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Testosterone Therapy in Men With Hypogonadism: An Endocrine Society Clinical Practice Guideline. <i>J. Clin. Endocrinol. Metab.<\/i>, <b>103<\/b>, 1715\u20131744 (2018).","DOI":"10.1210\/jc.2018-00229"},{"key":"2","unstructured":"2) Cattabiani C, Basaria S, Ceda GP, Luci M, Vignali A, Lauretani F, Valenti G, Volpi R, Maggio M. Relationship between testosterone deficiency and cardiovascular risk and mortality in adult men. <i>J. Endocrinol. Invest.<\/i>, <b>35<\/b>, 104\u2013120 (2012)."},{"key":"3","doi-asserted-by":"crossref","unstructured":"3) Willems S, David K, Decallonne B, Marcq P, Antonio L, Vanderschueren D. The effect of testosterone treatment on bone mineral density in Klinefelter syndrome: a retrospective cohort study. <i>Andrology<\/i>, <b>11<\/b>, 1295\u20131302 (2023).","DOI":"10.1111\/andr.13411"},{"key":"4","doi-asserted-by":"crossref","unstructured":"4) Beattie MC, Adekola L, Papadopoulos V, Chen H, Zirkin BR. Leydig cell aging and hypogonadism. <i>Exp. Gerontol.<\/i>, <b>68<\/b>, 87\u201391 (2015).","DOI":"10.1016\/j.exger.2015.02.014"},{"key":"5","doi-asserted-by":"crossref","unstructured":"5) Garza S, Papadopoulos V. Testosterone recovery therapy targeting dysfunctional Leydig cells. <i>Andrology<\/i>, <b>11<\/b>, 816\u2013825 (2023).","DOI":"10.1111\/andr.13304"},{"key":"6","doi-asserted-by":"crossref","unstructured":"6) Zirkin BR, Papadopoulos V. Leydig cells: formation, function, and regulation. <i>Biol. Reprod.<\/i>, <b>99<\/b>, 101\u2013111 (2018).","DOI":"10.1093\/biolre\/ioy059"},{"key":"7","doi-asserted-by":"crossref","unstructured":"7) Plant TM. 60 years of neuroendocrinology: the hypothalamo-pituitary-gonadal axis. <i>J. Endocrinol.<\/i>, <b>226<\/b>, T41\u2013T54 (2015).","DOI":"10.1530\/JOE-15-0113"},{"key":"8","doi-asserted-by":"crossref","unstructured":"8) Papadopoulos V, Miller WL. Role of mitochondria in steroidogenesis. <i>Best Pract. Res. Clin. Endocrinol. Metab.<\/i>, <b>26<\/b>, 771\u2013790 (2012).","DOI":"10.1016\/j.beem.2012.05.002"},{"key":"9","doi-asserted-by":"crossref","unstructured":"9) Barsoum IB, Kaur J, Ge RS, Cooke PS, Yao HH. Dynamic changes in fetal Leydig cell populations influence adult Leydig cell populations in mice. <i>FASEB J.<\/i>, <b>27<\/b>, 2657\u20132666 (2013).","DOI":"10.1096\/fj.12-225060"},{"key":"10","doi-asserted-by":"crossref","unstructured":"10) Koganti PP, Zhao AH, Selvaraj V. Exogenous cholesterol acquisition signaling in LH-responsive MA-10 Leydig cells and in adult mice. <i>J. Endocrinol.<\/i>, <b>254<\/b>, 187\u2013199 (2022).","DOI":"10.1530\/JOE-22-0043"},{"key":"11","doi-asserted-by":"crossref","unstructured":"11) Cheng H, Zhang X, Li Y, Cao D, Luo C, Zhang Q, Zhang S, Jiao Y. Age-related testosterone decline: mechanisms and intervention strategies. <i>Reprod. Biol. Endocrinol.<\/i>, <b>22<\/b>, 144 (2024).","DOI":"10.1186\/s12958-024-01316-5"},{"key":"12","doi-asserted-by":"crossref","unstructured":"12) Miller WL. Mechanism of StAR\u2019s regulation of mitochondrial cholesterol import. <i>Mol. Cell. Endocrinol.<\/i>, <b>265-266<\/b>, 46\u201350 (2007).","DOI":"10.1016\/j.mce.2006.12.002"},{"key":"13","doi-asserted-by":"crossref","unstructured":"13) Payne AH, Hales DB. Overview of steroidogenic enzymes in the pathway from cholesterol to active steroid hormones. <i>Endocr. Rev.<\/i>, <b>25<\/b>, 947\u2013970 (2004).","DOI":"10.1210\/er.2003-0030"},{"key":"14","doi-asserted-by":"crossref","unstructured":"14) Shen WJ, Zaidi SK, Patel S, Cortez Y, Ueno M, Azhar R, Azhar S, Kraemer FB. Ablation of vimentin results in defective steroidogenesis. <i>Endocrinology<\/i>, <b>153<\/b>, 3249\u20133257 (2012).","DOI":"10.1210\/en.2012-1048"},{"key":"15","doi-asserted-by":"crossref","unstructured":"15) Venugopal S, Martinez-Arguelles DB, Chebbi S, Hullin-Matsuda F, Kobayashi T, Papadopoulos V. Plasma membrane origin of the steroidogenic pool of cholesterol used in hormone-induced acute steroid formation in leydig cells. <i>J. Biol. Chem.<\/i>, <b>291<\/b>, 26109\u201326125 (2016).","DOI":"10.1074\/jbc.M116.740928"},{"key":"16","doi-asserted-by":"crossref","unstructured":"16) Miller WL, Auchus RJ. The molecular biology, biochemistry, and physiology of human steroidogenesis and its disorders. <i>Endocr. Rev.<\/i>, <b>32<\/b>, 81\u2013151 (2011).","DOI":"10.1210\/er.2010-0013"},{"key":"17","doi-asserted-by":"crossref","unstructured":"17) Costa RR, Reis RI, Aguiar JF, Varanda WA. Luteinizing hormone (LH) acts through PKA and PKC to modulate T-type calcium currents and intracellular calcium transients in mice Leydig cells. <i>Cell Calcium<\/i>, <b>49<\/b>, 191\u2013199 (2011).","DOI":"10.1016\/j.ceca.2011.02.003"},{"key":"18","doi-asserted-by":"crossref","unstructured":"18) Pearson G, Robinson F, Beers Gibson T, Xu BE, Karandikar M, Berman K, Cobb MH. Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. <i>Endocr. Rev.<\/i>, <b>22<\/b>, 153\u2013183 (2001).","DOI":"10.1210\/edrv.22.2.0428"},{"key":"19","doi-asserted-by":"crossref","unstructured":"19) Hsieh M, Conti M. G-protein-coupled receptor signaling and the EGF network in endocrine systems. <i>Trends Endocrinol. Metab.<\/i>, <b>16<\/b>, 320\u2013326 (2005).","DOI":"10.1016\/j.tem.2005.07.005"},{"key":"20","doi-asserted-by":"crossref","unstructured":"20) Shiraishi K, Ascoli M. Activation of the lutropin\/choriogonadotropin receptor in MA-10 cells stimulates tyrosine kinase cascades that activate ras and the extracellular signal regulated kinases (ERK1\/2). <i>Endocrinology<\/i>, <b>147<\/b>, 3419\u20133427 (2006).","DOI":"10.1210\/en.2005-1478"},{"key":"21","doi-asserted-by":"crossref","unstructured":"21) Yilmaz B, Kutlu S, Canpolat S, Sandal S, Ayar A, Mogulkoc R, Kelestimur H. Effects of paint thinner exposure on serum LH, FSH and testosterone levels and hypothalamic catecholamine contents in the male rat. <i>Biol. Pharm. Bull.<\/i>, <b>24<\/b>, 163\u2013166 (2001).","DOI":"10.1248\/bpb.24.163"},{"key":"22","doi-asserted-by":"crossref","unstructured":"22) Moriya M, Katagiri C, Ikebe M, Yagi K. Immunohistochemical detection of calmodulin and calmodulin-dependent protein kinase II in the mouse testis. <i>Zygote<\/i>, <b>8<\/b>, 303\u2013314 (2000).","DOI":"10.1017\/S0967199400001106"},{"key":"23","doi-asserted-by":"crossref","unstructured":"23) Santos GJ, Ferreira SM, Ortis F, Rezende LF, Li C, Naji A, Carneiro EM, Kaestner KH, Boschero AC. Metabolic memory of <i>\u03b2<\/i>-cells controls insulin secretion and is mediated by CaMKII. <i>Mol. Metab.<\/i>, <b>3<\/b>, 484\u2013489 (2014).","DOI":"10.1016\/j.molmet.2014.03.011"},{"key":"24","doi-asserted-by":"crossref","unstructured":"24) Bayer KU, Schulman H. CaM Kinase: Still Inspiring at 40. <i>Neuron<\/i>, <b>103<\/b>, 380\u2013394 (2019).","DOI":"10.1016\/j.neuron.2019.05.033"},{"key":"25","doi-asserted-by":"crossref","unstructured":"25) Yasuda R, Hayashi Y, Hell JW. CaMKII: a central molecular organizer of synaptic plasticity, learning and memory. <i>Nat. Rev. Neurosci.<\/i>, <b>23<\/b>, 666\u2013682 (2022).","DOI":"10.1038\/s41583-022-00624-2"},{"key":"26","doi-asserted-by":"crossref","unstructured":"26) Pellicena P, Schulman H. CaMKII inhibitors: from research tools to therapeutic agents. <i>Front. Pharmacol.<\/i>, <b>5<\/b>, 21 (2014).","DOI":"10.3389\/fphar.2014.00021"},{"key":"27","doi-asserted-by":"crossref","unstructured":"27) Moriya M, Fujinaga K, Yazawa M, Katagiri C. Immunohistochemical localization of the calcium\/calmodulin-dependent protein phosphatase, calcineurin, in the mouse testis: its unique accumulation in spermatid nuclei. <i>Cell Tissue Res.<\/i>, <b>281<\/b>, 273\u2013281 (1995).","DOI":"10.1007\/BF00583396"},{"key":"28","doi-asserted-by":"crossref","unstructured":"28) Jackson KJ, Walters CL, Damaj MI. Beta 2 subunit-containing nicotinic receptors mediate acute nicotine-induced activation of calcium\/calmodulin-dependent protein kinase II-dependent pathways <i>in vivo<\/i>. <i>J. Pharmacol. Exp. Ther.<\/i>, <b>330<\/b>, 541\u2013549 (2009).","DOI":"10.1124\/jpet.109.153171"},{"key":"29","doi-asserted-by":"crossref","unstructured":"29) Tokumitsu H, Chijiwa T, Hagiwara M, Mizutani A, Terasawa M, Hidaka H. KN-62, l-[<i>N,O<\/i>-Bis(5-isoquinolinesulfonyl)-<i>N<\/i>-methyl-L-tyrosyl]-4-phenylpiperazine, a specific inhibitor of Ca<sup>2+<\/sup>\/calmodulin-dependent protein kinase II. <i>J. Biol. Chem.<\/i>, <b>265<\/b>, 4315\u20134320 (1990).","DOI":"10.1016\/S0021-9258(19)39565-1"},{"key":"30","doi-asserted-by":"crossref","unstructured":"30) Fullerton PT Jr, Monsivais D, Kommagani R, Matzuk MM. Follistatin is critical for mouse uterine receptivity and decidualization. <i>Proc. Natl. Acad. Sci. U.S.A.<\/i>, <b>114<\/b>, E4772\u2013E4781 (2017).","DOI":"10.1073\/pnas.1620903114"},{"key":"31","doi-asserted-by":"crossref","unstructured":"31) Zhao YY, Tian Y, Zhang J, Xu F, Yang YP, Huang Y, Zhao HY, Zhang JW, Xue C, Lam MH, Yan L, Hu ZH, Dinglin XX, Zhang L. Effects of an oral allosteric AKT inhibitor (MK-2206) on human nasopharyngeal cancer <i>in vitro<\/i> and <i>in vivo<\/i>. <i>Drug Des. Devel. Ther.<\/i>, <b>8<\/b>, 1827\u20131837 (2014).","DOI":"10.2147\/DDDT.S67961"},{"key":"32","doi-asserted-by":"crossref","unstructured":"32) Jana J, Mondal S, Bhattacharjee P, Sengupta P, Roychowdhury T, Saha P, Kundu P, Chatterjee S. Chelerythrine down regulates expression of VEGFA, BCL2 and KRAS by arresting G-quadruplex structures at their promoter regions. <i>Sci. Rep.<\/i>, <b>7<\/b>, 40706 (2017).","DOI":"10.1038\/srep40706"},{"key":"33","doi-asserted-by":"crossref","unstructured":"33) Tariq M, Zhang JQ, Liang GK, He QJ, Ding L, Yang B. Gefitinib inhibits M2-like polarization of tumor-associated macrophages in Lewis lung cancer by targeting the STAT6 signaling pathway. <i>Acta Pharmacol. Sin.<\/i>, <b>38<\/b>, 1501\u20131511 (2017).","DOI":"10.1038\/aps.2017.124"},{"key":"34","doi-asserted-by":"crossref","unstructured":"34) Munoz KJ, Wang K, Sheehan LM, Tan M, Sutterlin C. The Small Molecule H89 Inhibits Chlamydia Inclusion Growth and Production of Infectious Progeny. <i>Infect. Immun.<\/i>, <b>89<\/b>, e0072920 (2021).","DOI":"10.1128\/IAI.00729-20"},{"key":"35","doi-asserted-by":"crossref","unstructured":"35) Shao W, Mishina YM, Feng Y, et al. Antitumor properties of RAF709, a highly selective and potent inhibitor of RAF kinase dimers, in tumors driven by mutant RAS or BRAF. <i>Cancer Res.<\/i>, <b>78<\/b>, 1537\u20131548 (2018).","DOI":"10.1158\/0008-5472.CAN-17-2033"},{"key":"36","doi-asserted-by":"crossref","unstructured":"36) Ishida T, Koyanagi-Aoi M, Yamamiya D, Onishi A, Sato K, Uehara K, Fujisawa M, Aoi T. Differentiation of human induced pluripotent stem cells into testosterone-producing Leydig-like cells. <i>Endocrinology<\/i>, <b>162<\/b>, bqab202 (2021).","DOI":"10.1210\/endocr\/bqab202"},{"key":"37","doi-asserted-by":"crossref","unstructured":"37) Bhattacharya I, Dey S. Emerging concepts on Leydig cell development in fetal and adult testis. <i>Front. Endocrinol.<\/i>, <b>13<\/b>, 1086276 (2023).","DOI":"10.3389\/fendo.2022.1086276"},{"key":"38","doi-asserted-by":"crossref","unstructured":"38) Abdou HS, Villeneuve G, Tremblay JJ. The calcium signaling pathway regulates Leydig cell steroidogenesis through a transcriptional cascade involving the nuclear receptor NR4A1 and the steroidogenic acute regulatory protein. <i>Endocrinology<\/i>, <b>154<\/b>, 511\u2013520 (2013).","DOI":"10.1210\/en.2012-1767"},{"key":"39","doi-asserted-by":"crossref","unstructured":"39) Davies SP, Reddy H, Caivano M, Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. <i>Biochem. J.<\/i>, <b>351<\/b>, 95\u2013105 (2000).","DOI":"10.1042\/bj3510095"},{"key":"40","doi-asserted-by":"crossref","unstructured":"40) Kahl CR, Means AR. Regulation of cell cycle progression by calcium\/calmodulin-dependent pathways. <i>Endocr. Rev.<\/i>, <b>24<\/b>, 719\u2013736 (2003).","DOI":"10.1210\/er.2003-0008"},{"key":"41","doi-asserted-by":"crossref","unstructured":"41) Martin LJ, Boucher N, Brousseau C, Tremblay JJ. The orphan nuclear receptor NUR77 regulates hormone-induced StAR transcription in Leydig cells through cooperation with Ca<sup>2+<\/sup>\/calmodulin-dependent protein kinase I. <i>Mol. Endocrinol.<\/i>, <b>22<\/b>, 2021\u20132037 (2008).","DOI":"10.1210\/me.2007-0370"},{"key":"42","doi-asserted-by":"crossref","unstructured":"42) Shan LX, Phillips DM, Bardin CW, Hardy MP. Differential regulation of steroidogenic enzymes during differentiation optimizes testosterone production by adult rat Leydig cells. <i>Endocrinology<\/i>, <b>133<\/b>, 2277\u20132283 (1993).","DOI":"10.1210\/endo.133.5.8404681"},{"key":"43","doi-asserted-by":"crossref","unstructured":"43) Lejeune H, Sanchez P, Chuzel F, Langlois D, Saez JM. Time-course effects of human recombinant luteinizing hormone on porcine Leydig cell specific differentiated functions. <i>Mol. Cell. Endocrinol.<\/i>, <b>144<\/b>, 59\u201369 (1998).","DOI":"10.1016\/S0303-7207(98)00153-1"},{"key":"44","doi-asserted-by":"crossref","unstructured":"44) Shiraishi K, Ascoli M. A co-culture system reveals the involvement of intercellular pathways as mediators of the lutropin receptor (LHR)-stimulated ERK1\/2 phosphorylation in Leydig cells. <i>Exp. Cell Res.<\/i>, <b>314<\/b>, 25\u201337 (2008).","DOI":"10.1016\/j.yexcr.2007.06.025"},{"key":"45","doi-asserted-by":"crossref","unstructured":"45) Brown CN, Bayer KU. Studying CaMKII: tools and standards. <i>Cell Rep.<\/i>, <b>43<\/b>, 113982 (2024).","DOI":"10.1016\/j.celrep.2024.113982"},{"key":"46","doi-asserted-by":"crossref","unstructured":"46) Evaul K, Hammes SR. Cross-talk between G protein-coupled and epidermal growth factor receptors regulates gonadotropin-mediated steroidogenesis in Leydig cells. <i>J. Biol. Chem.<\/i>, <b>283<\/b>, 27525\u201327533 (2008).","DOI":"10.1074\/jbc.M803867200"},{"key":"47","doi-asserted-by":"crossref","unstructured":"47) Yamashita S, Tai P, Charron J, Ko C, Ascoli M. The Leydig cell MEK\/ERK pathway is critical for maintaining a functional population of adult Leydig cells and for fertility. <i>Mol. Endocrinol.<\/i>, <b>25<\/b>, 1211\u20131222 (2011).","DOI":"10.1210\/me.2011-0059"},{"key":"48","doi-asserted-by":"crossref","unstructured":"48) Manna PR, Chandrala SP, Jo Y, Stocco DM. cAMP-independent signaling regulates steroidogenesis in mouse Leydig cells in the absence of StAR phosphorylation. <i>J. Mol. Endocrinol.<\/i>, <b>37<\/b>, 81\u201395 (2006).","DOI":"10.1677\/jme.1.02065"},{"key":"49","doi-asserted-by":"crossref","unstructured":"49) Baburski AZ, Andric SA, Kostic TS. Luteinizing hormone signaling is involved in synchronization of Leydig cell\u2019s clock and is crucial for rhythm robustness of testosterone productiondagger. <i>Biol. Reprod.<\/i>, <b>100<\/b>, 1406\u20131415 (2019).","DOI":"10.1093\/biolre\/ioz020"},{"key":"50","doi-asserted-by":"crossref","unstructured":"50) Jeon H, Tkacik E, Eck MJ. Signaling from RAS to RAF: the molecules and their mechanisms. <i>Annu. Rev. Biochem.<\/i>, <b>93<\/b>, 289\u2013316 (2024).","DOI":"10.1146\/annurev-biochem-052521-040754"},{"key":"51","doi-asserted-by":"crossref","unstructured":"51) Fan D, Yu S, Yang Y, Qu S. Low expression of Rasal2 promotes non-small cell lung cancer metastasis through Ras\/ERK Pathway. <i>Biol. Pharm. Bull.<\/i>, <b>44<\/b>, 992\u2013998 (2021).","DOI":"10.1248\/bpb.b21-00231"},{"key":"52","doi-asserted-by":"crossref","unstructured":"52) Wu Y, Jia Q, Tang Q, Chen L, Deng H, He Y, Tang F. A specific super-enhancer actuated by berberine regulates EGFR-mediated RAS-RAF1-MEK1\/2-ERK1\/2 pathway to induce nasopharyngeal carcinoma autophagy. <i>Cell. Mol. Biol. Lett.<\/i>, <b>29<\/b>, 92 (2024).","DOI":"10.1186\/s11658-024-00607-4"},{"key":"53","doi-asserted-by":"crossref","unstructured":"53) McTavish CJ, Berube-Janzen W, Wang X, Maitland MER, Salemi LM, Hess DA, Schild-Poulter C. Regulation of c-Raf stability through the CTLH Complex. <i>Int. J. Mol. Sci.<\/i>, <b>20<\/b>, 934 (2019).","DOI":"10.3390\/ijms20040934"},{"key":"54","doi-asserted-by":"crossref","unstructured":"54) Centuori SM, Gomes CJ, Trujillo J, Borg J, Brownlee J, Putnam CW, Martinez JD. Deoxycholic acid mediates non-canonical EGFR-MAPK activation through the induction of calcium signaling in colon cancer cells. <i>Biochim. Biophys. Acta Mol. Cell Biol. Lipids<\/i>, <b>1861<\/b>, 663\u2013670 (2016).","DOI":"10.1016\/j.bbalip.2016.04.006"},{"key":"55","doi-asserted-by":"crossref","unstructured":"55) Wang Y, Li H, Xue C, Chen H, Xue Y, Zhao F, Zhu MX, Cao Z. TRPV3 enhances skin keratinocyte proliferation through EGFR-dependent signaling pathways. <i>Cell Biol. Toxicol.<\/i>, <b>37<\/b>, 313\u2013330 (2021).","DOI":"10.1007\/s10565-020-09536-2"},{"key":"56","doi-asserted-by":"crossref","unstructured":"56) Dickenson RE, Pellon A, Ponde NO, Hepworth O, Daniels Gatward LF, Naglik JR, Moyes DL. EGR1 regulates oral epithelial cell responses to <i>Candida albicans via<\/i> the EGFR-ERK1\/2 pathway. <i>Virulence<\/i>, <b>15<\/b>, 2435374 (2024).","DOI":"10.1080\/21505594.2024.2435374"},{"key":"57","doi-asserted-by":"crossref","unstructured":"57) Moteki H, Kimura M, Ogihara M. Activation of extracellular-signal regulated kinase by epidermal growth factor is potentiated by cAMP-elevating agents in primary cultures of adult rat hepatocytes. <i>Biol. Pharm. Bull.<\/i>, <b>34<\/b>, 1542\u20131552 (2011).","DOI":"10.1248\/bpb.34.1542"},{"key":"58","doi-asserted-by":"crossref","unstructured":"58) Park SH, Lee S, Hong YK, Hwang S, Lee JH, Bang SM, Kim YK, Koo BS, Lee IS, Cho KS. Suppressive Effects of SuHeXiang Wan on Amyloid-<i>\u03b2<\/i>42-Induced Extracellular Signal-Regulated Kinase Hyperactivation and Glial Cell Proliferation in a Transgenic Drosophila Model of Alzheimer\u2019s Disease. <i>Biol. Pharm. Bull.<\/i>, <b>36<\/b>, 390\u2013398 (2013).","DOI":"10.1248\/bpb.b12-00792"},{"key":"59","doi-asserted-by":"crossref","unstructured":"59) Britschgi A, Bill A, Brinkhaus H, et al. Calcium-activated chloride channel ANO1 promotes breast cancer progression by activating EGFR and CAMK signaling. <i>Proc. Natl. Acad. Sci. 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