[1] Ruddraraju KV, Zhang ZY. Covalent inhibition of protein tyrosine phosphatases [J]. Mol Biosyst, 2017, 13(7):1257-1279. [2] Lountos GT, Raran-Kurussi S, Zhao BM, et al. High-resolution crystal structures of the D1 and D2 domains of protein tyrosine phosphatase epsilon for structure-based drug design [J]. Acta Crystallogr D Struct Biol, 2018, 74(10):1015-1026. [3] Frankson R, Yu ZH, Bai Y, et al. Therapeutic targeting of oncogenic tyrosine phosphatases [J]. Cancer Res, 2017, 77(21):5701-5705. [4] Sharma Y, Bashir S, Bhardwaj P, et al. Protein tyrosine phosphatase SHP-1: resurgence as new drug target for human autoimmune disorders [J]. Immunol Res, 2016, 64(4):804-819. [5] Gurzov EN, Stanley WJ, Brodnicki TC, et al. Protein tyrosine phosphatases: molecular switches in metabolism and diabetes [J]. Trends Endocrinol Metab, 2015, 26(1):30-39. [6] Shalev M, Elson A. The roles of protein tyrosine phosphatases in bone-resorbing osteoclasts [J]. Biochim Biophys Acta Mol Cell Res, 2019, 1866(1):114-123. [7] Lau KW, Sheng MH. A novel miR17/protein tyrosine phosphatase-oc/EphA4 regulatory axis of osteoclast activity [J]. Arch Biochem Biophys, 2018, 650: 30-38. [8] Wu LW, Baylink DJ, Lau KH. Molecular cloning and expression of a unique rabbit osteoclastic phosphotyrosyl phosphatase [J]. Biochem J,1996, 316(Pt 2): 515-523. [9] Roth L, Wakim J, Wasserman E, et al. Phosphorylation of the phosphatase PTPROt at Tyr399 is a molecular switch that controls osteoclast activity and bone mass in vivo [J]. Sci Signal, 2019, 12(563):eaau0240. [10] Amoui M, Baylink DJ, Tillman JB, et al. Expression of a structurally unique osteoclastic protein-tyrosine phosphatase is driven by an alternative intronic, cell-type-specific promoter [J]. J Biol Chem, 2003, 278(45): 44273-44280. [11] Yang JH, Amoui M, Lau KH. Targeted deletion of the osteoclast protein-tyrosine phosphatase (PTP-oc) promoter prevents RANKL-mediated osteoclastic differentiation of RAW264.7cells [J] . FEBS Lett, 2007, 581(13): 2503-2508. [12] Lau KH, Wu LW, Sheng MH, et al. A unique osteoclastic transmembrane protein-tyrosine phosphatase is a potential positive regulator of the c-src proteintyrosine kinase activity, a mediator of osteoclast activity [J]. J Cell Biochem, 2006, 97(5): 940-955. [13] Tharmalingam S, Hampson DR. The Calcium-sensing receptor and integrins in cellular differentiation and migration [J]. Front Physiol, 2016, 7:190. [14] Rucci N, Teti A. The "love-hate" relationship between osteoclasts and bone matrix [J]. Matrix Biol, 2016, 52-54:176-190. [15] Huntley R, Jensen E, Gopalakrishnan R. Bone morphogenetic proteins: Their role in regulating osteoclast differentiation [J]. Bone Rep, 2019, 10:100207. [16] Lau KH, Stiffel V, Amoui M. An osteoclastic protein-tyrosine phosphatase regulates the β3-integrin, syk, and shp1 signaling through respective src-dependent phosphorylation in osteoclasts [J]. Am J Physiol Cell Physiol, 2012, 302(11): C1676-C1686. [17] Chatterjee D, D'Souza A, Zhang Y. Interaction analyses of 14-3-3ζ, Dok1, and phosphorylated integrin β cytoplasmic tails reveal a bi-molecular switch in integrin regulation [J]. J Mol Biol, 2018, 430(21):4419-4430. [18] Amoui M, Sheng MH, Chen ST, et al. A transmembrane osteoclastic protein-tyrosine phosphatase regulates osteoclast activity in part by promoting osteoclast survival through c-Src-dependent activation of NFkappa B and JNK2 [J]. Arch Biochem Biophys, 2007, 463(1): 47-59. [19] Kang X, Kim J, Deng M, et al. Inhibitory leukocyte immunoglobulin-like receptors: Immune checkpoint proteins and tumor sustaining factors[J]. Cell Cycle, 2016, 15(1):25-40. [20] Stiffel V, Amoui M, Sheng MH, et al. EphA4 receptor is a novel negative regulator of osteoclast activity [J]. Bone Miner Res, 2014, 29(4):804-819. [21] Lau KH, Amoui M, Stiffel V, et al. An osteoclastic transmembrane protein-tyrosine phosphatase enhances osteoclast activity in part by dephosphorylating Eph A4 in osteoclasts [J]. J Cell Biochem, 2015, 116(8):1785-1796. [22] Bai X, Hua S, Zhang J, et al. The microRNA family both in normal development and in different diseases: The miR-17-92 cluster [J]. Biomed Res Int, 2019, 2019:9450240. [23] Cui C, Cui Y, Fu Y, et al. Microarray analysis reveals gene and microRNA signatures in diabetic kidney disease [J]. Mol Med Rep, 2018, 17(2):2161-2168. [24] Ji X, Chen X, Yu X. MicroRNAs in osteoclastogenesis and function: potential therapeutic targets for osteoporosis [J]. Int J Mol Sci, 2016, 17(3):349. [25] Lau KW, Stiffel VM, Rundle CH, et al. Conditional disruption of miR17~92 in osteoclasts led to activation of osteoclasts and loss of trabecular bone in part through suppression of the miR17-mediated downregulation of protein-tyrosine phosphatase-oc in mice [J]. JBMR Plus, 2017, 1(2):73-85. [26] Reddy RH, Kim H, Cha S, et al. Structure-based virtual screening of protein tyrosine phosphatase inhibitors: significance, challenges, and solutions [J]. J Microbiol Biotechnol, 2017, 27(5):878-895. |