{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T06:29:19Z","timestamp":1793860159542,"version":"4.6.1"},"reference-count":70,"publisher":"Springer Science and Business Media LLC","issue":"6","license":[{"start":{"date-parts":[[2026,7,9]],"date-time":"2026-07-09T00:00:00Z","timestamp":1783555200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,7,9]],"date-time":"2026-07-09T00:00:00Z","timestamp":1783555200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"name":"National Key R&D Program of China","award":["Foundation (Grant No. 2025GXNSFDA04240008)."],"award-info":[{"award-number":["Foundation (Grant No. 2025GXNSFDA04240008)."]}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Divers"],"DOI":"10.1007\/s11030-026-11650-y","type":"journal-article","created":{"date-parts":[[2026,7,9]],"date-time":"2026-07-09T11:30:14Z","timestamp":1783596614000},"page":"9303-9321","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Multicomponent reactions for protein tyrosine phosphatase inhibitors"],"prefix":"10.1007","volume":"30","author":[{"given":"Eyad A. H.","family":"Mohammed","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4250-3779","authenticated-orcid":false,"given":"Taoda","family":"Shi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1511-2614","authenticated-orcid":false,"given":"Wenhao","family":"Hu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,7,9]]},"reference":[{"issue":"2","key":"11650_CR1","doi-asserted-by":"publisher","first-page":"271","DOI":"10.3892\/ijmm.2017.3036","volume":"40","author":"F Ardito","year":"2017","unstructured":"Ardito F et al (2017) The crucial role of protein phosphorylation in cell signaling and its use as targeted therapy (Review). Int J Mol Med 40(2):271\u2013280. https:\/\/doi.org\/10.3892\/ijmm.2017.3036","journal-title":"Int J Mol Med"},{"key":"11650_CR2","doi-asserted-by":"publisher","unstructured":"Pang K, Wang W, Qin JX, Shi ZD, Hao L, Ma YY, Xu H, Wu ZX, Pan D, Chen ZS, Han CH (2020) Role of protein phosphorylation in cell signaling, disease, and the intervention therapy. MedComm 2022;3(4):e175. https:\/\/doi.org\/10.1002\/mco2.175.","DOI":"10.1002\/mco2.175"},{"issue":"5\u20136","key":"11650_CR3","doi-asserted-by":"publisher","first-page":"192","DOI":"10.1016\/j.bioorg.2011.07.004","volume":"39","author":"PA Schwartz","year":"2011","unstructured":"Schwartz PA, Murray BW (2011) Protein kinase biochemistry and drug discovery. Bioorg Chem 39(5\u20136):192\u2013210. https:\/\/doi.org\/10.1016\/j.bioorg.2011.07.004","journal-title":"Bioorg Chem"},{"issue":"11","key":"11650_CR4","doi-asserted-by":"publisher","first-page":"833","DOI":"10.1038\/nrm2039","volume":"7","author":"NK Tonks","year":"2006","unstructured":"Tonks NK (2006) Protein tyrosine phosphatases: from genes, to function, to disease. Nat Rev Mol Cell Biol 7(11):833\u2013846. https:\/\/doi.org\/10.1038\/nrm2039","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"3","key":"11650_CR5","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1016\/s0092-8674(00)81357-4","volume":"87","author":"NK Tonks","year":"1996","unstructured":"Tonks NK, Neel BG (1996) From form to function: signaling by protein tyrosine phosphatases. Cell 87(3):365\u2013368. https:\/\/doi.org\/10.1016\/s0092-8674(00)81357-4","journal-title":"Cell"},{"issue":"21","key":"11650_CR6","doi-asserted-by":"publisher","first-page":"7117","DOI":"10.1128\/MCB.21.21.7117-7136.2001","volume":"21","author":"JN Andersen","year":"2001","unstructured":"Andersen JN, Mortensen OH, Peters GH, Drake PG, Iversen LF, Olsen OH, Jansen PG, Andersen HS, Tonks NK, M\u00f8ller NP (2001) Structural and evolutionary relationships among protein tyrosine phosphatase domains. Mol Cell Biol 21(21):7117\u20137136. https:\/\/doi.org\/10.1128\/MCB.21.21.7117-7136.2001","journal-title":"Mol Cell Biol"},{"issue":"1","key":"11650_CR7","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1038\/s41392-022-01168-8","volume":"7","author":"Y Yang","year":"2022","unstructured":"Yang Y, Li S, Wang Y, Zhao Y, Li Q (2022) Protein tyrosine kinase inhibitor resistance in malignant tumors: molecular mechanisms and future perspective. Signal Transduct Target Ther 7(1):329. https:\/\/doi.org\/10.1038\/s41392-022-01168-8","journal-title":"Signal Transduct Target Ther"},{"issue":"6","key":"11650_CR8","doi-asserted-by":"publisher","first-page":"699","DOI":"10.1016\/j.cell.2004.05.018","volume":"117","author":"A Alonso","year":"2004","unstructured":"Alonso A, Sasin J, Bottini N, Friedberg I, Friedberg I, Osterman A, Godzik A, Hunter T, Dixon J, Mustelin T (2004) Protein tyrosine phosphatases in the human genome. Cell 117(6):699\u2013711. https:\/\/doi.org\/10.1016\/j.cell.2004.05.018","journal-title":"Cell"},{"issue":"4","key":"11650_CR9","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1038\/nrc1837","volume":"6","author":"A Ostman","year":"2006","unstructured":"Ostman A, Hellberg C, B\u00f6hmer FD (2006) Protein-tyrosine phosphatases and cancer. Nat Rev Cancer 6(4):307\u2013320. https:\/\/doi.org\/10.1038\/nrc1837","journal-title":"Nat Rev Cancer"},{"issue":"19","key":"11650_CR10","doi-asserted-by":"publisher","first-page":"14291","DOI":"10.1074\/jbc.M609626200","volume":"282","author":"SK Pandey","year":"2007","unstructured":"Pandey SK, Yu XX, Watts LM, Michael MD, Sloop KW, Rivard AR, Leedom TA, Manchem VP, Samadzadeh L, McKay RA, Monia BP, Bhanot S (2007) Reduction of low molecular weight protein-tyrosine phosphatase expression improves hyperglycemia and insulin sensitivity in obese mice. J Biol Chem 282(19):14291\u201314299. https:\/\/doi.org\/10.1074\/jbc.M609626200","journal-title":"J Biol Chem"},{"issue":"1","key":"11650_CR11","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1021\/jm200607g","volume":"55","author":"R Maccari","year":"2012","unstructured":"Maccari R, Ottan\u00e0 R (2012) Low molecular weight phosphotyrosine protein phosphatases as emerging targets for the design of novel therapeutic agents. J Med Chem 55(1):2\u201322. https:\/\/doi.org\/10.1021\/jm200607g","journal-title":"J Med Chem"},{"issue":"4","key":"11650_CR12","doi-asserted-by":"publisher","first-page":"1979","DOI":"10.1007\/s13277-013-0784-1","volume":"34","author":"I Alho","year":"2013","unstructured":"Alho I, Costa L, Bicho M, Coelho C (2013) The role of low-molecular-weight protein tyrosine phosphatase (LMW-PTP ACP1) in oncogenesis. Tumour Biol 34(4):1979\u20131989. https:\/\/doi.org\/10.1007\/s13277-013-0784-1","journal-title":"Tumour Biol"},{"issue":"1","key":"11650_CR13","doi-asserted-by":"publisher","first-page":"122","DOI":"10.1021\/acs.accounts.6b00537","volume":"50","author":"ZY Zhang","year":"2017","unstructured":"Zhang ZY (2017) Drugging the undruggable: therapeutic potential of targeting protein tyrosine phosphatases. Acc Chem Res 50(1):122\u2013129. https:\/\/doi.org\/10.1021\/acs.accounts.6b00537","journal-title":"Acc Chem Res"},{"issue":"11","key":"11650_CR14","doi-asserted-by":"publisher","first-page":"18414","DOI":"10.3390\/molecules191118414","volume":"19","author":"AK Brenner","year":"2014","unstructured":"Brenner AK, Reikvam H, Lavecchia A, Bruserud \u00d8 (2014) Therapeutic targeting the cell division cycle 25 (CDC25) phosphatases in human acute myeloid leukemia\u2013the possibility to target several kinases through inhibition of the various CDC25 isoforms. Molecules 19(11):18414\u201318447. https:\/\/doi.org\/10.3390\/molecules191118414","journal-title":"Molecules"},{"key":"11650_CR15","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1186\/s12935-020-01304-w","volume":"20","author":"K Liu","year":"2020","unstructured":"Liu K, Zheng M, Lu R, Du J, Zhao Q, Li Z, Li Y, Zhang S (2020) The role of CDC25C in cell cycle regulation and clinical cancer therapy: a systematic review. Cancer Cell Int 20:213. https:\/\/doi.org\/10.1186\/s12935-020-01304-w","journal-title":"Cancer Cell Int"},{"issue":"5","key":"11650_CR16","doi-asserted-by":"publisher","first-page":"1061","DOI":"10.1042\/BCJ20200511","volume":"478","author":"KA Young","year":"2021","unstructured":"Young KA, Biggins L, Sharpe HJ (2021) Protein tyrosine phosphatases in cell adhesion. Biochem J 478(5):1061\u20131083. https:\/\/doi.org\/10.1042\/BCJ20200511","journal-title":"Biochem J"},{"issue":"5","key":"11650_CR17","doi-asserted-by":"publisher","first-page":"e2769","DOI":"10.1038\/cddis.2017.177","volume":"8","author":"B Hilmarsdottir","year":"2017","unstructured":"Hilmarsdottir B, Briem E, Halldorsson S, Kricker J, Ingthorsson S, Gustafsdottir S, M\u00e6landsmo GM, Magnusson MK, Gudjonsson T (2017) Inhibition of PTP1B disrupts cell-cell adhesion and induces anoikis in breast epithelial cells. Cell Death Dis 8(5):e2769. https:\/\/doi.org\/10.1038\/cddis.2017.177","journal-title":"Cell Death Dis"},{"key":"11650_CR18","doi-asserted-by":"publisher","first-page":"145","DOI":"10.3389\/fonc.2018.00145","volume":"8","author":"V Gkretsi","year":"2018","unstructured":"Gkretsi V, Stylianopoulos T (2018) Cell adhesion and matrix stiffness: coordinating cancer cell invasion and metastasis. Front Oncol 8:145. https:\/\/doi.org\/10.3389\/fonc.2018.00145","journal-title":"Front Oncol"},{"issue":"5","key":"11650_CR19","doi-asserted-by":"publisher","first-page":"459","DOI":"10.1016\/j.ceb.2005.08.009","volume":"17","author":"J Lilien","year":"2005","unstructured":"Lilien J, Balsamo J (2005) The regulation of cadherin-mediated adhesion by tyrosine phosphorylation\/dephosphorylation of beta-catenin. Curr Opin Cell Biol 17(5):459\u2013465. https:\/\/doi.org\/10.1016\/j.ceb.2005.08.009","journal-title":"Curr Opin Cell Biol"},{"issue":"6964","key":"11650_CR20","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1038\/nature02093","volume":"426","author":"JP Rayapureddi","year":"2003","unstructured":"Rayapureddi JP, Kattamuri C, Steinmetz BD, Frankfort BJ, Ostrin EJ, Mardon G, Hegde RS (2003) Eyes absent represents a class of protein tyrosine phosphatases. Nature 426(6964):295\u2013298. https:\/\/doi.org\/10.1038\/nature02093","journal-title":"Nature"},{"issue":"2","key":"11650_CR21","doi-asserted-by":"publisher","first-page":"140","DOI":"10.1016\/j.ceb.2009.01.028","volume":"21","author":"T Hunter","year":"2009","unstructured":"Hunter T (2009) Tyrosine phosphorylation: thirty years and counting. Curr Opin Cell Biol 21(2):140\u2013146. https:\/\/doi.org\/10.1016\/j.ceb.2009.01.028","journal-title":"Curr Opin Cell Biol"},{"key":"11650_CR22","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1007\/978-1-4939-3649-6_3","volume-title":"Non-transmembrane PTPs in cancer. Protein Tyrosine Phosphatases in Cancer","author":"WJAJ Hendriks","year":"2016","unstructured":"Hendriks WJAJ (2016) and Frank-D. B\u00f6hmer. Non-transmembrane PTPs in cancer. Protein tyrosine phosphatases in cancer. Springer, New York, pp 47\u2013113. https:\/\/doi.org\/10.1007\/978-1-4939-3649-6_3"},{"issue":"30","key":"11650_CR23","doi-asserted-by":"publisher","first-page":"3885","DOI":"10.1038\/onc.2014.326","volume":"34","author":"S Zhao","year":"2015","unstructured":"Zhao S, Sedwick D, Wang Z (2015) Genetic alterations of protein tyrosine phosphatases in human cancers. Oncogene 34(30):3885\u20133894. https:\/\/doi.org\/10.1038\/onc.2014.326","journal-title":"Oncogene"},{"issue":"3","key":"11650_CR24","doi-asserted-by":"publisher","first-page":"30","DOI":"10.3892\/ijo.2025.5843","volume":"68","author":"N Zhang","year":"2026","unstructured":"Zhang N, Wang T, Bai B, Zhang X, Xu W, Chen W, Yu Y, Wang B (2026) PTPN18 functions as a tumor suppressor in breast cancer by negatively regulating cyclin E. Int J Oncol 68(3):30. https:\/\/doi.org\/10.3892\/ijo.2025.5843","journal-title":"Int J Oncol"},{"issue":"1","key":"11650_CR25","doi-asserted-by":"publisher","first-page":"e30447","DOI":"10.1371\/journal.pone.0030447","volume":"7","author":"PD Vermeer","year":"2012","unstructured":"Vermeer PD, Bell M, Lee K, Vermeer DW, Wieking BG, Bilal E, Bhanot G, Drapkin RI, Ganesan S, Klingelhutz AJ, Hendriks WJ, Lee JH (2012) ErbB2, EphrinB1, Src kinase and PTPN13 signaling complex regulates MAP kinase signaling in human cancers. PLoS ONE 7(1):e30447. https:\/\/doi.org\/10.1371\/journal.pone.0030447","journal-title":"PLoS ONE"},{"key":"11650_CR26","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1016\/j.phrs.2019.04.011","volume":"144","author":"C Lee","year":"2019","unstructured":"Lee C, Rhee I (2019) Important roles of protein tyrosine phosphatase PTPN12 in tumor progression. Pharmacol Res 144:73\u201378. https:\/\/doi.org\/10.1016\/j.phrs.2019.04.011","journal-title":"Pharmacol Res"},{"issue":"1","key":"11650_CR27","doi-asserted-by":"publisher","first-page":"19","DOI":"10.3892\/ol.2022.13605","volume":"25","author":"S Li","year":"2022","unstructured":"Li S, Wang X, Li Q, Li C (2022) Role of SHP2\/PTPN11 in the occurrence and prognosis of cancer: a systematic review and meta-analysis. Oncol Lett 25(1):19. https:\/\/doi.org\/10.3892\/ol.2022.13605","journal-title":"Oncol Lett"},{"issue":"1","key":"11650_CR28","doi-asserted-by":"publisher","first-page":"e12873","DOI":"10.1016\/j.heliyon.2023.e12873","volume":"9","author":"X Tang","year":"2023","unstructured":"Tang X, Sui X, Liu Y (2023) Immune checkpoint PTPN2 predicts prognosis and immunotherapy response in human cancers. Heliyon 9(1):e12873. https:\/\/doi.org\/10.1016\/j.heliyon.2023.e12873","journal-title":"Heliyon"},{"issue":"40","key":"11650_CR29","doi-asserted-by":"publisher","first-page":"e30826","DOI":"10.1097\/MD.0000000000030826","volume":"101","author":"J Zhou","year":"2022","unstructured":"Zhou J, Guo H, Zhang Y, Liu H, Dou Q (2022) The role of PTP1B (PTPN1) in the prognosis of solid tumors: a meta-analysis. Med (Baltim) 101(40):e30826. https:\/\/doi.org\/10.1097\/MD.0000000000030826","journal-title":"Med (Baltim)"},{"issue":"1","key":"11650_CR30","doi-asserted-by":"publisher","first-page":"23083","DOI":"10.1038\/s41598-024-74037-9","volume":"14","author":"P Cui","year":"2024","unstructured":"Cui P, Lian J, Liu Y, Zhang D, Lin Y, Lu L, Ye L, Chen H, An S, Huang J, Liang H (2024) Pan-cancer analysis of the prognostic and immunological roles of SHP-1\/ptpn6. Sci Rep 14(1):23083. https:\/\/doi.org\/10.1038\/s41598-024-74037-9","journal-title":"Sci Rep"},{"issue":"5","key":"11650_CR31","doi-asserted-by":"publisher","first-page":"867","DOI":"10.1111\/j.1742-4658","volume":"275","author":"L Tabernero","year":"2008","unstructured":"Tabernero L, Aricescu AR, Jones EY, Szedlacsek SE (2008) Protein tyrosine phosphatases: structure-function relationships. FEBS J 275(5):867\u2013882. https:\/\/doi.org\/10.1111\/j.1742-4658","journal-title":"FEBS J"},{"key":"11650_CR32","doi-asserted-by":"crossref","unstructured":"Burke TR Jr, Zhang ZY (1998) Protein-tyrosine phosphatases: structure, mechanism, and inhibitor discovery. Biopolymers 47(3):225\u2013241. https:\/\/doi.org\/10.1002\/(SICI)1097-0282(1998)47:3%3C225::AID-BIP3%3E3.0.CO;2-O","DOI":"10.1002\/(SICI)1097-0282(1998)47:3<225::AID-BIP3>3.0.CO;2-O"},{"key":"11650_CR33","doi-asserted-by":"publisher","first-page":"209","DOI":"10.1146\/annurev.pharmtox.42.083001","volume":"42","author":"ZY Zhang","year":"2002","unstructured":"Zhang ZY (2002) Protein tyrosine phosphatases: structure and function, substrate specificity, and inhibitor development. Annu Rev Pharmacol Toxicol 42:209\u2013234. https:\/\/doi.org\/10.1146\/annurev.pharmtox.42.083001","journal-title":"Annu Rev Pharmacol Toxicol"},{"issue":"14","key":"11650_CR34","doi-asserted-by":"publisher","first-page":"2225","DOI":"10.1089\/ars.2013.5710","volume":"20","author":"JL Low","year":"2014","unstructured":"Low JL, Chai CL, Yao SQ (2014) Bidentate inhibitors of protein tyrosine phosphatases. Antioxid Redox Signal 20(14):2225\u20132250. https:\/\/doi.org\/10.1089\/ars.2013.5710","journal-title":"Antioxid Redox Signal"},{"issue":"13","key":"11650_CR35","doi-asserted-by":"publisher","first-page":"7027","DOI":"10.3390\/ijms23137027","volume":"23","author":"R Liu","year":"2022","unstructured":"Liu R, Mathieu C, Berthelet J, Zhang W, Dupret JM, Rodrigues Lima F (2022) Human protein tyrosine phosphatase 1B (PTP1B): from structure to clinical inhibitor perspectives. Int J Mol Sci 23(13):7027. https:\/\/doi.org\/10.3390\/ijms23137027","journal-title":"Int J Mol Sci"},{"issue":"6","key":"11650_CR36","doi-asserted-by":"publisher","first-page":"938","DOI":"10.1021\/acscentsci.5c00041","volume":"11","author":"T Shi","year":"2025","unstructured":"Shi T, Li Y, Yang J, Weng W, Zhang M, Shu J, Qian Y, Zhang T, Hu W (2025) Multicatalysis-enabled multicomponent reactions generate a PTP1B inhibitor. ACS Cent Sci 11(6):938\u2013949. https:\/\/doi.org\/10.1021\/acscentsci.5c00041","journal-title":"ACS Cent Sci"},{"key":"11650_CR37","doi-asserted-by":"publisher","first-page":"3151","DOI":"10.3762\/bjoc.20.261","volume":"20","author":"L Campos-Prieto","year":"2024","unstructured":"Campos-Prieto L, Garc\u00eda-Rey A, Sotelo E, Mallo-Abreu A (2024) Multicomponent reactions driving the discovery and optimization of agents targeting central nervous system pathologies. Beilstein J Org Chem 20:3151\u20133173. https:\/\/doi.org\/10.3762\/bjoc.20.261","journal-title":"Beilstein J Org Chem"},{"issue":"4","key":"11650_CR38","doi-asserted-by":"publisher","first-page":"376","DOI":"10.1021\/acsmedchemlett.3c00012","volume":"14","author":"MJ Buskes","year":"2023","unstructured":"Buskes MJ, Coffin A, Troast DM, Stein R, Blanco MJ (2023) Accelerating drug discovery: synthesis of complex chemotypes via multicomponent reactions. ACS Med Chem Lett 14(4):376\u2013385. https:\/\/doi.org\/10.1021\/acsmedchemlett.3c00012","journal-title":"ACS Med Chem Lett"},{"issue":"6","key":"11650_CR39","doi-asserted-by":"publisher","first-page":"3083","DOI":"10.1021\/cr100233r","volume":"112","author":"A D\u00f6mling","year":"2012","unstructured":"D\u00f6mling A, Wang W, Wang K (2012) Chemistry and biology of multicomponent reactions. Chem Rev 112(6):3083\u20133135. https:\/\/doi.org\/10.1021\/cr100233r","journal-title":"Chem Rev"},{"key":"11650_CR40","doi-asserted-by":"publisher","unstructured":"Hulme C, Ayaz M, Martinez-Ariza G, Medda F, Shaw A (2015) Recent advances in multicomponent reaction chemistry. In: Czechtizky W, Hamley P (eds.) Small molecule medicinal chemistry. https:\/\/doi.org\/10.1002\/9781118771723.ch6","DOI":"10.1002\/9781118771723.ch6"},{"issue":"2","key":"11650_CR41","doi-asserted-by":"publisher","first-page":"1447","DOI":"10.1039\/d4ra06681b","volume":"15","author":"M Tandi","year":"2025","unstructured":"Tandi M, Sharma V, Gopal B, Sundriyal S (2025) Multicomponent reactions (MCRs) yielding medicinally relevant rings: a recent update and chemical space analysis of the scaffolds. RSC Adv 15(2):1447\u20131489. https:\/\/doi.org\/10.1039\/d4ra06681b","journal-title":"RSC Adv"},{"issue":"7","key":"11650_CR42","doi-asserted-by":"publisher","first-page":"1488","DOI":"10.3390\/biomedicines10071488","volume":"10","author":"P Nadal Rodr\u00edguez","year":"2022","unstructured":"Nadal Rodr\u00edguez P, Ghashghaei O, Bag\u00e1n A, Escolano C, Lavilla R (2022) Heterocycle-based multicomponent reactions in drug discovery: from hit finding to rational design. Biomedicines 10(7):1488. https:\/\/doi.org\/10.3390\/biomedicines10071488","journal-title":"Biomedicines"},{"issue":"19","key":"11650_CR43","doi-asserted-by":"publisher","first-page":"2849","DOI":"10.1016\/s0960-894x(99)00497-7","volume":"9","author":"G Bergnes","year":"1999","unstructured":"Bergnes G, Gilliam CL, Boisclair MD, Blanchard JL, Blake KV, Epstein DM, Pal K (1999) Generation of an Ugi library of phosphate mimic-containing compounds and identification of novel dual specific phosphatase inhibitors. Bioorg Med Chem Lett 9(19):2849\u20132854. https:\/\/doi.org\/10.1016\/s0960-894x(99)00497-7","journal-title":"Bioorg Med Chem Lett"},{"issue":"37","key":"11650_CR44","doi-asserted-by":"publisher","first-page":"4453","DOI":"10.1039\/c2cc31294h","volume":"48","author":"J Ge","year":"2012","unstructured":"Ge J, Cheng X, Tan LP, Yao SQ (2012) Ugi reaction-assisted rapid assembly of affinity-based probes against potential protein tyrosine phosphatases. Chem Commun (Camb) 48(37):4453\u20134455. https:\/\/doi.org\/10.1039\/c2cc31294h","journal-title":"Chem Commun (Camb)"},{"issue":"21","key":"11650_CR45","doi-asserted-by":"publisher","first-page":"4856","DOI":"10.1021\/ol101988q","volume":"12","author":"Z Chen","year":"2010","unstructured":"Chen Z, Wu J (2010) Efficient generation of biologically active H-pyrazolo [5, 1-a] isoquinolines via multicomponent reaction. Org Lett 12(21):4856\u20134859. https:\/\/doi.org\/10.1021\/ol101988q","journal-title":"Org Lett"},{"key":"11650_CR46","doi-asserted-by":"publisher","unstructured":"Yang J, Yu X, Wu JJS (2014) A facile route to H-Pyrazolo [5, 1-a] isoquinolines through a multicomponent reaction of 2-Alkynylbenzaldehyde, Sulfonylhydrazine, and Benzyne. 46(10):1362\u20131366. https:\/\/doi.org\/10.1055\/s-0033-1341102","DOI":"10.1055\/s-0033-1341102"},{"issue":"4","key":"11650_CR47","doi-asserted-by":"publisher","first-page":"1105","DOI":"10.1016\/j.bmcl.2016.11.055","volume":"27","author":"S Dong","year":"2017","unstructured":"Dong S, Lei Y, Jia S, Gao L, Li J, Zhu T, Liu S, Hu W (2017) Discovery of core-structurally novel PTP1B inhibitors with specific selectivity containing oxindole-fused spirotetrahydrofurochroman by one-pot reaction. Bioorg Med Chem Lett 27(4):1105\u20131108. https:\/\/doi.org\/10.1016\/j.bmcl.2016.11.055","journal-title":"Bioorg Med Chem Lett"},{"key":"11650_CR48","doi-asserted-by":"publisher","unstructured":"Jing C, Li Z, Jia K, Chen C, Liu X, Wang B, Hu W, Li J, Zhu T, Dong S (2017) Discovery of bisindole as a novel scaffold for protein tyrosine phosphatase 1B inhibitors. Arch Pharm (Weinheim). https:\/\/doi.org\/10.1002\/ardp.201600173","DOI":"10.1002\/ardp.201600173"},{"issue":"20","key":"11650_CR49","doi-asserted-by":"publisher","first-page":"2064","DOI":"10.1039\/c3cc38961h","volume":"49","author":"R He","year":"2013","unstructured":"He R, Zeng LF, He Y, Wu L, Gunawan AM, Zhang ZY (2013) Organocatalytic multicomponent reaction for the acquisition of a selective inhibitor of mPTPB, a virulence factor of tuberculosis. Chem Commun (Camb) 49(20):2064\u20132066. https:\/\/doi.org\/10.1039\/c3cc38961h","journal-title":"Chem Commun (Camb)"},{"key":"11650_CR50","doi-asserted-by":"publisher","unstructured":"Sini K, Sebastian S, Arun (2025) Expanding the synthetic horizons of Iqbal MCR to heterocyclics: bioisosteric \u03b1-Acylaminopyrazoles as Ugi \u03b1\u2010Acylamino carboxamide mimetics. ChemistrySelect 10(31):e04150. https:\/\/doi.org\/10.1002\/slct.202504150","DOI":"10.1002\/slct.202504150"},{"issue":"13","key":"11650_CR51","doi-asserted-by":"publisher","first-page":"9198","DOI":"10.1021\/acs.joc.3c02769","volume":"89","author":"SA K S S","year":"2024","unstructured":"K S S SA (2024) Fragment-based design and synthesis of symmetrical bis-peptidotriazoles using alkylidene bis-amide formations and subsequent triazole ligation with \u03b2-Acetamido carbonyl scaffolds. J Org Chem 89(13):9198\u20139209. https:\/\/doi.org\/10.1021\/acs.joc.3c02769","journal-title":"J Org Chem"},{"issue":"13","key":"11650_CR52","doi-asserted-by":"publisher","first-page":"7027","DOI":"10.3390\/ijms23137027","volume":"23","author":"R Liu","year":"2022","unstructured":"Liu R, Mathieu C, Berthelet J, Zhang W, Dupret JM, Rodrigues Lima F (2022) Human protein tyrosine phosphatase 1B (PTP1B): from structure to clinical inhibitor perspectives. Int J Mol Sci 23(13):7027. https:\/\/doi.org\/10.3390\/ijms23137027","journal-title":"Int J Mol Sci"},{"issue":"6","key":"11650_CR53","doi-asserted-by":"publisher","first-page":"426","DOI":"10.1021\/ar020127o","volume":"36","author":"TR Burke Jr","year":"2003","unstructured":"Burke TR Jr, Lee K (2003) Phosphotyrosyl mimetics in the development of signal transduction inhibitors. Acc Chem Res 36(6):426\u2013433. https:\/\/doi.org\/10.1021\/ar020127o","journal-title":"Acc Chem Res"},{"key":"11650_CR54","doi-asserted-by":"publisher","DOI":"10.1039\/D5CY00829H","author":"M Khurana","year":"2025","unstructured":"Khurana M, Satish Kumar A (2025) Metal\u2013organic frameworks as catalytic platforms for multicomponent reactions (MCRs): mechanistic and design insights (2020\u20132025 overview). Catal Sci Technol. https:\/\/doi.org\/10.1039\/D5CY00829H","journal-title":"Catal Sci Technol"},{"issue":"27","key":"11650_CR55","doi-asserted-by":"publisher","first-page":"3110","DOI":"10.2174\/0929867322666150812150036","volume":"22","author":"L Fanzani","year":"2015","unstructured":"Fanzani L, Porta F, Meneghetti F, Villa S, Gelain A, Lucarelli AP, Parisini E (2015) Mycobacterium tuberculosis low molecular weight phosphatases (MPtpA and MPtpB): from biological insight to inhibitors. Curr Med Chem 22(27):3110\u20133132. https:\/\/doi.org\/10.2174\/0929867322666150812150036","journal-title":"Curr Med Chem"},{"issue":"2","key":"11650_CR56","doi-asserted-by":"publisher","first-page":"219","DOI":"10.1016\/j.ymeth.2013.08.013","volume":"65","author":"KR Martin","year":"2014","unstructured":"Martin KR, Narang P, Medina-Franco JL, Meurice N, MacKeigan JP (2014) Integrating virtual and biochemical screening for protein tyrosine phosphatase inhibitor discovery. Methods 65(2):219\u2013228. https:\/\/doi.org\/10.1016\/j.ymeth.2013.08.013","journal-title":"Methods"},{"issue":"3","key":"11650_CR57","doi-asserted-by":"publisher","first-page":"463","DOI":"10.1021\/ar800214s","volume":"42","author":"B Ganem","year":"2009","unstructured":"Ganem B (2009) Strategies for innovation in multicomponent reaction design. Acc Chem Res 42(3):463\u2013472. https:\/\/doi.org\/10.1021\/ar800214s","journal-title":"Acc Chem Res"},{"issue":"1","key":"11650_CR58","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1016\/j.ymeth.2004.07.002","volume":"35","author":"J Montalibet","year":"2005","unstructured":"Montalibet J, Skorey KI, Kennedy BP (2005) Protein tyrosine phosphatase: enzymatic assays. Methods 35(1):2\u20138. https:\/\/doi.org\/10.1016\/j.ymeth.2004.07.002","journal-title":"Methods"},{"issue":"16","key":"11650_CR59","doi-asserted-by":"publisher","first-page":"5716","DOI":"10.1039\/c5an00970g","volume":"140","author":"J Zhang","year":"2015","unstructured":"Zhang J, Lv J, Wang X, Li D, Wang Z, Li G (2015) A simple and visible colorimetric method through Zr(4+)-phosphate coordination for the assay of protein tyrosine phosphatase 1B and screening of its inhibitors. Analyst 140(16):5716\u20135723. https:\/\/doi.org\/10.1039\/c5an00970g","journal-title":"Analyst"},{"issue":"17","key":"11650_CR60","doi-asserted-by":"publisher","first-page":"2095","DOI":"10.2174\/092986709788612693","volume":"16","author":"MA Blaskovich","year":"2009","unstructured":"Blaskovich MA (2009) Drug discovery and protein tyrosine phosphatases. Curr Med Chem 16(17):2095\u20132176. https:\/\/doi.org\/10.2174\/092986709788612693","journal-title":"Curr Med Chem"},{"issue":"1","key":"11650_CR61","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1089\/ars.2010.3611","volume":"15","author":"JJ Tanner","year":"2011","unstructured":"Tanner JJ, Parsons ZD, Cummings AH, Zhou H, Gates KS (2011) Redox regulation of protein tyrosine phosphatases: structural and chemical aspects. Antioxid Redox Signal 15(1):77\u201397","journal-title":"Antioxid Redox Signal"},{"issue":"5","key":"11650_CR62","doi-asserted-by":"publisher","first-page":"633","DOI":"10.1016\/s1367-5931(98)80095-1","volume":"2","author":"JM Denu","year":"1998","unstructured":"Denu JM, Dixon JE (1998) Protein tyrosine phosphatases: mechanisms of catalysis and regulation. Curr Opin Chem Biol 2(5):633\u2013641. https:\/\/doi.org\/10.1016\/s1367-5931(98)80095-1","journal-title":"Curr Opin Chem Biol"},{"issue":"4","key":"11650_CR63","doi-asserted-by":"publisher","first-page":"345","DOI":"10.1093\/jb\/mvr104","volume":"150","author":"A Ostman","year":"2011","unstructured":"Ostman A, Frijhoff J, Sandin A, B\u00f6hmer FD (2011) Regulation of protein tyrosine phosphatases by reversible oxidation. J Biochem 150(4):345\u2013356. https:\/\/doi.org\/10.1093\/jb\/mvr104","journal-title":"J Biochem"},{"issue":"1","key":"11650_CR64","doi-asserted-by":"publisher","first-page":"174","DOI":"10.1016\/j.cbpa.2010.10.022","volume":"15","author":"PA Johnston","year":"2011","unstructured":"Johnston PA (2011) Redox cycling compounds generate H2O2 in HTS buffers containing strong reducing reagents\u2013real hits or promiscuous artifacts? Curr Opin Chem Biol 15(1):174\u2013182. https:\/\/doi.org\/10.1016\/j.cbpa.2010.10.022","journal-title":"Curr Opin Chem Biol"},{"issue":"3","key":"11650_CR65","doi-asserted-by":"publisher","first-page":"261","DOI":"10.1016\/j.ymeth.2007.02.008","volume":"42","author":"S Zhang","year":"2007","unstructured":"Zhang S, Chen L, Kumar S, Wu L, Lawrence DS, Zhang ZY (2007) An affinity-based fluorescence polarization assay for protein tyrosine phosphatases. Methods 42(3):261\u2013267. https:\/\/doi.org\/10.1016\/j.ymeth.2007.02.008","journal-title":"Methods"},{"issue":"7","key":"11650_CR66","doi-asserted-by":"publisher","first-page":"739","DOI":"10.2174\/1568026033452302","volume":"3","author":"WQ Wang","year":"2003","unstructured":"Wang WQ, Sun JP, Zhang ZY (2003) An overview of the protein tyrosine phosphatase superfamily. Curr Top Med Chem 3(7):739\u2013748. https:\/\/doi.org\/10.2174\/1568026033452302","journal-title":"Curr Top Med Chem"},{"issue":"2","key":"11650_CR67","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1016\/j.ymeth.2013.07.032","volume":"65","author":"IE Gulerez","year":"2014","unstructured":"Gulerez IE, Gehring K (2014) X-ray crystallography and NMR as tools for the study of protein tyrosine phosphatases. Methods 65(2):175\u2013183. https:\/\/doi.org\/10.1016\/j.ymeth.2013.07.032","journal-title":"Methods"},{"issue":"5","key":"11650_CR68","doi-asserted-by":"publisher","first-page":"878","DOI":"10.4014\/jmb.1701.01079","volume":"27","author":"RH Reddy","year":"2017","unstructured":"Reddy RH, Kim H, Cha S, Lee B, Kim YJ (2017) Structure-based virtual screening of protein tyrosine phosphatase inhibitors: significance, challenges, and solutions. J Microbiol Biotechnol 27(5):878\u2013895. https:\/\/doi.org\/10.4014\/jmb.1701.01079","journal-title":"J Microbiol Biotechnol"},{"issue":"1","key":"11650_CR69","doi-asserted-by":"publisher","first-page":"390","DOI":"10.1021\/jm2012062","volume":"55","author":"LD Chiaradia","year":"2012","unstructured":"Chiaradia LD, Martins PG, Cordeiro MN, Guido RV, Ecco G, Andricopulo AD, Yunes RA, Vernal J, Nunes RJ, Terenzi H (2012) Synthesis, biological evaluation, and molecular modeling of chalcone derivatives as potent inhibitors of Mycobacterium tuberculosis protein tyrosine phosphatases (PtpA and PtpB). J Med Chem 55(1):390\u2013402. https:\/\/doi.org\/10.1021\/jm2012062","journal-title":"J Med Chem"},{"issue":"50","key":"11650_CR70","doi-asserted-by":"publisher","first-page":"17465","DOI":"10.1021\/jacs.8b07652","volume":"140","author":"DC Davis","year":"2018","unstructured":"Davis DC, Hoch DG, Wu L, Abegg D, Martin BS, Zhang ZY, Adibekian A, Dai M (2018) Total synthesis, biological evaluation, and target identification of rare abies sesquiterpenoids. J Am Chem Soc 140(50):17465\u201317473. https:\/\/doi.org\/10.1021\/jacs.8b07652","journal-title":"J Am Chem Soc"}],"container-title":["Molecular Diversity"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11030-026-11650-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11030-026-11650-y","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11030-026-11650-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T06:05:31Z","timestamp":1793858731000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11030-026-11650-y"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,9]]},"references-count":70,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2026,12]]}},"alternative-id":["11650"],"URL":"https:\/\/doi.org\/10.1007\/s11030-026-11650-y","relation":{},"ISSN":["1573-501X"],"issn-type":[{"value":"1573-501X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,9]]},"assertion":[{"value":"23 May 2026","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"29 June 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"9 July 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"Not applicable.","order":1,"name":"Ethics","label":"Consent for publication","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","label":"Conflict of interest","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Not applicable.","order":3,"name":"Ethics","label":"Ethical approval","group":{"name":"EthicsHeading","label":"Declarations"}}]}}