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Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
Abstract
Huntington disease is one of nine inherited neurodegenerative disorders caused by a polyglutamine tract expansion. Expanded polyglutamine proteins accumulate abnormally in intracellular aggregates. Here we show that mammalian target of rapamycin (mTOR) is sequestered in polyglutamine aggregates in cell models, transgenic mice and human brains. Sequestration of mTOR impairs its kinase activity and induces autophagy, a key clearance pathway for mutant huntingtin fragments. This protects against polyglutamine toxicity, as the specific mTOR inhibitor rapamycin attenuates huntingtin accumulation and cell death in cell models of Huntington disease, and inhibition of autophagy has the converse effects. Furthermore, rapamycin protects against neurodegeneration in a fly model of Huntington disease, and the rapamycin analog CCI-779 improved performance on four different behavioral tasks and decreased aggregate formation in a mouse model of Huntington disease. Our data provide proof-of-principle for the potential of inducing autophagy to treat Huntington disease.
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“Genetic and pharmacological restorations of autophagic/mitophagic clearance in animal models of these diseases ameliorate disease-defining pathologies and behavioral deficits (Fang et al., 2019; Ravikumar et al., 2004; Sliter et al., 2018).”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Ravikumar et al., 2004
In the citing paper
“For example, rapa mycin has been shown to reduce toxic-aggregate formation and disease progression by increasing autophagy in mouse and fly models of Huntington’s disease and tauopathy (59).”
From Neural mechanisms of ageing and cognitive decline (2010) · cites this paper as [59]
Citations
Cites
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
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
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
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
Self-citationHistone 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
Self-citationMammalian 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
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
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Polyglutamine-expanded androgen receptor interferes with TFEB to elicit autophagy defects in SBMA
Cortés, C. J., Miranda, H. C., Frankowski, H., Batlevi, Y., Young, J. E., Le, A. T., Ivanov, N., Sopher, B. L., Carromeu, C., Muotri, A. R., et al. (2014) · Nature Neuroscience · doi:10.1038/nn.3787 · Cited by 164
mTOR pathway inhibition as a new therapeutic strategy in epilepsy and epileptogenesis
Citraro, R., Leo, A., Constanti, A., Russo, E., & Sarro, G. D. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.03.039 · Cited by 165
Tryptophan metabolism: entering the field of aging and age-related pathologies
van der Goot, A. T., & Nollen, E. A. A. (2013) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2013.02.007 · Cited by 166
Small molecule enhancers of autophagy for neurodegenerative diseases
Sarkar, S., & Rubinsztein, D. C. (2008) · Molecular BioSystems · doi:10.1039/b804606a · Cited by 166
Self-citationHSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones
Vos, M. J., Zijlstra, M. P., Kanon, B., van Waarde-Verhagen, M. A. W. H., Brunt, E. R. P., Oosterveld-Hut, H. M. J., Carra, S., Sibon, O. C. M., & Kampinga, H. H. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq398 · Cited by 166
Guo, W., Qian, L., Zhang, J., Zhang, W., Morrison, A., Hayes, P. D., Wilson, S., Chen, T., & Zhao, J. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22725 · Cited by 163
Resveratrol as a Natural Autophagy Regulator for Prevention and Treatment of Alzheimer’s Disease
Kou, X., & Chen, N. (2017) · Nutrients · doi:10.3390/nu9090927 · Cited by 165
Constitutive autophagy: vital role in clearance of unfavorable proteins in neurons
Komatsu, M., Ueno, T., Waguri, S., Uchiyama, Y., Kominami, E., & Tanaka, K. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402120 · Cited by 170
Zhang, S., Binari, R., Zhou, R., & Perrimon, N. (2010) · Genetics · doi:10.1534/genetics.109.112516 · Cited by 160
Abeta42-Induced Neurodegeneration via an Age-Dependent Autophagic-Lysosomal Injury in Drosophila
Ling, D., Song, H., Garza, D., Neufeld, T. P., & Salvaterra, P. M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004201 · Cited by 170
Inflammatory aspects of epileptogenesis: contribution of molecular inflammatory mechanisms
Alyu, F., & Dikmen, M. (2016) · Acta Neuropsychiatrica · doi:10.1017/neu.2016.47 · Cited by 163
Host-Directed Therapeutic Strategies for Tuberculosis
Kolloli, A., & Subbian, S. (2017) · Frontiers in Medicine · doi:10.3389/fmed.2017.00171 · Cited by 164
Identification of combinatorial drug regimens for treatment of Huntington's disease using Drosophila
Agrawal, N., Pallos, J., Slepko, N., Apostol, B. L., Bodai, L., Chang, L.-W., Chiang, A., Thompson, L. M., & Marsh, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500055102 · Cited by 160
Autophagy Dysregulation in Amyotrophic Lateral Sclerosis
Chen, S., Zhang, X., Song, L., & Le, W. (2011) · Brain Pathology · doi:10.1111/j.1750-3639.2011.00546.x · Cited by 170
Houghton, P. J., Morton, C. L., Kolb, E. A., Gorlick, R. G., Lock, R. B., Carol, H., Reynolds, C. P., Maris, J. M., Keir, S. T., Billups, C. A., et al. (2007) · Pediatric Blood & Cancer · doi:10.1002/pbc.21296 · Cited by 159
mTOR/AMPK signaling in the brain: Cell metabolism, proteostasis and survival
Garza-Lombó, C., Schroder, A. L., Reyes‐Reyes, E. M., & Franco, R. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2018.05.002 · Cited by 169
Alzheimer’s Disease Pathogenesis: Role of Autophagy and Mitophagy Focusing in Microglia
Eshraghi, M., Adlimoghaddam, A., Mahmoodzadeh, A., Sharifzad, F., Yasavoli-Sharahi, H., Lorzadeh, S., Albensi, B. C., & Ghavami, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073330 · Cited by 158
Underwood, B. R., Imarisio, S., Fleming, A., Rose, C., Krishna, G., Heard, P. L., Quick, M., Korolchuk, V. I., Renna, M., Sarkar, S., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq253 · Cited by 159
Self-citationSilva, M. C., Nandi, G. A., Tentarelli, S., Gurrell, I. K., Jamier, T., Lucente, D., Dickerson, B. C., Brown, D. G., Brandon, N. J., & Haggarty, S. J. (2020) · Nature Communications · doi:10.1038/s41467-020-16984-1 · Cited by 157
Lee, H., Noh, J.-Y., Oh, Y., Kim, Y., Chang, J.-W., Chung, C.-W., Lee, S.-T., Kim, M., Ryu, H., & Jung, Y.-K. (2012) · Human Molecular Genetics · doi:10.1093/hmg/ddr445 · Cited by 157
Autophagy, a guardian against neurodegeneration
Garcı́a-Arencibia, M., Hochfeld, W. E., Toh, P. P. C., & Rubinsztein, D. C. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.02.008 · Cited by 159
Self-citationSpermidine protects against α-synuclein neurotoxicity
Büttner, S., Broeskamp, F., Sommer, C., Markaki, M., Habernig, L., Alavian‐Ghavanini, A., Carmona‐Gutiérrez, D., Eisenberg, T., Michael, E., Kroemer, G., et al. (2014) · Cell Cycle · doi:10.4161/15384101.2014.973309 · Cited by 157
Floto, R. A., Sarkar, S., Perlstein, E. O., Kampmann, B., Schreiber, S. L., & Rubinsztein, D. C. (2007) · Autophagy · doi:10.4161/auto.4898 · Cited by 157
Self-citationAutophagy-mediated clearance of aggresomes is not a universal phenomenon
Wong, E. S. P., Tan, J. M. M., Soong, W.-E., Hussein, K., Nukina, N., Dawson, V. L., Dawson, T. M., Cuervo, A. M., & Lim, K. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn157 · Cited by 162
Congenital disorders of autophagy: an emerging novel class of inborn errors of neuro-metabolism
Ebrahimi‐Fakhari, D., Saffari, A., Wahlster, L., Lu, J., Byrne, S., Hoffmann, G. F., Jungbluth, H., & Şahin, M. (2015) · Brain · doi:10.1093/brain/awv371 · Cited by 165
Calpain is required for macroautophagy in mammalian cells
Demarchi, F., Bertoli, C., Copetti, T., Tanida, I., Brancolini, C., Eskelinen, E.-L., & Schneider, C. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601024 · Cited by 156
Hamacher‐Brady, A., Brady, N. R., & Gottlieb, R. A. (2006) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-006-0583-7 · Cited by 159
Eat-Me: Autophagy, Phagocytosis, and Reactive Oxygen Species Signaling
Vernon, P. J., & Tang, D. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4810 · Cited by 161
The current clinical management of Huntington's disease
Phillips, W., Shannon, K. M., & Barker, R. A. (2008) · Movement Disorders · doi:10.1002/mds.21971 · Cited by 158
Neuronal macroautophagy: From development to degeneration
Boland, B., & Nixon, R. A. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.009 · Cited by 163
Autophagy Suppresses RIP Kinase-Dependent Necrosis Enabling Survival to mTOR Inhibition
Bray, K., Mathew, R., Lau, A., Kamphorst, J. J., Fan, J., Chen, J., Chen, H.-Y., Ghavami, A., Stein, M. N., DiPaola, R. S., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041831 · Cited by 159
New Insights into the Mechanisms of Macroautophagy in Mammalian Cells
Eskelinen, E. (2008) · International review of cytology · doi:10.1016/s1937-6448(07)66005-5 · Cited by 161
Piper, M. D. W., Selman, C., McElwee, J. J., & Partridge, L. (2008) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2007.01906.x · Cited by 159
Wold, M. S., Lim, J., Lachance, V., Deng, Z., & Yue, Z. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0141-0 · Cited by 153
Lysosome biogenesis in health and disease
Bajaj, L., Lotfi, P., Pal, R., Ronza, A. D., Sharma, J., & Sardiello, M. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14564 · Cited by 153
Reactive oxygen species regulation of autophagy in cancer: Implications for cancer treatment
Li, L., Ishdorj, G., & Gibson, S. B. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.07.011 · Cited by 154
Xing, Y., Wei, X., Liu, Y., Wang, M., Sui, Z., Wang, X., Zhu, W., Wu, M., Chen, L., Fei, Y.-H., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.2008752 · Cited by 155
Oxidative stress induces autophagy in response to multiple noxious stimuli in retinal ganglion cells
Lin, W., & Kuang, H. (2014) · Autophagy · doi:10.4161/auto.36076 · Cited by 154
Autophagy in cardiovascular disease
Martinet, W., Knaapen, M., Kockx, M. M., & Meyer, G. R. Y. D. (2007) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.08.004 · Cited by 155
Polyglutamine Diseases: Where does Toxicity Come from? What is Toxicity? Where are We Going?
Takahashi, T., Katada, S., & Onodera, O. (2010) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjq005 · Cited by 157
Coordinate Autophagy and mTOR Pathway Inhibition Enhances Cell Death in Melanoma
Xie, X., White, E. P., & Mehnert, J. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055096 · Cited by 150
Mammalian Target of Rapamycin: Hitting the Bull′s‐Eye for Neurological Disorders
Chong, Z. Z., Shang, Y., Zhang, L., Wang, S., & Maiese, K. (2010) · Oxidative Medicine and Cellular Longevity · doi:10.4161/oxim.3.6.14787 · Cited by 149
Wong, A. S. L., Lee, R. H. K., Cheung, A. Y., Yeung, P. K. K., Chung, S. K., Cheung, Z. H., & Ip, N. Y. (2011) · Nature Cell Biology · doi:10.1038/ncb2217 · Cited by 155
Iwamaru, A., Kondo, Y., Iwado, E., Aoki, H., Fujiwara, K., Yokoyama, T., Mills, G. B., & Kondo, S. (2006) · Oncogene · doi:10.1038/sj.onc.1209992 · Cited by 149
New Insights into Toxicity and Drug Testing
Gowder, S. J. (2013) · InTech eBooks · doi:10.5772/55886 · Cited by 149
Nakanishi, H., & Wu, Z. (2009) · Behavioural Brain Research · doi:10.1016/j.bbr.2009.02.001 · Cited by 153
Trochet, D., Hong, S. J., Lim, J., Brunet, J., Münnich, A., Kim, K., Lyonnet, S., Goridis, C., & Amiel, J. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi401 · Cited by 149
Reinstating Aberrant mTORC1 Activity in Huntington’s Disease Mice Improves Disease Phenotypes
Lee, J. H., Tecedor, L., Chen, Y. H., Mas, A., Sowada, M. J., Thompson, L. M., & Davidson, B. L. (2014) · Neuron · doi:10.1016/j.neuron.2014.12.019 · Cited by 151
Effect of autophagy on multiple myeloma cell viability
Hoang, B. Q., Benavides, A., Shi, Y., Frost, P., & Lichtenstein, A. K. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-1177 · Cited by 151
An anti-aging drug today: from senescence-promoting genes to anti-aging pill
Blagosklonny, M. V. (2007) · Drug Discovery Today · doi:10.1016/j.drudis.2007.01.004 · Cited by 150
Impaired proteolysis underlies autophagic dysfunction in Niemann–Pick type C disease
Elrick, M. J., Yu, T., Chung, C., & Lieberman, A. P. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds324 · Cited by 153
Law, B. Y. K., Wang, M., Ma, D., Al‐Mousa, F., Michelangeli, F., Cheng, S., Ng, M. H. L., To, K., Mok, A. Y. F., Ko, R. Y. Y., et al. (2010) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0700 · Cited by 149
The variability of autophagy and cell death susceptibility
Loos, B., Engelbrecht, A., Lockshin, R. A., Klionsky, D. J., & Zakeri, Z. (2013) · Autophagy · doi:10.4161/auto.25560 · Cited by 153
Jena, K. K., Kolapalli, S. P., Mehto, S., Nath, P., Das, B., Sahoo, P. K., Ahad, A., Syed, G. H., Raghav, S. K., Senapati, S., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798358 · Cited by 151
Emerging Anti-Aging Strategies - Scientific Basis and Efficacy
Shetty, A. K., Kodali, M., Upadhya, R., & Madhu, L. N. (2018) · Aging and Disease · doi:10.14336/ad.2018.1026 · Cited by 149
Nichols, C. D. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2006.05.012 · Cited by 153
Granulostasis: Protein Quality Control of RNP Granules
Alberti, S., Matějů, D., Mediani, L., & Carra, S. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00084 · Cited by 151
The many faces of autophagy dysfunction in Huntington's disease: from mechanism to therapy
Cortés, C. J., & Spada, A. R. L. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.02.014 · Cited by 150
Targeting autophagy in neurodegenerative diseases
Vidal, R. L., Matus, S., Bargsted, L., & Hetz, C. A. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.09.002 · Cited by 149
Atg5 and Bcl-2 provide novel insights into the interplay between apoptosis and autophagy
Luo, S., & Rubinsztein, D. C. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402149 · Cited by 149
Self-citationDisruption of Protein Quality Control in Parkinson's DiseasePreprint
Cook, C. N., Stetler, C. T., & Petrucelli, L. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009423 · Cited by 153
p62/SQSTM1 at the interface of aging, autophagy, and disease
Bitto, A., Lerner, C. A., Nacarelli, T., Crowe, E. P., Torres, C. A., & Sell, C. (2014) · AGE · doi:10.1007/s11357-014-9626-3 · Cited by 154
Wu, J., Shih, H.-P., Vigont, V. A., Hrdlicka, L., Diggins, L. T., Singh, C. M., Mahoney, M. B., Chesworth, R., Shapiro, G., Zimina, O. A., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.04.012 · Cited by 143
The cell biology of autophagy in metazoans: a developing story
Meléndez, A., & Neufeld, T. P. (2008) · Development · doi:10.1242/dev.016105 · Cited by 145
Premature aging in mice activates a systemic metabolic response involving autophagy induction
Mariño, G., Ugalde, A. P., Salvador-Montoliu, N., Varela, I., Quirós, P. M., Cadiñanos, J., van der Pluijm, I., Freije, J. M. P., & López-Otı́n, C. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn120 · Cited by 144
Mechanisms of Disease: histone modifications in Huntington's disease
Sadri‐Vakili, G., & Cha, J.-H. J. (2006) · Nature Clinical Practice Neurology · doi:10.1038/ncpneuro0199 · Cited by 143
Jia, K., Hart, A. C., & Levine, B. (2007) · Autophagy · doi:10.4161/auto.3528 · Cited by 145
Suppression of Huntington's disease pathology in Drosophila by human single-chain Fv antibodies
Wolfgang, W. J., Miller, T. W., Webster, J. M., Huston, J. S., Thompson, L. M., Marsh, J., & Messer, A. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505321102 · Cited by 146
Bartolomé, A., García-Aguilar, A., Asahara, S.-I., Kido, Y., Guillén, C., Pajvani, U. B., & Benito, M. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00441-17 · Cited by 141
Upregulated autophagy protects cardiomyocytes from oxidative stress-induced toxicity
Dutta, D., Xu, J., Js, K., Dunn, W. A., & Leeuwenburgh, C. (2013) · Autophagy · doi:10.4161/auto.22971 · Cited by 143
Mutant huntingtin impairs Ku70-mediated DNA repair
Enokido, Y., Tamura, T., Ito, H., Arumughan, A., Komuro, A., Shiwaku, H., Sone, M., Foulle, R., Sawada, H., Ishiguro, H., et al. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200905138 · Cited by 144
Malkus, K. A., Tsika, E., & Ischiropoulos, H. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-24 · Cited by 144
Oleuropein aglycone induces autophagy via the AMPK/mTOR signalling pathway: a mechanistic insight
Rigacci, S., Miceli, C., Nediani, C., Berti, A., Cascella, R., Pantano, D., Nardiello, P., Luccarini, I., Casamenti, F., & Stefani, M. (2015) · Oncotarget · doi:10.18632/oncotarget.6119 · Cited by 141
Uddin, M. S., Mamun, A. A., Labu, Z. K., Hidalgo‐Lanussa, O., Barreto, G. E., & Ashraf, G. M. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27588 · Cited by 141
Tuberous Sclerosis Complex: Neurological, Renal and Pulmonary Manifestations
Franz, D., Bissler, J., & McCormack, F. (2010) · Neuropediatrics · doi:10.1055/s-0030-1269906 · Cited by 138
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Pattison, J. S., Sanbe, A., Maloyan, A., Osińska, H. E., Klevitsky, R., & Robbins, J. M. (2008) · Circulation · doi:10.1161/circulationaha.107.750232 · Cited by 140
Neuroprotection by Hsp104 and Hsp27 in Lentiviral-based Rat Models of Huntington's Disease
Perrin, V., Régulier, E., Abbas‐Terki, T., Hässig, R., Brouillet, E., Aebischer, P., Luthi‐Carter, R., & Déglon, N. (2007) · Molecular Therapy · doi:10.1038/mt.sj.6300141 · Cited by 139
Use of sirolimus (rapamycin) to treat refractory Crohn’s disease
Massey, D. C. O., Bredin, F., & Parkes, M. (2008) · Gut · doi:10.1136/gut.2008.157297 · Cited by 144
Autophagy and misfolded proteins in neurodegeneration
Metcalf, D. J., García-Arencibia, M., Hochfeld, W. E., & Rubinsztein, D. C. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2010.11.003 · Cited by 138
Self-citationSleiman, S. F., Langley, B. C., Basso, M., Berlin, J., Li, X., Payappilly, J. B., Kharel, M. K., Guo, H., Marsh, J., Thompson, L. M., et al. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0710-11.2011 · Cited by 141
Lu, X., Mattis, V. B., Wang, N., Al‐Ramahi, I., van den Berg, N., Fratantoni, S. A., Waldvogel, H. J., Greiner, E. R., Osmand, A., Merz, K. E., et al. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3010523 · Cited by 142
Brady, N. R., Hamacher‐Brady, A., Yuan, H., & Gottlieb, R. A. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2007.05849.x · Cited by 137
Identification of MOAG-4/SERF as a regulator of age-related proteotoxicity
van Ham, T. J., Holmberg, M. A., van der Goot, A. T., Teuling, E., Garcia-Arencibia, M., Kim, H.-E., Du, D., Thijssen, K. L., Wiersma, M., Burggraaff, R., et al. (2010) · Cell · doi:10.1016/j.cell.2010.07.020 · Cited by 133
Self-citationProtein degradation, aggregation, and misfolding
Cuervo, A. M., Wong, E. S. P., & Martínez‐Vicente, M. (2010) · Movement Disorders · doi:10.1002/mds.22718 · Cited by 142
Neuropeptide Y (NPY) as a therapeutic target for neurodegenerative diseases
Duarte‐Neves, J., de Almeida, L. P., & Cavadas, C. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.07.022 · Cited by 144
Autophagy in the Retina: A Potential Role in Age-Related Macular Degeneration
Mitter, S. K., Rao, H. V., Qi, X., Cai, J., Sugrue, A., Dunn, W. A., Grant, M. B., & Boulton, M. E. (2012) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4614-0631-0_12 · Cited by 136
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Metadata
- Authors
- Ravikumar, B., Vacher, C., Berger, Z., Davies, J. E., Luo, S., Oroz, L. G., Scaravilli, F., Easton, D. F., Duden, R., O'Kane, C. J., & Rubinsztein, D. C.
- Affiliations
- University of Cambridge (GB)
- UCL Queen Square Institute of Neurology (GB)
- Addenbrooke's Hospital (GB)
- Corresponding author
- Rubinsztein, David C
- Venue
- Nature Genetics
- Published
- 2004-05-16
- Volume
- 36
- Issue
- 6
- Pages
- 585-595
- ISSN
- 1061-4036 (ISSN-L)
- 1546-1718
- OpenAlex
- W2111567059
- Cited by
- 2,347
- References
- 49
- Citations by year
- 2026: 39 · 2025: 43 · 2024: 56 · 2023: 61 · 2022: 94 · 2021: 113 · 2020: 101 · 2019: 110 · 2018: 114 · 2017: 94 · 2016: 126 · 2015: 145 · 2014: 148 · 2013: 153 · 2012: 159
- FWCI
- 29.14
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Genetics (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Wellcome Trust
- Commonwealth Scholarship Commission
- Cambridge Overseas Trust
- Directorate for Biological Sciences
- Medical Research Council
- Biotechnology and Biological Sciences Research Council
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- Huntington's disease, mTOR, autophagy, polyglutamine expansion, rapamycin, temsirolimus, mutant huntingtin, protein aggregation, neurodegeneration, kinase inhibition, therapeutic target
- MeSH terms
- Huntingtin Protein, Animals, Autophagy, Disease Models, Animal, Drosophila melanogaster, Female, Humans, Huntington Disease, Male, Mice, Transgenic, Mutation, Nerve Tissue Proteins, Nuclear Proteins, Peptides, Protein Kinases, Protein Biosynthesis, COS Cells, Sirolimus, Macromolecular Substances, Protein Kinase Inhibitors, Mice, TOR Serine-Threonine Kinases
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