Unraveling the link between neuropathy target esterase NTE/SWS, lysosomal storage diseases, inflammation, abnormal fatty acid metabolism, and leaky brain barrier
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Abstract
Mutations in Drosophila Swiss cheese (SWS) gene or its vertebrate orthologue neuropathy target esterase (NTE) lead to progressive neuronal degeneration in flies and humans. Despite its enzymatic function as a phospholipase is well established, the molecular mechanism responsible for maintaining nervous system integrity remains unclear. In this study, we found that NTE/SWS is present in surface glia that forms the blood-brain barrier (BBB) and that NTE/SWS is important to maintain its structure and permeability. Importantly, BBB glia-specific expression of Drosophila NTE/SWS or human NTE in the sws mutant background fully rescues surface glial organization and partially restores BBB integrity, suggesting a conserved function of NTE/SWS. Interestingly, sws mutant glia showed abnormal organization of plasma membrane domains and tight junction rafts accompanied by the accumulation of lipid droplets, lysosomes, and multilamellar bodies. Since the observed cellular phenotypes closely resemble the characteristics described in a group of metabolic disorders known as lysosomal storage diseases (LSDs), our data established a novel connection between NTE/SWS and these conditions. We found that mutants with defective BBB exhibit elevated levels of fatty acids, which are precursors of eicosanoids and are involved in the inflammatory response. Also, as a consequence of a permeable BBB, several innate immunity factors are upregulated in an age-dependent manner, while BBB glia-specific expression of NTE/SWS normalizes inflammatory response. Treatment with anti-inflammatory agents prevents the abnormal architecture of the BBB, suggesting that inflammation contributes to the maintenance of a healthy brain barrier. Considering the link between a malfunctioning BBB and various neurodegenerative diseases, gaining a deeper understanding of the molecular mechanisms causing inflammation due to a defective BBB could help to promote the use of anti-inflammatory therapies for age-related neurodegeneration.
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2 retracted
Rao, J. S., Rapoport, S. I., & Kim, H. (2011) · Translational Psychiatry · doi:10.1038/tp.2011.27 · Cited by 86 · see citing works
RetractedRao, J. S., Rapoport, S. I., & Kim, H. (2017) · Translational Psychiatry · doi:10.1038/tp.2017.97 · Cited by 10 · see citing works
RetractedHighly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
Brand, A. H., & Perrimon, N. (1993) · Development · doi:10.1242/dev.118.2.401 · Cited by 9,510 · see citing works
ColabFold - Making protein folding accessible to all
Mirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2021) · doi:10.1101/2021.08.15.456425 · Cited by 9,391 · see citing works
Inflamm‐aging: An Evolutionary Perspective on Immunosenescence
FRANCESCHI, C., BONAFÈ, M., VALENSIN, S., OLIVIERI, F., DE LUCA, M., OTTAVIANI, E., & DE BENEDICTIS, G. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06651.x · Cited by 5,358 · see citing works
Prostaglandins and Leukotrienes: Advances in Eicosanoid Biology
Funk, C. D. (2001) · Science · doi:10.1126/science.294.5548.1871 · Cited by 3,817 · see citing works
Inflammaging: a new immune–metabolic viewpoint for age-related diseases
Franceschi, C., Garagnani, P., Parini, P., Giuliani, C., & Santoro, A. (2018) · Nature Reviews Endocrinology · doi:10.1038/s41574-018-0059-4 · Cited by 3,586 · see citing works
Blood–brain barrier breakdown in Alzheimer disease and other neurodegenerative disorders
Sweeney, M. D., Sagare, A. P., & Zlokovic, B. V. (2018) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.188 · Cited by 3,076 · see citing works
Pericytes regulate the blood–brain barrier
Armulik, A., Genové, G., Mäe, M., Nisancioglu, M. H., Wallgard, E., Niaudet, C., He, L., Norlin, J., Lindblom, P., Strittmatter, K., et al. (2010) · Nature · doi:10.1038/nature09522 · Cited by 2,843 · see citing works
The mystery of membrane organization: composition, regulation and roles of lipid rafts
Sezgin, E., Levental, I., Mayor, S., & Eggeling, C. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.16 · Cited by 2,124 · see citing works
The machinery of macroautophagy
Feng, Y., He, D., Yao, Z., & Klionsky, D. J. (2014) · Cell Research · doi:10.1038/cr.2013.168 · Cited by 2,083 · see citing works
NLRP3 inflammasome activation: the convergence of multiple signalling pathways on ROS production?
Tschopp, J., & Schroder, K. (2010) · Nature reviews. Immunology · doi:10.1038/nri2725 · Cited by 1,859 · see citing works
A blood–brain barrier overview on structure, function, impairment, and biomarkers of integrity
Kadry, H., Noorani, B., & Cucullo, L. (2020) · Fluids and Barriers of the CNS · doi:10.1186/s12987-020-00230-3 · Cited by 1,853 · see citing works
The World Health Organization (WHO) approach to healthy ageing
Rudnicka, E., Napierała, P., Podfigurna, A., Męczekalski, B., Smolarczyk, R., & Grymowicz, M. (2020) · Maturitas · doi:10.1016/j.maturitas.2020.05.018 · Cited by 1,750 · see citing works
Model Systems, Lipid Rafts, and Cell Membranes
Simons, K., & Vaz, W. L. C. (2004) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.32.110601.141803 · Cited by 1,671 · see citing works
Role of neuroinflammation in neurodegeneration development
Zhang, W., Xiao, D., Mao, Q., & Xia, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01486-5 · Cited by 1,668 · cited 2× · see citing works
“Growing evidence suggests that inflammation plays a crucial role in age-related neurodegenerative diseases ( Zuo et al., 2019 ; Liu et al., 2018 ; Rojas-Gutierrez et al., 2017 ; Liu et al., 2017 ; Zhang et al., 2023 ).”
BackgroundInflammation and aging: signaling pathways and intervention therapies
Li, X., Li, C., Zhang, W., Wang, Y., Qian, P., & Huang, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01502-8 · Cited by 1,443 · cited 1× · see citing works
“…frequently develop chronic, low-grade inflammation, a condition often named inflammaging, which is characterized by a sustained increase in inflammatory markers without apparent infection or injury ( Chitnis and Weiner, 2017 ; Franceschi et al., 2018 ; McGeer and McGeer, 2004 ; Li et al., 2023 ).”
BackgroundAutophagy in healthy aging and disease
Aman, Y., Schmauck-Medina, T., Hansen, M., Morimoto, R. I., Simon, A. K., Bjedov, I., Palikaras, K., Simonsen, A., Johansen, T., Tavernarakis, N., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00098-4 · Cited by 1,313 · see citing works
The Toll and Imd pathways are the major regulators of the immune response in Drosophila
Gregorio, E. D., Spellman, P. T., Tzou, P., Rubin, G. M., & Lemaître, B. (2002) · The EMBO Journal · doi:10.1093/emboj/21.11.2568 · Cited by 936 · see citing works
Role of ROS and Nutritional Antioxidants in Human Diseases
Liu, Z., Ren, Z., Zhang, J., Chuang, C.-C., Kandaswamy, E., Zhou, T., & Zuo, L. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00477 · Cited by 860 · see citing works
Oxidative Stress in Neurodegenerative Diseases: From Molecular Mechanisms to Clinical Applications
Liu, Z., Zhou, T., Ziegler, A. C., Dimitrion, P., & Zuo, L. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/2525967 · Cited by 810 · see citing works
Takata, F., Nakagawa, S., Matsumoto, J., & Dohgu, S. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.661838 · Cited by 651 · see citing works
Inflammaging and Oxidative Stress in Human Diseases: From Molecular Mechanisms to Novel Treatments
Zuo, L., Prather, E. R., Stetskiv, M., Garrison, D. E., Meade, J. R., Peace, T. I., & Zhou, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184472 · Cited by 545 · see citing works
Inflammation and the Degenerative Diseases of Aging
McGeer, P. L., & McGeer, E. G. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1332.007 · Cited by 519 · see citing works
Drosophilatools and assays for the study of human diseases
Uğur, B., Chen, K., & Bellen, H. J. (2016) · Disease Models & Mechanisms · doi:10.1242/dmm.023762 · Cited by 519 · see citing works
Korbecki, J., & Bajdak-Rusinek, K. (2019) · Inflammation Research · doi:10.1007/s00011-019-01273-5 · Cited by 517 · see citing works
CNS inflammation and neurodegeneration
Chitnis, T., & Weiner, H. L. (2017) · Journal of Clinical Investigation · doi:10.1172/jci90609 · Cited by 484 · see citing works
Contacts between the endoplasmic reticulum and other membranes in neurons
Wu, Y., Whiteus, C., Xu, C. S., Hayworth, K. J., Weinberg, R. J., Hess, H. F., & Camilli, P. V. D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1701078114 · Cited by 481 · see citing works
Tight junctions are membrane microdomains
Nusrat, A., Parkos, C. A., Verkade, P., Foley, C. S., Liang, T. W., Innis‐Whitehouse, W., Eastburn, K., & Madara, J. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.10.1771 · Cited by 430 · see citing works
Striatal Blood–Brain Barrier Permeability in Parkinson'S Disease
Gray, M. T., & Woulfe, J. M. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2015.32 · Cited by 409 · see citing works
Multiple Roles of the Small GTPase Rab7
Guerra, F., & Bucci, C. (2016) · Cells · doi:10.3390/cells5030034 · Cited by 394 · see citing works
Oxidative stress and calcium dysregulation by palmitate in type 2 diabetes
Ly, L. D., Xu, S., Choi, S.-K., Ha, C.-M., Thoudam, T., Cha, S.-K., Wiederkehr, A., Wollheim, C. B., Lee, I.-K., & Park, K.-S. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.157 · Cited by 378 · see citing works
Involvement of Lipids in Alzheimer’s Disease Pathology and Potential Therapies
Chew, H., Solomon, V. A., & Fonteh, A. N. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00598 · Cited by 353 · see citing works
Nimrod, a Putative Phagocytosis Receptor with EGF Repeats in Drosophila Plasmatocytes
Kurucz, É., Márkus, R., Zsámboki, J., Medzihradszky, K. F., Darula, Z., Vilmos, P., Udvardy, A., Krausz, I., Lukácsovich, T., Gateff, E. A., et al. (2007) · Current Biology · doi:10.1016/j.cub.2007.02.041 · Cited by 347 · see citing works
Munji, R. N., Soung, A., Weiner, G., Sohet, F., Semple, B. D., Trivedi, A. A., Gimlin, K., Kotoda, M., Korai, M., Aydin, S., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0497-x · Cited by 332 · see citing works
Blood–Brain Barrier Dynamics to Maintain Brain Homeostasis
Segarra, M., Aburto, M. R., & Acker‐Palmer, A. (2021) · Trends in Neurosciences · doi:10.1016/j.tins.2020.12.002 · Cited by 304 · see citing works
Hayashi, S., Ito, K., Sado, Y., Taniguchi, M., Akimoto, A., Takeuchi, H., Aigaki, T., Matsuzaki, F., Nakagoshi, H., Tanimura, T., et al. (2002) · genesis · doi:10.1002/gene.10137 · Cited by 301 · see citing works
The glia of the adult D rosophila nervous system
Kremer, M. C., Jung, C., Batelli, S., Rubin, G. M., & Gaul, U. (2017) · Glia · doi:10.1002/glia.23115 · Cited by 297 · see citing works
Drosophila as a model for ageing
Piper, M. D. W., & Partridge, L. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.09.016 · Cited by 273 · see citing works
Drosophila melanogaster as a model organism for Alzheimer’s disease
Prüßing, K., Voigt, A., & Schulz, J. B. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-35 · Cited by 271 · see citing works
Lipid droplets in neurodegenerative disorders
Farmer, B. C., Walsh, A. E., Kluemper, J. C., & Johnson, L. A. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00742 · Cited by 270 · see citing works
Emerging Roles for the Lysosome in Lipid Metabolism
Thelen, A. M., & Zoncu, R. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.07.006 · Cited by 268 · see citing works
The Swiss Cheese Mutant Causes Glial Hyperwrapping and Brain Degeneration in Drosophila
Kretzschmar, D., Hasan, G., Sharma, S., Heisenberg, M., & Benzer, S. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-19-07425.1997 · Cited by 251 · see citing works
GPCR Signaling Is Required for Blood-Brain Barrier Formation in Drosophila
Schwabe, T., Bainton, R. J., Fetter, R. D., Heberlein, U., & Gaul, U. (2005) · Cell · doi:10.1016/j.cell.2005.08.037 · Cited by 247 · see citing works
Neuropathy Target Esterase Gene Mutations Cause Motor Neuron Disease
Rainier, S. R., Bui, M., Mark, E., Thomas, D., Tokarz, D. A., Ming, L., Delaney, C. E., Richardson, R. J., Albers, J. W., Matsunami, N., et al. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2007.12.018 · Cited by 245 · see citing works
Lysosomal dysfunction in neurodegeneration: emerging concepts and methods
Udayar, V., Chen, Y., Sidransky, E., & Jagasia, R. (2022) · Trends in Neurosciences · doi:10.1016/j.tins.2021.12.004 · Cited by 238 · see citing works
Bainton, R. J., Tsai, L. T.-Y., Schwabe, T., DeSalvo, M. K., Gaul, U., & Heberlein, U. (2005) · Cell · doi:10.1016/j.cell.2005.07.029 · Cited by 228 · see citing works
Validation of Serum Markers for Blood-Brain Barrier Disruption in Traumatic Brain Injury
Blyth, B. J., Farhavar, A., Gee, C., Hawthorn, B., He, H., Nayak, A., Stöcklein, V., & Bazarian, J. (2009) · Journal of Neurotrauma · doi:10.1089/neu.2008.0738 · Cited by 227 · see citing works
Synofzik, M., Gonzalez, M., Lourenço, C. M., Coutelier, M., Haack, T. B., Rebelo, A. P., Hannequin, D., Strom, T. M., Prokisch, H., Kernstock, C., et al. (2013) · Brain · doi:10.1093/brain/awt326 · Cited by 227 · see citing works
Tessitore, A., Martin, M. D. P., Sano, R., Ma, Y., Männ, L., Ingrassia, A. M. T., Laywell, E. D., Steindler, D. A., Hendershot, L. M., & d’Azzo, A. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.029 · Cited by 226 · see citing works
Targeting lysosomes in human disease: from basic research to clinical applications
Cao, M., Luo, X., Wu, K., & He, X. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00778-y · Cited by 225 · see citing works
Phospholipid subcellular localization and dynamics
Yang, Y., Lee, M., & Fairn, G. D. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.000582 · Cited by 224 · see citing works
Spastic paraplegia proteins spastizin and spatacsin mediate autophagic lysosome reformation
Chang, J., Lee, S., & Blackstone, C. D. (2014) · Journal of Clinical Investigation · doi:10.1172/jci77598 · Cited by 216 · see citing works
Zaccheo, O., Dinsdale, D. D., Meacock, P. A., & Glynn, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400830200 · Cited by 214 · see citing works
The Drosophila blood-brain barrier: development and function of a glial endothelium
Limmer, S., Weiler, A., Volkenhoff, A., Babatz, F., & Klämbt, C. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00365 · Cited by 214 · see citing works
Cao, Y., Chtarbanova, S., Petersen, A. J., & Ganetzky, B. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306220110 · Cited by 205 · see citing works
Rojas-Gutierrez, E., Muñoz‐Arenas, G., Treviño, S., Espinosa, B., Chávez, R., Rojas, K., Flores, G., Díaz, A., & Guevara, J. (2017) · Synapse · doi:10.1002/syn.21990 · Cited by 198 · see citing works
Circulating metabolites and general cognitive ability and dementia: evidence from 11 cohort studies
van der Lee, S. J., Teunissen, C. E., Pool, R., Shipley, M. J., Teumer, A., Chouraki, V., Melo van Lent, D., Tynkkynen, J., Fischer, K., Hernesniemi, J., et al. (2018) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2017.11.012 · Cited by 197 · see citing works
Kounatidis, I., Chtarbanova, S., Cao, Y., Hayne, M. R., Jayanth, D., Ganetzky, B., & Ligoxygakis, P. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.04.007 · Cited by 190 · see citing works
A research framework for the United Nations Decade of Healthy Ageing (2021–2030)
Keating, N. C. (2022) · European Journal of Ageing · doi:10.1007/s10433-021-00679-7 · Cited by 189 · see citing works
Drosophila glia: Few cell types and many conserved functions
Yildirim, K., Petri, J., Kottmeier, R., & Klämbt, C. (2018) · Glia · doi:10.1002/glia.23459 · Cited by 184 · see citing works
Brain-specific deletion of neuropathy target esterase/ swisscheese results in neurodegeneration
Akassoglou, K., Malester, B., Xu, J., Tessarollo, L., D, J. R. M., & Chao, M. V. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401030101 · Cited by 178 · see citing works
Morphological diversity and development of glia in Drosophila
Hartenstein, V. (2011) · Glia · doi:10.1002/glia.21162 · Cited by 172 · see citing works
Epithelial cell–cell junctions and plasma membrane domains
Giepmans, B. N. G., & van IJzendoorn, S. C. D. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.07.015 · Cited by 170 · see citing works
Grassi, S., Giussani, P., Mauri, L., Prioni, S., Sonnino, S., & Prinetti, A. (2019) · Journal of Lipid Research · doi:10.1194/jlr.tr119000427 · Cited by 169 · see citing works
Defects in ER–endosome contacts impact lysosome function in hereditary spastic paraplegia
Allison, R. J., Edgar, J. R., Pearson, G., Rizo, T., Newton, T. M., Günther, S., Berner, F., Hague, J., Connell, J. W., Winkler, J., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201609033 · Cited by 166 · see citing works
All vertebrates started out with a glial blood‐brain barrier 4–500 million years ago
Bundgaard, M., & Abbott, N. J. (2008) · Glia · doi:10.1002/glia.20642 · Cited by 163 · see citing works
Chapter 5 Biomarkers Related To Aging In Human Populations
Crimmins, E. M., Vasunilashorn, S. M., Kim, J. K., & Alley, D. E. (2008) · Advances in clinical chemistry · doi:10.1016/s0065-2423(08)00405-8 · Cited by 156 · see citing works
n -3 PUFA and inflammation: from membrane to nucleus and from bench to bedside
Calder, P. C. (2020) · Proceedings of The Nutrition Society · doi:10.1017/s0029665120007077 · Cited by 154 · see citing works
Vascular pathology in multiple sclerosis: reframing pathogenesis around the blood-brain barrier
Spencer, J. I., Bell, J. S., & DeLuca, G. C. (2017) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2017-316011 · Cited by 152 · see citing works
Issa, A.-R., Sun, J., Petitgas, C., Mesquita, A., Dulac, A., Robin, M., Mollereau, B., Jenny, A., Chérif‐Zahar, B., & Birman, S. (2018) · Autophagy · doi:10.1080/15548627.2018.1491489 · Cited by 152 · see citing works
Lush, M. J., Li, Y., Read, D. J., WILLIS, A. C., & Glynn, P. (1998) · Biochemical Journal · doi:10.1042/bj3320001 · Cited by 150 · see citing works
Lipid Transport and Metabolism at the Blood-Brain Interface: Implications in Health and Disease
Pifferi, F., Laurent, B., & Plourde, M. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.645646 · Cited by 149 · see citing works
Wilson, E. L., & Metzakopian, E. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00705-8 · Cited by 147 · see citing works
Kim, S., Zhang, Z., Hitomi, E., Lee, Y., & Mukherjee, A. B. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl105 · Cited by 147 · see citing works
Kim, S. Y., Buckwalter, M., Soreq, H., Vezzani, A., & Kaufer, D. (2012) · Epilepsia · doi:10.1111/j.1528-1167.2012.03701.x · Cited by 145 · see citing works
Mühlig-Versen, M., da Cruz, A. B., Tschäpe, J., Moser, M., Büttner, R., Athenstaedt, K., Glynn, P., & Kretzschmar, D. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.5097-04.2005 · Cited by 145 · see citing works
XuvTools: free, fast and reliable stitching of large 3D datasets
Emmenlauer, M., Ronneberger, O., Ponti, A., Schwarb, P., Griffa, A., Filippi, A., Nitschke, R., Driever, W., & BURKHARDT, H. (2009) · Journal of Microscopy · doi:10.1111/j.1365-2818.2008.03094.x · Cited by 142 · see citing works
Vesicle associated membrane protein B (VAPB) is decreased in ALS spinal cord
Anagnostou, G., Akbar, M. T., Paul, P., Angelinetta, C., Steiner, T. J., & de Belleroche, J. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.07.005 · Cited by 138 · see citing works
Dissecting muscle and neuronal disorders in a Drosophila model of muscular dystrophy
Shcherbata, H. R., Yatsenko, A. S., Patterson, L. B., Sood, V. D., Nudel, U., Yaffe, D., Baker, D. A., & Ruohola‐Baker, H. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601503 · Cited by 137 · see citing works
Self-citationAutophagy, Mitochondria and Cell Death in Lysosomal Storage Diseases
Kiselyov, K., Jennings, J., Rbaibi, Y., & Chu, C. T. (2007) · Autophagy · doi:10.4161/auto.3906 · Cited by 134 · see citing works
Yasuda, M., Tanaka, Y., Kume, S., Morita, Y., Chin-Kanasaki, M., Araki, H., Isshiki, K., Araki, S.-I., Koya, D., Haneda, M., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.04.001 · Cited by 123 · see citing works
Lysosomal abnormalities in hereditary spastic paraplegia types SPG 15 and SPG 11
Renvoisé, B., Chang, J., Singh, R., Yonekawa, S., FitzGibbon, E. J., Mankodi, A. K., Vanderver, A. L., Schindler, A. B., Toro, C., Gahl, W. A., et al. (2014) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.64 · Cited by 120 · see citing works
Neuropathy target esterase (NTE): overview and future
Richardson, R. J., Hein, N. D., Wijeyesakere, S. J., Fink, J. K., & Махаева, Г. Ф. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.10.024 · Cited by 115 · see citing works
Topaloglu, A. K., Lomniczi, A., Kretzschmar, D., Dissen, G. A., Kotan, L. D., McArdle, C. A., Koç, A., Hamel, B. C. J., Güçlü, M., Çakır, E. D. P., et al. (2014) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2014-1836 · Cited by 103 · see citing works
Prostaglandins and Other Eicosanoids in Insects: Biosynthesis and Biological Actions
STANLEY, D. W., & Kim, Y. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2018.01927 · Cited by 102 · see citing works
Hereditary spastic paraplegia‐linked REEP1 modulates endoplasmic reticulum/mitochondria contacts
Lim, Y., Cho, I., Schoel, L. J., Cho, G., & Golden, J. A. (2015) · Annals of Neurology · doi:10.1002/ana.24488 · Cited by 100 · see citing works
Neuropathy Target Esterase Is Required for Adult Vertebrate Axon Maintenance
Read, D. J., Li, Y., Chao, M. V., Cavanagh, J. B., & Glynn, P. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3007-09.2009 · Cited by 99 · see citing works
Innate and adaptive immune activation in the brain of MPS IIIB mouse model
DiRosario, J., DiCaprio, E. L., Wang, C., Etter, J. P., Charrier, A., Jukkola, P. I., Auer, H., Best, V., Newsom, D. L., McCarty, D. M., et al. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21912 · Cited by 98 · see citing works
Miao, H., Chen, L., Hao, L., Zhang, X., Chen, Y., Ruan, Z., & Liang, H. (2015) · Scientific Reports · doi:10.1038/srep13092 · Cited by 96 · see citing works
Glial Cell Migration in the Eye Disc
Silies, M., Yuva, Y., Engelen, D., Aho, A., Stork, T., & Klämbt, C. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3583-07.2007 · Cited by 91 · see citing works
Immunosuppression alters disease severity in juvenile Batten disease mice
Seehafer, S. S., Ramirez‐Montealegre, D., Wong, A. M. S., Chan, C., Castaneda, J. A., Horak, M., Ahmadi, S. M., Lim, M. J., Cooper, J. D., & Pearce, D. A. (2010) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2010.08.024 · Cited by 82 · see citing works
Fatty Acids, Antioxidants and Physical Activity in Brain Aging
Freitas, H. R., Ferreira, G. C., Trevenzoli, I. H., Oliveira, K. J., & Reis, R. A. D. M. (2017) · Nutrients · doi:10.3390/nu9111263 · Cited by 82 · see citing works
Preserving Lysosomal Function in the Aging Brain: Insights from Neurodegeneration
Peng, W., Minakaki, G., Nguyen, M., & Krainc, D. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00742-3 · Cited by 79 · see citing works
Neuropathy target esterase and phospholipid deacylation
Glynn, P. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2005.08.002 · Cited by 73 · see citing works
Namekawa, M., Muriel, M., Janer, A., Latouche, M., Dauphin, A., Debeir, T., Martin, E., Duyckaerts, C. J., Prigent, A., Depienne, C., et al. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.01.012 · Cited by 72 · see citing works
Emre, C., Do, K. V., Jun, B., Hjorth, E., Alcalde, S. G., Kautzmann, M.-A. I., Gordon, W. C., Nilsson, P., Bazan, N. G., & Schultzberg, M. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01216-4 · Cited by 71 · see citing works
Innate immune responses to paraquat exposure in a Drosophila model of Parkinson’s disease
Maitra, U., Scaglione, M., Chtarbanova, S., & O’Donnell, J. M. (2019) · Scientific Reports · doi:10.1038/s41598-019-48977-6 · Cited by 70 · see citing works
Vainio, S., Bykov, I., Hermansson, M., Jokitalo, E., Somerharju, P. J., & Ikonen, E. (2005) · Biochemical Journal · doi:10.1042/bj20050460 · Cited by 66 · see citing works
Calorimetric detection of curvature strain in phospholipid bilayers
Epand, R. M., & Epand, R. F. (1994) · Biophysical Journal · doi:10.1016/s0006-3495(94)80935-x · Cited by 66 · see citing works
da Cruz, A. B., Wentzell, J. S., & Kretzschmar, D. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.3015-08.2008 · Cited by 64 · see citing works
ER – lysosome contacts at a pre-axonal region regulate axonal lysosome availability
Özkan, N., Koppers, M., van Soest, I., van Harten, A., Jurriens, D., Liv, N., Klumperman, J., Kapitein, L. C., Hoogenraad, C. C., & Farı́as, G. G. (2021) · Nature Communications · doi:10.1038/s41467-021-24713-5 · Cited by 63 · see citing works
Cloning and expression of the murine sws/NTE gene
Moser, M., Stempfl, T., Li, Y., Glynn, P., Büttner, R., & Kretzschmar, D. (2000) · Mechanisms of Development · doi:10.1016/s0925-4773(99)00239-7 · Cited by 61 · see citing works
Richardson, R. J., Fink, J. K., Glynn, P., Hufnagel, R. B., Махаева, Г. Ф., & Wijeyesakere, S. J. (2020) · Advances in neurotoxicology · doi:10.1016/bs.ant.2020.01.001 · Cited by 61 · see citing works
Regulska, M., Szuster-Głuszczak, M., Trojan, E., Leśkiewicz, M., & Basta‐Kaim, A. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200807144530 · Cited by 60 · see citing works
Kondo, Y., Wenger, D. A., Gallo, V., & Duncan, I. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506473102 · Cited by 57 · see citing works
Li, C., Qian, T., He, R., Wan, C., Liu, Y., & Yu, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.627700 · Cited by 57 · see citing works
Oxidative Stress Is Activated by Free Fatty Acids in Cultured Human Hepatocytes
Soardo, G., Donnini, D., Domenis, L., Catena, C., Silvestri, D. D., Cappello, D., Dibenedetto, A., Carnelutti, A., Bonasia, V., Pagano, C., et al. (2011) · Metabolic Syndrome and Related Disorders · doi:10.1089/met.2010.0140 · Cited by 56 · see citing works
Gaedke, F., Naffin, E., & Klämbt, C. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.10.002 · Cited by 55 · see citing works
Yi, P., Johnson, A. N., Han, Z., Wu, J., & Olson, E. N. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.10.001 · Cited by 54 · see citing works
van Alphen, B., Stewart, S., Iwanaszko, M., Xu, F., Li, K., Rozenfeld, S., Ramakrishnan, A., Itoh, T. Q., Sisobhan, S., Qin, Z., et al. (2022) · PLoS Biology · doi:10.1371/journal.pbio.3001456 · Cited by 53 · see citing works
Neuropathy target esterase: Immunolocalization to neuronal cell bodies and axons
Glynn, P., Holton, J. L., Nolan, C. C., Read, D. J., Brown, L., Hubbard, A., & Cavanagh, J. B. (1998) · Neuroscience · doi:10.1016/s0306-4522(97)00388-6 · Cited by 53 · see citing works
Winkler, B., Funke, D., Benmimoun, B., Spéder, P., Rey, S., Logan, M. A., & Klämbt, C. (2021) · Science Advances · doi:10.1126/sciadv.abh0050 · Cited by 53 · see citing works
Drosophila melanogasteras a model system for the evaluation of anti-aging compounds
Jafari, M. (2010) · Fly · doi:10.4161/fly.4.3.11997 · Cited by 48 · see citing works
Paraffin-Embedded and Frozen Sections of Drosophila Adult Muscles
Kucherenko, M. M., Marrone, A. K., Rishko, V. M., Yatsenko, A. S., Klepzig, A., & Shcherbata, H. R. (2010) · Journal of Visualized Experiments · doi:10.3791/2438 · Cited by 47 · see citing works
Self-citationA systematic screening to identifyde novomutations causing sporadic early-onset Parkinson's disease
Kun‐Rodrigues, C., Ganos, C., Guerreiro, R. J., Schneider, S. A., Schulte, C., Lesage, S., Darwent, L., Holmans, P., Singleton, A., Bhatia, K. P., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv376 · Cited by 45 · see citing works
Dutta, S., Rieche, F., Eckl, N., Duch, C., & Kretzschmar, D. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.022236 · Cited by 45 · see citing works
A lipid-protein hybrid model for tight junction
Lee, D. B. N., Jamgotchian, N. J., Allen, S. G., Abeles, M. B., & Ward, H. J. (2008) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00097.2008 · Cited by 41 · see citing works
Toward a Consensus in the Repertoire of Hemocytes Identified in Drosophila
Cattenoz, P. B., Monticelli, S., Pavlidaki, A., & Giangrande, A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.643712 · Cited by 39 · see citing works
Conserved signaling pathways genetically associated with longevity across the species
Khan, A. H., Zou, Z., Yang, X. D., Chen, S., & Tian, X. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.09.001 · Cited by 37 · see citing works
Compound heterozygous PNPLA6 mutations cause Boucher–Neuhäuser syndrome with late-onset ataxia
Deik, A., Johannes, B. A., Rucker, J. C., Sánchez, E., Brodie, S. E., Deegan, E. M., Landy, K., Kajiwara, Y., Scelsa, S. N., Saunders-Pullman, R. J., et al. (2014) · Journal of Neurology · doi:10.1007/s00415-014-7516-3 · Cited by 36 · see citing works
Regulska, M. (2021) · Current Neuropharmacology · doi:10.2174/18756190mta4dotmh0 · Cited by 35 · see citing works
'Fly-ing' from rare to common neurodegenerative disease mechanisms
Ma, M., Moulton, M. J., Lu, S., & Bellen, H. J. (2022) · Trends in Genetics · doi:10.1016/j.tig.2022.03.018 · Cited by 34 · see citing works
Infection and inflammation: New perspectives on Alzheimer's disease
Whitson, H. E., Colton, C. A., Khoury, J. B. E., Gate, D., Goate, A., Heneka, M. T., Kaddurah‐Daouk, R., Klein, R. S., Shinohara, M. L., Sisodia, S. S., et al. (2022) · Brain Behavior & Immunity - Health · doi:10.1016/j.bbih.2022.100462 · Cited by 33 · see citing works
ER responses play a key role in Swiss-Cheese/Neuropathy Target Esterase-associated neurodegeneration
Sunderhaus, E. R., Law, A. D., & Kretzschmar, D. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104520 · Cited by 32 · see citing works
Oxidised metabolites of the omega-6 fatty acid linoleic acid activate dFOXO
Kwon, S. Y., Massey, K. A., Watson, M. A., Hussain, T., Volpe, G., Buckley, C. D., Nicolaou, A., & Badenhorst, P. W. (2020) · Life Science Alliance · doi:10.26508/lsa.201900356 · Cited by 32 · see citing works
The Drosophila blood-brain barrier emerges as a model for understanding human brain diseases
Contreras, E. G., & Klämbt, C. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106071 · Cited by 32 · see citing works
McFerrin, J., Patton, B. L., Sunderhaus, E. R., & Kretzschmar, D. (2017) · Glia · doi:10.1002/glia.23127 · Cited by 32 · see citing works
Role of Glial Immunity in Lifespan Determination: A Drosophila Perspective
Kounatidis, I., & Chtarbanova, S. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01362 · Cited by 31 · see citing works
Using Drosophila as a platform for drug discovery from natural products in Parkinson's disease
Maitra, U., & Ciesla, L. M. (2019) · MedChemComm · doi:10.1039/c9md00099b · Cited by 31 · see citing works
Hebbar, S., Khandelwal, A., Jayashree, R., Hindle, S. J., Chiang, Y. N., Yew, J. Y., Sweeney, S. T., & Schwudke, D. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-09-0674 · Cited by 31 · see citing works
Cholesterol-rich domain formation mediated by ZO proteins is essential for tight junction formation
Shigetomi, K., Ono, Y., Matsuzawa, K., & Ikenouchi, J. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2217561120 · Cited by 31 · see citing works
Schwabe, T., Li, X., & Gaul, U. (2017) · Biology Open · doi:10.1242/bio.020669 · Cited by 28 · see citing works
Wentzell, J. S., Cassar, M., & Kretzschmar, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087526 · Cited by 24 · see citing works
Trébuchet, G., Cattenoz, P. B., Zsámboki, J., Mazaud, D., Siekhaus, D. E., Fanto, M., & Giangrande, A. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1059-18.2018 · Cited by 24 · see citing works
Distant activation of Notch signaling induces stem cell niche assembly
Yatsenko, A. S., & Shcherbata, H. R. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009489 · Cited by 23 · see citing works
Self-citationSynofzik, M., Kernstock, C., Haack, T. B., & Schöls, L. J. (2014) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2014-307793 · Cited by 23 · see citing works
PNPLA6/NTE, an Evolutionary Conserved Phospholipase Linked to a Group of Complex Human Diseases
Kretzschmar, D. (2022) · Metabolites · doi:10.3390/metabo12040284 · Cited by 23 · see citing works
Treatment for Lysosomal Storage Disorders
Sheth, J. J., & Nair, A. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666201015154932 · Cited by 22 · see citing works
Li, X., Fetter, R. D., Schwabe, T., Jung, C., Liu, L., Steller, H., & Gaul, U. (2021) · eLife · doi:10.7554/elife.68275 · Cited by 22 · see citing works
Beneficial effects of rapamycin in a Drosophila model for hereditary spastic paraplegia
Xu, S., Stern, M., & McNew, J. A. (2016) · Journal of Cell Science · doi:10.1242/jcs.196741 · Cited by 22 · see citing works
Cp1/cathepsin L is required for autolysosomal clearance in Drosophila
Xu, T., Nicolson, S., Sandow, J. J., Dayan, S., Jiang, X., Manning, J. A., Webb, A. I., Kumar, S., & Denton, D. (2020) · Autophagy · doi:10.1080/15548627.2020.1838105 · Cited by 21 · see citing works
Rahmani, Z., Surabhi, S., Rojo-Cortés, F., Dulac, A., Jenny, A., & Birman, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113078 · Cited by 21 · see citing works
Domon, M. M., Besson, F., Bandorowicz‐Pikuła, J., & Pikuła, S. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.12.138 · Cited by 20 · see citing works
Melentev, P. A., Ryabova, E. V., Surina, N. V., Zhmujdina, D. R., Komissarov, A. E., Ivanova, E. A., Boltneva, N. P., Махаева, Г. Ф., Tsap, M. I., Yatsenko, A. S., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158275 · Cited by 19 · see citing works
Self-citationZhou, Y.-T., Xu, Y.-N., Ren, X., & Zhang, X. (2023) · Food and Chemical Toxicology · doi:10.1016/j.fct.2023.113692 · Cited by 19 · see citing works
Chang, P., He, L. F., Wang, Y., Heier, C., Wu, Y., & Huang, F. (2019) · Biomolecules · doi:10.3390/biom9120848 · Cited by 19 · see citing works
Sujkowski, A. L., Rainier, S. R., Fink, J. K., & Wessells, R. J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0145356 · Cited by 18 · see citing works
Morpho-Functional Consequences of Swiss Cheese Knockdown in Glia of Drosophila melanogaster
Ryabova, E., Melentev, P., Komissarov, A., Surina, N. V., Ivanova, E., Matiytsiv, N., Shcherbata, H., & Sarantseva, S. (2021) · Cells · doi:10.3390/cells10030529 · Cited by 17 · see citing works
Self-citationHajji, K., Mteyrek, A., Sun, J., Cassar, M., Mezghani, S., Leprince, J., Vaudry, D., Masmoudi‐Kouki, O., & Birman, S. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz031 · Cited by 17 · see citing works
Fereshtehnejad, S., Saleh, P. A., de Oliveira, L. M., Patel, N., Bhowmick, S. S., Saranza, G., & Kalia, L. V. (2022) · Neurological Sciences · doi:10.1007/s10072-022-06516-8 · Cited by 16 · see citing works
von Hanstein, A., Tsikas, D., Lenzen, S., Jörns, A., & Plötz, T. (2023) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202200582 · Cited by 13 · see citing works
Self-citationYatsenko, A. S., Kucherenko, M. M., Xie, Y., Urlaub, H., & Shcherbata, H. R. (2021) · eLife · doi:10.7554/elife.63868 · Cited by 11 · see citing works
Self-citationDumas, J. A., Bunn, J. Y., LaMantia, M. A., McIsaac, C., Miller, A. S., Nop, O., Testo, A. A., Soares, B. P., Mank, M. M., Poynter, M. E., et al. (2023) · Aging Brain · doi:10.1016/j.nbas.2023.100072 · Cited by 10 · see citing works
Shu, S., Jiang, M., Deng, X., Yue, W., Cao, X., Zhang, K., Wang, Z., He, H., Cui, J., Wang, Q., et al. (2023) · Aging Cell · doi:10.1111/acel.13947 · Cited by 9 · see citing works
Carney, T. D., Hebalkar, R. Y., Edeleva, E. V., Çiçek, I. Ö., & Shcherbata, H. R. (2023) · Disease Models & Mechanisms · doi:10.1242/dmm.049862 · Cited by 9 · see citing works
Self-citationAn anti-inflammatory transcriptional cascade conserved from flies to humans
Pavlidaki, A., Panic, R., Monticelli, S., Riet, C., Yuasa, Y., Cattenoz, P. B., Nait‐Oumesmar, B., & Giangrande, A. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111506 · Cited by 8 · see citing works
Yon, M., Decoville, M., Sarou‐Kanian, V., Fayon, F., & Birman, S. (2020) · Scientific Reports · doi:10.1038/s41598-020-66218-z · Cited by 7 · see citing works
Mariani, S., Li, T., Hegermann, J., Bounader, K., Hanke, J. S., Meyer, T. S., Jannsen‐Peters, H., Haverich, A., Schmitto, J. D., & Doğan, G. (2021) · Artificial Organs · doi:10.1111/aor.14149 · Cited by 7 · see citing works
Self-citationCorrection to: Preserving Lysosomal Function in the Aging Brain: Insights from Neurodegeneration
Peng, W., Minakaki, G., Nguyen, M. N., & Krainc, D. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00756-x · Cited by 2 · see citing works
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Tsap, M. I., & Shcherbata, H. R. (2025) · Progress in Lipid Research · doi:10.1016/j.plipres.2025.101341 · Cited by 11 · see citing works
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Invertebrate glial barriers as a model for understanding blood–brain barrier evolution
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Tsikas, D. (2025) · Journal of Chromatography B · doi:10.1016/j.jchromb.2025.124578 · Cited by 4 · see citing works
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Drosophila as a model in organophosphate toxicology
Tkachuk, M., & Matiytsiv, N. P. (2026) · Fly · doi:10.1080/19336934.2026.2695497
Neuroprotective Potential of Spermidine in Drosophila sws Neurodegenerative Model
Raspopina, A., Tkachuk, M., & Matiytsiv, N. P. (2026) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.70201
Esterase Profile: Functional Features and Diagnostic Potential
Belinskaia, D. A., Voronina, P. A., Samodurova, K. V., & Goncharov, N. V. (2026) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s0022093026040034
- Authors
- Tsap, M. I., Yatsenko, A. S., Hegermann, J., Beckmann, B., Tsikas, D., & Shcherbata, H. R.
- Affiliations
- Medizinische Hochschule Hannover (DE)
- Mount Desert Island Biological Laboratory (US)
- Corresponding author
- Shcherbata, Halyna R
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2024-04-25
- Volume
- 13
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC11090517
- OpenAlex
- W4395454199
- Cited by
- 8
- References
- 161
- Citations by year
- 2026: 3 · 2025: 5
- FWCI
- 1.24
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Volkswagen Foundation (90218, 97750)
- Deutsche Forschungsgemeinschaft (521749003, INST 192/574-1 FUGG)
- European Molecular Biology Organization (Young Investigator Programme)
- Topics
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Health Sciences › Medicine › Physiology › Lysosomal Storage Disorders Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- neuropathy target esterase, blood-brain barrier, lysosomal storage disease, fatty acid metabolism, eicosanoids, neuroinflammation, innate immunity, lipid droplets, multilamellar bodies, plasma membrane domains, age-related neurodegeneration, anti-inflammatory therapy, Drosophila
- MeSH terms
- Animals, Blood-Brain Barrier, Carboxylic Ester Hydrolases, Drosophila melanogaster, Fatty Acids, Humans, Inflammation, Neuroglia, Lysosomal Storage Diseases, Drosophila Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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