The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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
Flagged first, then by citations
Cited by
Sorted by citations
Items 601–700 of 1,011
Autophagy takes flight in Drosophila
Chang, Y.-Y., & Neufeld, T. P. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.006 · Cited by 110
Self-eating in the plaque: what macrophage autophagy reveals about atherosclerosis
Sergin, I., & Razani, B. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2014.03.010 · Cited by 111
Obara, I., Tochiki, K. K., Géranton, S. M., Carr, F. B., Lumb, B. M., Liu, Q., & Hunt, S. P. (2011) · Pain · doi:10.1016/j.pain.2011.07.025 · Cited by 110
Autophagy Controls p38 Activation to Promote Cell Survival under Genotoxic Stress
Qiang, L., Wu, C., Ming, M., Viollet, B., & He, Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.415224 · Cited by 113
Hwang, J.-Y., Gertner, M. J., Pontarelli, F., Court-Vazquez, B. L., Bennett, M. V. L., Ofengeim, D., & Zukin, R. S. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.140 · Cited by 113
Toyooka, K., Moriyasu, Y., Goto, Y., Takeuchi, M., Fukuda, H., & Matsuoka, K. (2006) · Autophagy · doi:10.4161/auto.2.2.2366 · Cited by 109
Autophagy in neurodegenerative diseases: From pathogenic dysfunction to therapeutic modulation
Martínez‐Vicente, M. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.03.005 · Cited by 114
Ferroptosis regulation through Nrf2 and implications for neurodegenerative diseases
Xiang, Y., Song, X., & Long, D. (2024) · Archives of Toxicology · doi:10.1007/s00204-023-03660-8 · Cited by 116
Characterization of α‐synuclein aggregation and synergistic toxicity with protein tau in yeast
Zabrocki, P., Pellens, K., Vanhelmont, T., Vandebroek, T., Griffioen, G., Wera, S., LEUVEN, F. V., & Winderickx, J. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04571.x · Cited by 111
The pathogenesis of Niemann–Pick type C disease: a role for autophagy?
Pacheco, C. D., & Lieberman, A. P. (2008) · Expert Reviews in Molecular Medicine · doi:10.1017/s146239940800080x · Cited by 115
Oxidant Stress and Signal Transduction in the Nervous System with the PI 3-K, Akt, and mTOR Cascade
Maiese, K., Chong, Z. Z., Wang, S., & Shang, Y. C. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms131113830 · Cited by 109
Fine Structure of the Autophagosome
Eskelinen, E. (2008) · Methods in molecular biology · doi:10.1007/978-1-59745-157-4_2 · Cited by 110
IRS2 increases mitochondrial dysfunction and oxidative stress in a mouse model of Huntington disease
Sadagurski, M., Cheng, Z., Rozzo, A., Palazzolo, I., Kelley, G. R., Dong, X., Krainc, D., & White, M. F. (2011) · Journal of Clinical Investigation · doi:10.1172/jci46305 · Cited by 107
Cortés, C. J., Qin, K., Cook, J., Solanki, A., & Mastrianni, J. A. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.6189-11.2012 · Cited by 113
Metzger, S., Saukko, M., Che, H. V., Tong, L., Puder, Y., Rieß, O., & Nguyen, H. P. (2010) · Human Genetics · doi:10.1007/s00439-010-0873-9 · Cited by 108
Translation of HTT mRNA with expanded CAG repeats is regulated by the MID1–PP2A protein complex
Krauß, S., Griesche, N., Jastrzebska, E., Chen, C., Rutschow, D., Achmüller, C., Dorn, S., Boesch, S., Lalowski, M. M., Wanker, E. E., et al. (2013) · Nature Communications · doi:10.1038/ncomms2514 · Cited by 108
Dysregulation and crosstalk of cellular signaling pathways in colon carcinogenesis
Wu, W. K. K., Wang, X., Cheng, A. S. L., Luo, M. X. M., Ng, S. S. M., To, K. F., Chan, F. K. L., Cho, C. H., Sung, J. J. �., & Yu, J. Q. (2012) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2012.11.009 · Cited by 111
Review: Autophagy in neurodegeneration: firefighter and/or incendiarist?
Rami, A. (2009) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2009.01034.x · Cited by 112
Wu, A., Wong, V. K. W., Xu, S., Chan, W.-K., Ng, P. C. I., Liu, L., & Law, B. Y. K. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms141122618 · Cited by 108
Autophagy in rat annulus fibrosus cells: evidence and possible implications
Shen, C., Yan, J., Jiang, L., & Dai, L. (2011) · Arthritis Research & Therapy · doi:10.1186/ar3443 · Cited by 107
Kassai, H., Sugaya, Y., Noda, S., Nakao, K., Maeda, T., Kano, M., & Aiba, A. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.048 · Cited by 107
Autophagy: Supporting cellular and organismal homeostasis by self-eating
Eskelinen, E. (2019) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2019.03.010 · Cited by 110
Different Approaches to Modulation of Microglia Phenotypes After Spinal Cord Injury
Akhmetzyanova, E. R., Kletenkov, K., Mukhamedshina, Y. O., & Rizvanov, A. A. (2019) · Frontiers in Systems Neuroscience · doi:10.3389/fnsys.2019.00037 · Cited by 110
The Multiple Roles of Autophagy in Neural Function and Diseases
Li, Y., Qin, Z., & Sheng, R. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-023-01120-y · Cited by 109
Cell death and autophagy in tuberculosis
Moraco, A. H., & Kornfeld, H. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2014.10.001 · Cited by 111
Protein aggregation as a paradigm of aging
Lindner, A. B., & Démarez, A. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.06.005 · Cited by 111
Autophagy in ageing and ageing-associated diseases
He, L., Lu, J., & Yue, Z. (2013) · Acta Pharmacologica Sinica · doi:10.1038/aps.2012.188 · Cited by 107
Role of Microtubules in Extracellular Release of Poliovirus
Taylor, M. P., Burgon, T. B., Kirkegaard, K., & Jackson, W. T. (2009) · Journal of Virology · doi:10.1128/jvi.01819-08 · Cited by 106
The pathophysiology of defective proteostasis in the hypothalamus — from obesity to ageing
Cavadas, C., Aveleira, C. A., Souza, G. F. P., & Velloso, L. A. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.107 · Cited by 105
mTOR-Related Brain Dysfunctions in Neuropsychiatric Disorders
Ryskalin, L., Limanaqi, F., Frati, A., Busceti, C. L., & Fornai, F. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082226 · Cited by 110
Controlling the mass action of α‐synuclein in Parkinson’s disease
Kim, C., & Lee, S. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05612.x · Cited by 108
Role of Autophagy in Early Brain Injury after Experimental Subarachnoid Hemorrhage
Wang, Z., Shi, X.-Y., Yin, J., Zuo, G., Zhang, J., & Chen, G. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9575-6 · Cited by 105
Defining the Role of Ubiquitin-interacting Motifs in the Polyglutamine Disease Protein, Ataxin-3
Berke, S. J. S., Chai, Y., Marrs, G. L., Wen, H., & Paulson, H. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506084200 · Cited by 105
Wang, S., Zheng, S., Zhang, Q., Yang, Z., Yin, K., & Xu, S. (2018) · Environmental Pollution · doi:10.1016/j.envpol.2018.08.070 · Cited by 105
Guedes-Dias, P., de Proença, J., Soares, T. R., Leitão-Rocha, A., Pinho, B. R., Duchen, M. R., & Oliveira, J. M. A. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.012 · Cited by 107
Huntington Disease and the Huntingtin Protein
Zheng, Z., & Diamond, M. I. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00010-2 · Cited by 118
Oncosuppressive Functions of Autophagy
Morselli, E., Galluzzi, L., Kepp, O., Mariño, G., Michaud, M., Vitale, I., Maiuri, M. C., & Kroemer, G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3478 · Cited by 112
Neuroprotective effects of dietary restriction: Evidence and mechanisms
Pani, G. (2015) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2015.03.004 · Cited by 103
Autophagy and polyglutamine diseases
Jiménez-Sánchez, M., Thomson, F., Zavodszky, E., & Rubinsztein, D. C. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.08.013 · Cited by 105
Self-citationReactive Oxygen Species as a Link between Antioxidant Pathways and Autophagy
Li, D., Ding, Z., Du, K., Ye, X., & Cheng, S. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/5583215 · Cited by 107
Autophagy and cancer: Dynamism of the metabolism of tumor cells and tissues
Tsuchihara, K., Fujii, S., & Esumi, H. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.09.040 · Cited by 105
Dissection of autophagy in human platelets
Feng, W., Chang, C., Luo, D., Su, H., Yu, S., Hua, W., Chen, Z., Hu, H., & Liu, W. (2014) · Autophagy · doi:10.4161/auto.27832 · Cited by 102
Protein folding diseases and neurodegeneration: Lessons learned from yeast
Winderickx, J., Delay, C., Vos, A. D., Klinger, H., Pellens, K., Vanhelmont, T., LEUVEN, F. V., & Zabrocki, P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.01.020 · Cited by 108
Mazucanti, C. H., Cabral‐Costa, J. V., Vasconcelos, A. R., Andreotti, D. Z., Scavone, C., & Kawamoto, E. M. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150610125715 · Cited by 103
PARP-1 Inhibition Is Neuroprotective in the R6/2 Mouse Model of Huntington’s Disease
Cardinale, A., Paldino, E., Giampà, C., Bernardi, G., & Fusco, F. R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134482 · Cited by 105
Ubiquitin signaling in neurodegenerative diseases: an autophagy and proteasome perspective
Guerroué, F. L., & Youle, R. J. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00667-x · Cited by 108
JIANG, J., Jiang, J., Zuo, Y., & Gu, Z. (2013) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2013.1280 · Cited by 101
BAG3: a new player in the heart failure paradigm
Knezevic, T., Myers, V. D., Gordon, J., Tilley, D. G., Sharp, T. E., Wang, J., Khalili, K., Cheung, J. Y., & Feldman, A. M. (2015) · Heart Failure Reviews · doi:10.1007/s10741-015-9487-6 · Cited by 101
Autophagy in Neurodegenerative Diseases and Metal Neurotoxicity
Zhang, Z., Miah, M. R., Culbreth, M. E., & Aschner, M. (2016) · Neurochemical Research · doi:10.1007/s11064-016-1844-x · Cited by 101
Progress and Challenges in Targeted Protein Degradation for Neurodegenerative Disease Therapy
Fang, Y., Wang, J., Zhao, M., Zheng, Q., Ren, C., Wang, Y., & Zhang, J. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00844 · Cited by 100
Staufen1 links RNA stress granules and autophagy in a model of neurodegeneration
Paul, S., Dansithong, W., Figueroa, K. P., Scoles, D. R., & Pulst, S. M. (2018) · Nature Communications · doi:10.1038/s41467-018-06041-3 · Cited by 104
Tourette, C., Li, B., Bell, R. N., O’Hare, S., Kaltenbach, L. S., Mooney, S. D., & Hughes, R. E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.523696 · Cited by 100
Butler, D., & Bahr, B. A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.185 · Cited by 104
Zhou, S.-F., Li, J., Yang, Y., Liu, Q., Pan, S., He, Z., Zhang, X., Yang, T., Chen, X., Wang, D., et al. (2015) · Drug Design Development and Therapy · doi:10.2147/dddt.s75378 · Cited by 99
RetractedRheb controls misfolded protein metabolism by inhibiting aggresome formation and autophagy
Zhou, X., Ikenoue, T., Chen, X., Li, L., Inoki, K., & Guan, K. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903621106 · Cited by 101
Yang, Y.-S., Kato, M., Wu, X., Litsios, A., Sutter, B. M., Wang, Y., Hsu, C.-H., Wood, N. E., Lemoff, A. S., Mirzaei, H., et al. (2019) · Cell · doi:10.1016/j.cell.2019.02.043 · Cited by 99
Mouse behavioural analysis in systems biology
van Meer, P., & Raber, J. (2005) · Biochemical Journal · doi:10.1042/bj20042023 · Cited by 107
Cellular and Molecular Pathways Triggering Neurodegeneration in the Spinocerebellar Ataxias
Matilla‐Dueñas, A., Sánchez, I., Corral‐Juan, M., Dávalos, A., Álvarez, R., & Latorre, P. (2009) · The Cerebellum · doi:10.1007/s12311-009-0144-2 · Cited by 101
Hou, K., Xu, D., Li, F., Chen, S., & Li, Y. (2019) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2019.03.015 · Cited by 99
Seidel, K., Vinet, J., den Dunnen, W. F. A., Brunt, E. R. P., Meister, M., Boncoraglio, A., Zijlstra, M. P., Boddeke, H. W. G. M., Rüb, U., Kampinga, H. H., et al. (2011) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2011.01198.x · Cited by 101
Insights into CNS ageing from animal models of senescence
Yeoman, M. S., Scutt, G., & Faragher, R. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3230 · Cited by 98
Shacka, J., Klocke, B., Young, C., Shibata, M., Olney, J., Uchiyama, Y., Saftig, P., & Roth, K. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.5577-06.2007 · Cited by 97
Autophagy-regulating small molecules and their therapeutic applications
Baek, K.-H., Park, J., & Shin, I. (2012) · Chemical Society Reviews · doi:10.1039/c2cs15328a · Cited by 101
Wu, H., Chen, S., Al-Baadani, A., Xu, J., Wu, Q., Pan, K., Zhang, J., & Hong, Y. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8933-0 · Cited by 103
Transcriptional regulation of the stress response by mTOR
Aramburu, J. F., Ortells, M. C., Vaquero, S. T., Buxadé, M., & López‐Rodríguez, C. (2014) · Science Signaling · doi:10.1126/scisignal.2005326 · Cited by 100
Autophagy: Highlighting a novel player in the autoimmunity scenario
Lleò, A., Invernizzi, P., Selmi, C. F., Coppel, R. L., Alpini, G. D., Podda, M., Mackay, I. R., & Gershwin, M. E. (2007) · Journal of Autoimmunity · doi:10.1016/j.jaut.2007.06.003 · Cited by 98
Potential autophagy enhancers attenuate rotenone-induced toxicity in SH-SY5Y
Xiong, N., Jia, M., Chen, C., Xiong, J., Zhang, Z., Huang, J., Hou, L., Yang, H., Cao, X., Liang, Z., et al. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.10.031 · Cited by 99
Autophagy and ionizing radiation in tumors: The “survive or not survive” dilemma
Palumbo, S., & Comincini, S. (2012) · Journal of Cellular Physiology · doi:10.1002/jcp.24118 · Cited by 99
A new look at an old drug: neuroprotective effects and therapeutic potentials of lithium salts
Carmassi, C., Grande, C. D., Gesi, C., Musetti, L., & Dell’Osso, L. (2016) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s106479 · Cited by 102
The role of mTOR signaling pathway in spinal cord injury
Kanno, H., Ozawa, H., Sekiguchi, A., Yamaya, S., Tateda, S., Yahata, K., & Itoi, E. (2012) · Cell Cycle · doi:10.4161/cc.21262 · Cited by 97
Ciammola, A., Sassone, J., Alberti, L., Meola, G., Mancinelli, E., Russo, M. A., Squitieri, F., & Silani, V. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401967 · Cited by 99
The Role of Tau in Neurodegenerative Diseases and Its Potential as a Therapeutic Target
Wolfe, M. S. (2012) · Scientifica · doi:10.6064/2012/796024 · Cited by 105
Molitoris, J. K., McColl, K. S., Swerdlow, S., Matsuyama, M., Lam, M., Finkel, T. H., Matsuyama, S., & Distelhorst, C. W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.245423 · Cited by 96
Nascimento-Ferreira, I., Nóbrega, C., Vasconcelos-Ferreira, A., Onofre, I., Albuquerque, D., Aveleira, C., Hirai, H., Déglon, N., & Pereira de Almeida, L. (2013) · Brain · doi:10.1093/brain/awt144 · Cited by 96
Gabandé‐Rodríguez, E., Heras, M. M. G. D. L., & Mittelbrunn, M. (2019) · Cells · doi:10.3390/cells9010082 · Cited by 101
Optineurin: The autophagy connection
Ying, H., & Yue, B. Y. J. T. (2015) · Experimental Eye Research · doi:10.1016/j.exer.2015.06.029 · Cited by 106
Visualization of pulmonary inflammation using noninvasive fluorescence molecular imaging
Haller, J., Hyde, D. E., Deliolanis, N. C., de Kleine, R. H. J., Niedre, M. J., & Ntziachristos, V. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00959.2007 · Cited by 96
Therapeutic implication of autophagy in neurodegenerative diseases
Rahman, M. A., & Rhim, H. (2017) · BMB Reports · doi:10.5483/bmbrep.2017.50.7.069 · Cited by 100
Chiang, M.-C., Chen, H.-M., Lee, Y.-H., Chang, H.-H., Wu, Y.-C., Soong, B.-W., Chen, C.-M., Wu, Y.-R., Liu, C.-S., Niu, D.-M., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddl481 · Cited by 95
Probing Mechanisms That Underlie Human Neurodegenerative Diseases in Drosophila
Jaiswal, M., Sandoval, H., Zhang, K., Bayat, V., & Bellen, H. J. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110711-155456 · Cited by 100
Crippa, V., Cicardi, M. E., Ramesh, N., Seguin, S. J., Ganassi, M., Bigi, I., Diacci, C., Zelotti, E., Baratashvili, M., Gregory, J. M., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw232 · Cited by 96
Amyotrophic Lateral Sclerosis and Autophagy: Dysfunction and Therapeutic Targeting
Amin, A., Perera, N. D., Beart, P. M., Turner, B. J., & Shabanpoor, F. (2020) · Cells · doi:10.3390/cells9112413 · Cited by 103
Chaperone-mediated autophagy in aging and neurodegeneration: Lessons from α-synuclein
Bandyopadhyay, U., & Cuervo, A. M. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.05.019 · Cited by 103
Fox, J. H., Connor, T., Chopra, V., Dorsey, K., Kama, J. A., Bleckmann, D., Betschart, C., Hoyer, D., Frentzel, S., DiFiglia, M., et al. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-26 · Cited by 94
“Given the discrepancy between our findings using everolimus in R6/2 mice and Ravikumar et al [7] using CCI-779 in N171-82Q mice, side-by-side testing of these molecules in both R6/2 and N171-82Q mice, and perhaps as well in a full-length huntingtin mouse model, would provide additional insight into the value of this c…”
BackgroundMethodResultInfluentialAutophagy Is Increased in Postmortem Brains of Persons With HIV-1-Associated Encephalitis
Zhou, D., Masliah, E., & Spector, S. A. (2011) · The Journal of Infectious Diseases · doi:10.1093/infdis/jir163 · Cited by 95
Antitumor Activity of Rapamycin in a Transgenic Mouse Model of ErbB2-Dependent Human Breast Cancer
Liu, M., Howes, A. L., Lesperance, J., Stallcup, W. B., Hauser, C. A., Kadoya, K., Oshima, R. G., & Abraham, R. T. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4589 · Cited by 97
Relieving Autophagy and 4EBP1 from Rapamycin Resistance
Nyfeler, B., Bergman, P., Triantafellow, E., Wilson, C. J., Zhu, Y., Radetich, B., Finan, P. M., Klionsky, D. J., & Murphy, L. O. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05430-11 · Cited by 94
Stimulation of autophagy prevents intestinal mucosal inflammation and ameliorates murine colitis
Macias-Ceja, D. C., Cosín‐Roger, J., Ortiz‐Masiá, D., Salvador, P., Hernández, C., Esplugues, J. V., Calatayud, S., & Barrachina, M. D. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13860 · Cited by 94
CRISPR/Cas9 Mediated Therapeutic Approach in Huntington’s Disease
Alkanlı, S. S., Alkanlı, N., Ay, A., & Albeniz, İ. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-03150-5 · Cited by 94
Polyglutamine expansion in huntingtin alters its interaction with phospholipids
Kegel, K. B., Sapp, E., Alexander, J. S., Valencia, A., Reeves, P., Li, X., Masso, N., Sobin, L. B., D, N. A. M., & DiFiglia, M. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06255.x · Cited by 94
Macroautophagy Is Regulated by the UPR–Mediator CHOP and Accentuates the Phenotype of SBMA Mice
Yu, Z., Wang, A. M., Adachi, H., Katsuno, M., Sobue, G., Yue, Z., Robins, D. M., & Lieberman, A. P. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002321 · Cited by 97
Maynard, C. J., Böttcher, C., Ortega, Z., Smith, R. A., Florea, B. I., Dı́az-Hernández, M., Brundin, P., Overkleeft, H. S., Li, J., Lucas, J. J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906463106 · Cited by 98
Of Flies and Man:Drosophilaas a Model for Human Complex Traits
Mackay, T. F. C., & Anholt, R. R. H. (2006) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.7.080505.115758 · Cited by 96
Autophagy activators suppress cystogenesis in an autosomal dominant polycystic kidney disease model
Zhu, P., Sieben, C. J., Xu, X., Harris, P. C., & Lin, X. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw376 · Cited by 95
Beclin-1: a therapeutic target at the intersection of autophagy, immunotherapy, and cancer treatment
Cao, Z., Tian, K., Ran, Y., Zhou, H., Zhou, L., Ding, Y., & Tang, X. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1506426 · Cited by 101
Tanji, K., Miki, Y., Maruyama, A., Mimura, J., Matsumiya, T., Mori, F., Imaizumi, T., Itoh, K., & Wakabayashi, K. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.08.076 · Cited by 94
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
Weber, J. D., & Gutmann, D. H. (2012) · Cell Cycle · doi:10.4161/cc.11.2.19022 · Cited by 97
Fortun, J., Verrier, J. D., Go, J. C., Madorsky, I., Dunn, W. A., & Notterpek, L. M. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.09.018 · Cited by 96
Removing Protein Aggregates: The Role of Proteolysis in Neurodegeneration
Nijholt, D. A. T., Kimpe, L. D., Elfrink, H. L., Hoozemans, J. J. M., & Scheper, W. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711795843236 · Cited by 96
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
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review