Cited by 436Autophagy in Disease and TherapyCalcium signaling and nucleotide metabolismAlzheimer's disease research and treatments

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The Autophagy–Lysosomal Pathway in Neurodegeneration: A TFEB Perspective

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Martini-Stoica, Heidi, Xu, Yin, Ballabio, Andrea, Zheng, Hui·2016·Trends in Neurosciences

DOI 10.1016/j.tins.2016.02.002PMC PMC4928589

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Abstract

The autophagy-lysosomal pathway (ALP) is involved in the degradation of long-lived proteins. Deficits in the ALP result in protein aggregation, the generation of toxic protein species, and accumulation of dysfunctional organelles, which are hallmarks of Alzheimer's disease (AD), Parkinson's disease (PD), Huntington's disease (HD), and prion disease. Decades of research have therefore focused on enhancing the ALP in neurodegenerative diseases. More recently, transcription factor EB (TFEB), a major regulator of autophagy and lysosomal biogenesis, has emerged as a leading factor in addressing disease pathology. We review the regulation of the ALP and TFEB and their impact on neurodegenerative diseases. We also offer our perspective on the complex role of autophagy and TFEB in disease pathogenesis and its therapeutic implications through the examination of prion disease.

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Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
An RNA-Sequencing Transcriptome and Splicing Database of Glia, Neurons, and Vascular Cells of the Cerebral Cortex
Zhang, Y., Chen, K., Sloan, S. A., Bennett, M. L., Scholze, A. R., O'Keeffe, S., Phatnani, H. P., Guarnieri, P., Caneda, C., Ruderisch, N., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.1860-14.2014 · Cited by 4,875
mTOR: from growth signal integration to cancer, diabetes and ageing
Zoncu, R., Efeyan, A., & Sabatini, D. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3025 · Cited by 3,941
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Bcl-2 Antiapoptotic Proteins Inhibit Beclin 1-Dependent Autophagy
Pattingre, S., Tassa, A., Qu, X., Garuti, R., Liang, X. H., Mizushima, N., Packer, M., Schneider, M. D., & Levine, B. (2005) · Cell · doi:10.1016/j.cell.2005.07.002 · Cited by 3,536
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
TFEB Links Autophagy to Lysosomal Biogenesis
Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365
Self-citation
The Role of Atg Proteins in Autophagosome Formation
Mizushima, N., Yoshimori, T., & Ohsumi, Y. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154005 · Cited by 2,978
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774
Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563

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“All of these organelles show the capacity to store ARV nanoparticles (26, 55).”
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Retromer subunit, VPS29, regulates synaptic transmission and is required for endolysosomal function in the aging brain
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“We next examined well-established markers of lysosomal autophagy, which plays a critical role in nervous system homeostasis and neurodegeneration (Martini-Stoica et al., 2016; Menzies et al., 2015).”
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“In recent years, there has been an increasing appreciation of the dysregulation of Tfeb in neurodegenerative diseases ( 21 – 25 ), which has led to attempts toward enhancing cellular clearance by overexpressing Tfeb to activate autophagy and lysosomal pathways in cell culture or animal models of…”
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Xu, S., Yang, P., Qian, K., Li, Y., Guo, Q., Wang, P., Meng, R., Wu, J., Cao, J., Cheng, Y., et al. (2021) · Bioactive Materials · doi:10.1016/j.bioactmat.2021.09.017 · Cited by 48
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Sun, Y., Zhang, T., Zhang, Y., Li, J., Jin, L., Sun, Y., Shi, N., Liu, K., & Sun, X. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2599-3 · Cited by 45
“TFEB promotes the autophagosomal-lysosomal fusion for protein clearance and prevents accumulation of autophagosomes [52, 53].”
Background
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Wang, H., Zhou, R., Xu, F., Yang, K., Zheng, L., Zhao, P., Shi, G., Dai, L., Xu, C., Yu, L., et al. (2023) · Biomaterials Research · doi:10.1186/s40824-023-00385-8 · Cited by 48
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Background
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“14,15).”
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Song, H., Chen, Y., Chen, Y., Park, J., Zheng, M., Surh, Y., Kim, U., Park, J. W., Yu, R., Chung, H., et al. (2020) · Free Radical Research · doi:10.1080/10715762.2020.1791843 · Cited by 44
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Background
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“, 2015), longlived protein aggregates (Martini-Stoica et al., 2016), and lipid droplets (Settembre et al.”
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Background
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Background
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Background
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Background
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Background
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“TFEB, a master regulator of ALP [63, 65], has been widely demonstrated to ameliorate pathology in these diseases [4, 10, 47, 50].”
Background
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“Furthermore, pharmacological or genetic inhibition of mTOR activity is shown to improve autophagic clearance, reverse DA neuronal damage and alleviate PD symptoms (Jahrling and Laberge, 2015; Martini-Stoica et al., 2016).”
Background
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Background
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Background
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Background
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“Based on the emerging role of autophagy in neurodegeneration, the inducers of transcription factor EB (TFEB), a major regulator of autophagy and lysosomal biogenesis, have received considerable attention [17, 18].”
Background
20-Deoxyingenol alleviates osteoarthritis by activating TFEB in chondrocytes
Gu, M., Jin, J., Ren, C., Chen, X., Pan, Z., Wu, Y., Tian, N., Sun, L., Wu, A., Gao, W., et al. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2020.105361 · Cited by 33
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Fathalizadeh, A., Rahnemayan, S., Rajabi, H., Vahed, N., Kashani, H. R. K., Rezabakhsh, A., & Sanaie, S. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105839 · Cited by 33
Cyclodextrin has conflicting actions on autophagy flux in vivo in brains of normal and Alzheimer model mice
Yang, D.-S., Stavrides, P. H., Kumar, A. R., Jiang, Y., Mohan, P. S., Ohno, M., Dobrenis, K., Davidson, C. D., Saito, M., Pawlik, M., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx001 · Cited by 33
“To obtain insights into the underlying mechanism(s) for the increases in cathepsin levels and activity, we first examined if CYCLO induced alterations of TFEB and TFE3, members of the MiT family of transcription factors that drive the expression of most lysosomal genes, including cathepsins, as well as a number of oth…”
Background
TNEA therapy promotes the autophagic degradation of NLRP3 inflammasome in a transgenic mouse model of Alzheimer’s disease via TFEB/TFE3 activation
Lin, W., Zhao, L., Liang, G., Zhou, R., Zheng, X., Tao, R., Huo, Q., Su, C.-F., Li, M., Xu, N., et al. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02698-w · Cited by 32
Advanced oxidation protein products attenuate the autophagy-lysosome pathway in ovarian granulosa cells by modulating the ROS-dependent mTOR-TFEB pathway
Zhou, X., Lai, Y.-H., Zhang, J., Li, Y., Wu, X., Yang, Y., Zhang, X., Ma, L., Zheng, K.-M., Liu, Y., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06540-w · Cited by 32
“Therefore, we sought to investigate whether the inhibitory effects of AOPPs on autophagy and lysosomal biogenesis in the present study were also mediated by ROS.”
Pseudoginsenoside F11 ameliorates the dysfunction of the autophagy-lysosomal pathway by activating calcineurin-mediated TFEB nuclear translocation in neuron during permanent cerebral ischemia
Fu, X., Liu, Y., Zhang, H., Yu, X., Wang, X., Wu, C., & Yang, J. (2021) · Experimental Neurology · doi:10.1016/j.expneurol.2021.113598 · Cited by 31
Chlorogenic acid enhances autophagy by upregulating lysosomal function to protect against SH‑SY5Y cell injury induced by H2O2
Gao, L., Dai, Y., Li, X., Meng, S., Zhong, Z., & Xu, S. (2021) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2021.9843 · Cited by 31
“Defects of the ALP are strongly associated with AD and the ALP has been reported to regulate APP turnover and Aβ metabolism (43).”
Background
Molecular mechanisms of programmed cell death in methamphetamine-induced neuronal damage
Guo, D., Huang, X., Xiong, T., Wang, X., Zhang, J., Wang, Y., & Liang, J. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.980340 · Cited by 31
The Role of Traditional Chinese Medicine Natural Products in β-Amyloid Deposition and Tau Protein Hyperphosphorylation in Alzheimer’s Disease
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“150–152 Yang et al 153 demonstrated that celastrol, a new TFEB activator, facilitates the translocation of TFEB from the cytoplasm to the nucleus.”
Background
3-Hydroxybutyrate ameliorates sepsis-associated acute lung injury by promoting autophagy through the activation of GPR109α in macrophages
Mingxin, H., Yu, Y., Tang, X., Dong, R., Li, X., Li, F., Jin, Y., Gong, S., Wang, X., Zeng, Z., et al. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115632 · Cited by 30
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“This mechanism highlights the interplay between oxidative stress and lysosomal function, underscoring the critical role of MCOLN1 in regulating TFEB activity and maintaining cellular homeostasis through enhanced lysosomal and autophagic responses (Martini-Stoica et al. 2016).”
Loss of function of transcription factor EB remodels lipid metabolism and cell death pathways in the cardiomyocyte
Trivedi, P. C., Bartlett, J. J., Mercer, A., Slade, L., Surette, M. E., Ballabio, A., Flibotte, S., Hussein, B., Rodrigues, B. B., Kienesberger, P. C., et al. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165832 · Cited by 31
Self-citation
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“TFEB has been considered a therapeutic target with implications in various human diseases that are associated with defects in autophagy and lysosome-mediated degradation [1, 11].”
Highly Dynamic Changes in the Activity and Regulation of Macroautophagy in Hearts Subjected to Increased Proteotoxic Stress
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“…HF and essential for HF genesis as well (Wang et al., 2001a,b, 2011; Sanbe et al., 2004, 2007, 2009; Rajasekaran et al., 2007; Tannous et al., 2008b; McLendon and Robbins, 2011; Li et al., 2011a,b, 2017; Bhuiyan et al., 2013; Rajagopalan et al., 2013; Willis and Patterson, 2013; Meijering et …”
Background
Significance of cytosolic cathepsin D in Alzheimer's disease pathology: Protective cellular effects of PLGA nanoparticles against β‐amyloid‐toxicity
Wang, Y., Wu, Q., Anand, B. G., Karthivashan, G., Phukan, G., Yang, J., Thinakaran, G., Westaway, D. A., & Kar, S. (2020) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12647 · Cited by 29
Mask mitigates MAPT- and FUS-induced degeneration by enhancing autophagy through lysosomal acidification
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“Recently, research has emerged showing TFEB as a potent regulator of the autophagy-lysosomal pathway,(51,52) whose activation can promote lysosomal function and mitigate disease in a range of neurodegenerative disorders.(53) Here we show that”
Background
Autophagy-lysosomal defect in human CADASIL vascular smooth muscle cells
Hanemaaijer, E. S., Panahi, M., Swaddiwudhipong, N., Tikka, S., Winblad, B. G., Viitanen, M. H., Piras, A., & Behbahani, H. (2018) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2018.10.001 · Cited by 30
“Deficits in the autophagy-lysosomal pathway result in protein aggregation, generation of toxic protein species, and accumulation of dysfunctional organelles, which are hallmarks of many neurodegenerative disorders (Ciechanover and Kwon, 2015; Martini-Stoica et al., 2016; Zhang et al., 2009).”
Background
Lysosomes and signaling pathways for maintenance of quiescence in adult neural stem cells
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Exposure to 835 MHz radiofrequency electromagnetic field induces autophagy in hippocampus but not in brain stem of mice
Kim, J. H., Yu, D.-H., Kim, H., Huh, Y. H., Cho, S., Lee, J.-K., Kim, H., & Kim, H. R. (2017) · Toxicology and Industrial Health · doi:10.1177/0748233717740066 · Cited by 28
The role S‐nitrosylation in manganese‐induced autophagy dysregulation in SH‐SY5Y cells
Ma, Z., Wang, C., Liu, C., Yan, D., Deng, Y. L., Liu, W., Yang, T., Xu, Z., & Xu, B. (2017) · Environmental Toxicology · doi:10.1002/tox.22457 · Cited by 27
“The autophagy-lysosomal pathway is the major degradation pathway by which longer-lived macromolecules and dysfunctional organelles are cleared.(7) Macroautophagy is the most common autophagic process,”
Background
Effect of atorvastatin on Aβ1–42-induced alteration of SESN2, SIRT1, LC3II and TPP1 protein expressions in neuronal cell cultures
Çelik, H., Karahan, H., & Kelicen‐Uğur, P. (2019) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.13208 · Cited by 28
“[19–21] Many studies have shown the potential of statins to prevent the onset and development of AD.”
BackgroundInfluential
Trehalose ameliorates prodromal non-motor deficits and aberrant protein accumulation in a rotenone-induced mouse model of Parkinson’s disease
Moon, S.-H., Kwon, Y., Huh, Y. E., & Choi, H. J. (2022) · Archives of Pharmacal Research · doi:10.1007/s12272-022-01386-2 · Cited by 27
TFEB regulates sulfur amino acid and coenzyme A metabolism to support hepatic metabolic adaptation and redox homeostasis
Matye, D. J., Gunewardena, S., Chen, J., Wang, H., Wang, Y., Hasan, M. N., Gu, L., Clayton, Y. D., Du, Y., Chen, C., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33465-9 · Cited by 27
Bafilomycin A1 increases the sensitivity of tongue squamous cell carcinoma cells to cisplatin by inhibiting the lysosomal uptake of platinum ions but not autophagy
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Neuronal BAG3 attenuates tau hyperphosphorylation, synaptic dysfunction, and cognitive deficits induced by traumatic brain injury via the regulation of autophagy-lysosome pathway
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PPARα serves as a new receptor of aspirin for neuroprotection
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Autophagy and Redox Homeostasis in Parkinson’s: A Crucial Balancing Act
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“TFEB translocation is regulated primarily by phosphorylation [313, 315], via ERK2 (at S142), and via the autophagy inhibitor mTORC1 (at S211 and S142), to retain TFEB in the cytoplasm by binding to 14-3-3 proteins [314, 316, 317].”
Background
Inhibition of the TLR/NF‐κB Signaling Pathway and Improvement of Autophagy Mediates Neuroprotective Effects of Plumbagin in Parkinson’s Disease
Su, Y., Mao, L., Wang, Q., Xu, X., Qin, P., Huang, H., Zhang, Y., Zhou, Y., & Yan, J. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/1837278 · Cited by 26
“Numerous studies have suggested that TFEB is a promising therapeutic target for PD [52].”
Background
Premature senescence is regulated by crosstalk among TFEB, the autophagy lysosomal pathway and ROS derived from damaged mitochondria in NaAsO2-exposed auditory cells
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“Autophagy (macroauto-phagy) is a highly conserved eukaryotic cellular process that degrades intracellular macromolecules in lysosomes [34] and is particularly important in nondividing cells such as auditory hair cells [35] and neurons [32] because it maintains homeostasis and protects hearing.”
Background
Exosome Release Is Modulated by the Mitochondrial-Lysosomal Crosstalk in Parkinson’s Disease Stress Conditions
Currim, F., Singh, J., Shinde, A., Gohel, D., Roy, M., Singh, K., Shukla, S., Mane, M., Vasiyani, H., & Singh, R. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02243-3 · Cited by 26
Oxidative Stress Enhances Autophagy-Mediated Death Of Stem Cells Through Erk1/2 Signaling Pathway – Implications For Neurotransplantations
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Deacetylation of ZKSCAN3 by SIRT1 induces autophagy and protects SN4741 cells against MPP+-induced oxidative stress
Wu, X. G., Ren, Y., Wen, Y., Lu, S. S., Li, H., Yu, H., Li, W., & Zou, F. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.02.001 · Cited by 25
Impaired autophagy in amyloid-beta pathology: A traditional review of recent Alzheimer's research
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Catalase-deficient mice induce aging faster through lysosomal dysfunction
Dutta, R. K., Lee, J. N., Maharjan, Y., Park, C., Choe, S., Ho, Y., Kwon, H. M., & Park, R. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00969-2 · Cited by 29
“Hence TFEB, a major regulator of autophagy and lysosomal biogenesis, phosphorylates and trafficked to nucleus for clearance of damaged lysosomes [35].”
Background
Multidimensional autophagy nano-regulator boosts Alzheimer's disease treatment by improving both extra/intraneuronal homeostasis
Li, Y., Yang, P., Meng, R., Xu, S., Zhou, L., Qian, K., Wang, P., Cheng, Y., Sheng, D., Xu, M., et al. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.10.009 · Cited by 26
“Additionally, the augment of the nuclear and total expression of TFEB, a critical regulator of lysosomal function and biogenesis, whose transcriptional activity is activated upon nuclear translocation 37 , explained the mechanism by which RT-NM/ (Rapa þ GP-17) achieved lysosome regulation (Fig.”
Background
Early Mitochondrial Fragmentation and Dysfunction in a Drosophila Model for Alzheimer’s Disease
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PPARα Between Aspirin and Plaque Clearance
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“Lyso-somal adaptation under different physiological as well as pathological scenario is dependent on a regulatory gene network known as CLEAR (coordinated lysosomal expression and regulation), with the master regulator TFEB at its core [69, 70].”
TFEB Dependent Autophagy-Lysosomal Pathway: An Emerging Pharmacological Target in Sepsis
Liu, X., Zheng, X., Lu, Y., Chen, Q., Zheng, J., & Zhou, H. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.794298 · Cited by 24
“TFEB is a master transcriptional factor of the ALP (Martini-Stoica et al., 2016) and was initially identified as a master regulator of lysosomal biogenesis and degradation (Sardiello et al.”
BackgroundInfluential
Hinokitiol protects primary neuron cells against prion peptide-induced toxicity via autophagy flux regulated by hypoxia inducing factor-1
Moon, J.-H., Lee, J., Lee, Y.-J., & Park, S. (2016) · Oncotarget · doi:10.18632/oncotarget.8670 · Cited by 24
DNA Repair Inhibition Leads to Active Export of Repetitive Sequences to the Cytoplasm Triggering an Inflammatory Response
Song, X., Aw, J. T. M., Ma, F., Cheung, M. F., Leung, D., & Herrup, K. (2021) · The Journal of Neuroscience · doi:10.1523/jneurosci.0845-21.2021 · Cited by 23
Modulation of Tau Pathology in Alzheimer’s Disease by Dietary Bioactive Compounds
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“A variety of dietary bioactive compounds have been reported to significantly inhibit tau aggregation as well as promote tau depolymerization in vivo and in vitro [166–168].”
Background

Authors: Martini-Stoica, H., Xu, Y., Ballabio, A., & Zheng, H.
Affiliations: Baylor College of Medicine (US)
Corresponding author: Zheng, Hui
ORCID: Xu, Yin
Ballabio, Andrea
Zheng, Hui
Venue: Trends in Neurosciences
Publisher: Elsevier BV
Published: 2016-04
Volume: 39
Issue: 4
Pages: 221-234
ISSN: 0166-2236 (ISSN-L)
DOI: 10.1016/j.tins.2016.02.002
PMC: PMC4928589
OpenAlex: W2293027573
Cited by: 436
References: 127
Citations by year: 2026: 38 · 2025: 41 · 2024: 46 · 2023: 65 · 2022: 48 · 2021: 53 · 2020: 43 · 2019: 34 · 2018: 27 · 2017: 31 · 2016: 10
FWCI: 4.61
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in Neurosciences (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Institute on Aging (RF1AG020670, F30AG050412, R01AG020670)
National Institute of Neurological Disorders and Stroke (R01NS076117, RF1NS093652, R01NS078072, R01NS093652)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Keywords: autophagy-lysosome pathway, TFEB, neurodegenerative diseases, lysosomal biogenesis, protein aggregation, Alzheimer's disease, Parkinson's disease, Huntington's disease, prion disease, autophagy regulation, therapeutic target
MeSH terms: Animals, Autophagy, Brain, Humans, Lysosomes, Nerve Degeneration, Neurodegenerative Diseases, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors

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The Autophagy–Lysosomal Pathway in Neurodegeneration: A TFEB Perspective

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