BMB Reports : eISSN 1976-670X

Cited by CrossRef (15)

  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
    https://doi.org/10.3389/fcell.2022.937753
  2. Zhi-Guo Lu, Jie Shen, Jun Yang, Jing-Wen Wang, Rui-Chen Zhao, Tian-Lu Zhang, Jing Guo, Xin Zhang. Nucleic acid drug vectors for diagnosis and treatment of brain diseases. Sig Transduct Target Ther 2023;8
    https://doi.org/10.1038/s41392-022-01298-z
  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
  5. Sadegh Moradi Vastegani, Ava Nasrolahi, Shahab Ghaderi, Rafie Belali, Masome Rashno, Maryam Farzaneh, Seyed Esmaeil Khoshnam. Mitochondrial Dysfunction and Parkinson’s Disease: Pathogenesis and Therapeutic Strategies. Neurochem Res 2023;48:2285
    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
    https://doi.org/10.1523/ENEURO.0092-22.2022
  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. 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
  9. 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
  10. 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
  11. 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
  12. 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
  13. 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
    https://doi.org/10.1007/s00018-023-05006-0
  14. Elham Aryapour, Thomas Kietzmann. Mitochondria, mitophagy, and the role of deubiquitinases as novel therapeutic targets in liver pathology. J of Cellular Biochemistry 2022;123:1634
    https://doi.org/10.1002/jcb.30312
  15. 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