Abstract
Death-associated protein 3 (DAP3) is a highly conserved guanosine triphosphate (GTP) binding protein. As a component of the mitochondrial ribosome 28 S small subunit, DAP3 is involved in apoptosis pathways and plays a vital role in mitochondrial dynamics, mitochondrial protein synthesis, anoikis, and autophagy. Recently, DAP3 has been reported to participate in the development and progression of various cancers. In this review, we provide a brief overview of recent findings regarding the structure, subcellular localization, and function of DAP3 as well as its role in cancer development and progression.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Data availability
Not applicable.
References
Berger, T., & Kretzler, M. (2002). Interaction of DAP3 and FADD only after cellular disruption. Nature Immunology, 3(1), 3–5. https://doi.org/10.1038/ni0102-3b.
Boonstra, J., & Post, J., A (2004). Molecular events associated with reactive oxygen species and cell cycle progression in mammalian cells. Gene, 337, 1–13. https://doi.org/10.1016/j.gene.2004.04.032.
Cavdar, K. E., Ranasinghe, A., Burkhart, W., Blackburn, K., Koc, H., Moseley, A., & Spremulli, L. L. (2001). A new face on apoptosis: Death-associated protein 3 and PDCD9 are mitochondrial ribosomal proteins. FEBS Letters, 492(1–2), 166–170. https://doi.org/10.1016/s0014-5793(01)02250-5.
Chimento, A., Arianna, D. L., D’Amico, M., Francesca, D., A., & Pezzi, V. (2023). The involvement of natural polyphenols in molecular mechanisms inducing apoptosis in tumor cells: A promising adjuvant in Cancer Therapy. International Journal of Molecular Sciences, 24(2), 1680. https://doi.org/10.3390/ijms24021680.
Debnath, J., Gammoh, N., & Ryan, K. M. (2023). Autophagy and autophagy-related pathways in cancer. Nature Reviews Molecular Cell Biology, 24(8), 560–575. https://doi.org/10.1038/s41580-023-00585-z.
Feng, Q. L., Hu, K., Hu, H., Lu, Y., Zhang, H., Wang, G. L., Zhang, Q., Xu, Z., Gao, X. J., Jia, X., Zhu, H., Song, D., Yi, H., Peng, Y., Wu, X., Li, B., Zhu, W., & Shi, J. (2023). Berberine derivative DCZ0358 induce oxidative damage by ROS-mediated JNK signaling in DLBCL cells. International Immunopharmacology, 125(Pt A). https://doi.org/10.1016/j.intimp.2023.111139.
Festa, B. P., Siddiqi, F. H., Jimenez-Sanchez, M., Won, H., Rob, M., Djajadikerta, A., Stamatakou, E., & Rubinsztein, D., C (2023). Microglial-to-neuronal CCR5 signaling regulates autophagy in neurodegeneration. Neuron, 111(13), 2021–2037. https://doi.org/10.1016/j.neuron.2023.04.006.
Fox, L., Joanna, M. F., & Marion (2016). Targeting cell death signalling in cancer: Minimising ‘Collateral damage’. British Journal of Cancer, 115(1), 5–11. https://doi.org/10.1038/bjc.2016.111.
Franke, T., Hornik, C., Segev, L., Shostak, G., & Sugimoto, C. (2003). PI3K/Akt and apoptosis: Size matters. Oncogene, 22(56), 8983–8998. https://doi.org/10.1038/sj.onc.1207115.
Graef, M., & Nunnari, J. (2011). Mitochondria regulate autophagy by conserved signalling pathways. EMBO Journal, 30(11), 2101–2114. https://doi.org/10.1038/emboj.2011.104.
Guo, J., Yang, N., Zhang, J., Huang, Y., Xiang, Q., Wen, J., Chen, Y., Hu, T., Qiuyan, L., & Rao, C. (2024). Neurotoxicity study of ethyl acetate extract of Zanthoxylum armatum DC. On SH-SY5Y based on ROS mediated mitochondrial apoptosis pathway. Journal of Ethnopharmacology, 319(Pt3), 117321. https://doi.org/10.1016/j.jep.2023.117321.
Hailey, D. W., Rambold, A. S., Satpute-Krishnan, P., Mitra, K., Sougrat, R., Kim, P., K., & Lippincott-Schwartz, J. (2010). Mitochondria supply membranes for autophagosome biogenesis during starvation. Cell, 141(4), 656–667. https://doi.org/10.1016/j.cell.2010.04.009.
Han, J., An, O., Hong, H., Chan, T. H., M, & Chen, L. (2020). Suppression of adenosine-to-inosine (A-to-I) RNA editome by death associated protein 3 (DAP3) promotes cancer progression. Science Advances, 6(25), eaba5136. https://doi.org/10.1126/sciadvaba5136.
Han, J., An, O., Ren, X., Song, Y., Tang, S. J., Shen, H., Ke, X., Ng, V. H. E., Tay, D. J. T., Tan, H. Q., Kappei, D., Yang, H., & Chen, L. (2022). Multilayered control of splicing regulatory networks by DAP3 leads to widespread alternative splicing changes in cancer. Nature Communications, 13(1), 1793. https://doi.org/10.1038/s41467-022-29400-7.
Harada, T., Iwai, A., & Miyazaki, T. (2010). Identification of DELE, a novel DAP3-binding protein which is crucial for death receptor-mediated apoptosis induction. Apoptosis, 15(10), 1247–1255. https://doi.org/10.1007/s10495-010-0519-3.
Hulkko, S. M., & Zilliacus, J. (2002). Functional interaction between the pro-apoptotic DAP3 and the glucocorticoid receptor. Biochemical and Biophysical Research Communications, 295(3), 749–755. https://doi.org/10.1016/S0006-291X(02)00713-1.
Hulkko, S. M., Wakui, H., & Zilliacus, J. (2000). The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the glucocorticoid receptor and affects the receptor function. Biochemical Journal, 349(Pt 3), 885–893. https://doi.org/10.1042/bj3490885.
Jacques, C., Chevrollier, A., Loiseau, D., Lagoutte, L., Savagner, F., Malthiery, Y., & Reynier, P. (2006). mtDNA controls expression of the Death Associated protein 3. Experimental Cell Research, 312(6), 737–745. https://doi.org/10.1016/j.yexcr.2005.11.027.
Jacques, C., Fontaine, J., Franc, F., Mirebeau-Prunier, B., Triau, D., Savagner, S., F., & Malthiery, F. (2009). Death-associated protein 3 is overexpressed in human thyroid oncocytic tumours. British Journal of Cancer, 101(1), 132–138. https://doi.org/10.1038/sj.bjc.6605111.
Jia, Y., Ye, L., Ji, K., Zhang, L., Hargest, R., Ji, J., & Jiang, W., J (2014). Death-associated protein-3, DAP-3, correlates with preoperative chemotherapy effectiveness and prognosis of gastric cancer patients following perioperative chemotherapy and radical gastrectomy. British Journal of Cancer, 110(2), 421–429. https://doi.org/10.1038/bjc.2013.712.
Kim, H. R., Chae, H. J., Thomas, M., Miyazaki, T., Monosov, A., Monosov, E., Krajewska, M., Krajewski, S., & Reed, J. C. (2007). Mammalian dap3 is an essential gene required for mitochondrial homeostasis in vivo and contributing to the extrinsic pathway for apoptosis. The FASEB Journal, 21(1), 188–196. https://doi.org/10.1096/fj.06-6283com.
Kiraz, Y., Adan, A., Kartal, Y. M., & Baran, Y. (2016). Major apoptotic mechanisms and genes involved in apoptosis. Tumour Biology, 37(7), 8471–8486. https://doi.org/10.1007/s13277-016-5035-9.
Kissil, J. L., & Kimchi, A. (1997). Assignment of death associated protein 3 (DAP3) to human chromosome 1q21 by in situ hybridization. Cytogenetics and Cell Genetics, 77(3–4). https://doi.org/10.1159/000134587.
Kissil, J. L., & Kimchi, A. (1998). Death-associated proteins: From gene identification to the analysis of their apoptotic and tumour suppressive functions. Molecular Medicine Today, 4(6), 268–274. https://doi.org/10.1016/S1357-4310(98)01263-5.
Kissil, J. L., Deiss, L. P., Bayewitch, M., Raveh, T., Khaspekov, G., & Kimchi, A. (1995). Isolation of DAP3, a novel mediator of interferon-gamma-induced cell death. Journal of Biological Chemistry, 270(46), 27932–27936. https://doi.org/10.1074/jbc.270.46.27932.
Kissil, J. L., Cohen, O., Raveh, T., & Kimchi, A. (1999). Structure-function analysis of an evolutionary conserved protein, DAP3, which mediates TNF-alpha - and Fas-induced cell death. EMBO Journal, 18(2), 353–362. https://doi.org/10.1093/emboj/18.2.353.
Klionsky, D. J., Petroni, G., Amaravadi, R. K., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo-San, P. J., Cadwell, M., Cecconi, K., Choi, F., Choi, A. M. K., Chu, M. E., Codogno, C. T., Colombo, P., Cuervo, M. I., Deretic, A. M., Dikic, V., Elazar, I., Eskelinen, Z., … Pietrocola, F. (2021). Autophagy in major human diseases. EMBO Journal, 40(19). https://doi.org/10.15252/embj.2021108863.
Koren, I., Reem, E., & Kimchi, A. (2010). DAP1, a novel substrate of mTOR, negatively regulates autophagy. Current Biology, 20(12), 1093–1098. https://doi.org/10.1016/j.cub.2010.04.041.
Lee, H. Y., Son, S. W., Moeng, S., Choi, S. Y., & Park, J. K. (2021). The role of noncoding RNAs in the regulation of anoikis and anchorage-independent growth in cancer. International Journal of Molecular Sciences, 22(2). https://doi.org/10.3390/ijms22020627.
Lee, D., Kang, H. W., Kim, S. Y., Kim, M. J., Jeong, J. W., Hong, W. C., Fang, S., Kim, H. S., Lee, Y. S., Kim, H. J., & Park, J. S. (2022). Ivermectin and gemcitabine combination treatment induces apoptosis of pancreatic cancer cells via mitochondrial dysfunction. Frontiers in Pharmacology, 13, 934746. https://doi.org/10.3389/fphar.2022.934746.
Lee, H., Lee, T. J., Galloway, C. A., Zhi, W., Xiao, W., Mesy, B. K. L., Sharma, A., Teng, Y., Sesaki, H., & Yoon, Y. (2023). The mitochondrial fusion protein OPA1 is dispensable in the liver and its absence induces mitohormesis to protect liver from drug-induced injury. Nature Communications, 14(1), 6721–6721. https://doi.org/10.1038/S41467-023-42564-0.
Li, H. M., Fujikura, D., Harada, T., Uehara, J., Kawai, K., Akira, S., Reed, J. C., Iwai, A., & Miyazaki, T. (2009). IPS-1 is crucial for DAP3-mediated anoikis induction by caspase-8 activation. Cell Death & Differentiation, 16(2), 1615–1621. https://doi.org/10.1086/520246.
Lu, J., Li, Y., Gong, S., Wang, J., Lu, X., Jin, Q., Lu, B., & Chen, Q. (2022). Ciclopirox targets cellular bioenergetics and activates ER stress to induce apoptosis in non-small cell lung cancer cells. Cell Communication and Signaling, 20(1), 37. https://doi.org/10.1186/s12964-022-00847-x.
Malik, Q., & Herbert, K. E. (2012). Oxidative and non-oxidative DNA damage and cardiovascular disease. Free Radical Research, 46(4), 554–564. https://doi.org/10.3109/10715762.2012.663913.
Mariani, L., Beaudry, C., Mcdonough, W., Hoelzinger, S., Kaczmarek, D. B., Ponce, E., Coons, F., Giese, S. W., Seiler, A., R. W., & Berens, M. E. (2001). Death-associated protein 3 (Dap-3) is overexpressed in invasive glioblastoma cells in vivo and in glioma cell lines with induced motility phenotype in vitro. Clinical Cancer Research, 7(8), 2480–2489. https://doi.org/10.1093/carcin/22.8.1327.
Marsh, T., & Debnath, J. (2020). Autophagy suppresses breast cancer metastasis by degrading NBR1. Autophagy, 16(6), 1164–1165. https://doi.org/10.1080/15548627.2020.1753001.
Meggyeshazi, N., Andocs, G., Balogh, L., Balla, P., Kiszner, G., Teleki, I., Jeney, A., & Krenacs, T. (2014). DNA fragmentation and caspase-independent programmed cell death by modulated electrohyperthermia. Strahlentherapie Und Onkologie, 190(9), 815–822. https://doi.org/10.1007/s00066-014-0617-1.
Miller, D. R., & Thorburn, A. (2021). Autophagy and organelle homeostasis in cancer. Developmental Cell, 56(7), 906–918. https://doi.org/10.1016/j.devcel.2021.02.010.
Miller, J. L., Koc, H., & Koc, E., C (2008). Identification of phosphorylation sites in mammalian mitochondrial ribosomal protein DAP3. Protein Science, 17(2), 251–260. https://doi.org/10.1110/ps.073185608.
Miyazaki, T., & Reed, J. C. (2001). A GTP-binding adapter protein couples TRAIL receptors to apoptosis-inducing proteins. Nature Immunology, 2(6), 493–500. https://doi.org/10.1038/88684.
Miyazaki, T., Shen, M., Fujikura, D., Tosa, N., Kim, H. R., Kon, S., Uede, T., & Reed, J. C. (2004). Functional role of death-associated protein 3 (DAP3) in anoikis. Journal of Biological Chemistry, 279(43), 44667–44672. https://doi.org/10.1074/jbc.M408101200.
Morgan, C. J., Jacques, C., Savagner, F., Tourmen, Y., Mirebeau, D. P., Malthiery, Y., & Reynier, P. (2001). A conserved N-terminal sequence targets human DAP3 to mitochondria. Biochemical and Biophysical Research Communications, 280(1), 177–181. https://doi.org/10.1006/bbrc.2000.4119.
Mukamel, Z., & Kimchi, A. (2004). Death-associated protein 3 localizes to the mitochondria and is involved in the process of mitochondrial fragmentation during cell death. Journal of Biological Chemistry, 279(35), 36732–36738. https://doi.org/10.1074/jbc.M400041200.
Murata, Y., Wakoh, T., Uekawa, N., Sugimoto, M., Asai, A., Miyazaki, T., & Maruyama, M. (2006). Death-associated protein 3 regulates cellular senescence through oxidative stress response. FEBS Letters, 580(26), 6093–6099. https://doi.org/10.1016/j.febslet.2006.10.004.
Musicco, C., Signorile, A., Pesce, V., Loguercio, P. P., & Cormio, A. (2023). Mitochondria deregulations in cancer offer several potential targets of therapeutic interventions. International Journal of Molecular Sciences, 24(13), 10420. https://doi.org/10.3390/IJMS241310420.
O’Brien, T. W. (2003). Properties of human mitochondrial ribosomes. IUBMB Life, 55(9), 505–513. https://doi.org/10.1080/15216540310001626610.
Popov, S. V., Mukhomedzyanov, A. V., Voronkov, N. S., Derkachev, I. A., Boshchenko, A. A., Fu, F., Sufianova, G., Khlestkina, Z., M,S., & Maslov, L., N (2023). Regulation of autophagy of the heart in ischemia and reperfusion. Apoptosis, 28(1–2), 55–80. https://doi.org/10.1007/s10495-022-01786-1.
Sasaki, H., Ide, N., Yukiue, H., Kobayashi, Y., Fukai, I., Yamakawa, Y., & Fujii, Y. (2004). Arg and DAP3 expression was correlated with human thymoma stage. Clinical & Experimental Metastasis, 21(6), 507–513. https://doi.org/10.1007/s10585-004-2153-3.
Sato, Y., Yoshino, H., Kashiwakura, I., & Tsuruga, E. (2021). DAP3 is involved in modulation of cellular radiation response by RIG-I-Like receptor agonist in human lung adenocarcinoma cells. International Journal of Molecular Sciences, 22(1), 420. https://doi.org/10.3390/ijms22010420.
Sato, Y., Yoshino, H., Sato, K., Kashiwakura, I., & Tsuruga, E. (2023). DAP3-mediated cell cycle regulation and its association with radioresistance in human lung adenocarcinoma cell lines. Journal of Radiation Research, 64(3), 520–529. https://doi.org/10.1093/jrr/rrad016.
Saveanu, C., Fromont-Racine, M., Harington, A., Ricard, F., Namane, A., & Jacquier, A. (2001). Identification of 12 new yeast mitochondrial ribosomal proteins including 6 that have no prokaryotic homologues. Journal of Biological Chemistry, 276(19), 15861–15867. https://doi.org/10.1074/jbc.M010864200.
Schwickert, T. A., Tagoh, H., Schindler, K., Fischer, M., Jaritz, M., & Busslinger, M. (2019). Ikaros prevents autoimmunity by controlling anergy and toll-like receptor signaling in B cells. Nature Immunology, 20(11), 1517–1529. https://doi.org/10.1038/s41590-019-0490-2.
Smith, D. P., Rayter, S., Niederlander, I., Spicer, G., Jones, J.,C, M., & Ashworth, A. (2001). LIP1, a cytoplasmic protein functionally linked to the Peutz-Jeghers syndrome kinase LKB1. Human Molecular Genetics, 10(25), 2869–2877. https://doi.org/10.1093/hmg/10.25.2869.
Sui, L., Ye, L., Sanders, A., Yang, J., Hao, Y., Hargest, C. R., & Jiang, W. G. (2021). Expression of death associated proteins DAP1 and DAP3 in human pancreatic cancer. Anticancer Research, 41(5), 2357–2362. https://doi.org/10.21873/anticanres.15010.
Sui, L., Zeng, J., Zhao, H., Ye, L., Martin, T. A., Sanders, A., Ruge, J., Jiang, F., Dou, A., Hargest, Q. P., Song, R. X., & Jiang, W., J (2023). Death associated protein–3 (DAP3) and DAP3 binding cell death enhancer–1 (DELE1) in human colorectal cancer, and their impacts on clinical outcome and chemoresistance. International Journal of Oncology, 62(1), 7. https://doi.org/10.3892/ijo.2022.5455.
Suzuki, T., Terasaki, M., Takemoto-Hori, C., Hanada, T., Ueda, T., Wada, A., & Watanabe, K. (2001). Proteomic analysis of the mammalian mitochondrial ribosome. Identification of protein components in the 28 S small subunit. Journal of Biological Chemistry, 276(35), 33181–33195. https://doi.org/10.1074/jbc.M103236200.
Takeda, S., Iwai, A., Nakashima, M., Fujikura, D., Chiba, S., Li, H. M., Uehara, J., Kawaguchi, S., Kaya, M., Nagoya, S., Wada, T., Yuan, J., Rayter, S., Ashworth, A., Reed, J., Yamashita, C., Uede, T., T., & Miyazaki, T. (2007). LKB1 is crucial for TRAIL-mediated apoptosis induction in osteosarcoma. Anticancer Research, 27(2), 761–768. https://doi.org/10.1021/cm059988s.
Tosa, N., Iwai, A., Tanaka, T., Kumagai, T., Nitta, T., Chiba, S., Maeda, M., Takahama, Y., Uede, T., & Miyazaki, T. (2010). Critical function of death-associated protein 3 in T cell receptor-mediated apoptosis induction. Biochemical and Biophysical Research Communications, 395(3), 356–360. https://doi.org/10.1016/j.bbrc.2010.04.018.
Wang, J., Huang, F., Bai, Z., Chi, B., Wu, J., & Chen, X. (2015). Curcumol inhibits growth and induces apoptosis of colorectal cancer LoVo Cell line via IGF-1R and p38 MAPK pathway. International Journal of Molecular Sciences, 16(8), 19851–19867. https://doi.org/10.3390/ijms160819851.
Wang, J., Zhang, Y., Cao, J., Wang, Y., Anwar, N., Zhang, Z., Zhang, D., Ma, Y., Xiao, Y., Xiao, L., & Wang, X. (2023). The role of autophagy in bone metabolism and clinical significance. Autophagy, 19(9), 2409–2427. https://doi.org/10.1080/15548627.2023.2186112.
Wazir, U., Jiang, W. G., Sharma, A. K., & Mokbel, K. (2012). The mRNA expression of DAP3 in human breast cancer: Correlation with clinicopathological parameters. Anticancer Research, 32(2), 671–674. https://doi.org/10.1007/s10014-011-0075-8.
Wazir, U., Orakzai, M. M., Khanzada, Z. S., Jiang, W. G., Sharma, A. K., Kasem, A., & Mokbel, K. (2015). The role of death-associated protein 3 in apoptosis, anoikis and human cancer. Cancer Cell International, 15, 39. https://doi.org/10.1186/s12935-015-0187-z.
Xiao, L., Xian, H., Lee, K. Y., Xiao, B., Wang, H., Yu, F., Shen, H. M., & Liou, Y. C. (2015). Death-associated protein 3 regulates mitochondrial-encoded protein synthesis and mitochondrial dynamics. Journal of Biological Chemistry, 290(41), 24961–24974. https://doi.org/10.1074/jbc.M115.673343.
Yasumura, K., Sugimura, I., Igarashi, K., Kakinuma, S., Nishimura, M., Doi, M., & Shimada, Y. (2004). Altered expression of tfg and Dap3 in Ikaros-defective T-cell lymphomas induced by X-irradiation in B6C3F1 mice. British Journal of Haematology, 124(2), 179–185. https://doi.org/10.1046/j.1365-2141.2003.04768.x.
Yepuri, G., Ramirez, L. M., Theophall, G. G., Reverdatto, S. V., Quadri, N., Hasan, S. N., Bu, L., Thiagarajan, D., Wilson, R., Diez, R. L., Gugger, P. F., Mangar, K., Narula, N., Katz, S. D., Zhou, B., Li, H., Stotland, A. B., Gottlieb, R. A., Schmidt, A. M., Shekhtman, A., & Ramasamy, R. (2023). DIAPH1-MFN2 interaction regulates mitochondria-SR/ER contact and modulates ischemic/hypoxic stress. Nature Communications, 14(1), 6900. https://doi.org/10.1038/s41467-023-42521-x.
Yin, Y. J., Zhang, Y. H., Wang, Y., Jiang, H., Zhang, J. B., Liang, S., & Yuan, B. (2023). Ferulic acid ameliorates the quality of in vitro-aged bovine oocytes by suppressing oxidative stress and apoptosis. Aging (Albany NY), 15(21), 12497–12512. https://doi.org/10.18632/aging.205193.
Zhang, S., Zhang, Y., Feng, Y., Wu, J., Hu, Y., Lin, L., Xu, C., Chen, J., Tang, Z., Tian, H., & Chen, X. (2022). Biomineralized two-enzyme nanoparticles regulate tumor glycometabolism inducing tumor cell pyroptosis and robust antitumor immunotherapy. Advanced Materials, 34(50). https://doi.org/10.1002/adma.202206851.
Zhao, W., Zhang, L., Zhang, Y., Jiang, Z., Lu, H., Xie, Y., Han, W., Zhao, W., He, J., Shi, Z., Yang, H., Chen, J., Chen, S., Li, Z., Mao, J., Zhou, L., Gao, X., Li, W., Tan, G., Zhang, B., & Wang, Z. (2023). The CDK inhibitor AT7519 inhibits human glioblastoma cell growth by inducing apoptosis, pyroptosis and cell cycle arrest. Cell Death & Disease, 14(1). https://doi.org/10.1038/s41419-022-05528-8.
Zhu, M., Wang, J., & Zhou, R. (2022). Combination of metformin and oxaliplatin inhibits gastric cancer cell proliferation and induces apoptosis. Acta Biochimica Polonica, 69(2), 321–326. https://doi.org/10.18388/abp.2020_5750.
Acknowledgements
This study was supported by National Natural Science Foundation of China (31771534, and 32370741); Scientific Research Foundation of University of South China (211RJC002); The Special Funding for the Construction of Innovative Provinces in Hunan (2021SK4031).
Author information
Authors and Affiliations
Corresponding authors
Ethics declarations
Competing interests
The authors declare that they have no competing interests.
Additional information
Publisher’s Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.
About this article
Cite this article
Cao, T., Luo, X., Zheng, B. et al. Death-associated protein 3 in cell death and beyond. GENOME INSTAB. DIS. 5, 51–60 (2024). https://doi.org/10.1007/s42764-024-00125-9
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s42764-024-00125-9