Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease

LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.

Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605

Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice

Mangiarini, L., Sathasivam, K., Seller, M., Cozens, B., Harper, A., Hetherington, C., Lawton, M., Trottier, Y., Lehrach, H., Davies, S. W., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81369-0 · Cited by 3,073

Formation of Neuronal Intranuclear Inclusions Underlies the Neurological Dysfunction in Mice Transgenic for the HD Mutation

Davies, S. W., Turmaine, M., Cozens, B. A., DiFiglia, M., Sharp, A. H., Ross, C. A., Scherzinger, E., Wanker, E. E., Mangiarini, L., & Bates, G. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80513-9 · Cited by 2,188

TOR, a Central Controller of Cell Growth

Schmelzle, T., & Hall, M. N. (2000) · Cell · doi:10.1016/s0092-8674(00)00117-3 · Cited by 1,914

Huntingtin Acts in the Nucleus to Induce Apoptosis but Death Does Not Correlate with the Formation of Intranuclear Inclusions

Saudou, F., Finkbeiner, S. M., Devys, D., & Greenberg, M. E. (1998) · Cell · doi:10.1016/s0092-8674(00)81782-1 · Cited by 1,598

α-Synuclein Is Degraded by Both Autophagy and the Proteasome

Webb, J. L., Ravikumar, B., Atkins, J., Skepper, J. N., & Rubinsztein, D. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300227200 · Cited by 1,429

Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila

Steffan, J. S., Bodai, L., Pallos, J., Poelman, M., McCampbell, A., Apostol, B. L., Kazantsev, A., Schmidt, E., Zhu, Y.-Z., Greenwald, M., et al. (2001) · Nature · doi:10.1038/35099568 · Cited by 1,228

Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy

Ravikumar, B. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.9.1107 · Cited by 1,099

Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E

Fingar, D. C., Salama, S., Tsou, C., Harlow, E., & Blenis, J. (2002) · Genes & Development · doi:10.1101/gad.995802 · Cited by 1,093

GβL, a Positive Regulator of the Rapamycin-Sensitive Pathway Required for the Nutrient-Sensitive Interaction between Raptor and mTOR

Kim, D., Sarbassov, D. D., Ali, S. M., Latek, R. R., Guntur, K., Erdjument‐Bromage, H., Tempst, P., & Sabatini, D. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00114-x · Cited by 992

Autophagy, Cellular Aging and Age-related Human Diseases

Cheon, S. Y., Kim, H. J., Rubinsztein, D. C., & Lee, J. E. (2019) · Experimental Neurobiology · doi:10.5607/en.2019.28.6.643 · Cited by 95

Autophagic pathways and metabolic stress

Kaushik, S., Singh, R., & Cuervo, A. M. (2010) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01263.x · Cited by 95

Autophagy Gene Disruption Reveals a Non-vacuolar Cell Death Pathway in Dictyostelium

Kosta, A., Roisin-Bouffay, C., Luciani, M., Otto, G. P., Kessin, R. H., & Golstein, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408924200 · Cited by 92

Accumulation of Rhodopsin in Late Endosomes Triggers Photoreceptor Cell Degeneration

Chinchore, Y., Mitra, A., & Dolph, P. J. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000377 · Cited by 92

Inhibition of Hsp70 by Methylene Blue Affects Signaling Protein Function and Ubiquitination and Modulates Polyglutamine Protein Degradation

Wang, A. M., Morishima, Y., Clapp, K. M., Peng, H., Pratt, W. B., Gestwicki, J. E., Osawa, Y., & Lieberman, A. P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.098806 · Cited by 91

Autophagy and Its Impact on Neurodegenerative Diseases: New Roles for TDP-43 and C9orf72

Budini, M., Buratti, E., Morselli, E., & Criollo, A. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00170 · Cited by 102

Molecular Strategies to Target Protein Aggregation in Huntington’s Disease

Jarosińska, O. D., & Rüdiger, S. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.769184 · Cited by 92

Chapter 5 Autophagic Clearance of Aggregate‐Prone Proteins Associated with Neurodegeneration

Sarkar, S., Ravikumar, B., & Rubinsztein, D. C. (2009) · Methods in Enzymology · doi:10.1016/s0076-6879(08)04005-6 · Cited by 79

Molecular pathogenesis of seipin/BSCL2‐related motor neuron diseases

Ito, D., & Suzuki, N. (2007) · Annals of Neurology · doi:10.1002/ana.21070 · Cited by 92

Protein oxidation in Huntington disease affects energy production and vitamin B6 metabolism

Sorolla, M. A., Colman, M. J. R., Tamarit, J., Ortega, Z., Lucas, J. J., Ferrer, I., Ros, J., & Cabiscol, E. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.05.016 · Cited by 95

Alterations in ROS Activity and Lysosomal pH Account for Distinct Patterns of Macroautophagy in LINCL and JNCL Fibroblasts

Vidal-Donet, J. M., Cárcel‐Trullols, J., Casanova, B., Aguado, C., & Knecht, E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055526 · Cited by 91

Transcriptional repression induces a slowly progressive atypical neuronal death associated with changes of YAP isoforms and p73

Hoshino, M., Qi, M., Yoshimura, N., Miyashita, T., Tagawa, K., Wada, Y.-I., Enokido, Y., Marubuchi, S., Harjes, P., Arai, N., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200509132 · Cited by 91

Identification of the Drosophila Ortholog of HSPB8

Carra, S., Boncoraglio, A., Kanon, B., Brunsting, J. F., Minoia, M., Rana, A., Vos, M. J., Seidel, K., Sibon, O. C. M., & Kampinga, H. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.127498 · Cited by 95

Discovery and Preclinical Characterization of 5-[4,6-Bis({3-oxa-8-azabicyclo[3.2.1]octan-8-yl})-1,3,5-triazin-2-yl]-4-(difluoromethyl)pyridin-2-amine (PQR620), a Highly Potent and Selective mTORC1/2 Inhibitor for Cancer and Neurological Disorders

Rageot, D., Bohnacker, T., Melone, A., Langlois, J.-B., Borsari, C., Hillmann, P., Sele, A., Beaufils, F., Zvelebil, M., Hebeisen, P., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01262 · Cited by 91

Inhibition of Rho kinases enhances the degradation of mutant huntingtin

Bauer, P. O., Wong, H. K., Oyama, F., Goswami, A., Okuno, M., Kino, Y., Miyazaki, H., & Nukina, N. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809229200 · Cited by 102

The mTOR Signaling Pathway in the Brain: Focus on Epilepsy and Epileptogenesis

Russo, E., Citraro, R., Constanti, A., & Sarro, G. D. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8314-5 · Cited by 91

Everolimus-Induced mTOR Inhibition Selectively Depletes Macrophages in Atherosclerotic Plaques by Autophagy

Martinet, W., Verheye, S., & Meyer, G. R. Y. D. (2007) · Autophagy · doi:10.4161/auto.3711 · Cited by 90

Cisplatin-induced macroautophagy occurs prior to apoptosis in proximal tubules in vivo

Inoue, K., Kuwana, H., Shimamura, Y., Ogata, K., Taniguchi, Y., Kagawa, T., Horino, T., Takao, T., Morita, T., Sasaki, S., et al. (2009) · Clinical and Experimental Nephrology · doi:10.1007/s10157-009-0254-7 · Cited by 91

A Conditional Pan-NeuronalDrosophilaModel of Spinocerebellar Ataxia 7 with a Reversible Adult Phenotype Suitable for Identifying Modifier Genes

Latouche, M., Lasbleiz, C., Martin, E., Monnier, V., Debeir, T., Prigent, A., Muriel, M., Morel, L. J., Ruberg, M., Brice, A., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.5453-06.2007 · Cited by 92

Inhibiting the ubiquitin–proteasome system leads to preferential accumulation of toxic N-terminal mutant huntingtin fragments

Li, X., Wang, C.-E., Huang, S., Xu, X., Li, X., Li, H., & Li, S. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq127 · Cited by 93

Ubiquitin-specific protease-14 reduces cellular aggregates and protects against mutant huntingtin-induced cell degeneration: involvement of the proteasome and ER stress-activated kinase IRE1

Hyrskyluoto, A., Bruelle, C., Lundh, S. H., Do, H. T., Kivinen, J., Rappou, E., Reijonen, S., Waltimo, T., Petersén, Å., Lindholm, D., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu317 · Cited by 90

Functions of Autophagy in Pathological Cardiac Hypertrophy

Li, Z., Wang, J., & Yang, X. Y. (2015) · International Journal of Biological Sciences · doi:10.7150/ijbs.11883 · Cited by 93

Autophagy and antigen presentation

Münz, C. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00714.x · Cited by 93

The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics

Pritchard, S. M., Dolan, P. J., Vitkus, A., & Johnson, G. V. W. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01273.x · Cited by 89

Autophagy inDrosophila: From Historical Studies to Current Knowledge

Mulakkal, N. C., Nagy, P., Takáts, S., Tusco, R., Juhász, G., & Nezis, I. P. (2014) · BioMed Research International · doi:10.1155/2014/273473 · Cited by 93

Melatonin antagonizes cadmium‐induced neurotoxicity by activating the transcription factor EB ‐dependent autophagy–lysosome machinery in mouse neuroblastoma cells

Li, M., Pi, H., Yang, Z., Reiter, R. J., Xu, S., Chen, X., Chen, C., Zhang, L., Yang, M., Li, Y., et al. (2016) · Journal of Pineal Research · doi:10.1111/jpi.12353 · Cited by 89

Autophagy stimulation as a promising approach in treatment of neurodegenerative diseases

Pierzynowska, K., Gaffke, L., Cyske, Z., Puchalski, M., Rintz, E., Bartkowski, M., Osiadły, M., Pierzynowski, M., Mantej, J., Piotrowska, E., et al. (2018) · Metabolic Brain Disease · doi:10.1007/s11011-018-0214-6 · Cited by 93

Targeting the proteostasis network in Huntington’s disease

Soares, T. R., Reis, S., Pinho, B. R., Duchen, M. R., & Oliveira, J. M. A. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.11.006 · Cited by 93

Sonic hedgehog promotes autophagy of vascular smooth muscle cells

Li, H., Li, J., Li, Y., Singh, P., Cao, L., Xu, L., Li, D., Wang, Y., Xie, Z., Gui, Y., et al. (2012) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00160.2012 · Cited by 91

RAB3GAP1 and RAB3GAP2 modulate basal and rapamycin-induced autophagy

Spang, N., Feldmann, A., Huesmann, H., Bekbulat, F., Schmitt, V., Hiebel, C., Koziollek‐Drechsler, I., Clement, A. M., Moosmann, B., Jung, J., et al. (2014) · Autophagy · doi:10.4161/15548627.2014.994359 · Cited by 96

Selective autophagy in the maintenance of cellular homeostasis in aging organisms

Hubbard, V. M., Valdor, R., Macián, F., & Cuervo, A. M. (2011) · Biogerontology · doi:10.1007/s10522-011-9331-x · Cited by 90

IGF-1 receptor antagonism inhibits autophagy

Renna, M., Bento, C. F., Fleming, A., Menzies, F. M., Siddiqi, F. H., Ravikumar, B., Puri, C., García-Arencibia, M., Sadiq, O., Corrochano, S., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt300 · Cited by 92

Neuropeptide Y stimulates autophagy in hypothalamic neurons

Aveleira, C. A., Botelho, M., Carmo‐Silva, S., Pascoal, J. F., Ferreira‐Marques, M., Nóbrega, C., Cortes, L., Valero, J., Sousa-Ferreira, L., Álvaro, A. R., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1416609112 · Cited by 89

The Role of Autophagy in Age-Related Neurodegeneration

McCray, B. A., & Taylor, J. P. (2007) · Neurosignals · doi:10.1159/000109761 · Cited by 90

The emerging role of autophagy in Parkinson's disease

Cheung, Z. H., & Ip, N. Y. (2009) · Molecular Brain · doi:10.1186/1756-6606-2-29 · Cited by 92

Sestrin2 protects dopaminergic cells against rotenone toxicity through AMPK-Dependent autophagy activation

Hou, Y.-S., Guan, J.-J., Xu, H.-D., Wu, F., Sheng, R., & Qin, Z.-H. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00285-15 · Cited by 87

Glycolytic-to-oxidative fiber-type switch and mTOR signaling activation are early-onset features of SBMA muscle modified by high-fat diet

Rocchi, A., Milioto, C., Parodi, S., Armirotti, A., Borgia, D., Pellegrini, M., Urciuolo, A., Molon, S., Morbidoni, V., Marabita, M., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1550-4 · Cited by 90

Dementia with Lewy bodies — from scientific knowledge to clinical insights

Arnaoutoglou, N. A., O'Brien, J. T., & Underwood, B. R. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0107-7 · Cited by 89

Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies

Silva, M. C., & Haggarty, S. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238948 · Cited by 89

Rapamycin activates autophagy in Hutchinson-Gilford progeria syndrome

Graziotto, J. J., Cao, K., Collins, F. S., & Krainc, D. (2012) · Autophagy · doi:10.4161/auto.8.1.18331 · Cited by 91

The novel estrogen-induced gene EIG121 regulates autophagy and promotes cell survival under stress

Deng, L., Feng, J., & Broaddus, R. R. (2010) · Cell Death and Disease · doi:10.1038/cddis.2010.9 · Cited by 89

Promoting Autophagic Clearance: Viable Therapeutic Targets in Alzheimer's Disease

Friedman, L. G., Qureshi, Y. H., & Yu, W. H. (2014) · Neurotherapeutics · doi:10.1007/s13311-014-0320-z · Cited by 89

Puromycin‐sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation

Bhutani, N., Venkatraman, P., & Goldberg, A. L. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601592 · Cited by 89

Autophagy modulators from traditional Chinese medicine: Mechanisms and therapeutic potentials for cancer and neurodegenerative diseases

Wang, S.-F., Wu, M.-Y., Cai, C.-Z., Li, M., & Lu, J. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.10.069 · Cited by 88

The Fly as a Model for Neurodegenerative Diseases: Is It Worth the Jump?

Cauchi, R. J., & van den Heuvel, M. (2006) · Neurodegenerative Diseases · doi:10.1159/000097303 · Cited by 91

DJ-1 in neurodegenerative diseases: Pathogenesis and clinical application

Huang, M., & Chen, S. (2021) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2021.102114 · Cited by 88

The beneficial role of autophagy in multiple sclerosis: Yes or No?

Al-Kuraishy, H. M., Jabir, M. S., Al-Gareeb, A. I., Saad, H. M., Batiha, G. E., & Klionsky, D. J. (2023) · Autophagy · doi:10.1080/15548627.2023.2259281 · Cited by 89

Activation of Autophagy Pathway Suppresses the Expression of iNOS, IL6 and Cell Death of LPS-Stimulated Microglia Cells

Han, H.-E., Kim, T., Son, H.-J., Park, W. J., & Han, P. (2013) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2012.089 · Cited by 86

Autophagy Control by the VEGF-C/NRP-2 Axis in Cancer and Its Implication for Treatment Resistance

Stanton, M. J., Dutta, S., Zhang, H., Polavaram, N. S., Leontovich, A. A., Hönscheid, P., Sinicrope, F. A., Tindall, D. J., Muders, M. H., & Datta, K. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-3635 · Cited by 86

Huntingtin and the Synapse

Barron, J. C., Hurley, E. P., & Parsons, M. P. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.689332 · Cited by 85

Apoptosis-Modulating Drugs for Improved Cancer Therapy

Ocker, M., & Höpfner, M. (2012) · European Surgical Research · doi:10.1159/000336875 · Cited by 87

Build-UPS and break-downs: metabolism impacts on proteostasis and aging

Ottens, F., Franz, A., & Hoppe, T. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-020-00682-y · Cited by 88

Role of autophagy in the pathogenesis of amyotrophic lateral sclerosis

Lee, J. K., Shin, J. H., Lee, J. E., & Choi, E.-J. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.005 · Cited by 91

A neuroprotective phase precedes striatal degeneration upon nucleolar stress

Kreiner, G., Bierhoff, H., Armentano, M., Parkitna, J. M. R., Sowodniok, K., Naranjo, J. R., Bonfanti, L., Liss, B., Schütz, G., Grummt, I., et al. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.66 · Cited by 85

Randomized, double-blind, placebo-controlled trial of rapamycin in amyotrophic lateral sclerosis

Mandrioli, J., D’Amico, R., Zucchi, E., Biasi, S. D., Banchelli, F., Martinelli, I., Simonini, C., Tartaro, D. L., Vicini, R., Fini, N., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40734-8 · Cited by 88

Autophagic activity in neuronal cell death

Button, R. W., Luo, S., & Rubinsztein, D. C. (2015) · Neuroscience Bulletin · doi:10.1007/s12264-015-1528-y · Cited by 88

Tanshinone IIA Induces Autophagic Cell Death via Activation of AMPK and ERK and Inhibition of mTOR and p70 S6K in KBM‐5 Leukemia Cells

Yun, S., Jung, J. H., Jeong, S., Sohn, E. J., Kim, B., & Kim, S. (2013) · Phytotherapy Research · doi:10.1002/ptr.5015 · Cited by 84

Activation of AMPK-induced autophagy ameliorates Huntington disease pathology in vitro

Walter, C., Clemens, L. E., Müller, A. J., Fallier‐Becker, P., Proikas‐Cezanne, T., Rieß, O., Metzger, S., & Nguyen, H. P. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.04.041 · Cited by 85

RNAi mechanisms in Huntington’s disease therapy: siRNA versus shRNA

Aguiar, S. P., van der Gaag, B., & Cortese, F. A. B. (2017) · Translational Neurodegeneration · doi:10.1186/s40035-017-0101-9 · Cited by 84

Autophagy, lithium, and amyotrophic lateral sclerosis

Pasquali, L., Longone, P., Isidoro, C., Ruggieri, S. A., Paparelli, A., & Fornai, F. (2009) · Muscle & Nerve · doi:10.1002/mus.21423 · Cited by 84

Eat your heart out: Role of autophagy in myocardial ischemia/reperfusion

Gustafsson, Å. B., & Gottlieb, R. A. (2008) · Autophagy · doi:10.4161/auto.5655 · Cited by 85

Activation of autophagy in retinal ganglion cells

Kim, S., Munemasa, Y., Kwong, J. M. K., Ahn, J. H., Mareninov, S., Gordon, L. K., Caprioli, J., & Piri, N. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21738 · Cited by 83

Autophagy in Hydra: A response to starvation and stress in early animal evolution

Chera, S., Buzgariu, W., Ghila, L., & Galliot, B. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.03.010 · Cited by 83

Neuronal Autophagy as a Mediator of Life and Death

Puyal, J., Ginet, V., Grishchuk, Y., Truttmann, A. C., & Clarke, P. G. H. (2011) · The Neuroscientist · doi:10.1177/1073858411404948 · Cited by 89

Mammalian target of rapamycin (mTOR) as a potential therapeutic target in various diseases

Kaur, A., & Sharma, S. (2017) · Inflammopharmacology · doi:10.1007/s10787-017-0336-1 · Cited by 85

Fasting activates macroautophagy in neurons of Alzheimer’s disease mouse model but is insufficient to degrade amyloid-beta

Chen, X., Kondo, K., Motoki, K., Homma, H., & Okazawa, H. (2015) · Scientific Reports · doi:10.1038/srep12115 · Cited by 83

Selective autophagy as a therapeutic target for neurological diseases

Xu, W., Ocak, U., Gao, L., Tu, S., Lenahan, C., Zhang, J., & Shao, A. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03667-9 · Cited by 84

Rapamycin extends life- and health span because it slows aging

Blagosklonny, M. V. (2013) · Aging · doi:10.18632/aging.100591 · Cited by 82

Cellular Protein Aggregates: Formation, Biological Effects, and Ways of Elimination

Wen, J.-H., He, X., Feng, Z.-S., Li, D.-Y., Tang, J., & Liu, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24108593 · Cited by 87

Autophagy, Redox Signaling, and Ventricular Remodeling

Gurusamy, N., & Das, D. K. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2524 · Cited by 83

Let-7 Coordinately Suppresses Components of the Amino Acid Sensing Pathway to Repress mTORC1 and Induce Autophagy

Dubinsky, A. N., Dastidar, S. G., Hsu, C. L., Zahra, R., Djakovic, S. N., Duarte, S., Esau, C., Spencer, B. J., Ashe, T. D., Fischer, K. M., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.09.001 · Cited by 84

Ataxin-3 Protein and RNA Toxicity in Spinocerebellar Ataxia Type 3: Current Insights and Emerging Therapeutic Strategies

Evers, M. M., Toonen, L. J. A., & van Roon‐Mom, W. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8596-2 · Cited by 84

Puromycin-sensitive aminopeptidase protects against aggregation-prone proteins via autophagy

Menzies, F. M., Hourez, R., Imarisio, S., Raspe, M. A., Sadiq, O., Chandraratna, D., O’Kane, C. J., Rock, K. L., Reits, E. A., Goldberg, A. L., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq385 · Cited by 81

mTORC1‐ and mTORC2‐interacting proteins keep their multifunctional partners focused

Bracho‐Valdés, I., Moreno‐Alvarez, P., Valencia‐Martínez, I., Robles‐Molina, E., Chávez‐Vargas, L., & Vázquez‐Prado, J. (2011) · IUBMB Life · doi:10.1002/iub.558 · Cited by 84

Tetrandrine, an Activator of Autophagy, Induces Autophagic Cell Death via PKC-α Inhibition and mTOR-Dependent Mechanisms

Wong, V. K. W., Wu, J., Chen, J., Yao, X., Leung, E. L., Wang, Q., Chiu, P., Ko, B. C. B., & Law, B. Y. K. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00351 · Cited by 84

Preventing mutant huntingtin proteolysis and intermittent fasting promote autophagy in models of Huntington disease

Ehrnhoefer, D. E., Martin, D. D. O., Schmidt, M. E., Qiu, X., Ladha, S., Caron, N. S., Skotte, N. H., Nguyen, Y. T. N., Vaid, K., Southwell, A. L., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0518-0 · Cited by 81

Autophagy in intracellular bacterial infection

Hu, W., Chan, H., Lu, L., Wong, S. H., Wong, S. H., Li, M. X., Xiao, Z. G., Cho, C. H., Gin, T., Chan, M. T. V., et al. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.07.014 · Cited by 84

Autophagy Protects Renal Tubular Cells Against Ischemia / Reperfusion Injury in a Time-Dependent Manner

Guan, X., Qian, Y., Shen, Y. L., Zhang, L., Du, Y., Dai, H., Qian, J., & Yan, Y. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000374071 · Cited by 80

The use of sirolimus (rapamycin) in the management of refractory inflammatory bowel disease in children

Mutalib, M., Borrelli, O., Blackstock, S. J., Kiparissi, F., Elawad, M., Shah, N., & Lindley, K. J. (2014) · Journal of Crohn s and Colitis · doi:10.1016/j.crohns.2014.08.014 · Cited by 89

Neferine Attenuates the Protein Level and Toxicity of Mutant Huntingtin in PC-12 Cells via Induction of Autophagy

Wong, V. K. W., Wu, A., Wang, J., Liu, L., & Law, B. Y. K. (2015) · Molecules · doi:10.3390/molecules20033496 · Cited by 81

Poly(ADP-ribose)polymerase-1 hyperactivation in neurodegenerative diseases: The death knell tolls for neurons

Narne, P., Pandey, V., Simhadri, P. K., & Phanithi, P. B. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.11.007 · Cited by 80

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

Review: Autophagy and neurodegeneration: survival at a cost?

Cherra, S. J., Dagda, R. K., & Chu, C. T. (2010) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2010.01062.x · Cited by 81

Glial alterations from early to late stages in a model of A lzheimer's disease: Evidence of autophagy involvement in A β internalization

Pomilio, C. J., Pavía, P., Gorojod, R. M., Vinuesa, Á., Alaimo, A., Galván, V., Kotler, M. L., Beauquis, J., & Saravia, F. (2015) · Hippocampus · doi:10.1002/hipo.22503 · Cited by 82

A novel therapeutic strategy for polyglutamine diseases by stabilizing aggregation-prone proteins with small molecules

Tanaka, M., Machida, Y., & Nukina, N. (2005) · Journal of Molecular Medicine · doi:10.1007/s00109-004-0632-2 · Cited by 79

The family of mammalian small heat shock proteins (HSPBs): Implications in protein deposit diseases and motor neuropathies

Boncoraglio, A., Minoia, M., & Carra, S. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.03.011 · Cited by 81

Cell death pathology: Cross-talk with autophagy and its clinical implications

Amelio, I., Melino, G., & Knight, R. A. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.09.080 · Cited by 79

Neuroprotective action of lithium in disorders of the central nervous system.

Chiu, C., & Chuang, D. (2011) · PubMed · doi:10.3969/j.issn.1672-7347.2011.06.001 · Cited by 78

Convergent pathogenic pathways in Alzheimer's and Huntington's diseases: shared targets for drug development

Ehrnhoefer, D. E., Wong, B. K. Y., & Hayden, M. R. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3556 · Cited by 78

Activation of AMPK/mTORC1-mediated autophagy by metformin reverses Clk1 deficiency-sensitized dopaminergic neuronal death

Yan, Q., Han, C., Wang, G., Waddington, J. L., Zheng, L., & Zhen, X. (2017) · Molecular Pharmacology · doi:10.1124/mol.117.109512 · Cited by 77

Zebrafish models of BAG3 myofibrillar myopathy suggest a toxic gain of function leading to BAG3 insufficiency

Ruparelia, A. A., Oorschot, V. M. J., Vaz, R., Ramm, G., & Bryson‐Richardson, R. J. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1344-5 · Cited by 77

Impairment of Lysosome Function and Autophagy in Rare Neurodegenerative Diseases

Darios, F. D., & Stévanin, G. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.033 · Cited by 79

Nonstructural protein 6 of porcine epidemic diarrhea virus induces autophagy to promote viral replication via the PI3K/Akt/mTOR axis

Lin, H., Li, B., Liu, M., Zhou, H., He, K., & Fan, H. (2020) · Veterinary Microbiology · doi:10.1016/j.vetmic.2020.108684 · Cited by 77

Lysosomal Stress Response (LSR): Physiological Importance and Pathological Relevance

Lakpa, K. L., Khan, N., Afghah, Z., Chen, X., & Geiger, J. D. (2021) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-021-09990-7 · Cited by 81

Role of autophagy in the clearance of mutant huntingtin: A step towards therapy?

Ravikumar, B., & Rubinsztein, D. C. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.008 · Cited by 78

Does Huntingtin play a role in selective macroautophagy?

Steffan, J. S. (2010) · Cell Cycle · doi:10.4161/cc.9.17.12718 · Cited by 81

Autophagy and neurodegeneration

Ventruti, A., & Cuervo, A. M. (2007) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-007-0068-5 · Cited by 82

Control of the structural landscape and neuronal proteotoxicity of mutant Huntingtin by domains flanking the polyQ tract

Shen, K., Calamini, B., Fauerbach, J. A., Ma, B., Shahmoradian, S. H., Lachapel, I. L. S., Chiu, W., Lo, D. C., & Frydman, J. (2016) · eLife · doi:10.7554/elife.18065 · Cited by 77

Therapeutic role of mammalian target of rapamycin (mTOR) inhibition in preventing epileptogenesis

McDaniel, S. S., & Wong, M. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.02.037 · Cited by 78

Autophagy—from molecular mechanisms to clinical relevance

Lippai, M., & Szatmári, Z. (2016) · Cell Biology and Toxicology · doi:10.1007/s10565-016-9374-5 · Cited by 80

Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies

Sarkar, S., Ravikumar, B., Floto, R. A., & Rubinsztein, D. C. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2008.110 · Cited by 578

Induction of autophagy with catalytic mTOR inhibitors reduces huntingtin aggregates in a neuronal cell model

Roscic, A., Baldo, B., Crochemore, C., Marcellin, D., & Paganetti, P. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07435.x · Cited by 92

Rapamycin alleviates toxicity of different aggregate-prone proteins

Berger, Z., Ravikumar, B., Menzies, F. M., Oroz, L. G., Underwood, B. R., Pangalos, M. N., Schmitt, I., Wullner, U., Evert, B. O., O'Kane, C. J., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi458 · Cited by 657

alleviates toxicity of different aggregate-prone proteins. Hum Mol Genet

Berger, Z., Ravikumar, B., Menzies, F. M., Garcia-Oroz, L., Underwood, B. R., Pangalos, M. N., Schmitt, I., Wullner, U., Evert, B. O., O’Kane, C. J., et al. (2015)

Potential therapeutics targeting on autophagy for Huntington disease

Zheng-hong, Q. (2011)