{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T14:49:45Z","timestamp":1790952585842,"version":"4.1.0"},"reference-count":170,"publisher":"American Association for the Advancement of Science (AAAS)","funder":[{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["2021290"],"award-info":[{"award-number":["2021290"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["2003629"],"award-info":[{"award-number":["2003629"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["1127156"],"award-info":[{"award-number":["1127156"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Guangzhou Elite Overseas Scholarship","award":["N\/A"],"award-info":[{"award-number":["N\/A"]}]},{"DOI":"10.13039\/501100010843","name":"Guangzhou Science, Technology and Innovation Commission","doi-asserted-by":"publisher","award":["2023A03J0987"],"award-info":[{"award-number":["2023A03J0987"]}],"id":[{"id":"10.13039\/501100010843","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100024253","name":"Western Australian Future Health and Innovation Fund, Government of Western Australia","doi-asserted-by":"publisher","award":["N\/A"],"award-info":[{"award-number":["N\/A"]}],"id":[{"id":"10.13039\/501100024253","id-type":"DOI","asserted-by":"publisher"}]},{"name":"WA Near-miss Awards","award":["Ideas Grants 2022-23 program"],"award-info":[{"award-number":["Ideas Grants 2022-23 program"]}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["82350110800"],"award-info":[{"award-number":["82350110800"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Shenzhen Medical Research Fund","award":["B2302005"],"award-info":[{"award-number":["B2302005"]}]}],"content-domain":{"domain":["spj.science.org"],"crossmark-restriction":true},"short-container-title":["Research"],"published-print":{"date-parts":[[2025,1]]},"abstract":"<jats:p>Osteoporosis, a widespread skeletal disorder, arises from excessive bone loss, heightening fragility and fracture risk. Osteoclasts, the major type of bone-resorbing cells, are believed to contribute to this loss. Osteoclast bone resorption relies on 2 important organelles: lysosomes for matrix degradation and mitochondria for energy supply. Iron, a critical linker between lysosomes and mitochondria, has emerged as a critical mediator of osteoclast activity. However, the intricate interplay between lysosomes, mitochondria, and iron in osteoclasts and osteoporosis remains poorly understood. This review aims to bridge this knowledge gap by examining the lysosome\u2013iron\u2013mitochondria axis in osteoclasts. Firstly, we summarized the modulatory function of lysosomes in iron metabolism and iron\u2019s involvement in lysosomal biogenesis and function. Next, we conducted a comprehensive analysis on the contribution of iron in mitochondrial function and its implications for osteoclast activity. Subsequently, we highlighted emerging insights into the lysosome\u2013mitochondria crosstalk in iron metabolism. Finally, we delved into the discussion of how dysregulation of this lysosome\u2013iron\u2013mitochondria axis may drive osteoporosis progression and proposed innovative therapeutic strategies targeting this axis to mitigate osteoclast-mediated bone loss.<\/jats:p>","DOI":"10.34133\/research.0840","type":"journal-article","created":{"date-parts":[[2025,7,28]],"date-time":"2025-07-28T12:31:11Z","timestamp":1753705871000},"update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark_01","source":"Crossref","is-referenced-by-count":13,"title":["Lysosome\u2013Iron\u2013Mitochondria Axis in Osteoclasts: Iron as a Central Player"],"prefix":"10.34133","volume":"8","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1307-0481","authenticated-orcid":false,"given":"Shengnan","family":"Qin","sequence":"first","affiliation":[{"name":"School of Biomedical Science, \rThe University of Western Australia, Perth, Australia."},{"name":"Harry Perkins Institute of Medical Research","place":["Australia"]},{"name":"Guangzhou Institute of Traumatic Surgery, Guangzhou Red Cross Hospital, Medical College, \rJinan University, Guangzhou, China."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kathleen","family":"Davern","sequence":"additional","affiliation":[{"name":"Harry Perkins Institute of Medical Research","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Scott G.","family":"Wilson","sequence":"additional","affiliation":[{"name":"School of Biomedical Science, \rThe University of Western Australia, Perth, Australia."},{"name":"Department of Endocrinology & Diabetes, Sir Charles Gairdner Hospital","place":["Australia"]},{"name":"Department of Twin Research & Genetic Epidemiology, King\u2019s College London","place":["UK"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kai","family":"Chen","sequence":"additional","affiliation":[{"name":"School of Biomedical Science, \rThe University of Western Australia, Perth, Australia."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aiguo","family":"Li","sequence":"additional","affiliation":[{"name":"Guangzhou Institute of Traumatic Surgery, Guangzhou Red Cross Hospital, Medical College, \rJinan University, Guangzhou, China."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiake","family":"Xu","sequence":"additional","affiliation":[{"name":"School of Biomedical Science, \rThe University of Western Australia, Perth, Australia."},{"name":"Shenzhen Institute of Advanced Technology, Chinese Academic of Sciences, Shenzhen, China."},{"name":"Shenzhen University of Advanced Technology","place":["China"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","published-online":{"date-parts":[[2025,8,14]]},"reference":[{"key":"e_1_3_2_2_2","unstructured":"Australian Institute of Health and Welfare. Osteoporosis and minimal trauma fractures. Canberra: Australian Institute of Health and Welfare; 2024."},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"S6","DOI":"10.1016\/S0140-6736(20)32426-0","article-title":"Prevalence of osteoporosis and its spatiotemporal patterns in a community-dwelling Chinese population: A systematic review and meta-analysis of data from 982 563 individuals","volume":"396","author":"Tian S","year":"2020","unstructured":"Tian S, Liu Y, Xu Y, Feng A. Prevalence of osteoporosis and its spatiotemporal patterns in a community-dwelling Chinese population: A systematic review and meta-analysis of data from 982 563 individuals. Lancet. 2020;396:S6.","journal-title":"Lancet"},{"issue":"2","key":"e_1_3_2_4_2","doi-asserted-by":"crossref","first-page":"S3","DOI":"10.1007\/s00198-004-1702-6","article-title":"Epidemiology of osteoporotic fractures","volume":"16","author":"Johnell O","year":"2005","unstructured":"Johnell O, Kanis J. Epidemiology of osteoporotic fractures. Osteoporos Int. 2005;16(Suppl 2):S3\u2013S7.","journal-title":"Osteoporos Int"},{"key":"e_1_3_2_5_2","volume-title":"Epidemiology of osteoporosis and fragility fractures","year":"2025","unstructured":"Epidemiology of osteoporosis and fragility fractures. Nyon (Switzerland): International Osteoporosis Foundation; 2025."},{"key":"e_1_3_2_6_2","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2024.1431566","article-title":"Lysosomal biogenesis and function in osteoclasts: A comprehensive review","volume":"12","author":"Jiang J","year":"2024","unstructured":"Jiang J, Ren R, Fang W, Miao J, Wen Z, Wang X, Xu J, Jin H. Lysosomal biogenesis and function in osteoclasts: A comprehensive review. Front Cell Dev Biol. 2024;12: Article 1431566.","journal-title":"Front Cell Dev Biol"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1042\/BST20180445"},{"issue":"9","key":"e_1_3_2_8_2","doi-asserted-by":"crossref","first-page":"2758","DOI":"10.1073\/pnas.79.9.2758","article-title":"Identification and characterization of a proton pump on lysosomes by fluorescein-isothiocyanate-dextran fluorescence","volume":"79","author":"Ohkuma S","year":"1982","unstructured":"Ohkuma S, Moriyama Y, Takano T. Identification and characterization of a proton pump on lysosomes by fluorescein-isothiocyanate-dextran fluorescence. Proc Natl Acad Sci USA. 1982;79(9):2758\u20132762.","journal-title":"Proc Natl Acad Sci USA"},{"issue":"1","key":"e_1_3_2_9_2","doi-asserted-by":"crossref","DOI":"10.1038\/s41413-024-00360-6","article-title":"Osteoclasts control endochondral ossification via regulating acetyl-CoA availability","volume":"12","author":"Deng D","year":"2024","unstructured":"Deng D, Liu X, Huang W, Yuan S, Liu G, Ai S, Fu Y, Xu H, Zhang X, Li S, et al. Osteoclasts control endochondral ossification via regulating acetyl-CoA availability. Bone Res. 2024;12(1): Article 49.","journal-title":"Bone Res"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tibs.2021.07.003"},{"issue":"9","key":"e_1_3_2_11_2","first-page":"1809","article-title":"Bone and joint involvement in genetic hemochromatosis: Role of cirrhosis and iron overload","volume":"24","author":"Sinigaglia L","year":"1997","unstructured":"Sinigaglia L, Fargion S, Fracanzani AL, Binelli L, Battafarano N, Varenna M, Piperno A, Fiorelli G. Bone and joint involvement in genetic hemochromatosis: Role of cirrhosis and iron overload. J Rheumatol. 1997;24(9):1809\u20131813.","journal-title":"J Rheumatol"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev-pathmechdis-031521-040919"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2016.12.034"},{"key":"e_1_3_2_14_2","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.73539","article-title":"Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton","volume":"11","author":"Das BK","year":"2022","unstructured":"Das BK, Wang L, Fujiwara T, Zhou J, Aykin-Burns N, Krager KJ, Lan R, Mackintosh SG, Edmondson R, Jennings ML, et al. Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton. eLife. 2022;11: Article e73539.","journal-title":"eLife"},{"key":"e_1_3_2_15_2","doi-asserted-by":"crossref","DOI":"10.1155\/2022\/2634431","article-title":"Ferroptosis: A new regulatory mechanism in osteoporosis","volume":"2022","author":"Liu P","year":"2022","unstructured":"Liu P, Wang W, Li Z, Li Y, Yu X, Tu J, Zhang Z. Ferroptosis: A new regulatory mechanism in osteoporosis. Oxidative Med Cell Longev. 2022;2022: Article 2634431.","journal-title":"Oxidative Med Cell Longev"},{"key":"e_1_3_2_16_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.pharmthera.2022.108168","article-title":"Advances in pathogenesis and therapeutic strategies for osteoporosis","volume":"237","author":"Song S","year":"2022","unstructured":"Song S, Guo Y, Yang Y, Fu D. Advances in pathogenesis and therapeutic strategies for osteoporosis. Pharmacol Ther. 2022;237: Article 108168.","journal-title":"Pharmacol Ther"},{"issue":"6","key":"e_1_3_2_17_2","doi-asserted-by":"crossref","first-page":"3305","DOI":"10.1007\/s10565-023-09834-5","article-title":"NRF2 is essential for iron-overload stimulated osteoclast differentiation through regulation of redox and iron homeostasis","volume":"39","author":"Zhang J","year":"2023","unstructured":"Zhang J, Zhang L, Yao G, Zhao H, Wu S. NRF2 is essential for iron-overload stimulated osteoclast differentiation through regulation of redox and iron homeostasis. Cell Biol Toxicol. 2023;39(6):3305\u20133321.","journal-title":"Cell Biol Toxicol"},{"issue":"5","key":"e_1_3_2_18_2","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/j.cmet.2009.04.005","article-title":"Osteoclasts pump iron","volume":"9","author":"Roodman GD","year":"2009","unstructured":"Roodman GD. Osteoclasts pump iron. Cell Metab. 2009;9(5):405\u2013406.","journal-title":"Cell Metab"},{"issue":"8","key":"e_1_3_2_19_2","doi-asserted-by":"crossref","DOI":"10.1093\/jbmrpl\/ziae064","article-title":"Iron and bones: Effects of iron overload, deficiency and anemia treatments on bone","volume":"8","author":"Brackel FN","year":"2024","unstructured":"von Brackel FN, Oheim R. Iron and bones: Effects of iron overload, deficiency and anemia treatments on bone. JBMR Plus. 2024;8(8): Article ziae064.","journal-title":"JBMR Plus"},{"issue":"3","key":"e_1_3_2_20_2","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1038\/nm.1910","article-title":"Coordination of PGC-1\u03b2 and iron uptake in mitochondrial biogenesis and osteoclast activation","volume":"15","author":"Ishii K-a","year":"2009","unstructured":"Ishii K-a, Fumoto T, Iwai K, Takeshita S, Ito M, Shimohata N, Aburatani H, Taketani S, Lelliott CJ, Vidal-Puig A, et al. Coordination of PGC-1\u03b2 and iron uptake in mitochondrial biogenesis and osteoclast activation. Nat Med. 2009;15(3):259\u2013266.","journal-title":"Nat Med"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrendo.2013.137"},{"issue":"1","key":"e_1_3_2_22_2","doi-asserted-by":"crossref","DOI":"10.1038\/s41413-023-00294-5","article-title":"Structure and function of the membrane microdomains in osteoclasts","volume":"11","author":"Hou J","year":"2023","unstructured":"Hou J, Liu J, Huang Z, Wang Y, Yao H, Hu Z, Shi C, Xu J, Wang Q. Structure and function of the membrane microdomains in osteoclasts. Bone Res. 2023;11(1): Article 61.","journal-title":"Bone Res"},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.job.2017.01.004"},{"issue":"2","key":"e_1_3_2_24_2","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1016\/S0021-9258(17)42227-7","article-title":"Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts","volume":"269","author":"Tezuka KI","year":"1994","unstructured":"Tezuka KI, Tezuka Y, Maejima A, Sato T, Nemoto K, Kamioka H, Hakeda Y, Kumegawa M. Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts. J Biol Chem. 1994;269(2):1106\u20131109.","journal-title":"J Biol Chem"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.biocel.2011.08.016"},{"issue":"4","key":"e_1_3_2_26_2","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1002\/biof.1088","article-title":"DMT1 as a candidate for non-transferrin-bound iron uptake in the peripheral nervous system","volume":"39","author":"Vivot RM","year":"2013","unstructured":"Vivot RM, Goitia B, Usach V, Setton-Avruj PC. DMT1 as a candidate for non-transferrin-bound iron uptake in the peripheral nervous system. Biofactors. 2013;39(4):476\u2013484.","journal-title":"Biofactors"},{"key":"e_1_3_2_27_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.mce.2023.112103","article-title":"SPI1 exacerbates iron accumulation and promotes osteoclast formation through inhibiting the expression of Hepcidin","volume":"580","author":"Liu LL","year":"2024","unstructured":"Liu LL, Liu ZR, Xiao YS, Xiao JH, Huang WM, Liu WY, Zhao K, Ye YJ. SPI1 exacerbates iron accumulation and promotes osteoclast formation through inhibiting the expression of Hepcidin. Mol Cell Endocrinol. 2024;580: Article 112103.","journal-title":"Mol Cell Endocrinol"},{"key":"e_1_3_2_28_2","doi-asserted-by":"publisher","DOI":"10.1182\/bloodadvances.2021005609"},{"key":"e_1_3_2_29_2","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.22693","article-title":"The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115, control HIF1\u03b1 prolyl hydroxylation by regulating cellular iron levels","volume":"6","author":"Miles AL","year":"2017","unstructured":"Miles AL, Burr SP, Grice GL, Nathan JA. The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115, control HIF1\u03b1 prolyl hydroxylation by regulating cellular iron levels. eLife. 2017;6: Article e22693.","journal-title":"eLife"},{"issue":"11","key":"e_1_3_2_30_2","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.1080\/14787210.2020.1792291","article-title":"Repurposing of well-known medications as antivirals: Hydroxychloroquine and chloroquine \u2013 From HIV-1 infection to COVID-19","volume":"18","author":"Naghipour S","year":"2020","unstructured":"Naghipour S, Ghodousi M, Rahsepar S, Elyasi S. Repurposing of well-known medications as antivirals: Hydroxychloroquine and chloroquine \u2013 From HIV-1 infection to COVID-19. Expert Rev Anti-Infect Ther. 2020;18(11):1119\u20131133.","journal-title":"Expert Rev Anti-Infect Ther"},{"issue":"11","key":"e_1_3_2_31_2","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1016\/S1473-3099(03)00806-5","article-title":"Effects of chloroquine on viral infections: An old drug against today\u2019s diseases","volume":"3","author":"Savarino A","year":"2003","unstructured":"Savarino A, Boelaert JR, Cassone A, Majori G, Cauda R. Effects of chloroquine on viral infections: An old drug against today\u2019s diseases. Lancet Infect Dis. 2003;3(11):722\u2013727.","journal-title":"Lancet Infect Dis"},{"key":"e_1_3_2_32_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/dkv018"},{"issue":"3","key":"e_1_3_2_33_2","first-page":"C445","article-title":"Release of iron from ferritin requires lysosomal activity","volume":"291","author":"Kidane TZ","year":"2006","unstructured":"Kidane TZ, Sauble E, Linder MC. Release of iron from ferritin requires lysosomal activity. Am J Phys Cell Phys. 2006;291(3):C445\u2013C455.","journal-title":"Am J Phys Cell Phys"},{"key":"e_1_3_2_34_2","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.51031","article-title":"Impaired lysosomal acidification triggers iron deficiency and inflammation in\u00a0vivo","volume":"8","author":"Yambire KF","year":"2019","unstructured":"Yambire KF, Rostosky C, Watanabe T, Pacheu-Grau D, Torres-Odio S, Sanchez-Guerrero A, Senderovich O, Meyron-Holtz EG, Milosevic I, Frahm J, et al. Impaired lysosomal acidification triggers iron deficiency and inflammation in\u00a0vivo. eLife. 2019;8: Article e251031.","journal-title":"eLife"},{"key":"e_1_3_2_35_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molcel.2020.01.003"},{"issue":"8","key":"e_1_3_2_36_2","doi-asserted-by":"crossref","first-page":"2071","DOI":"10.3324\/haematol.2019.224899","article-title":"Transferrin receptor 1-mediated iron uptake plays an essential role in hematopoiesis","volume":"105","author":"Wang S","year":"2020","unstructured":"Wang S, He X, Wu Q, Jiang L, Chen L, Yu Y, Zhang P, Huang X, Wang J, Ju Z, et al. Transferrin receptor 1-mediated iron uptake plays an essential role in hematopoiesis. Haematologica. 2020;105(8):2071\u20132082.","journal-title":"Haematologica"},{"key":"e_1_3_2_37_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2022.102407","article-title":"Integrated regulation of stress responses, autophagy and survival by altered intracellular iron stores","volume":"55","author":"Wang Y","year":"2022","unstructured":"Wang Y, Wang M, Liu Y, Tao H, Banerjee S, Srinivasan S, Nemeth E, Czaja MJ, He P. Integrated regulation of stress responses, autophagy and survival by altered intracellular iron stores. Redox Biol. 2022;55: Article 102407.","journal-title":"Redox Biol"},{"issue":"5","key":"e_1_3_2_38_2","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0156713","article-title":"Chronic iron overload results in impaired bacterial killing of THP-1 derived macrophage through the inhibition of lysosomal acidification","volume":"11","author":"Kao JK","year":"2016","unstructured":"Kao JK, Wang SC, Ho LW, Huang SW, Chang SH, Yang RC, Ke YY, Wu CY, Wang JY, Shieh JJ. Chronic iron overload results in impaired bacterial killing of THP-1 derived macrophage through the inhibition of lysosomal acidification. PLOS ONE. 2016;11(5): Article e0156713.","journal-title":"PLOS ONE"},{"issue":"10","key":"e_1_3_2_39_2","doi-asserted-by":"crossref","first-page":"3052","DOI":"10.1093\/brain\/awy230","article-title":"Iron overload is accompanied by mitochondrial and lysosomal dysfunction in WDR45 mutant cells","volume":"141","author":"Seibler P","year":"2018","unstructured":"Seibler P, Burbulla LF, Dulovic M, Zittel S, Heine J, Schmidt T, Rudolph F, Westenberger A, Rakovic A, M\u00fcnchau A, et al. Iron overload is accompanied by mitochondrial and lysosomal dysfunction in WDR45 mutant cells. Brain. 2018;141(10):3052\u20133064.","journal-title":"Brain"},{"issue":"3","key":"e_1_3_2_40_2","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1038\/nm.1910","article-title":"Coordination of PGC-1beta and iron uptake in mitochondrial biogenesis and osteoclast activation","volume":"15","author":"Ishii KA","year":"2009","unstructured":"Ishii KA, Fumoto T, Iwai K, Takeshita S, Ito M, Shimohata N, Aburatani H, Taketani S, Lelliott CJ, Vidal-Puig A, et al. Coordination of PGC-1beta and iron uptake in mitochondrial biogenesis and osteoclast activation. Nat Med. 2009;15(3):259\u2013266.","journal-title":"Nat Med"},{"issue":"4","key":"e_1_3_2_41_2","doi-asserted-by":"crossref","DOI":"10.1002\/prp2.991","article-title":"Influence of prazosin on systemic iron levels and the associated iron metabolic alterations in spontaneously hypertensive rats","volume":"10","author":"Chang H","year":"2022","unstructured":"Chang H, Zhang D, Xin Z, Zhang P, Ding W, Chang YZ. Influence of prazosin on systemic iron levels and the associated iron metabolic alterations in spontaneously hypertensive rats. Pharmacol Res Perspect. 2022;10(4): Article e00991.","journal-title":"Pharmacol Res Perspect"},{"key":"e_1_3_2_42_2","doi-asserted-by":"publisher","DOI":"10.1038\/nchembio807"},{"issue":"31","key":"e_1_3_2_43_2","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2321929121","article-title":"Iron regulatory protein 2 contributes to antimicrobial immunity by preserving lysosomal function in macrophages","volume":"121","author":"Cheng C","year":"2024","unstructured":"Cheng C, Xing Z, Zhang W, Zheng L, Zhao H, Zhang X, Ding Y, Qiao T, Li Y, Meyron-Holtz EG, et al. Iron regulatory protein 2 contributes to antimicrobial immunity by preserving lysosomal function in macrophages. Proc Natl Acad Sci USA. 2024;121(31): Article e2321929121.","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_2_44_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.freeradbiomed.2023.09.004"},{"key":"e_1_3_2_45_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.matbio.2016.04.003","article-title":"Skeletal biology: Where matrix meets mineral","volume":"52","author":"Young MF","year":"2016","unstructured":"Young MF. Skeletal biology: Where matrix meets mineral. Matrix Biol. 2016;52-54:1\u20136.","journal-title":"Matrix Biol"},{"key":"e_1_3_2_46_2","unstructured":"Melkonian EA Schury MP . Biochemistry anaerobic glycolysis. Treasure Island (FL): StatPearls Publishing; 2023."},{"key":"e_1_3_2_47_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.bonr.2023.101688","article-title":"Oxidative phosphorylation in bone cells","volume":"18","author":"Sabini E","year":"2023","unstructured":"Sabini E, Arboit L, Khan MP, Lanzolla G, Schipani E. Oxidative phosphorylation in bone cells. Bone Rep. 2023;18: Article 101688.","journal-title":"Bone Rep"},{"key":"e_1_3_2_48_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.conb.2023.102684","article-title":"Apolipoprotein E4 targets mitochondria and the mitochondria-associated membrane complex in neuropathology, including Alzheimer\u2019s disease","volume":"79","author":"Mahley RW","year":"2023","unstructured":"Mahley RW. Apolipoprotein E4 targets mitochondria and the mitochondria-associated membrane complex in neuropathology, including Alzheimer\u2019s disease. Curr Opin Neurobiol. 2023;79: Article 102684.","journal-title":"Curr Opin Neurobiol"},{"key":"e_1_3_2_49_2","doi-asserted-by":"publisher","DOI":"10.1007\/s11914-023-00825-3"},{"key":"e_1_3_2_50_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.medj.2020.10.004"},{"key":"e_1_3_2_51_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bone.2017.12.021"},{"issue":"3","key":"e_1_3_2_52_2","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1016\/j.cmet.2014.07.011","article-title":"Mitochondrial complex I activity suppresses inflammation and enhances bone resorption by shifting macrophage-osteoclast polarization","volume":"20","author":"Jin Z","year":"2014","unstructured":"Jin Z, Wei W, Yang M, Du Y, Wan Y. Mitochondrial complex I activity suppresses inflammation and enhances bone resorption by shifting macrophage-osteoclast polarization. Cell Metab. 2014;20(3):483\u2013498.","journal-title":"Cell Metab"},{"issue":"3","key":"e_1_3_2_53_2","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/j.molmet.2013.05.004","article-title":"Mice lacking PGC-1\u03b2 in adipose tissues reveal a dissociation between mitochondrial dysfunction and insulin resistance","volume":"2","author":"Enguix N","year":"2013","unstructured":"Enguix N, Pardo R, Gonz\u00e1lez A, L\u00f3pez VM, Sim\u00f3 R, Kralli A, Villena JA. Mice lacking PGC-1\u03b2 in adipose tissues reveal a dissociation between mitochondrial dysfunction and insulin resistance. Mol Metab. 2013;2(3):215\u2013226.","journal-title":"Mol Metab"},{"issue":"7","key":"e_1_3_2_54_2","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1161\/CIRCRESAHA.111.243964","article-title":"PGC-1\u03b2 deficiency accelerates the transition to heart failure in pressure overload hypertrophy","volume":"109","author":"Riehle C","year":"2011","unstructured":"Riehle C, Wende AR, Zaha VG, Pires KM, Wayment B, Olsen C, Bugger H, Buchanan J, Wang X, Moreira AB, et al. PGC-1\u03b2 deficiency accelerates the transition to heart failure in pressure overload hypertrophy. Circ Res. 2011;109(7):783\u2013793.","journal-title":"Circ Res"},{"key":"e_1_3_2_55_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cmet.2006.11.003"},{"issue":"6","key":"e_1_3_2_56_2","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1002\/jbmr.3398","article-title":"PGC1\u03b2 organizes the osteoclast cytoskeleton by mitochondrial biogenesis and activation","volume":"33","author":"Zhang Y","year":"2018","unstructured":"Zhang Y, Rohatgi N, Veis DJ, Schilling J, Teitelbaum SL, Zou W. PGC1\u03b2 organizes the osteoclast cytoskeleton by mitochondrial biogenesis and activation. J Bone Miner Res. 2018;33(6):1114\u20131125.","journal-title":"J Bone Miner Res"},{"key":"e_1_3_2_57_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2019.06.017"},{"issue":"3","key":"e_1_3_2_58_2","doi-asserted-by":"crossref","DOI":"10.3390\/cells9030579","article-title":"From synthesis to utilization: The ins and outs of mitochondrial heme","volume":"9","author":"Swenson SA","year":"2020","unstructured":"Swenson SA, Moore CM, Marcero JR, Medlock AE, Reddi AR, Khalimonchuk O. From synthesis to utilization: The ins and outs of mitochondrial heme. Cells. 2020;9(3): Article 579.","journal-title":"Cells"},{"issue":"1","key":"e_1_3_2_59_2","doi-asserted-by":"crossref","first-page":"S81","DOI":"10.1016\/j.freeradbiomed.2018.10.182","article-title":"Heme oxygenase-1 is required for iron homeostasis and mitochondrial respiration","volume":"128","author":"Carr J","year":"2018","unstructured":"Carr J, La P, Dennery P. Heme oxygenase-1 is required for iron homeostasis and mitochondrial respiration. Free Radic Biol Med. 2018;128(Suppl 1):S81.","journal-title":"Free Radic Biol Med"},{"key":"e_1_3_2_60_2","article-title":"Heme allocation in eukaryotic cells relies on mitochondrial heme export through FLVCR1b to cytosolic GAPDH","author":"Jayaram DT","year":"2024","unstructured":"Jayaram DT, Sivaram P, Biswas P, Dai Y, Sweeny EA, Stuehr DJ. Heme allocation in eukaryotic cells relies on mitochondrial heme export through FLVCR1b to cytosolic GAPDH. Res Sq. 2024.","journal-title":"Res Sq"},{"key":"e_1_3_2_61_2","doi-asserted-by":"publisher","DOI":"10.1053\/j.gastro.2014.01.053"},{"issue":"5","key":"e_1_3_2_62_2","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1093\/jbmr\/zjaf040","article-title":"Heme metabolism mediates RANKL-induced osteoclastogenesis via mitochondrial oxidative phosphorylation","volume":"40","author":"Qiu H","year":"2025","unstructured":"Qiu H, Jin H, Miao J, Li H, Chen J, Yang X, Chen X, Mullin BH, Chen K, Gu R, et al. Heme metabolism mediates RANKL-induced osteoclastogenesis via mitochondrial oxidative phosphorylation. J Bone Miner Res. 2025;40(5):639\u2013655.","journal-title":"J Bone Miner Res"},{"key":"e_1_3_2_63_2","doi-asserted-by":"publisher","DOI":"10.1096\/fj.05-4278fje"},{"issue":"1","key":"e_1_3_2_64_2","doi-asserted-by":"crossref","first-page":"28","DOI":"10.14740\/wjon1739","article-title":"Oxygen and iron availability shapes metabolic adaptations of cancer cells","volume":"15","author":"Wang R","year":"2024","unstructured":"Wang R, Hussain A, Guo QQ, Jin XW, Wang MM. Oxygen and iron availability shapes metabolic adaptations of cancer cells. World J Oncol. 2024;15(1):28\u201337.","journal-title":"World J Oncol"},{"key":"e_1_3_2_65_2","doi-asserted-by":"publisher","DOI":"10.1242\/dmm.009019"},{"issue":"3","key":"e_1_3_2_66_2","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.mpaic.2019.01.003","article-title":"Iron metabolism","volume":"20","author":"Conway D","year":"2019","unstructured":"Conway D, Henderson MA. Iron metabolism. Anaesth Intensive Care Med. 2019;20(3):175\u2013177.","journal-title":"Anaesth Intensive Care Med"},{"issue":"1","key":"e_1_3_2_67_2","doi-asserted-by":"crossref","DOI":"10.1186\/s12967-024-05740-4","article-title":"The role of mitochondria in iron overload-induced damage","volume":"22","author":"Zhao Y","year":"2024","unstructured":"Zhao Y, Yang M, Liang X. The role of mitochondria in iron overload-induced damage. J Transl Med. 2024;22(1): Article 1057.","journal-title":"J Transl Med"},{"issue":"3","key":"e_1_3_2_68_2","first-page":"197","article-title":"Exploring the impact of iron overload on mitochondrial DNA in \u03b2-thalassemia: A comprehensive review","volume":"23","author":"Narahari JM","year":"2024","unstructured":"Narahari JM, Guruswamy P, Jagadeesha NM, Shivashakar KK, Kumar DP, Narayana PS, Vishwanath PM, Prashant A. Exploring the impact of iron overload on mitochondrial DNA in \u03b2-thalassemia: A comprehensive review. Gene Expr. 2024;23(3):197\u2013210.","journal-title":"Gene Expr"},{"key":"e_1_3_2_69_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2019.108241","article-title":"The effects of iron overload on mitochondrial function, mitochondrial dynamics, and ferroptosis in cardiomyocytes","volume":"680","author":"Sumneang N","year":"2020","unstructured":"Sumneang N, Siri-Angkul N, Kumfu S, Chattipakorn SC, Chattipakorn N. The effects of iron overload on mitochondrial function, mitochondrial dynamics, and ferroptosis in cardiomyocytes. Arch Biochem Biophys. 2020;680: Article 108241.","journal-title":"Arch Biochem Biophys"},{"key":"e_1_3_2_70_2","doi-asserted-by":"publisher","DOI":"10.1369\/jhc.7A7273.2007"},{"key":"e_1_3_2_71_2","doi-asserted-by":"publisher","DOI":"10.1182\/blood-2004-07-2722"},{"issue":"14","key":"e_1_3_2_72_2","doi-asserted-by":"crossref","DOI":"10.3390\/ijms20143576","article-title":"Reactive oxygen species in osteoclast differentiation and possible pharmaceutical targets of ROS-mediated osteoclast diseases","volume":"20","author":"Agidigbi TS","year":"2019","unstructured":"Agidigbi TS, Kim C. Reactive oxygen species in osteoclast differentiation and possible pharmaceutical targets of ROS-mediated osteoclast diseases. Int J Mol Sci. 2019;20(14): Article 3576.","journal-title":"Int J Mol Sci"},{"key":"e_1_3_2_73_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.bonr.2023.101664","article-title":"The role of reactive oxygen species in bone cell physiology and pathophysiology","volume":"19","author":"Marques-Carvalho A","year":"2023","unstructured":"Marques-Carvalho A, Kim H-N, Almeida M. The role of reactive oxygen species in bone cell physiology and pathophysiology. Bone Rep. 2023;19: Article 101664.","journal-title":"Bone Rep"},{"issue":"4","key":"e_1_3_2_74_2","doi-asserted-by":"crossref","first-page":"393","DOI":"10.37349\/emed.2022.00102","article-title":"Paradoxical role of reactive oxygen species in bone remodelling: Implications in osteoporosis and possible nanotherapeutic interventions","volume":"3","author":"Biswas L","year":"2022","unstructured":"Biswas L, Niveria K, Verma AK. Paradoxical role of reactive oxygen species in bone remodelling: Implications in osteoporosis and possible nanotherapeutic interventions. Explor Med. 2022;3(4):393\u2013413.","journal-title":"Explor Med"},{"issue":"4","key":"e_1_3_2_75_2","doi-asserted-by":"crossref","DOI":"10.3390\/ijms24043772","article-title":"Oxidative stress and inflammation in osteoporosis: Molecular mechanisms involved and the relationship with microRNAs","volume":"24","author":"Iantomasi T","year":"2023","unstructured":"Iantomasi T, Romagnoli C, Palmini G, Donati S, Falsetti I, Miglietta F, Aurilia C, Marini F, Giusti F, Brandi ML. Oxidative stress and inflammation in osteoporosis: Molecular mechanisms involved and the relationship with microRNAs. Int J Mol Sci. 2023;24(4): Article 3772.","journal-title":"Int J Mol Sci"},{"key":"e_1_3_2_76_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M409332200"},{"key":"e_1_3_2_77_2","doi-asserted-by":"publisher","DOI":"10.1038\/nchembio.1416"},{"issue":"17","key":"e_1_3_2_78_2","doi-asserted-by":"crossref","DOI":"10.3390\/molecules27175451","article-title":"Current use of Fenton reaction in drugs and food","volume":"27","author":"Abe C","year":"2022","unstructured":"Abe C, Miyazawa T, Miyazawa T. Current use of Fenton reaction in drugs and food. Molecules. 2022;27(17): Article 5451.","journal-title":"Molecules"},{"key":"e_1_3_2_79_2","doi-asserted-by":"publisher","DOI":"10.1152\/physrev.00026.2013"},{"key":"e_1_3_2_80_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2023.102926","article-title":"Mitochondrial complex I ROS production and redox signaling in hypoxia","volume":"67","author":"Okoye CN","year":"2023","unstructured":"Okoye CN, Koren SA, Wojtovich AP. Mitochondrial complex I ROS production and redox signaling in hypoxia. Redox Biol. 2023;67: Article 102926.","journal-title":"Redox Biol"},{"issue":"8","key":"e_1_3_2_81_2","doi-asserted-by":"crossref","first-page":"1600","DOI":"10.2741\/4869","article-title":"Role of reactive oxygen species and iron in host defense against infection","volume":"25","author":"Dickson KB","year":"2020","unstructured":"Dickson KB, Zhou J. Role of reactive oxygen species and iron in host defense against infection. Front Biosci. 2020;25(8):1600\u20131616.","journal-title":"Front Biosci"},{"issue":"6","key":"e_1_3_2_82_2","doi-asserted-by":"crossref","first-page":"1634","DOI":"10.7150\/thno.30206","article-title":"Pseurotin a inhibits osteoclastogenesis and prevents ovariectomized-induced bone loss by suppressing reactive oxygen species","volume":"9","author":"Chen K","year":"2019","unstructured":"Chen K, Qiu P, Yuan Y, Zheng L, He J, Wang C, Guo Q, Kenny J, Liu Q, Zhao J, et al. Pseurotin a inhibits osteoclastogenesis and prevents ovariectomized-induced bone loss by suppressing reactive oxygen species. Theranostics. 2019;9(6):1634\u20131650.","journal-title":"Theranostics"},{"issue":"1","key":"e_1_3_2_83_2","doi-asserted-by":"crossref","DOI":"10.1038\/s41420-023-01729-y","article-title":"Metallothionein 3 promotes osteoclast differentiation and survival by regulating the intracellular Zn2+ concentration and NRF2 pathway","volume":"9","author":"Arisumi S","year":"2023","unstructured":"Arisumi S, Fujiwara T, Yasumoto K, Tsutsui T, Saiwai H, Kobayakawa K, Okada S, Zhao H, Nakashima Y. Metallothionein 3 promotes osteoclast differentiation and survival by regulating the intracellular Zn2+ concentration and NRF2 pathway. Cell Death Discov. 2023;9(1): Article 436.","journal-title":"Cell Death Discov"},{"issue":"5","key":"e_1_3_2_84_2","doi-asserted-by":"crossref","DOI":"10.1242\/jeb.221606","article-title":"Are mitochondria the main contributor of reactive oxygen species in cells?","volume":"224","author":"Zhang Y","year":"2021","unstructured":"Zhang Y, Wong HS. Are mitochondria the main contributor of reactive oxygen species in cells? J Exp Biol. 2021;224(Pt 5): Article jeb221606.","journal-title":"J Exp Biol"},{"issue":"23","key":"e_1_3_2_85_2","doi-asserted-by":"crossref","first-page":"14807","DOI":"10.1073\/pnas.192585799","article-title":"Heme deficiency may be a factor in the mitochondrial and neuronal decay of aging","volume":"99","author":"Atamna H","year":"2002","unstructured":"Atamna H, Killilea DW, Killilea AN, Ames BN. Heme deficiency may be a factor in the mitochondrial and neuronal decay of aging. Proc Natl Acad Sci USA. 2002;99(23):14807\u201314812.","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_2_86_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.mce.2015.03.022"},{"issue":"1","key":"e_1_3_2_87_2","doi-asserted-by":"crossref","first-page":"12","DOI":"10.4110\/in.2009.9.1.12","article-title":"Heme oxygenase-1: Its therapeutic roles in inflammatory diseases","volume":"9","author":"Pae HO","year":"2009","unstructured":"Pae HO, Chung HT. Heme oxygenase-1: Its therapeutic roles in inflammatory diseases. Immune Netw. 2009;9(1):12\u201319.","journal-title":"Immune Netw"},{"key":"e_1_3_2_88_2","doi-asserted-by":"publisher","DOI":"10.1111\/jnc.15969"},{"issue":"5","key":"e_1_3_2_89_2","doi-asserted-by":"crossref","first-page":"429","DOI":"10.2174\/138161208783597407","article-title":"Heme oxygenase-1 as a therapeutic target in neurodegenerative diseases and brain infections","volume":"14","author":"Cuadrado A","year":"2008","unstructured":"Cuadrado A, Rojo AI. Heme oxygenase-1 as a therapeutic target in neurodegenerative diseases and brain infections. Curr Pharm Des. 2008;14(5):429\u2013442.","journal-title":"Curr Pharm Des"},{"issue":"1","key":"e_1_3_2_90_2","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-018-29122-1","article-title":"Various roles of heme oxygenase-1 in response of bone marrow macrophages to RANKL and in the early stage of osteoclastogenesis","volume":"8","author":"Florczyk-Soluch U","year":"2018","unstructured":"Florczyk-Soluch U, J\u00f3zefczuk E, St\u0119pniewski J, Bukowska-Strakova K, Mendel M, Viscardi M, Nowak WN, J\u00f3zkowicz A, Dulak J. Various roles of heme oxygenase-1 in response of bone marrow macrophages to RANKL and in the early stage of osteoclastogenesis. Sci Rep. 2018;8(1): Article 10797.","journal-title":"Sci Rep"},{"key":"e_1_3_2_91_2","doi-asserted-by":"publisher","DOI":"10.1038\/s41418-022-00932-1"},{"issue":"8","key":"e_1_3_2_92_2","doi-asserted-by":"crossref","first-page":"1679","DOI":"10.1016\/j.cmet.2024.03.005","article-title":"A clinical-stage Nrf2 activator suppresses osteoclast differentiation via the iron-ornithine axis","volume":"36","author":"Dong Y","year":"2024","unstructured":"Dong Y, Kang H, Peng R, Liu Z, Liao F, Hu SA, Ding W, Wang P, Yang P, Zhu M, et al. A clinical-stage Nrf2 activator suppresses osteoclast differentiation via the iron-ornithine axis. Cell Metab. 2024;36(8):1679\u20131695.e6.","journal-title":"Cell Metab"},{"key":"e_1_3_2_93_2","doi-asserted-by":"crossref","DOI":"10.3389\/fendo.2022.813057","article-title":"The role of NRF2 in bone metabolism\u2014Friend or foe?","volume":"13","author":"Han J","year":"2022","unstructured":"Han J, Yang K, An J, Jiang N, Fu S, Tang X. The role of NRF2 in bone metabolism\u2014Friend or foe? Front Endocrinol. 2022;13: Article 813057.","journal-title":"Front Endocrinol"},{"key":"e_1_3_2_94_2","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2021.728172","article-title":"Nrf2 is a potential modulator for orchestrating iron homeostasis and redox balance in cancer cells","volume":"9","author":"Zhang L","year":"2021","unstructured":"Zhang L, Zhang J, Jin Y, Yao G, Zhao H, Qiao P, Wu S. Nrf2 is a potential modulator for orchestrating iron homeostasis and redox balance in cancer cells. Front Cell Dev Biol. 2021;9: Article 728172.","journal-title":"Front Cell Dev Biol"},{"key":"e_1_3_2_95_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.biopha.2023.115748","article-title":"Nrf2: A promising therapeutic target in bone-related diseases","volume":"168","author":"Che J","year":"2023","unstructured":"Che J, Yang X, Jin Z, Xu C. Nrf2: A promising therapeutic target in bone-related diseases. Biomed Pharmacother. 2023;168: Article 115748.","journal-title":"Biomed Pharmacother"},{"issue":"17","key":"e_1_3_2_96_2","doi-asserted-by":"crossref","first-page":"1756","DOI":"10.1089\/ars.2017.7176","article-title":"The roles of NRF2 in modulating cellular iron homeostasis","volume":"29","author":"Kerins MJ","year":"2017","unstructured":"Kerins MJ, Ooi A. The roles of NRF2 in modulating cellular iron homeostasis. Antioxid Redox Signal. 2017;29(17):1756\u20131773.","journal-title":"Antioxid Redox Signal"},{"key":"e_1_3_2_97_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2025.103551","article-title":"Nrf2 activators for the treatment of rare iron overload diseases: From bench to bedside","volume":"81","author":"Dong Y","year":"2025","unstructured":"Dong Y, Zheng M, Ding W, Guan H, Xiao J, Li F. Nrf2 activators for the treatment of rare iron overload diseases: From bench to bedside. Redox Biol. 2025;81: Article 103551.","journal-title":"Redox Biol"},{"key":"e_1_3_2_98_2","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.reth.2020.02.001","article-title":"Nrf2 is required for suppressing osteoclast RANKL-induced differentiation in RAW 264.7 cells via inactivating cannabinoid receptor type 2 with AM630","volume":"14","author":"Li W","year":"2020","unstructured":"Li W, Sun Y. Nrf2 is required for suppressing osteoclast RANKL-induced differentiation in RAW 264.7 cells via inactivating cannabinoid receptor type 2 with AM630. Regen Ther. 2020;14:191\u2013195.","journal-title":"Regen Ther"},{"issue":"1","key":"e_1_3_2_99_2","doi-asserted-by":"crossref","DOI":"10.1186\/s12929-015-0212-5","article-title":"Role of Nrf2 in bone metabolism","volume":"22","author":"Sun Y-X","year":"2015","unstructured":"Sun Y-X, Xu A-H, Yang Y, Li J. Role of Nrf2 in bone metabolism. J Biomed Sci. 2015;22(1): Article 101.","journal-title":"J Biomed Sci"},{"key":"e_1_3_2_100_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2023.06.080"},{"issue":"4","key":"e_1_3_2_101_2","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1128\/MCB.01685-08","article-title":"Regulation of mitochondrial iron import through differential turnover of mitoferrin 1 and mitoferrin 2","volume":"29","author":"Paradkar PN","year":"2009","unstructured":"Paradkar PN, Zumbrennen KB, Paw BH, Ward DM, Kaplan J. Regulation of mitochondrial iron import through differential turnover of mitoferrin 1 and mitoferrin 2. Mol Cell Biol. 2009;29(4):1007\u20131016.","journal-title":"Mol Cell Biol"},{"key":"e_1_3_2_102_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.201602069"},{"key":"e_1_3_2_103_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2016.09.008"},{"issue":"1","key":"e_1_3_2_104_2","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1182\/blood-2007-01-068148","article-title":"Direct interorganellar transfer of iron from endosome to mitochondrion","volume":"110","author":"Sheftel AD","year":"2007","unstructured":"Sheftel AD, Zhang A-S, Brown C, Shirihai OS, Ponka P. Direct interorganellar transfer of iron from endosome to mitochondrion. Blood. 2007;110(1):125\u2013132.","journal-title":"Blood"},{"issue":"1","key":"e_1_3_2_105_2","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-017-18584-4","article-title":"A role for divalent metal transporter (DMT1) in mitochondrial uptake of iron and manganese","volume":"8","author":"Wolff NA","year":"2018","unstructured":"Wolff NA, Garrick MD, Zhao L, Garrick LM, Ghio AJ, Th\u00e9venod F. A role for divalent metal transporter (DMT1) in mitochondrial uptake of iron and manganese. Sci Rep. 2018;8(1): Article 211.","journal-title":"Sci Rep"},{"key":"e_1_3_2_106_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature25486"},{"issue":"1","key":"e_1_3_2_107_2","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1038\/s41392-023-01503-7","article-title":"The mitophagy pathway and its implications in human diseases","volume":"8","author":"Wang S","year":"2023","unstructured":"Wang S, Long H, Hou L, Feng B, Ma Z, Wu Y, Zeng Y, Cai J, Zhang DW, Zhao G. The mitophagy pathway and its implications in human diseases. Signal Transduct Target Ther. 2023;8(1):304.","journal-title":"Signal Transduct Target Ther"},{"issue":"11","key":"e_1_3_2_108_2","doi-asserted-by":"crossref","DOI":"10.15252\/embr.202050202","article-title":"Iron loss triggers mitophagy through induction of mitochondrial ferritin","volume":"21","author":"Hara Y","year":"2020","unstructured":"Hara Y, Yanatori I, Tanaka A, Kishi F, Lemasters JJ, Nishina S, Sasaki K, Hino K. Iron loss triggers mitophagy through induction of mitochondrial ferritin. EMBO Rep. 2020;21(11): Article e50202.","journal-title":"EMBO Rep"},{"key":"e_1_3_2_109_2","doi-asserted-by":"publisher","DOI":"10.1038\/s41556-021-00798-4"},{"key":"e_1_3_2_110_2","doi-asserted-by":"crossref","DOI":"10.3389\/fnins.2019.00048","article-title":"Noxious iron-calcium connections in neurodegeneration","volume":"13","author":"N\u00fa\u00f1ez MT","year":"2019","unstructured":"N\u00fa\u00f1ez MT, Hidalgo C. Noxious iron-calcium connections in neurodegeneration. Front Neurosci. 2019;13: Article 48.","journal-title":"Front Neurosci"},{"issue":"3","key":"e_1_3_2_111_2","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/j.bbrc.2010.02.025","article-title":"Interaction of calcium with the human divalent metal-ion transporter-1","volume":"393","author":"Shawki A","year":"2010","unstructured":"Shawki A, Mackenzie B. Interaction of calcium with the human divalent metal-ion transporter-1. Biochem Biophys Res Commun. 2010;393(3):471\u2013475.","journal-title":"Biochem Biophys Res Commun"},{"issue":"6","key":"e_1_3_2_112_2","doi-asserted-by":"crossref","first-page":"C1791","DOI":"10.1152\/ajpcell.00411.2022","article-title":"Calcium is a noncompetitive inhibitor of DMT1 on the intestinal iron absorption process: Empirical evidence and mathematical modeling analysis","volume":"323","author":"Cegarra L","year":"2022","unstructured":"Cegarra L, Aguirre P, Nu\u00f1ez MT, Gerdtzen ZP, Salgado JC. Calcium is a noncompetitive inhibitor of DMT1 on the intestinal iron absorption process: Empirical evidence and mathematical modeling analysis. Am J Physiol Cell Physiol. 2022;323(6):C1791\u2013C1806.","journal-title":"Am J Physiol Cell Physiol"},{"key":"e_1_3_2_113_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.ceca.2023.102751","article-title":"Calcium signaling in lysosome-dependent cell death","volume":"113","author":"Milani M","year":"2023","unstructured":"Milani M, Pih\u00e1n P, Hetz C. Calcium signaling in lysosome-dependent cell death. Cell Calcium. 2023;113: Article 102751.","journal-title":"Cell Calcium"},{"key":"e_1_3_2_114_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2003236117"},{"key":"e_1_3_2_115_2","doi-asserted-by":"crossref","DOI":"10.21037\/dmr.2018.09.03","article-title":"TFEB, a master regulator of lysosome biogenesis and autophagy, is a new player in alcoholic liver disease","volume":"1","author":"Bala S","year":"2018","unstructured":"Bala S, Szabo G. TFEB, a master regulator of lysosome biogenesis and autophagy, is a new player in alcoholic liver disease. Dig Med Res. 2018;1: Article 16.","journal-title":"Dig Med Res"},{"key":"e_1_3_2_116_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.biopha.2020.110272","article-title":"Emerging role of transcription factor EB in mitochondrial quality control","volume":"128","author":"Wang S","year":"2020","unstructured":"Wang S, Chen Y, Li X, Zhang W, Liu Z, Wu M, Pan Q, Liu H. Emerging role of transcription factor EB in mitochondrial quality control. Biomed Pharmacother. 2020;128: Article 110272.","journal-title":"Biomed Pharmacother"},{"issue":"12","key":"e_1_3_2_117_2","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1038\/s41419-022-05504-2","article-title":"Iron-induced cytotoxicity mediated by endolysosomal TRPML1 channels is reverted by TFEB","volume":"13","author":"Fern\u00e1ndez B","year":"2022","unstructured":"Fern\u00e1ndez B, Olmedo P, Gil F, Fdez E, Naaldijk Y, Rivero-R\u00edos P, Bracher F, Grimm C, Churchill GC, Hilfiker S. Iron-induced cytotoxicity mediated by endolysosomal TRPML1 channels is reverted by TFEB. Cell Death Dis. 2022;13(12):1047.","journal-title":"Cell Death Dis"},{"issue":"5","key":"e_1_3_2_118_2","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/j.cmet.2012.10.001","article-title":"mTOR regulates cellular iron homeostasis through tristetraprolin","volume":"16","author":"Bayeva M","year":"2012","unstructured":"Bayeva M, Khechaduri A, Puig S, Chang HC, Patial S, Blackshear PJ, Ardehali H. mTOR regulates cellular iron homeostasis through tristetraprolin. Cell Metab. 2012;16(5):645\u2013657.","journal-title":"Cell Metab"},{"key":"e_1_3_2_119_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cytogfr.2023.06.002"},{"issue":"11","key":"e_1_3_2_120_2","doi-asserted-by":"crossref","DOI":"10.1038\/s41419-023-06262-5","article-title":"mTOR inhibition suppresses salinomycin-induced ferroptosis in breast cancer stem cells by ironing out mitochondrial dysfunctions","volume":"14","author":"Cosialls E","year":"2023","unstructured":"Cosialls E, Pacreau E, Duruel C, Ceccacci S, Elhage R, Desterke C, Roger K, Guerrera C, Ducloux R, Souquere S, et al. mTOR inhibition suppresses salinomycin-induced ferroptosis in breast cancer stem cells by ironing out mitochondrial dysfunctions. Cell Death Dis. 2023;14(11): Article 744.","journal-title":"Cell Death Dis"},{"key":"e_1_3_2_121_2","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2017.00054","article-title":"Regulation of osteoclast growth and fusion by mTOR\/raptor and mTOR\/rictor\/Akt","volume":"5","author":"Tiedemann K","year":"2017","unstructured":"Tiedemann K, Le Nihouannen D, Fong JE, Hussein O, Barralet JE, Komarova SV. Regulation of osteoclast growth and fusion by mTOR\/raptor and mTOR\/rictor\/Akt. Front Cell Dev Biol. 2017;5: Article 54.","journal-title":"Front Cell Dev Biol"},{"key":"e_1_3_2_122_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.cdd.4401285"},{"key":"e_1_3_2_123_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.canlet.2011.09.026"},{"issue":"1","key":"e_1_3_2_124_2","doi-asserted-by":"crossref","DOI":"10.1038\/s41413-017-0004-5","article-title":"mTOR signaling in skeletal development and disease","volume":"6","author":"Chen J","year":"2018","unstructured":"Chen J, Long F. mTOR signaling in skeletal development and disease. Bone Res. 2018;6(1): Article 1.","journal-title":"Bone Res"},{"key":"e_1_3_2_125_2","doi-asserted-by":"publisher","DOI":"10.1038\/s41388-020-1366-5"},{"issue":"10","key":"e_1_3_2_126_2","doi-asserted-by":"crossref","DOI":"10.15252\/embr.201947911","article-title":"Iron overload inhibits late stage autophagic flux leading to insulin resistance","volume":"20","author":"Jahng JWS","year":"2019","unstructured":"Jahng JWS, Alsaadi RM, Palanivel R, Song E, Hipolito VEB, Sung HK, Botelho RJ, Russell RC, Sweeney G. Iron overload inhibits late stage autophagic flux leading to insulin resistance. EMBO Rep. 2019;20(10): Article e47911.","journal-title":"EMBO Rep"},{"issue":"18","key":"e_1_3_2_127_2","doi-asserted-by":"crossref","first-page":"12901","DOI":"10.1074\/jbc.M112.424499","article-title":"Mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation stabilizes ISCU protein: Implications for iron metabolism","volume":"288","author":"La P","year":"2013","unstructured":"La P, Yang G, Dennery PA. Mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation stabilizes ISCU protein: Implications for iron metabolism. J Biol Chem. 2013;288(18):12901\u201312909.","journal-title":"J Biol Chem"},{"key":"e_1_3_2_128_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.freeradbiomed.2025.05.390"},{"key":"e_1_3_2_129_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2020.101670","article-title":"Hypoxia inhibits ferritinophagy, increases mitochondrial ferritin, and protects from ferroptosis","volume":"36","author":"Fuhrmann DC","year":"2020","unstructured":"Fuhrmann DC, Mondorf A, Beifu\u00df J, Jung M, Br\u00fcne B. Hypoxia inhibits ferritinophagy, increases mitochondrial ferritin, and protects from ferroptosis. Redox Biol. 2020;36: Article 101670.","journal-title":"Redox Biol"},{"key":"e_1_3_2_130_2","doi-asserted-by":"publisher","DOI":"10.1053\/j.gastro.2011.03.007"},{"issue":"5","key":"e_1_3_2_131_2","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1172\/JCI38499","article-title":"HIF-2alpha, but not HIF-1alpha, promotes iron absorption in mice","volume":"119","author":"Mastrogiannaki M","year":"2009","unstructured":"Mastrogiannaki M, Matak P, Keith B, Simon MC, Vaulont S, Peyssonnaux C. HIF-2alpha, but not HIF-1alpha, promotes iron absorption in mice. J Clin Invest. 2009;119(5):1159\u20131166.","journal-title":"J Clin Invest"},{"issue":"11","key":"e_1_3_2_132_2","doi-asserted-by":"crossref","DOI":"10.3390\/cancers11111653","article-title":"Oxygen tension regulates lysosomal activation and receptor tyrosine kinase degradation","volume":"11","author":"Hong J","year":"2019","unstructured":"Hong J, Wuest TR, Min Y, Lin PC. Oxygen tension regulates lysosomal activation and receptor tyrosine kinase degradation. Cancer. 2019;11(11): Article 1653.","journal-title":"Cancer"},{"issue":"2","key":"e_1_3_2_133_2","doi-asserted-by":"crossref","DOI":"10.1002\/jev2.12310","article-title":"Hypoxia promotes EV secretion by impairing lysosomal homeostasis in HNSCC through negative regulation of ATP6V1A by HIF-1\u03b1","volume":"12","author":"Wang X","year":"2023","unstructured":"Wang X, Wu R, Zhai P, Liu Z, Xia R, Zhang Z, Qin X, Li C, Chen W, Li J, et al. Hypoxia promotes EV secretion by impairing lysosomal homeostasis in HNSCC through negative regulation of ATP6V1A by HIF-1\u03b1. J Extracell Vesicles. 2023;12(2): Article e12310.","journal-title":"J Extracell Vesicles"},{"key":"e_1_3_2_134_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2016.11.088"},{"issue":"7","key":"e_1_3_2_135_2","doi-asserted-by":"crossref","DOI":"10.1038\/s41419-021-03979-z","article-title":"Effect of the mitochondrial unfolded protein response on hypoxic death and mitochondrial protein aggregation","volume":"12","author":"Yan J","year":"2021","unstructured":"Yan J, Sun C-L, Shin S, Van Gilst M, Crowder CM. Effect of the mitochondrial unfolded protein response on hypoxic death and mitochondrial protein aggregation. Cell Death Dis. 2021;12(7): Article 711.","journal-title":"Cell Death Dis"},{"key":"e_1_3_2_136_2","doi-asserted-by":"crossref","DOI":"10.3389\/fphys.2022.925752","article-title":"Iron supplementation inhibits hypoxia-induced mitochondrial damage and protects zebrafish liver cells from death","volume":"13","author":"Hu R","year":"2022","unstructured":"Hu R, Li G, Xu Q, Chen L. Iron supplementation inhibits hypoxia-induced mitochondrial damage and protects zebrafish liver cells from death. Front Physiol. 2022;13: Article 925752.","journal-title":"Front Physiol"},{"issue":"1","key":"e_1_3_2_137_2","doi-asserted-by":"crossref","DOI":"10.1186\/1743-7075-9-104","article-title":"Iron deficiency causes a shift in AMP-activated protein kinase (AMPK) subunit composition in rat skeletal muscle","volume":"9","author":"Merrill JF","year":"2012","unstructured":"Merrill JF, Thomson DM, Hardman SE, Hepworth SD, Willie S, Hancock CR. Iron deficiency causes a shift in AMP-activated protein kinase (AMPK) subunit composition in rat skeletal muscle. Nutr Metab (Lond). 2012;9(1): Article 104.","journal-title":"Nutr Metab (Lond)"},{"key":"e_1_3_2_138_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ccr.2011.07.018"},{"key":"e_1_3_2_139_2","doi-asserted-by":"crossref","DOI":"10.1182\/blood-2018-99-112175","article-title":"AMPK regulates the expression of the Fe-S cluster assembly enzyme (ISCU) and ALAS2, modulating cellular iron metabolism and increasing hemoglobin synthesis","volume":"132","author":"La P","year":"2018","unstructured":"La P, Pires Lourenco S, Breda L, Rivella S. AMPK regulates the expression of the Fe-S cluster assembly enzyme (ISCU) and ALAS2, modulating cellular iron metabolism and increasing hemoglobin synthesis. Blood. 2018;132: Article 851.","journal-title":"Blood"},{"issue":"14","key":"e_1_3_2_140_2","doi-asserted-by":"crossref","DOI":"10.1242\/dev.200536","article-title":"AMPK activates the Nrf2-Keap1 pathway to govern dendrite pruning via the insulin pathway in drosophila","volume":"149","author":"Yuh Chew L","year":"2022","unstructured":"Yuh Chew L, He J, Wong JJL, Li S, Yu F. AMPK activates the Nrf2-Keap1 pathway to govern dendrite pruning via the insulin pathway in drosophila. Development. 2022;149(14): Article dev200536.","journal-title":"Development"},{"issue":"6642","key":"e_1_3_2_141_2","doi-asserted-by":"crossref","DOI":"10.1126\/science.abj5559","article-title":"Induction of lysosomal and mitochondrial biogenesis by AMPK phosphorylation of FNIP1","volume":"380","author":"Malik N","year":"2023","unstructured":"Malik N, Ferreira BI, Hollstein PE, Curtis SD, Trefts E, Weiser Novak S, Yu J, Gilson R, Hellberg K, Fang L, et al. Induction of lysosomal and mitochondrial biogenesis by AMPK phosphorylation of FNIP1. Science. 2023;380(6642): Article eabj5559.","journal-title":"Science"},{"issue":"3","key":"e_1_3_2_142_2","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1007\/s00223-015-0087-1","article-title":"Extracellular iron is a modulator of the differentiation of osteoclast lineage cells","volume":"98","author":"Xie W","year":"2016","unstructured":"Xie W, Lorenz S, Dolder S, Hofstetter W. Extracellular iron is a modulator of the differentiation of osteoclast lineage cells. Calcif Tissue Int. 2016;98(3):275\u2013283.","journal-title":"Calcif Tissue Int"},{"key":"e_1_3_2_143_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.mce.2022.111559","article-title":"ELAV-like RNA binding protein 1 regulates osteogenesis in diabetic osteoporosis: Involvement of divalent metal transporter 1","volume":"546","author":"Ren Y","year":"2022","unstructured":"Ren Y, Yang M, Wang X, Xu B, Xu Z, Su B. ELAV-like RNA binding protein 1 regulates osteogenesis in diabetic osteoporosis: Involvement of divalent metal transporter 1. Mol Cell Endocrinol. 2022;546: Article 111559.","journal-title":"Mol Cell Endocrinol"},{"key":"e_1_3_2_144_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.RA119.012023"},{"key":"e_1_3_2_145_2","doi-asserted-by":"publisher","DOI":"10.1002\/cbin.10013"},{"key":"e_1_3_2_146_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.213827.113"},{"issue":"12","key":"e_1_3_2_147_2","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1007\/s00198-005-1934-0","article-title":"Bone mineral density in men with genetic hemochromatosis and HFE gene mutation","volume":"16","author":"Guggenbuhl P","year":"2005","unstructured":"Guggenbuhl P, Deugnier Y, Boisdet JF, Rolland Y, Perdriger A, Pawlotsky Y, Chal\u00e8s G. Bone mineral density in men with genetic hemochromatosis and HFE gene mutation. Osteoporos Int. 2005;16(12):1809\u20131814.","journal-title":"Osteoporos Int"},{"issue":"4","key":"e_1_3_2_148_2","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1007\/s00198-008-0701-4","article-title":"Association between iron overload and osteoporosis in patients with hereditary hemochromatosis","volume":"20","author":"Valenti L","year":"2009","unstructured":"Valenti L, Varenna M, Fracanzani AL, Rossi V, Fargion S, Sinigaglia L. Association between iron overload and osteoporosis in patients with hereditary hemochromatosis. Osteoporos Int. 2009;20(4):549\u2013555.","journal-title":"Osteoporos Int"},{"issue":"6","key":"e_1_3_2_149_2","doi-asserted-by":"crossref","first-page":"430","DOI":"10.7326\/0003-4819-110-6-430","article-title":"Osteoporosis in hemochromatosis: Iron excess, gonadal deficiency, or other factors?","volume":"110","author":"Diamond T","year":"1989","unstructured":"Diamond T, Stiel D, Posen S. Osteoporosis in hemochromatosis: Iron excess, gonadal deficiency, or other factors? Ann Intern Med. 1989;110(6):430\u2013436.","journal-title":"Ann Intern Med"},{"issue":"1","key":"e_1_3_2_150_2","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1002\/ajh.10313","article-title":"Iron in sickle cell disease: A review why less is better","volume":"73","author":"Koduri PR","year":"2003","unstructured":"Koduri PR. Iron in sickle cell disease: A review why less is better. Am J Hematol. 2003;73(1):59\u201363.","journal-title":"Am J Hematol"},{"issue":"11","key":"e_1_3_2_151_2","doi-asserted-by":"crossref","first-page":"2279","DOI":"10.1002\/jbmr.1692","article-title":"Iron overload accelerates bone loss in healthy postmenopausal women and middle-aged men: A 3-year retrospective longitudinal study","volume":"27","author":"Kim BJ","year":"2012","unstructured":"Kim BJ, Ahn SH, Bae SJ, Kim EH, Lee SH, Kim HK, Choe JW, Koh JM, Kim GS. Iron overload accelerates bone loss in healthy postmenopausal women and middle-aged men: A 3-year retrospective longitudinal study. J Bone Miner Res. 2012;27(11):2279\u20132290.","journal-title":"J Bone Miner Res"},{"issue":"12","key":"e_1_3_2_152_2","doi-asserted-by":"crossref","first-page":"3409","DOI":"10.1007\/s00198-016-3719-z","article-title":"Thalassemia-associated osteoporosis: A systematic review on treatment and brief overview of the disease","volume":"27","author":"Dede AD","year":"2016","unstructured":"Dede AD, Trovas G, Chronopoulos E, Triantafyllopoulos IK, Dontas I, Papaioannou N, Tournis S. Thalassemia-associated osteoporosis: A systematic review on treatment and brief overview of the disease. Osteoporos Int. 2016;27(12):3409\u20133425.","journal-title":"Osteoporos Int"},{"key":"e_1_3_2_153_2","doi-asserted-by":"publisher","DOI":"10.1182\/blood-2009-12-260083"},{"issue":"8","key":"e_1_3_2_154_2","doi-asserted-by":"crossref","first-page":"2313","DOI":"10.1007\/s00198-010-1456-2","article-title":"Bone status in a mouse model of genetic hemochromatosis","volume":"22","author":"Guggenbuhl P","year":"2011","unstructured":"Guggenbuhl P, Fergelot P, Doyard M, Libouban H, Roth MP, Gallois Y, Chal\u00e8s G, Lor\u00e9al O, Chappard D. Bone status in a mouse model of genetic hemochromatosis. Osteoporos Int. 2011;22(8):2313\u20132319.","journal-title":"Osteoporos Int"},{"key":"e_1_3_2_155_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.gene.2014.02.023"},{"key":"e_1_3_2_156_2","doi-asserted-by":"publisher","DOI":"10.4161\/cc.25825"},{"issue":"2","key":"e_1_3_2_157_2","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1002\/jbmr.2986","article-title":"Lysosomal ca2+ signaling is essential for Osteoclastogenesis and bone remodeling","volume":"32","author":"Erkhembaatar M","year":"2017","unstructured":"Erkhembaatar M, Gu DR, Lee SH, Yang YM, Park S, Muallem S, Shin DM, Kim MS. Lysosomal ca2+ signaling is essential for Osteoclastogenesis and bone remodeling. J Bone Miner Res. 2017;32(2):385\u2013396.","journal-title":"J Bone Miner Res"},{"issue":"1","key":"e_1_3_2_158_2","doi-asserted-by":"crossref","DOI":"10.1038\/s41413-024-00326-8","article-title":"RUFY4 deletion prevents pathological bone loss by blocking endo-lysosomal trafficking of osteoclasts","volume":"12","author":"Kim M","year":"2024","unstructured":"Kim M, Park JH, Go M, Lee N, Seo J, Lee H, Kim D, Ha H, Kim T, Jeong MS, et al. RUFY4 deletion prevents pathological bone loss by blocking endo-lysosomal trafficking of osteoclasts. Bone Res. 2024;12(1): Article 29.","journal-title":"Bone Res"},{"issue":"15","key":"e_1_3_2_159_2","doi-asserted-by":"crossref","first-page":"1767","DOI":"10.1242\/jcs.110.15.1767","article-title":"Endocytic pathway from the basal plasma membrane to the ruffled border membrane in bone-resorbing osteoclasts","volume":"110","author":"Palokangas H","year":"1997","unstructured":"Palokangas H, Mulari M, V\u00e4\u00e4n\u00e4nen HK. Endocytic pathway from the basal plasma membrane to the ruffled border membrane in bone-resorbing osteoclasts. J Cell Sci. 1997;110(Pt 15):1767\u20131780.","journal-title":"J Cell Sci"},{"key":"e_1_3_2_160_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M010999200"},{"issue":"17","key":"e_1_3_2_161_2","doi-asserted-by":"crossref","DOI":"10.1172\/jci.insight.86330","article-title":"PLEKHM1\/DEF8\/RAB7 complex regulates lysosome positioning and bone homeostasis","volume":"1","author":"Fujiwara T","year":"2016","unstructured":"Fujiwara T, Ye S, Castro-Gomes T, Winchell CG, Andrews NW, Voth DE, Varughese KI, Mackintosh SG, Feng Y, Pavlos N, et al. PLEKHM1\/DEF8\/RAB7 complex regulates lysosome positioning and bone homeostasis. JCI Insight. 2016;1(17): Article e86330.","journal-title":"JCI Insight"},{"key":"e_1_3_2_162_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(01)00206-9"},{"key":"e_1_3_2_163_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.biopha.2021.111380","article-title":"Therapeutic potential of iron chelators on osteoporosis and their cellular mechanisms","volume":"137","author":"Zhang J","year":"2021","unstructured":"Zhang J, Zhao H, Yao G, Qiao P, Li L, Wu S. Therapeutic potential of iron chelators on osteoporosis and their cellular mechanisms. Biomed Pharmacother. 2021;137: Article 111380.","journal-title":"Biomed Pharmacother"},{"issue":"4","key":"e_1_3_2_164_2","doi-asserted-by":"crossref","DOI":"10.3390\/ph11040107","article-title":"Influence of iron on bone homeostasis","volume":"11","author":"Balogh E","year":"2018","unstructured":"Balogh E, Paragh G, Jeney V. Influence of iron on bone homeostasis. Pharmaceuticals. 2018;11(4): Article 107.","journal-title":"Pharmaceuticals"},{"issue":"1","key":"e_1_3_2_165_2","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-023-38165-6","article-title":"Restoration of lysosomal acidification rescues autophagy and metabolic dysfunction in non-alcoholic fatty liver disease","volume":"14","author":"Zeng J","year":"2023","unstructured":"Zeng J, Acin-Perez R, Assali EA, Martin A, Brownstein AJ, Petcherski A, Fern\u00e1ndez-del-Rio L, Xiao R, Lo CH, Shum M, et al. Restoration of lysosomal acidification rescues autophagy and metabolic dysfunction in non-alcoholic fatty liver disease. Nat Commun. 2023;14(1): Article 2573.","journal-title":"Nat Commun"},{"key":"e_1_3_2_166_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2020.02.021"},{"key":"e_1_3_2_167_2","doi-asserted-by":"publisher","DOI":"10.12998\/wjcc.v9.i30.8967"},{"issue":"2","key":"e_1_3_2_168_2","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S0167-4889(03)00042-9","article-title":"Effects of \u03b2-adrenergic agonists on bone-resorbing activity in human osteoclast-like cells","volume":"1640","author":"Arai M","year":"2003","unstructured":"Arai M, Nagasawa T, Koshihara Y, Yamamoto S, Togari A. Effects of \u03b2-adrenergic agonists on bone-resorbing activity in human osteoclast-like cells. Biochim Biophys Acta. 2003;1640(2):137\u2013142.","journal-title":"Biochim Biophys Acta"},{"key":"e_1_3_2_169_2","doi-asserted-by":"publisher","DOI":"10.1002\/jor.22133"},{"issue":"1","key":"e_1_3_2_170_2","doi-asserted-by":"crossref","DOI":"10.1186\/s12964-024-02021-x","article-title":"The SIRT5-JIP4 interaction promotes osteoclastogenesis by modulating RANKL-induced signaling transduction","volume":"23","author":"Zhu K","year":"2025","unstructured":"Zhu K, Sheng C, Zhang L, Yang Y, Chen X, Jiang T, Song J, Zhang D, Wang X, Zhao H, et al. The SIRT5-JIP4 interaction promotes osteoclastogenesis by modulating RANKL-induced signaling transduction. Cell Commun Signal. 2025;23(1): Article 26.","journal-title":"Cell Commun Signal"},{"key":"e_1_3_2_171_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cmet.2015.07.020"}],"container-title":["Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/spj.science.org\/doi\/pdf\/10.34133\/research.0840","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,11,17]],"date-time":"2025-11-17T19:24:58Z","timestamp":1763407498000},"score":1,"resource":{"primary":{"URL":"https:\/\/spj.science.org\/doi\/10.34133\/research.0840"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,1]]},"references-count":170,"alternative-id":["10.34133\/research.0840"],"URL":"https:\/\/doi.org\/10.34133\/research.0840","relation":{},"ISSN":["2639-5274"],"issn-type":[{"value":"2639-5274","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,1]]},"assertion":[{"value":"2025-06-09","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2025-07-25","order":1,"name":"revised","label":"Revised","group":{"name":"publication_history","label":"Publication History"}},{"value":"2025-07-25","order":2,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2025-08-14","order":3,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}],"article-number":"0840"}}