyon

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Knockdown MTMR14 promotes cell apoptosis and inhibits migration in liver cancer cells

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Recent Advances in Genetic Code Expansion Techniques for Protein Phosphorylation Studies

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Role of Src-family kinases in formation of the cortical actin cap at the dorsal cell surface

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Overproduction, purification and structure determination of human dual-specificity phosphatase 14

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An enriched look at tyrosine phosphorylation

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Two Homologous Putative Protein Tyrosine Phosphatases, OsPFA-DSP2 and AtPFA-DSP4, Negatively Regulate the Pathogen Response in Transgenic Plants

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Overexpression of FgPtp3 Is Involved in Fludioxonil Resistance in Fusarium graminearum by Inhibiting the Phosphorylation of FgHog1

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A Bioinformatics Analysis of Protein Tyrosine Phosphatases in Humans

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Mitogen-Activated Protein Kinase Phosphatases: No Longer Undruggable?

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Integrated use of ligand and structure-based virtual screening, molecular dynamics, free energy calculation and ADME prediction for the identification of potential PTP1B inhibitors

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Tyrosine dephosphorylation enhances the therapeutic target activity of epidermal growth factor receptor (EGFR) by disrupting its interaction with estrogen receptor (ER)

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Receptor protein tyrosine phosphatases are expressed by cycling retinal progenitor cells and involved in neuronal development of mouse retina

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Characterization of novel oxidation products of cysteine in an active site motif peptide of PTP1B

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A Decade of the Human Genome Sequence—How Does the Medicinal Chemist Benefit?

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The evolving landscape of protein kinases in breast cancer: Clinical implications

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Spatial Phosphoprotein Profiling Reveals a Compartmentalized Extracellular Signal-regulated Kinase Switch Governing Neurite Growth and Retraction

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Interaction of PTPRO and TLR4 signaling in hepatocellular carcinoma

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Regulation of Lymphoid Tyrosine Phosphatase Activity: Inhibition of the Catalytic Domain by the Proximal Interdomain

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Double Click Reaction for the Acquisition of a Highly Potent and Selective mPTPB Inhibitor

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The crystal structure of human receptor protein tyrosine phosphatase κ phosphatase domain 1

Eswaran, J., Debreczeni, J. E., Longman, E., Barr, A., & Knapp, S. (2006) · Protein Science · doi:10.1110/ps.062128706 · Cited by 22

Protein Tyrosine Phosphatases

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

Kinases/Phosphatases | Protein Tyrosine Phosphatases

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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

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Novel putative protein tyrosine phosphatases identified by the polymerase chain reaction

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