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Cell <b>42<\/b>, 581\u2013588.","journal-title":"Cell","ISSN":"https:\/\/id.crossref.org\/issn\/0092-8674","issn-type":"print"},{"key":"2","first-page":"571","year":"1988","unstructured":"2) Takahashi, M., Buma, Y., Iwamoto, T., Inaguma, Y., Ikeda, H. and Hiai, H. (1988) Cloning and expression of the <i>ret<\/i> proto-oncogene encoding a tyrosine kinase with two potential transmembrane domains. Oncogene <b>13<\/b>, 571\u2013578.","journal-title":"Oncogene","ISSN":"https:\/\/id.crossref.org\/issn\/0950-9232","issn-type":"print"},{"key":"3","first-page":"1087","year":"1993","unstructured":"3) Iwamoto, T., Taniguchi, M., Asai, N., Ohkusu, K., Nakashima, I. and Takahashi, M. (1993) cDNA cloning of mouse <i>ret<\/i> proto-oncogene and its sequence similarity to the cadherin superfamily. Oncogene <b>8<\/b>, 1087\u20131091.","journal-title":"Oncogene","ISSN":"https:\/\/id.crossref.org\/issn\/0950-9232","issn-type":"print"},{"key":"4","doi-asserted-by":"crossref","unstructured":"4) Ib\u00e1\u00f1ez, C.F. (2013) Structure and physiology of the RET receptor tyrosine kinase. Cold Spring Harb. Perspect. Biol. <b>5<\/b>, a009134.","DOI":"10.1101\/cshperspect.a009134"},{"key":"5","doi-asserted-by":"crossref","unstructured":"5) Takahashi, M. (2001) The GDNF\/RET signaling pathway and human diseases. Cytokine Growth Factor Rev. <b>12<\/b>, 361\u2013373.","DOI":"10.1016\/S1359-6101(01)00012-0"},{"key":"6","doi-asserted-by":"publisher","unstructured":"6) Nozaki, C., Asai, N., Murakami, H., Iwashita, T., Iwata, Y., Horibe, K. et al. (1998) Calcium-dependent Ret activation by GDNF and neurturin. Oncogene <b>16<\/b>, 293\u2013299.","DOI":"10.1038\/sj.onc.1201548"},{"key":"7","doi-asserted-by":"crossref","unstructured":"7) Kawamoto, Y., Takeda, K., Okuno, Y., Yamakawa, Y., Ito, Y., Taguchi, R. et al. (2004) Identification of RET autophosphorylation sites by mass spectrometry. J. Biol. Chem. <b>279<\/b>, 14213\u201314224.","DOI":"10.1074\/jbc.M312600200"},{"key":"8","doi-asserted-by":"crossref","unstructured":"8) Kawai, K. and Takahashi, M. (2020) Intracellular RET signaling pathways activated by GDNF. Cell Tissue Res. <b>382<\/b>, 113\u2013123.","DOI":"10.1007\/s00441-020-03262-1"},{"key":"9","doi-asserted-by":"crossref","unstructured":"9) Asai, N., Murakami, H., Iwashita, T. and Takahashi, M. (1996) A mutation at tyrosine 1062 in MEN2A-Ret and MEN2B-Ret impairs their transforming activity and association with shc adaptor proteins. J. Biol. Chem. <b>271<\/b>, 17644\u201317649.","DOI":"10.1074\/jbc.271.30.17644"},{"key":"10","doi-asserted-by":"crossref","unstructured":"10) Hayashi, H., Ichihara, M., Iwashita, T., Murakami, H., Shimono, Y., Kawai, K. et al. (2000) Characterization of intracellular signals via tyrosine 1062 in RET activated by glial cell line-derived neurotrophic factor. Oncogene <b>19<\/b>, 4469\u20134475.","DOI":"10.1038\/sj.onc.1203799"},{"key":"11","doi-asserted-by":"crossref","unstructured":"11) Kurokawa, K., Iwashita, T., Murakami, H., Hayashi, H., Kawai, K. and Takahashi, M. (2001) Identification of SNT\/FRS2 docking site on RET receptor tyrosine kinase and its role for signal transduction. Oncogene <b>20<\/b>, 1929\u20131938.","DOI":"10.1038\/sj.onc.1204290"},{"key":"12","doi-asserted-by":"crossref","unstructured":"12) Borrello, M.G., Alberti, L., Arighi, E., Bongarzone, I., Battistini, C., Bardelli, A. et al. (1996) The full oncogenic activity of Ret\/ptc2 depends on tyrosine 539, a docking site for phospholipace C-g. Mol. Cell. Biol. <b>16<\/b>, 2151\u20132163.","DOI":"10.1128\/MCB.16.5.2151"},{"key":"13","first-page":"458","year":"1993","unstructured":"13) Mulligan, L.M., Kwok, J.B.J., Healey, C.S., Elsdon, M.J., Eng, C., Gardner, E. et al. (1993) Germ-line mutations of the <i>RET<\/i> proto-oncogene in multiple endocrine neoplasia type 2A. Nature <b>363<\/b>, 458\u2013460.","journal-title":"?Nature","ISSN":"https:\/\/id.crossref.org\/issn\/0028-0836","issn-type":"print"},{"key":"14","doi-asserted-by":"crossref","unstructured":"14) Donis-Keller, H., Dou, S., Chi, D., Carlson, K.M., Toshima, K., Lairmore, T.C. et al. (1993) Mutations in the <i>RET<\/i> protooncogene are associated with MEN 2A and FMTC. Hum. Mol. Genet. <b>2<\/b>, 851\u2013856.","DOI":"10.1093\/hmg\/2.7.851"},{"key":"15","first-page":"375","year":"1994","unstructured":"15) Hofstra, R.M.W., Landsvater, R.M., Ceccherini, I., Stulp, R.P., Stelwagen, T., Luo, Y. et al. (1994) A mutation in the <i>RET<\/i> proto-oncogene associated with multiple endocrine neoplasia type 2B and sporadic medullary thyroid carcinoma. Nature <b>367<\/b>, 375\u2013376.","journal-title":"?Nature","ISSN":"https:\/\/id.crossref.org\/issn\/0028-0836","issn-type":"print"},{"key":"16","doi-asserted-by":"crossref","unstructured":"16) Carlson, K.M., Dou, S., Chi, D., Scavarda, N., Toshima, K., Jackson, C.E. et al. (1994) Single missense mutation in the tyrosine kinase catalytic domain of the <i>RET<\/i> protooncogene is associated with multiple endocrine neoplasia type 2B. Proc. Natl. Acad. Sci. U.S.A. <b>91<\/b>, 1579\u20131583.","DOI":"10.1073\/pnas.91.4.1579"},{"key":"17","doi-asserted-by":"publisher","unstructured":"17) Grieco, M., Santoro, M., Berlingieri, M.T., Melillo, R.M., Donghi, R., Bongarzone, I. et al. (1990) PTC is a novel rearranged form of the ret proto-oncogene and is frequently detected in vivo in human thyroid papillary carcinomas. Cell <b>60<\/b>, 557\u2013563.","DOI":"10.1016\/0092-8674(90)90659-3"},{"key":"18","doi-asserted-by":"crossref","unstructured":"18) Nikiforov, Y.E. (2002) <i>RET\/PTC<\/i> rearrangement in thyroid tumors. Endocr. Pathol. <b>13<\/b>, 3\u201316.","DOI":"10.1385\/EP:13:1:03"},{"key":"19","doi-asserted-by":"crossref","unstructured":"19) Romei, C., Ciampi, R. and Elisei, R. (2016) A comprehensive overview of the role of the <i>RET<\/i> proto-oncogene in thyroid carcinoma. Nat. Rev. Endocrinol. <b>12<\/b>, 192\u2013202.","DOI":"10.1038\/nrendo.2016.11"},{"key":"20","doi-asserted-by":"crossref","unstructured":"20) Kohno, T., Ichikawa, H., Totoki, Y., Yasuda, K., Hiramoto, M., Nammo, T. et al. (2012) <i>KIF5B-RET<\/i> fusion in lung cancer. Nat. Med. <b>18<\/b>, 375\u2013377.","DOI":"10.1038\/nm.2644"},{"key":"21","doi-asserted-by":"crossref","unstructured":"21) Takeuchi, K., Soda, M., Togashi, Y., Suzuki, R., Sakata, S., Hatano, S. et al. (2012) RET, ROS and ALK fusions in lung cancer. Nat. Med. <b>18<\/b>, 378\u2013381.","DOI":"10.1038\/nm.2658"},{"key":"22","doi-asserted-by":"crossref","unstructured":"22) Lipson, D., Capelletti, M., Yelensky, R., Otto, G., Parker, A., Jarosz, M. et al. (2012) Identification of new <i>ALK<\/i> and <i>RET<\/i> gene fusions from colorectal and lung cancer biopsies. Nat. Med. <b>18<\/b>, 382\u2013384.","DOI":"10.1038\/nm.2673"},{"key":"23","doi-asserted-by":"crossref","unstructured":"23) Ju, Y.S., Lee, W.-C., Shin, J.-Y., Lee, S., Bleazard, T., Won, J.-K. et al. (2012) A transforming <i>KIF5B<\/i> and <i>RET<\/i> gene fusion in lung adenocarcinoma revealed from whole-genome and transcriptome sequencing. Genome Res. <b>22<\/b>, 436\u2013445.","DOI":"10.1101\/gr.133645.111"},{"key":"24","doi-asserted-by":"crossref","unstructured":"24) Sk\u00e1lov\u00e1, A., Vanecek, T., Uro-Coste, E., Bishop, J.A., Weinreb, I., Thompson, L.D.R. et al. (2018) Molecular profiling of salivary gland intraductal carcinoma revealed a subset of tumors harboring <i>NCOA4-RET<\/i> and novel <i>TRM27-RET<\/i> fusions: A report of 17 cases. Am. J. Surg. Pathol. <b>42<\/b>, 1445\u20131455.","DOI":"10.1097\/PAS.0000000000001133"},{"key":"25","first-page":"377","year":"1994","unstructured":"25) Romeo, G., Ronchetto, P., Luo, Y., Barone, v., Seri, M., Ceccherini, I. et al. (1994) Point mutations affecting the tyrosine kinase domain of the <i>RET<\/i> proto-oncogene in Hirschsprung\u2019s disease. Nature <b>367<\/b>, 377\u2013378.","journal-title":"?Nature","ISSN":"https:\/\/id.crossref.org\/issn\/0028-0836","issn-type":"print"},{"key":"26","first-page":"378","year":"1994","unstructured":"26) Edery, P., Lyonnet, S., Mulligan, L.M., Pelet, A., Dow, E., Abel, L. et al. (1994) Mutations of the <i>RET<\/i> protooncogene in Hirschsprung\u2019s disease. Nature <b>367<\/b>, 378\u2013380.","journal-title":"?Nature","ISSN":"https:\/\/id.crossref.org\/issn\/0028-0836","issn-type":"print"},{"key":"27","doi-asserted-by":"crossref","unstructured":"27) Lin, L.F., Doherty, D.H., Lile, J.D., Bektesh, S. and Collins, F. (1993) GDNF: a glial cell line-derived neurotrophic factor for midbrain dopaminergic neurons. Science <b>260<\/b>, 1130\u20131132.","DOI":"10.1126\/science.8493557"},{"key":"28","doi-asserted-by":"crossref","unstructured":"28) Airaksinen, M.S. and Saarma, M. (2002) The GDNF family: signalling, biological functions and therapeutic value. Nat. Rev. Neurosci. <b>3<\/b>, 383\u2013394.","DOI":"10.1038\/nrn812"},{"key":"29","doi-asserted-by":"publisher","unstructured":"29) Jing, S., Wen, D., Yu, Y., Holst, P.L., Luo, Y., Fang, M. et al. (1996) GDNF-induced activation of the ret protein tyrosine kinase is mediated by GDNFR-alpha, a novel receptor for GDNF. Cell <b>85<\/b>, 1113\u20131124.","DOI":"10.1016\/S0092-8674(00)81311-2"},{"key":"30","first-page":"80","year":"1996","unstructured":"30) Treanor, J.J., Goodman, L., de Sauvage, F., Stone, D.M., Poulsen, K.T., Beck, C.D. et al. (1996) Characterization of a multicomponent receptor for GDNF. Nature <b>382<\/b>, 80\u201383.","journal-title":"?Nature","ISSN":"https:\/\/id.crossref.org\/issn\/0028-0836","issn-type":"print"},{"key":"31","first-page":"717","year":"1997","unstructured":"31) Klein, R.D., Sherman, D., Ho, W.-H., Stone, D., Bennett, G.L., Moffat, B. et al. (1997) A GPI-linked protein that interacts with Ret to form a candidate neurturin receptor. Nature <b>387<\/b>, 717\u2013721.","journal-title":"?Nature","ISSN":"https:\/\/id.crossref.org\/issn\/0028-0836","issn-type":"print"},{"key":"32","first-page":"721","year":"1997","unstructured":"32) Buj-Bello, A., Adu, J., Pinon, L.G., Horton, A., Thompson, J., Rosenthal, A. et al. (1997) Neurturin responsiveness requires a GPI-linked receptor and the <i>Ret<\/i> receptor tyrosine kinase. Nature <b>387<\/b>, 721\u2013724.","journal-title":"?Nature","ISSN":"https:\/\/id.crossref.org\/issn\/0028-0836","issn-type":"print"},{"key":"33","doi-asserted-by":"crossref","unstructured":"33) Bigalke, J.M., Aibara, S., Roth, R., Dahl, G., Gordon, E., Dorb\u00e9us, S. et al. (2019) Cryo-EM structure of the activated RET signaling complex reveals the importance of its cysteine-rich domain. Sci. Adv. <b>5<\/b>, eaau4202.","DOI":"10.1126\/sciadv.aau4202"},{"key":"34","first-page":"e47650","year":"2019","unstructured":"34) Li, J., Shang, G., Chen, Y.J., Brautigam, C.A., Liou, J., Zhang, X. et al. (2019) Cryo-EM analyses reveal the common mechanism and diversification in the activation of RET by different ligands. eLife <b>8<\/b>, e47650.","journal-title":"eLife","ISSN":"https:\/\/id.crossref.org\/issn\/2050-084X","issn-type":"print"},{"key":"35","doi-asserted-by":"crossref","unstructured":"35) Adams, S.E., Purkiss, A.G., Knowles, P.P., Nans, A., Briggs, D.C., Borg, A. et al. (2021) A two-site flexible clamp mechanism for RET-GDNF-GFRa1 assembly reveals both conformational adaptation and strict geometric spacing. Structure <b>29<\/b>, 1\u201315.","DOI":"10.1016\/j.str.2020.12.012"},{"key":"36","doi-asserted-by":"crossref","unstructured":"36) Breit, S.N., Brown, D.A. and Tsai, V.W.-W. (2021) The GDF15-GFRAL pathway in health and metabolic disease: Friend or foe? Annu. Rev. Physiol. <b>83<\/b>, 127\u2013151.","DOI":"10.1146\/annurev-physiol-022020-045449"},{"key":"37","doi-asserted-by":"publisher","unstructured":"37) Schuchardt, A., D\u2019Agati, V., Larsson-Blomberg, L., Costantini, F. and Pachnis, V. (1994) Defects in the kidney and enteric nervous system of mice lacking the tyrosine kinase receptor Ret. Nature <b>367<\/b>, 380\u2013383.","DOI":"10.1038\/367380a0"},{"key":"38","doi-asserted-by":"publisher","unstructured":"38) S\u00e1nchez, M.P., Silos-Santiago, I., Fris\u00e9n, J., He, B., Lira, S.A. and Barbacid, M. (1996) Renal agenesis and the absence of enteric neurons in mice lacking GDNF. Nature <b>382<\/b>, 70\u201373.","DOI":"10.1038\/382070a0"},{"key":"39","first-page":"73","year":"1996","unstructured":"39) Pichel, J.G., Shen, L., Sheng, H.Z., Granholm, A.C., Drago, J., Grinberg, A. et al. (1996) Defects in enteric innervation and kidney development in mice lacking GDNF. Nature <b>382<\/b>, 73\u201376.","journal-title":"?Nature","ISSN":"https:\/\/id.crossref.org\/issn\/0028-0836","issn-type":"print"},{"key":"40","first-page":"76","year":"1996","unstructured":"40) Moore, M.W., Klein, R.D., Fari\u00f1as, I., Sauer, H., Armanini, M., Phillips, H. et al. (1996) Renal and neuronal abnormalities in mice lacking GDNF. Nature <b>382<\/b>, 76\u201379.","journal-title":"?Nature","ISSN":"https:\/\/id.crossref.org\/issn\/0028-0836","issn-type":"print"},{"key":"41","doi-asserted-by":"publisher","unstructured":"41) Cacalano, G., Fari\u00f1as, I., Wang, L.-C., Hagler, K., Forgie, A., Moore, M. et al. (1998) GFR\u03b11 is an essential receptor component for GDNF in the developing nervous system and kidney. Neuron <b>21<\/b>, 53\u201362.","DOI":"10.1016\/S0896-6273(00)80514-0"},{"key":"42","doi-asserted-by":"publisher","unstructured":"42) Enomoto, H., Araki, T., Jackman, A., Heuckeroth, R.O., Snider, W.D., Johnson, E.M. Jr. et al. (1998) GFRa1-deficient mice have deficits in the enteric nervous system and kidneys. Neuron <b>21<\/b>, 317\u2013324.","DOI":"10.1016\/S0896-6273(00)80541-3"},{"key":"43","doi-asserted-by":"crossref","unstructured":"43) Jijiwa, M., Fukuda, T., Kawai, K., Nakamura, A., Kurokawa, K., Murakumo, Y. et al. (2004) A targeting mutation of tyrosine 1062 in ret causes a marked decrease of enteric neurons and renal hypoplasia. Mol. Cell. Biol. <b>24<\/b>, 8026\u20138036.","DOI":"10.1128\/MCB.24.18.8026-8036.2004"},{"key":"44","doi-asserted-by":"crossref","unstructured":"44) Wong, A., Bogni, S., Kotka, P., de Graaff, E., D\u2019Agati, V., Costantini, F. et al. (2005) Phosphotyrosine 1062 is critical for the in vivo activity of the Ret9 receptor tyrosine kinase isoform. Mol. Cell. Biol. <b>25<\/b>, 9661\u20139673.","DOI":"10.1128\/MCB.25.21.9661-9673.2005"},{"key":"45","doi-asserted-by":"crossref","unstructured":"45) Lake, J.I. and Heuckeroth, R.O. (2013) Enteric nervous system development: migration, differentiation, and disease. Am. J. Physiol. Gastrointest. Liver Physiol. <b>305<\/b>, G1\u2013G24.","DOI":"10.1152\/ajpgi.00452.2012"},{"key":"46","doi-asserted-by":"crossref","unstructured":"46) Tomuschat, C. and Puri, P. (2015) RET gene is a major risk factor for Hirschsprung\u2019s disease: a meta-analysis. Pediatr. Surg. Int. <b>31<\/b>, 701\u2013710.","DOI":"10.1007\/s00383-015-3731-y"},{"key":"47","doi-asserted-by":"crossref","unstructured":"47) Takahashi, M., Kawai, K. and Asai, N. (2020) Roles of the <i>RET<\/i> proto-oncogene in cancer and development. JMA J. <b>3<\/b>, 175\u2013181.","DOI":"10.31662\/jmaj.2020-0021"},{"key":"48","doi-asserted-by":"crossref","unstructured":"48) Iwashita, T., Murakami, H., Asai, N. and Takahashi, M. (1996) Mechanisms of Ret dysfunction by Hirschsprung mutations affecting its extracellular domain. Hum. Mol. Genet. <b>5<\/b>, 1577\u20131580.","DOI":"10.1093\/hmg\/5.10.1577"},{"key":"49","doi-asserted-by":"crossref","unstructured":"49) Carlomagno, F., De Vita, G., Berlingieri, M.T., de Franciscis, V., Melillo, R.M., Colantuoni, V. et al. (1996) Molecular heterogeneity of <i>RET<\/i> loss of function in Hirschsprung\u2019s disease. EMBO J. <b>15<\/b>, 2717\u20132725.","DOI":"10.1002\/j.1460-2075.1996.tb00632.x"},{"key":"50","doi-asserted-by":"crossref","unstructured":"50) Cosma, M.P., Cardone, M., Carlomagno, F. and Colantuoni, V. (1998) Mutations in the extracellular domain cause RET loss of function by a dominant negative mechanism. Mol. Cell. Biol. <b>18<\/b>, 3321\u20133329.","DOI":"10.1128\/MCB.18.6.3321"},{"key":"51","doi-asserted-by":"crossref","unstructured":"51) Pasini, B., Borrello, M.G., Greco, A., Bongarzone, I., Luo, Y., Mondellini, P. et al. (1995) Loss of function effect of <i>RET<\/i> mutations causing Hirschsprung disease. Nat. Genet. <b>10<\/b>, 35\u201340.","DOI":"10.1038\/ng0595-35"},{"key":"52","doi-asserted-by":"crossref","unstructured":"52) Pelet, A., Geneste, O., Edery, P., Pasini, A., Chappuis, S., Attie, T. et al. (1998) Various mechanisms cause RET-mediated signaling defects in Hirschsprung\u2019s disease. J. Clin. Invest. <b>101<\/b>, 1415\u20131423.","DOI":"10.1172\/JCI375"},{"key":"53","doi-asserted-by":"publisher","unstructured":"53) Iwashita, T., Kurokawa, K., Qiao, S., Murakami, H., Asai, N., Hashimoto, M. et al. (2001) Functional analysis of RET with Hirschsprung\u2019s mutations affecting its kinase domain. Gastroenterology <b>121<\/b>, 24\u201333.","DOI":"10.1053\/gast.2001.25515"},{"key":"54","doi-asserted-by":"crossref","unstructured":"54) Geneste, O., Bidaud, C., De Vita, G., Hofstra, R.M.W., Tartare-Deckert, S., Buys, C.H.C.M. et al. (1999) Two distinct mutations of the RET receptor causing Hirschsprung\u2019s disease impair the binding of signaling effector to a multifunctional docking site. Hum. Mol. Genet. <b>8<\/b>, 1989\u20131999.","DOI":"10.1093\/hmg\/8.11.1989"},{"key":"55","doi-asserted-by":"publisher","unstructured":"55) Ishiguro, Y., Iwashita, T., Murakami, H., Asai, N., Iida, K., Goto, H. et al. (1999) The role of amino acids surrounding tyrosine 1062 in Ret in specific binding of the Shc phosphotyrosine-binding domain. Endocrinology <b>140<\/b>, 3992\u20133998.","DOI":"10.1210\/endo.140.9.7003"},{"key":"56","doi-asserted-by":"publisher","unstructured":"56) Emison, E.S., MaCallion, A.S., Kashuk, C.S., Bush, R.T., Grice, E., Lin, S. et al. (2005) A common sex-dependent mutation in a <i>RET<\/i> enhancer underlies Hirschsprung disease risk. Nature <b>434<\/b>, 857\u2013863.","DOI":"10.1038\/nature03467"},{"key":"57","doi-asserted-by":"crossref","unstructured":"57) Mani\u00e9, S., Santoro, M., Fusco, A. and Billaud, M. (2001) The RET receptor: function in development and dysfunction in congenital malformation. Trends Genet. <b>17<\/b>, 580\u2013589.","DOI":"10.1016\/S0168-9525(01)02420-9"},{"key":"58","doi-asserted-by":"crossref","unstructured":"58) Sergi, C.M., Caluseriu, O., McColl, H. and Eisenstat, D. (2017) Hirschsprung\u2019s disease: clinical dysmophology, genes, micro-RNA, and future perspectives. Pediatr. Res. <b>81<\/b>, 177\u2013191.","DOI":"10.1038\/pr.2016.202"},{"key":"59","doi-asserted-by":"publisher","unstructured":"59) Costantini, F. and Shakya, R. (2006) GDNF\/Ret signaling and the development of the kidney. BioEssays <b>28<\/b>, 117\u2013127.","DOI":"10.1002\/bies.20357"},{"key":"60","doi-asserted-by":"crossref","unstructured":"60) Chi, X., Michos, O., Shakya, R., Riccio, P., Enomoto, H., Lichit, J.D. et al. (2009) <i>Ret<\/i>-dependent cell rearrangements in the Wolffian duct epithelium initiate ureteric bud morphogenesis. Dev. Cell <b>17<\/b>, 199\u2013209.","DOI":"10.1016\/j.devcel.2009.07.013"},{"key":"61","doi-asserted-by":"crossref","unstructured":"61) Michos, O. (2009) Kidney development: from ureteric bud formation to branching morphogenesis. Curr. Opin. Genet. Dev. <b>19<\/b>, 484\u2013490.","DOI":"10.1016\/j.gde.2009.09.003"},{"key":"62","doi-asserted-by":"crossref","unstructured":"62) Davis, T.K., Hoshi, M. and Jain, S. (2014) To bud or not to bud: the RET perspective in CAKUT. Pediatr. Nephrol. <b>29<\/b>, 597\u2013608.","DOI":"10.1007\/s00467-013-2606-5"},{"key":"63","doi-asserted-by":"crossref","unstructured":"63) Lu, B.C., Cebrian, C., Chi, X., Kuure, S., Kuo, R., Bates, C.M. et al. (2009) Etv4 and Etv5 are required downstream of GDNF and Ret for kidney branching morphogenesis. Nat. Genet. <b>41<\/b>, 1295\u20131302.","DOI":"10.1038\/ng.476"},{"key":"64","doi-asserted-by":"crossref","unstructured":"64) Riccio, P., Cebrian, C., Zong, H., Hippenmeyer, S. and Costantini, F. (2016) <i>Ret<\/i> and <i>Etv4<\/i> promote directed movements of progenitor cells during renal branching morphogenesis. PLoS Biol. <b>14<\/b>, e1002382.","DOI":"10.1371\/journal.pbio.1002382"},{"key":"65","doi-asserted-by":"crossref","unstructured":"65) Skinner, M.A., Safford, S.D., Reeves, J.G., Jackson, M.E. and Freemerman, A.J. (2008) Renal aplasia in humans is associated with <i>RET<\/i> mutations. Am. J. Hum. Genet. <b>82<\/b>, 344\u2013351.","DOI":"10.1016\/j.ajhg.2007.10.008"},{"key":"66","doi-asserted-by":"crossref","unstructured":"66) Jeanpierre, C., Mace, G., Parisot, M., Moriniere, V., Pawtowsky, A., Benabou, M. et al. (2011) <i>RET<\/i> and <i>GDNF<\/i> mutations are rare in fetuses with renal agenesis or other severe kidney development defects. J. Med. Genet. <b>48<\/b>, 497\u2013504.","DOI":"10.1136\/jmg.2010.088526"},{"key":"67","doi-asserted-by":"crossref","unstructured":"67) Chatterjee, R., Ramos, E., Hoffman, M., VanWinkle, J., Martin, D.R., Davis, T.K. et al. (2012) Traditional and targeted exome sequencing reveals common, rare and novel functional deleterious variants in RET-signaling complex in a cohort of living US patients with urinary tract malformations. Hum. Genet. <b>131<\/b>, 1725\u20131738.","DOI":"10.1007\/s00439-012-1181-3"},{"key":"68","doi-asserted-by":"crossref","unstructured":"68) Hwang, D.-W., Dworschak, G.C., Kohl, S., Saisawat, P., Vivante, A., Hilger, A.C. et al. (2014) Mutations in 12 known dominant disease-causing genes clarify many congenital anomalies of the kidney and urinary tract. Kidney Int. <b>85<\/b>, 1429\u20131433.","DOI":"10.1038\/ki.2013.508"},{"key":"69","doi-asserted-by":"crossref","unstructured":"69) Johnen, H., Lin, S., Kuffner, T., Brown, D.A., Tsai, V.W., Bauskin, A.R. et al. (2007) Tumor-induced anorexia and weight loss are mediated by the TGF-beta superfamily cytokine MIC-1. Nat. Med. <b>13<\/b>, 1333\u20131340.","DOI":"10.1038\/nm1677"},{"key":"70","doi-asserted-by":"crossref","unstructured":"70) Tsai, V.W.W., Husaini, Y., Sainsbury, A., Brown, D.A. and Breit, S.N. (2018) The MIC-1\/GDF15-GFRAL pathway in energy homeostasis: Implications for obesity, cachexia, and other associated diseases. Cell Metab. <b>28<\/b>, 353\u2013368.","DOI":"10.1016\/j.cmet.2018.07.018"},{"key":"71","doi-asserted-by":"crossref","unstructured":"71) Wollert, K.C., Kempf, T. and Wallentin, L. (2017) Growth differentiation factor 15 as a biomarker in cardiovascular disease. Clin. Chem. <b>63<\/b>, 140\u2013151.","DOI":"10.1373\/clinchem.2016.255174"},{"key":"72","doi-asserted-by":"crossref","unstructured":"72) Luan, H.H., Wang, A., Hilliard, B.K., Carvalho, F., Rosen, C.E., Ahasic, A.M. et al. (2019) GDF15 is an inflammation-induced central mediator of tissue tolerance. Cell <b>178<\/b>, 1231\u20131244.","DOI":"10.1016\/j.cell.2019.07.033"},{"key":"73","doi-asserted-by":"crossref","unstructured":"73) Hsu, J.Y., Crawley, S., Chen, M., Ayupova, D.A., Lindhout, D.A., Higbee, J. et al. (2017) Non-homeostatic body weight regulation through a brainstem-restricted receptor for GDF15. Nature <b>550<\/b>, 255\u2013259.","DOI":"10.1038\/nature24042"},{"key":"74","doi-asserted-by":"crossref","unstructured":"74) Mullican, S.E., Lin-Schmidt, X., Chin, C.N., Chavez, J.A., Furman, J.L., Armstrong, A.A. et al. (2017) GFRAL is the receptor for GDF15 and the ligand promotes weight loss in mice and nonhuman primates. Nat. Med. <b>23<\/b>, 1150\u20131157.","DOI":"10.1038\/nm.4392"},{"key":"75","doi-asserted-by":"crossref","unstructured":"75) Yang, L., Chang, C.C., Sun, Z., Madsen, D., Zhu, H., Padkj\u00e6r, S.B. et al. (2017) GFRAL is the receptor for GDF15 and is required for the anti-obesity effects of the ligand. Nat. Med. <b>23<\/b>, 1158\u20131166.","DOI":"10.1038\/nm.4394"},{"key":"76","doi-asserted-by":"crossref","unstructured":"76) Emmerson, P.J., Wang, F., Du, Y., Liu, Q., Pickard, R.T., Gonciarz, M.D. et al. (2017) The metabolic effects of GDF15 are mediated by the orphan receptor GFRAL. Nat. Med. <b>23<\/b>, 1215\u20131219.","DOI":"10.1038\/nm.4393"},{"key":"77","doi-asserted-by":"crossref","unstructured":"77) Ahmed, D.S., Isnard, S., Lin, J., Routy, B. and Routy, J.-P. (2021) GDF15\/GFRAL pathway as a metabolic signature for cachexia in patients with cancer. J. Cancer <b>12<\/b>, 1125\u20131132.","DOI":"10.7150\/jca.50376"},{"key":"78","doi-asserted-by":"crossref","unstructured":"78) Suriben, R., Chen, M., Higbee, J., Oeffinger, J., Ventura, R., Li, B. et al. (2020) Antibody-mediated inhibition of GDF15-GFRAL activity reverses cancer cachexia in mice. Nat. Med. <b>26<\/b>, 1264\u20131270.","DOI":"10.1038\/s41591-020-0945-x"},{"key":"79","doi-asserted-by":"crossref","unstructured":"79) Subbiah, V., Yang, D., Velcheti, V., Drilon, A. and Meric-Bernstam, F. (2020) State-of-the-art strategies for targeting RET-dependent cancers. J. Clin. Oncol. <b>38<\/b>, 1209\u20131221.","DOI":"10.1200\/JCO.19.02551"},{"key":"80","doi-asserted-by":"crossref","unstructured":"80) Ricarte-Filho, J.C., Li, S., Garcia-Rendueles, M.E., Montero-Conde, C., Voza, F., Knauf, J.A. et al. (2013) Identification of kinase fusion oncogenes in post-Chernobyl radiation-induced thyroid cancers. J. Clin. Invest. <b>123<\/b>, 4935\u20134944.","DOI":"10.1172\/JCI69766"},{"key":"81","unstructured":"81) Rabes, H.M., Demidchik, E.P., Sidorow, J.D., Lengfelder, E., Beimfohr, C., Hoelzel, D. et al. (2000) Pattern of radiation-induced <i>RET<\/i> and <i>NTRK1<\/i> rearrangements in 191 post-chernobyl papillary thyroid carcinomas: biological, phenotypic, and clinical implications. Clin. Cancer Res. <b>6<\/b>, 1093\u20131103."},{"key":"82","doi-asserted-by":"crossref","unstructured":"82) Elisei, R., Romei, C., Vorontsova, T., Cosci, B., Veremeychik, V., Kuchinskaya, E. et al. (2001) RET\/PTC rearrangements in thyroid nodules: studies in irradiated and not irradiated, malignant and benign thyroid lesions in children and adults. J. Clin. Endocrinol. Metab. <b>86<\/b>, 3211\u20133216.","DOI":"10.1210\/jc.86.7.3211"},{"key":"83","doi-asserted-by":"crossref","unstructured":"83) Hamatani, K., Eguchi, H., Ito, R., Mukai, M., Takahashi, K., Taga, M. et al. (2008) <i>RET\/PTC<\/i> rearrangements preferentially occurred in papillary thyroid cancer among atomic bomb survivors exposed to high radiation dose. Cancer Res. <b>68<\/b>, 7176\u20137182.","DOI":"10.1158\/0008-5472.CAN-08-0293"},{"key":"84","unstructured":"84) Kohno, T., Nakaoku, T., Tsuta, K., Tsuchihara, K., Matsumoto, S., Yoh, K. et al. (2015) Beyond <i>ALK-RET<\/i>, <i>ROS1<\/i> and other oncogene fusions in lung cancer. Transl. Lung Cancer Res. <b>4<\/b>, 156\u2013164."},{"key":"85","doi-asserted-by":"publisher","unstructured":"85) Le Rolle, A.-F., Klempner, S.J., Garrett, C.R., Seery, T., Sanford, E.M., Balasubramanian, S. et al. (2015) Identification of characterization of <i>RET<\/i> fusion in advanced colorectal cancer. Oncotarget <b>6<\/b>, 28929\u201328937.","DOI":"10.18632\/oncotarget.4325"},{"key":"86","doi-asserted-by":"crossref","unstructured":"86) Paratala, B.S., Chung, J.H., Williams, C.B., Yilmazel, B., Petrosky, W., Williams, K. et al. (2018) <i>RET<\/i> rearrangement are actionable alterations in breast cancer. Nat. Commun. <b>9<\/b>, 4821.","DOI":"10.1038\/s41467-018-07341-4"},{"key":"87","doi-asserted-by":"crossref","unstructured":"87) Kato, S., Subbiah, V., Marchlik, E., Elkin, S.K., Carter, J.L. and Kurzrock, R. (2017) <i>RET<\/i> aberration in diverse cancers: Next-generation sequencing of 4871 patients. Clin. Cancer Res. <b>23<\/b>, 1988\u20131997.","DOI":"10.1158\/1078-0432.CCR-16-1679"},{"key":"88","doi-asserted-by":"publisher","unstructured":"88) Ballerini, P., Struski, S., Cresson, C., Prade, N., Toujani, S., Deswarte, C. et al. (2012) <i>RET<\/i> fusion genes are associated with chronic myelomonocytic leukemia and enhance monocytic differentiation. Leukemia <b>26<\/b>, 2384\u20132389.","DOI":"10.1038\/leu.2012.109"},{"key":"89","doi-asserted-by":"crossref","unstructured":"89) Wiesner, T., He, J., Yelensky, R., Esteve-Puig, R., Botton, T., Yeh, I. et al. (2014) Kinase fusions are frequent in Spitz tumours and spitzoid melanomas. Nat. Commun. <b>5<\/b>, 3116.","DOI":"10.1038\/ncomms4116"},{"key":"90","doi-asserted-by":"crossref","unstructured":"90) Sk\u00e1lov\u00e1, A., Pt\u00e1kov\u00e1, N., Santana, T., Agaimy, A., Ihrler, S., Uro-Coste, E. et al. (2019) <i>NCOA4-RET<\/i> and <i>TRIM27-RET<\/i> are characteristic gene fusions in salivary intraductal carcinoma, including invasive and metastatic tumors: Is \u201cintraductal\u201d correct? Am. J. Surg. Pathol. <b>43<\/b>, 1303\u20131313.","DOI":"10.1097\/PAS.0000000000001301"},{"key":"91","doi-asserted-by":"crossref","unstructured":"91) Mulligan, L.M. (2014) RET revisited: expanding the oncogenic portfolio. Nat. Rev. Cancer <b>14<\/b>, 173\u2013186.","DOI":"10.1038\/nrc3680"},{"key":"92","doi-asserted-by":"crossref","unstructured":"92) Mulligan, L.M., Eng, C., Healey, C.S., Clayton, D., Kwok, J.B., Gardner, E. et al. (1994) Specific mutations of the <i>RET<\/i> proto-oncogene are related to disease phenotype in MEN 2A and FMTC. Nat. Genet. <b>6<\/b>, 70\u201374.","DOI":"10.1038\/ng0194-70"},{"key":"93","doi-asserted-by":"publisher","unstructured":"93) Eng, C., Clayton, D., Schuffenecker, I., Lenoir, G., Cote, G., Gagel, R.F. et al. (1996) The relationship between specific RET proto-oncogene mutations and disease phenotype in multiple endocrine neoplasia type 2. JAMA <b>276<\/b>, 1575\u20131579.","DOI":"10.1001\/jama.276.19.1575"},{"key":"94","doi-asserted-by":"crossref","unstructured":"94) Asai, N., Iwashita, T., Matsuyama, M. and Takahashi, M. (1995) Mechanism of activation of the <i>ret<\/i> proto-oncogene by multiple endocrine neoplasia 2A mutations. Mol. Cell. Biol. <b>15<\/b>, 1613\u20131619.","DOI":"10.1128\/MCB.15.3.1613"},{"key":"95","first-page":"381","year":"1995","unstructured":"95) Santoro, M., Carlomagno, F., Romano, A., Bottaro, D.P., Dathan, N.A., Grieco, M. et al. (1995) Activation of <i>RET<\/i> as a dominant transforming gene by germline mutations of MEN2A and MEN2B. Science <b>267<\/b>, 381\u2013383.","journal-title":"Science","ISSN":"https:\/\/id.crossref.org\/issn\/0036-8075","issn-type":"print"},{"key":"96","unstructured":"96) Ito, S., Iwashita, T., Asai, N., Murakami, H., Iwata, Y., Sobue, G. et al. (1997) Biological properties of Ret with cysteine mutations correlate with multiple endocrine neoplasia type 2A, familial medullary thyroid carcinoma, and Hirschsprung\u2019s disease phenotype. Cancer Res. <b>57<\/b>, 2870\u20132872."},{"key":"97","doi-asserted-by":"crossref","unstructured":"97) Takahashi, M., Iwashita, T., Santoro, M., Lyonnet, S., Lenoir, G.M. and Billaud, M. (1999) Co-segregation of MEN2 and Hirschsprung\u2019s disease: the same mutation of RET with both gain and loss-of-function? Hum. Mutat. <b>13<\/b>, 331\u2013336.","DOI":"10.1002\/(SICI)1098-1004(1999)13:4<331::AID-HUMU11>3.0.CO;2-#"},{"key":"98","doi-asserted-by":"publisher","unstructured":"98) Castro, M.R., Thomas, B.C., Richards, M.L., Zhang, J. and Morris, J.C. (2013) Multiple endocrine neoplasia type 2A due to an exon 8 (G533C) in a large North American kindred. Thyroid <b>23<\/b>, 1547\u20131552.","DOI":"10.1089\/thy.2012.0599"},{"key":"99","doi-asserted-by":"publisher","unstructured":"99) Smith, D.P., Houghton, C. and Ponder, B.A. (1997) Germline mutation of RET codon 883 in two cases of de novo MEN 2B. Oncogene <b>15<\/b>, 1213\u20131217.","DOI":"10.1038\/sj.onc.1201481"},{"key":"100","first-page":"536","year":"1995","unstructured":"100) Songyang, Z., Carraway, K.L. 3rd, Eck, M.J., Harrison, S.C., Feldman, R.A., Mohammadi, M. et al. (1995) Catalytic specificity of protein-tyrosine kinases is critical for selective signalling. Nature <b>373<\/b>, 536\u2013539.","journal-title":"?Nature","ISSN":"https:\/\/id.crossref.org\/issn\/0028-0836","issn-type":"print"},{"key":"101","doi-asserted-by":"crossref","unstructured":"101) Murakami, H., Iwashita, T., Asai, N., Shimono, Y., Iwata, Y., Kawai, K. et al. (1999) Enhanced phosphatidylinositol 3-kinase activity and high phosphorylation state of its downstream signalling molecules mediated by ret with the MEN 2B mutation. Biochem. Biophys. Res. Commun. <b>262<\/b>, 68\u201375.","DOI":"10.1006\/bbrc.1999.1186"},{"key":"102","doi-asserted-by":"crossref","unstructured":"102) Gujral, T.S., Singh, V.K., Jia, Z. and Mulligan, L.M. (2006) Molecular mechanisms of RET receptor-mediated oncogenesis in multiple endocrine neoplasia 2B. Cancer Res. <b>66<\/b>, 10741\u201310749.","DOI":"10.1158\/0008-5472.CAN-06-3329"},{"key":"103","doi-asserted-by":"crossref","unstructured":"103) Plaza-Menacho, I., Barnouin, K., Goodman, K., Mart\u00ednez-Torres, R.J., Borg, A., Murray-Rust, J. et al. (2014) Oncogenic RET kinase domain mutations perturb the autophosphorylation trajectory by enhancing substrate presentation in trans. Mol. Cell <b>53<\/b>, 738\u2013751.","DOI":"10.1016\/j.molcel.2014.01.015"},{"key":"104","doi-asserted-by":"crossref","unstructured":"104) Mendes Oliveira, D., Grillone, K., Mignogna, C., De Falco, V., Laudanna, C., Biamonte, F. et al. (2018) Next-generation sequencing analysis of receptor-type tyrosine kinase genes in surgically resected colon cancer: identification of gain-of-function mutations in the RET proto-oncogene. J. Exp. Clin. Cancer Res. <b>37<\/b>, 84.","DOI":"10.1186\/s13046-018-0746-y"},{"key":"105","doi-asserted-by":"crossref","unstructured":"105) Drilon, A., Hu, Z.I., Lai, G.G.Y. and Tan, D.S.W. (2018) Targeting RET-driven cancers: lessons from evolving preclinical and clinical landscapes. Nat. Rev. Clin. Oncol. <b>15<\/b>, 151\u2013167.","DOI":"10.1038\/nrclinonc.2017.175"},{"key":"106","doi-asserted-by":"crossref","unstructured":"106) Dagogo-Jack, I., Stevens, S.E., Lin, J.J., Nagy, R., Ferris, L., Shaw, A.T. et al. (2018) Emergence of a <i>RET<\/i> V804M gatekeeper mutation during treatment with vandetanib in <i>RET<\/i>-rearranged NSCLC. J. Thorac. Oncol. <b>13<\/b>, e226\u2013e227.","DOI":"10.1016\/j.jtho.2018.06.021"},{"key":"107","doi-asserted-by":"crossref","unstructured":"107) Huang, Q., Schneeberger, V.E., Luetteke, N., Jin, C., Afzal, R., Budzevich, M.M. et al. (2016) Preclinical modeling of KIF5B-RET fusion lung adenocarcinoma. Mol. Cancer Ther. <b>15<\/b>, 2521\u20132529.","DOI":"10.1158\/1535-7163.MCT-16-0258"},{"key":"108","doi-asserted-by":"crossref","unstructured":"108) Subbiah, V., Gainor, J.F., Rahal, R., Brubaker, J.D., Kim, J.L., Maynard, M. et al. (2018) Precision targeted therapy with BLU-667 for <i>RET<\/i>-driven cancers. Cancer Discov. <b>8<\/b>, 836\u2013849.","DOI":"10.1158\/2159-8290.CD-18-0338"},{"key":"109","doi-asserted-by":"crossref","unstructured":"109) Wirth, L.J., Sherman, E., Robinson, B., Solomon, B., Kang, H., Lorch, J. et al. (2020) Efficacy of selpercatinib in <i>RET<\/i>-altered thyroid cancers. N. Engl. J. Med. <b>383<\/b>, 825\u2013835.","DOI":"10.1056\/NEJMoa2005651"},{"key":"110","doi-asserted-by":"crossref","unstructured":"110) Drilon, A., Oxnard, G.R., Tan, D.S.W., Loong, H.H.F., Johnson, M., Gainor, J. et al. (2020) Efficacy of selpercatinib in <i>RET<\/i> fusion-positive non-small-cell lung cancer. N. Engl. J. Med. <b>383<\/b>, 813\u2013824.","DOI":"10.1056\/NEJMoa2005653"},{"key":"111","doi-asserted-by":"crossref","unstructured":"111) Subbiah, V., Gainor, J.F., Oxnard, G.R., Tan, D.S.W., Owen, D.H., Cho, B.C. et al. (2021) Intracranial efficacy of selpercatinib in <i>RET<\/i> fusion-positive non-small cell lung cancers on the LIBRETTO-001 trial. Clin. Cancer Res. <b>27<\/b>, 4160\u20134167.","DOI":"10.1158\/1078-0432.CCR-21-0800"},{"key":"112","doi-asserted-by":"crossref","unstructured":"112) Mehta, G.U., Barone, A.K., Bradford, D., Larkins, E., Kim, J., Pai-Scherf, L. et al. (2021) US Food and Drug Administration regulatory updates in neuro-oncology. J. Neurooncol. <b>53<\/b>, 375\u2013381.","DOI":"10.1007\/s11060-021-03789-5"},{"key":"113","doi-asserted-by":"crossref","unstructured":"113) Meng, X., Lindahl, M., Hyv\u00f6nen, M.E., Parvinen, M., de Rooij, D.G., Hess, M.W. et al. (2000) Regulation of cell fate decision of undifferentiated spermatogonia by GDNF. Science <b>287<\/b>, 1489\u20131493.","DOI":"10.1126\/science.287.5457.1489"},{"key":"114","doi-asserted-by":"crossref","unstructured":"114) Jijiwa, M., Kawai, K., Fukihara, J., Nakamura, A., Hasegawa, M., Suzuki, C. et al. (2008) GDNF-mediated signaling via RET tyrosine 1062 is essential for maintenance of spermatogonial stem cells. Genes Cells <b>13<\/b>, 365\u2013374.","DOI":"10.1111\/j.1365-2443.2008.01171.x"},{"key":"115","doi-asserted-by":"publisher","unstructured":"115) Takashima, S., Kanatsu-Shinohara, M., Tanaka, T., Morimoto, H., Inoue, K., Ogonuki, N. et al. (2015) Functional differences between GDNF-dependent and FGF2-dependent mouse spermatogonial stem cell self-renewal. Stem Cell Reports <b>4<\/b>, 489\u2013502.","DOI":"10.1016\/j.stemcr.2015.01.010"},{"key":"116","first-page":"98","year":"2014","unstructured":"116) Fonseca-Pereira, D., Arroz-Madeira, S., Rodrigues-Campos, M., Barbosa, I.A., Domingues, R.G., Bento, T. et al. (2014) The neurotrophic factor receptor RET drives haematopoietic stem cell survival and function. Nature <b>514<\/b>, 98\u2013101.","journal-title":"?Nature","ISSN":"https:\/\/id.crossref.org\/issn\/0028-0836","issn-type":"print"},{"key":"117","doi-asserted-by":"publisher","unstructured":"117) Veiga-Fernandes, H., Coles, M.C., Foster, K.E., Patel, A., Williams, A., Natarajan, D. et al. (2007) Tyrosine kinase receptor RET is a key regulator of Peyer\u2019s patch organogenesis. Nature <b>446<\/b>, 547\u2013551.","DOI":"10.1038\/nature05597"},{"key":"118","doi-asserted-by":"crossref","unstructured":"118) Ibiza, S., Garc\u00eda-Cassani, B., Ribeiro, H., Carvalho, T., Almeida, L., Marques, R. et al. (2016) Glial-cell-derived neuroregulators control type 3 innate lymphoid cells and gut defense. Nature <b>535<\/b>, 440\u2013443.","DOI":"10.1038\/nature18644"},{"key":"119","doi-asserted-by":"crossref","unstructured":"119) Mahato, A.K. and Sidorova, Y.A. (2020) RET receptor tyrosine kinase: Role in neurodegeneration, obesity, and cancer. Int. J. Mol. Sci. <b>21<\/b>, 7108.","DOI":"10.3390\/ijms21197108"}],"container-title":["Proceedings of the Japan Academy, Series B"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/pjab\/98\/3\/98_PJA9803B-02\/_pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,5,9]],"date-time":"2024-05-09T05:03:33Z","timestamp":1715231013000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/pjab\/98\/3\/98_PJA9803B-02\/_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,3,11]]},"references-count":119,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2022]]}},"URL":"https:\/\/doi.org\/10.2183\/pjab.98.008","relation":{},"ISSN":["0386-2208","1349-2896"],"issn-type":[{"value":"0386-2208","type":"print"},{"value":"1349-2896","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,3,11]]},"article-number":"PJA9803B-02"}}