BMB Reports : eISSN 1976-670X

Cited by CrossRef (20)

  1. Zuzana Nahacka, Jaromir Novak, Renata Zobalova, Jiri Neuzil. Miro proteins and their role in mitochondrial transfer in cancer and beyond. Front. Cell Dev. Biol. 2022;10
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  3. Byung Chul Jung, Sung Hoon Kim, Yoonjung Cho, Yoon Suk Kim. Tumor suppressor Parkin induces p53-mediated cell cycle arrest in human lung and colorectal cancer cells. BMB Rep 2023;56:557
    https://doi.org/10.5483/BMBRep.2023-0134
  4. M. Florencia Camus, Abhilesh S Dhawanjewar. Multilevel selection on mitochondrial genomes. Current Opinion in Genetics & Development 2023;80:102050
    https://doi.org/10.1016/j.gde.2023.102050
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    https://doi.org/10.1007/s11064-023-03904-0
  6. Alexsandra S. Zelentsova, Alexei V. Deykin, Vladislav O. Soldatov, Anastasia A. Ulezko, Alina Y. Borisova, Veronika S. Belyaeva, Marina Y. Skorkina, Plamena R. Angelova. P2X7 Receptor and Purinergic Signaling: Orchestrating Mitochondrial Dysfunction in Neurodegenerative Diseases. eNeuro 2022;9:ENEURO.0092-22.2022
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  7. Silas A. Buck, M. Quincy Erickson-Oberg, Sai H. Bhatte, Chase D. McKellar, Vishan P. Ramanathan, Sophie A. Rubin, Zachary Freyberg. Roles of VGLUT2 and Dopamine/Glutamate Co-Transmission in Selective Vulnerability to Dopamine Neurodegeneration. ACS Chem. Neurosci. 2022;13:187
    https://doi.org/10.1021/acschemneuro.1c00741
  8. Sheng Li, Yanbing Liu, Sen Lu, Jiayi Xu, Xiaokun Liu, Di Yang, Yuxuan Yang, Lin Hou, Ning Li. A crazy trio in Parkinson's disease: metabolism alteration, α-synuclein aggregation, and oxidative stress. Mol Cell Biochem 2025;480:139
    https://doi.org/10.1007/s11010-024-04985-3
  9. Seunghee Lee, Sangguk Lee, Seon-Jin Lee, Su Wol Chung. Inhibition of mitoNEET induces Pink1-Parkin-mediated mitophagy. BMB Rep 2022;55:354
    https://doi.org/10.5483/BMBRep.2022.55.7.040
  10. Xiaoming Xi, Liang Han. Exploring the relationship between novel Coronavirus pneumonia and Parkinson’s disease. 2022;101:e31813
    https://doi.org/10.1097/MD.0000000000031813
  11. Qi Wu, Zhihong Wang, Siqi Chen, Xiaowei She, Shengyu Zhu, Pengcheng Li, Lang Liu, Chongchong Zhao, Kangdi Li, Anyi Liu, Changsheng Huang, Yaqi Chen, Fuqing Hu, Guihua Wang, Junbo Hu. USP26 promotes colorectal cancer tumorigenesis by restraining PRKN-mediated mitophagy. Oncogene 2024;43:1581
    https://doi.org/10.1038/s41388-024-03009-0
  12. Olga Buneeva, Alexei Medvedev. Ubiquitin Carboxyl-Terminal Hydrolase L1 and Its Role in Parkinson’s Disease. IJMS 2024;25:1303
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    https://doi.org/10.1016/B978-0-443-15260-3.00021-1
  14. Nur Aziz, Eunji Kim, Yanyan Yang, Han Gyung Kim, Tao Yu, Jae Youl Cho. p38-dependent c-Jun degradation contributes to reduced PGE2 production in sodium orthovanadate-treated macrophages. BMB Rep 2022;55:389
    https://doi.org/10.5483/BMBRep.2022.55.8.115
  15. Pernille Y. Ø. Nielsen, Justyna Okarmus, Morten Meyer. Role of Deubiquitinases in Parkinson’s Disease—Therapeutic Perspectives. Cells 2023;12:651
    https://doi.org/10.3390/cells12040651
  16. Garima Singh, Namrata Mittra, Chetna Singh. Impaired Mitochondrial Function and Ubiquitin Proteasome System Activate α-Synuclein Aggregation in Zinc-Induced Neurotoxicity: Effect of Antioxidants. J Mol Neurosci 2025;75
    https://doi.org/10.1007/s12031-024-02293-5
  17. Tracy-Shi Zhang Fang, Yu Sun, Andrew C. Pearce, Simona Eleuteri, Mark Kemp, Christopher A. Luckhurst, Rachel Williams, Ross Mills, Sarah Almond, Laura Burzynski, Nóra M. Márkus, Christopher J. Lelliott, Natasha A. Karp, David J. Adams, Stephen P. Jackson, Jin-Feng Zhao, Ian G. Ganley, Paul W. Thompson, Gabriel Balmus, David K. Simon. Knockout or inhibition of USP30 protects dopaminergic neurons in a Parkinson’s disease mouse model. Nat Commun 2023;14
    https://doi.org/10.1038/s41467-023-42876-1
  18. Shouhai Wu, Tongxiang Lin, Yang Xu. Polymorphic USP8 allele promotes Parkinson’s disease by inducing the accumulation of α-synuclein through deubiquitination. Cell. Mol. Life Sci. 2023;80
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  20. Woo Hyun Shin, Kwang Chul Chung. Tollip negatively regulates mitophagy by promoting the mitochondrial processing and cytoplasmic release of PINK1. BMB Rep 2022;55:494
    https://doi.org/10.5483/BMBRep.2022.55.10.082