Identification and expression of the family of classical protein-tyrosine phosphatases in zebrafish. by Mark van Eekelen, John Overvoorde, Carina van Rooijen, Jeroen den Hertog

“…Protein-tyrosine phosphatases (PTPs) have an important role in cell survival, differentiation, proliferation, migration and other cellular processes in conjunction with protein-tyrosine kinases. …”
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Protein tyrosine phosphatase, opisthorchiasis and dengue: A proteomics interrelationship by Sora Yasri, Viroj Wiwanitkit

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Determination of the molecular reach of the protein tyrosine phosphatase SHP-1 by Clemens, L, Kutuzov, M, Bayer, KV, Goyette, J, Allard, J, Dushek, O

Receptor protein tyrosine phosphatase micro: measuring where to stick. by Aricescu, A, Siebold, C, Jones, E

“…We review here recent results on the structure and function of a receptor protein tyrosine phosphatase, RPTPmicro. In addition to their intercellular catalytic domains which bear the phosphatase activity, the RPTPs are cell-surface-receptor-type molecules and in many cases have large extracellular regions. …”

Intramolecular interactions in protein tyrosine phosphatase RPTPmu: kinetic evidence. by Aricescu, A, Fulga, T, Cismasiu, V, Goody, R, Szedlacsek, SE

“…The receptor-like protein tyrosine phosphatase RPTPmu contains three intracellular domains: the juxtamembrane (JM) and two phosphatase domains (D1 and D2). …”

Receptor protein tyrosine phosphatase μ: Measuring where to stick by Radu Aricescu, A, Siebold, C, Yvonne Jones, E

“…We review here recent results on the structure and function of a receptor protein tyrosine phosphatase, RPTPμ. In addition to their intercellular catalytic domains which bear the phosphatase activity, the RPTPs are cell-surface-receptor-type molecules and in many cases have large extracellular regions. …”

Regulation of brown fat adipogenesis by protein tyrosine phosphatase 1B. by Kosuke Matsuo, Ahmed Bettaieb, Naoto Nagata, Izumi Matsuo, Heike Keilhack, Fawaz G Haj

“…Protein-tyrosine phosphatase 1B (PTP1B) is a physiological regulator of insulin signaling and energy balance, but its role in brown fat adipogenesis requires additional investigation.To precisely determine the role of PTP1B in adipogenesis, we established preadipocyte cell lines from wild type and PTP1B knockout (KO) mice. …”
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The mode of action of the Protein tyrosine phosphatase 1B inhibitor Ertiprotafib. by Ganesan Senthil Kumar, Rebecca Page, Wolfgang Peti

“…Protein tyrosine phosphatase 1B (PTP1B) is a validated therapeutic target for the treatment of diabetes and obesity. …”
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Chemical inhibition of bacterial protein tyrosine phosphatase suppresses capsule production. by Alistair J Standish, Angela A Salim, Hua Zhang, Robert J Capon, Renato Morona

“…The biosynthesis of Wzy-dependent capsules in both gram-negative and -positive bacteria is regulated by a system involving a protein tyrosine phosphatase (PTP) and a protein tyrosine kinase. …”
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Role of Receptor Protein Tyrosine Phosphatases (RPTPs) in Insulin Signaling and Secretion by Julio Sevillano, María Gracia Sánchez-Alonso, Javier Pizarro-Delgado, María del Pilar Ramos-Álvarez

Subjects: “…receptor protein tyrosine phosphatases (RPTP)…”
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Protein Tyrosine Phosphatases in Neuroblastoma: Emerging Roles as Biomarkers and Therapeutic Targets by Caroline E. Nunes-Xavier, Caroline E. Nunes-Xavier, Laura Zaldumbide, Lorena Mosteiro, Ricardo López-Almaraz, Nagore García de Andoin, Pablo Aguirre, Maite Emaldi, Leire Torices, José I. López, José I. López, Rafael Pulido, Rafael Pulido

Subjects: “…protein tyrosine phosphatases…”
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Targeting protein tyrosine phosphatases for CDK6-induced immunotherapy resistance by Xueliang Gao, Yongxia Wu, Joel M. Chick, Andrea Abbott, Baishan Jiang, David J. Wang, Susana Comte-Walters, Roger H. Johnson, Nathaniel Oberholtzer, Michael I. Nishimura, Steven P. Gygi, Anand Mehta, Denis C. Guttridge, Lauren Ball, Shikhar Mehrotra, Piotr Sicinski, Xue-Zhong Yu, Haizhen Wang

“…Targeting protein tyrosine phosphatases (PTPs) might be an effective strategy for cancer patients who resist immunotherapy treatment.…”
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Minimally disruptive optical control of protein tyrosine phosphatase 1B by Akarawin Hongdusit, Peter H. Zwart, Banumathi Sankaran, Jerome M. Fox

“…Protein tyrosine phosphatases regulate many cellular processes but are difficult to study in their native context. …”
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Role of the protein tyrosine phosphatase Shp2 in homeostasis of the intestinal epithelium. by Hironori Yamashita, Takenori Kotani, Jung-Ha Park, Yoji Murata, Hideki Okazawa, Hiroshi Ohnishi, Yonson Ku, Takashi Matozaki

“…The role of protein tyrosine phosphatases in such homeostatic regulation of IECs has remained largely unknown, however. …”
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Involvement of protein tyrosine phosphatases in adipogenesis: New anti-obesity targets? by Kwang-Hee Bae

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Heparan sulfate proteoglycans are ligands for receptor protein tyrosine phosphatase sigma. by Aricescu, A, McKinnell, I, Halfter, W, Stoker, A

“…RPTPsigma is a cell adhesion molecule-like receptor protein tyrosine phosphatase involved in nervous system development. …”

Diverse levels of sequence selectivity and catalytic efficiency of protein-tyrosine phosphatases. by Selner, N, Luechapanichkul, R, Chen, X, Neel, BG, Zhang, Z, Knapp, S, Bell, C, Pei, D

“…The sequence selectivity of 14 classical protein-tyrosine phosphatases (PTPs) (PTPRA, PTPRB, PTPRC, PTPRD, PTPRO, PTP1B, SHP-1, SHP-2, HePTP, PTP-PEST, TCPTP, PTPH1, PTPD1, and PTPD2) was systematically profiled by screening their catalytic domains against combinatorial peptide libraries. …”

Protein Tyrosine Phosphatase PRL-3: A Key Player in Cancer Signaling by Haidong Liu, Xiao Li, Yin Shi, Zu Ye, Xiangdong Cheng

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NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22 by Marianne R. Spalinger, Stephanie Kasper, Claudia Gottier, Silvia Lang, Kirstin Atrott, Stephan R. Vavricka, Sylvie Scharl, Petrus M. Gutte, Markus G. Grütter, Hans-Dietmar Beer, Emmanuel Contassot, Andrew C. Chan, Xuezhi Dai, David J. Rawlings, Florian Mair, Burkhard Becher, Werner Falk, Michael Fried, Gerhard Rogler, Michael Scharl

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Protein Tyrosine Phosphatase 1B Inhibitors from the Roots of Cudrania tricuspidata by Tran Hong Quang, Nguyen Thi Thanh Ngan, Chi-Su Yoon, Kwang-Ho Cho, Dae Gill Kang, Ho Sub Lee, Youn-Chul Kim, Hyuncheol Oh

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