en Experimental Neurobiology

Cited by CrossRef (13)

  1. María Teresa Ibarra-Gutiérrez, Norma Serrano-García, Marisol Orozco-Ibarra. Rotenone-Induced Model of Parkinson’s Disease: Beyond Mitochondrial Complex I Inhibition. Mol Neurobiol 2023;60:1929
    https://doi.org/10.1007/s12035-022-03193-8
  2. Qingxi Zhang, Yin Huang, Anbiao Wu, Qingrui Duan, Peikun He, Haifeng Huang, Yuyuan Gao, Kun Nie, Qicai Liu, Lijuan Wang. Calcium/calmodulin-dependent serine protein kinase exacerbates mitochondrial calcium uniporter-related mitochondrial calcium overload by phosphorylating α-synuclein in Parkinson’s disease. The International Journal of Biochemistry & Cell Biology 2023;157:106385
    https://doi.org/10.1016/j.biocel.2023.106385
  3. Jing Zhang, Bohao Sun, Jifeng Yang, Zhuo Chen, Zhengzheng Li, Nan Zhang, Hongzhi Li, Luxi Shen. Comparison of the effect of rotenone and 1‑methyl‑4‑phenyl‑1,2,3,6‑tetrahydropyridine on inducing chronic Parkinson's disease in mouse models. Mol Med Rep 2022;25
    https://doi.org/10.3892/mmr.2022.12607
  4. Peng Zhang, Madiha Rasheed, Junhan Liang, Chaolei Wang, Lin Feng, Zixuan Chen. Emerging Potential of Exosomal Non-coding RNA in Parkinson’s Disease: A Review. Front. Aging Neurosci. 2022;14
    https://doi.org/10.3389/fnagi.2022.819836
  5. Hajung Yoo, Jeongmin Lee, Bokwang Kim, Heechang Moon, Huisu Jeong, Kyungmi Lee, Woo Jeung Song, Junho K. Hur, Yohan Oh. Role of post-translational modifications on the alpha-synuclein aggregation-related pathogenesis of Parkinson’s disease. BMB Rep 2022;55:323
    https://doi.org/10.5483/BMBRep.2022.55.7.073
  6. Wenbo Zhang. Dapk1 promoted inflammation of infantile pneumonia by p38MAPK/NF-κB signaling pathway. Mol. Cell. Toxicol. 2021;17:297
    https://doi.org/10.1007/s13273-021-00136-7
  7. Carmela Conte, Angela Ingrassia, John Breve, John J. Bol, Evelien Timmermans-Huisman, Anne-Marie van Dam, Tommaso Beccari, Wilma D. J. van de Berg. Toll-like Receptor 4 Is Upregulated in Parkinson’s Disease Patients and Co-Localizes with pSer129αSyn: A Possible Link with the Pathology. Cells 2023;12:1368
    https://doi.org/10.3390/cells12101368
  8. Vladimir F. Lazarev, Elizaveta A. Dutysheva, Igor E. Kanunikov, Irina V. Guzhova, Boris A. Margulis. Protein Interactome of Amyloid-β as a Therapeutic Target. Pharmaceuticals 2023;16:312
    https://doi.org/10.3390/ph16020312
  9. Tao Zhang, Byeong Mo Kim, Tae Ho Lee. Death-associated protein kinase 1 as a therapeutic target for Alzheimer's disease. Transl Neurodegener 2024;13
    https://doi.org/10.1186/s40035-023-00395-5
  10. Sina Shadfar, Shristi Khanal, Ganesh Bohara, Geumjin Kim, Saeed Sadigh-Eteghad, Saeid Ghavami, Hyukjae Choi, Dong-Young Choi. Methanolic Extract of Boswellia serrata Gum Protects the Nigral Dopaminergic Neurons from Rotenone-Induced Neurotoxicity. Mol Neurobiol 2022;59:5874
    https://doi.org/10.1007/s12035-022-02943-y
  11. Alma Karen Lomeli-Lepe, Jose Luis Castañeda-Cabral, Silvia Josefina López-Pérez. Synucleinopathies: Intrinsic and Extrinsic Factors. Cell Biochem Biophys 2023;81:427
    https://doi.org/10.1007/s12013-023-01154-z
  12. Dongxiao Liang, Han Liu, Ruoqi Jin, Renyi Feng, Jiuqi Wang, Chi Qin, Rui Zhang, Yongkang Chen, Jingwen Zhang, Junfang Teng, Beisha Tang, Xuebing Ding, Xuejing Wang. Escherichia coli triggers α-synuclein pathology in the LRRK2 transgenic mouse model of PD . Gut Microbes 2023;15
    https://doi.org/10.1080/19490976.2023.2276296
  13. Yuan Tian, Xiaoqing Zheng, Ruomeng Li, Li Hu, Xindong Shui, Long Wang, Dongmei Chen, Tae Ho Lee, Tao Zhang. Quantitative Proteomic and Phosphoproteomic Analyses Reveal a Role of Death-Associated Protein Kinase 1 in Regulating Hippocampal Synapse. Mol Neurobiol 2023
    https://doi.org/10.1007/s12035-023-03674-4