Could sirtuin activities modify ALS onset and progression?
Open accessAbstract
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease with a complex etiology. Sirtuins have been implicated as disease-modifying factors in several neurological disorders, and in the past decade, attempts have been made to check if manipulating Sirtuin activities and levels could confer benefit in terms of neuroprotection and survival in ALS models. The efforts have largely focused on mutant SOD1, and while limited in scope, the results were largely positive. Here, the body of work linking Sirtuins with ALS is reviewed, with discussions on how Sirtuins and their activities may impact on the major etiological mechanisms of ALS. Moving forward, it is important that the potentially beneficial effect of Sirtuins in ALS disease onset and progression are assessed in ALS models with TDP-43, FUS, and C9orf72 mutations.
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SIRT1 activators, including resveratrol, slow disease progression in ALS animal models.
“treatment with SIRT1 activators, including resveratrol, ameliorates the disease progress in ALS animal models”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Tang, 2017
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2 retracted
Das, S., Mitrovsky, G., Vasanthi, H. R., & Das, D. K. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/345105 · Cited by 173 · see citing works
RetractedSong, L., Chen, L., Zhang, X., Li, J., & Le, W. (2014) · BioMed Research International · doi:10.1155/2014/483501 · Cited by 71 · see citing works
RetractedRosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062 · see citing works
Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576 · see citing works
DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., Nicholson, A. M., Finch, N. A., Flynn, H., Adamson, J., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.011 · Cited by 4,936 · see citing works
A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD
Renton, A. E., Majounie, E., Waite, A., Simón-Sánchez, J., Rollinson, S., Gibbs, J. R., Schymick, J. C., Laaksovirta, H., van Swieten, J. C., Myllykangas, L., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.010 · Cited by 4,409 · see citing works
Resveratrol improves health and survival of mice on a high-calorie diet
Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290 · see citing works
Lagouge, M., Argmann, C., Gerhart-Hines, Z., Meziane, H., Lerin, C., Daussin, F., Messadeq, N., Milne, J., Lambert, P., Elliott, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.11.013 · Cited by 4,057 · see citing works
Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796 · see citing works
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510 · see citing works
Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160 · see citing works
Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.093 · Cited by 2,732 · see citing works
hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,653 · see citing works
Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6
Vance, C. A., Rogelj, B., Hortobágyi, T., Vos, K. J. D., Nishimura, A. L., Sreedharan, J., Hu, X., Smith, B. N., Ruddy, D., Wright, P. D., et al. (2009) · Science · doi:10.1126/science.1165942 · Cited by 2,531 · see citing works
Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis
Kwiatkowski, T. J., Bosco, D. A., LeClerc, A. L., Tamrazian, E., Vanderburg, C. R., Russ, C., Davis, A., Gilchrist, J. M., Kasarskis, E. J., Munsat, T. L., et al. (2009) · Science · doi:10.1126/science.1166066 · Cited by 2,526 · see citing works
St-Pierre, J., Drori, S., Uldry, M., Silvaggi, J. M., Rhee, J., Jäger, S., Handschin, C., Zheng, K., Lin, J., Yang, W., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.024 · Cited by 2,233 · see citing works
Mammalian Sirtuins: Biological Insights and Disease Relevance
Haigis, M. C., & Sinclair, D. A. (2010) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092250 · Cited by 2,085 · see citing works
Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081 · see citing works
Sirtuins as regulators of metabolism and healthspan
Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008 · see citing works
Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., Kessler, B., Howitz, K. T., Gorospe, M., de Cabo, R., & Sinclair, D. A. (2004) · Science · doi:10.1126/science.1099196 · Cited by 1,924 · see citing works
Sirtuin activators mimic caloric restriction and delay ageing in metazoans
Wood, J. G., Rogina, B., Lavu, S., Howitz, K., Helfand, S. L., Tatar, M., & Sinclair, D. (2004) · Nature · doi:10.1038/nature02789 · Cited by 1,868 · see citing works
Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707 · see citing works
SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687 · see citing works
Onset and Progression in Inherited ALS Determined by Motor Neurons and Microglia
Boillée, S., Yamanaka, K., Lobsiger, C. S., Copeland, N. G., Jenkins, N. A., Kassiotis, G., Kollias, G., & Cleveland, D. W. (2006) · Science · doi:10.1126/science.1123511 · Cited by 1,623 · see citing works
State of play in amyotrophic lateral sclerosis genetics
Renton, A. E., Chiò, A., & Traynor, B. J. (2013) · Nature Neuroscience · doi:10.1038/nn.3584 · Cited by 1,563 · see citing works
A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy
Lee, I. H., Cao, L., Mostoslavsky, R., Lombard, D. B., Liu, J., Bruns, N. E., Tsokos, M., Alt, F. W., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712145105 · Cited by 1,473 · see citing works
Resveratrol Ameliorates Aging-Related Metabolic Phenotypes by Inhibiting cAMP Phosphodiesterases
Park, S. J., Ahmad, F., Philp, A., Baar, K., Williams, T., Luo, H., Ke, H., Rehmann, H., Taussig, R., Brown, A. L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.01.017 · Cited by 1,352 · see citing works
Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC‐1α
Gerhart‐Hines, Z., Rodgers, J. T., Bare, O., Lerin, C., Kim, S., Mostoslavsky, R., Alt, F. W., Wu, Z., & Puigserver, P. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601633 · Cited by 1,294 · see citing works
Mutations of optineurin in amyotrophic lateral sclerosis
Maruyama, H., Morino, H., Ito, H., Izumi, Y., Kato, H., Watanabe, Y., Kinoshita, Y., Kamada, M., Nodera, H., Suzuki, H., et al. (2010) · Nature · doi:10.1038/nature08971 · Cited by 1,265 · see citing works
Astrocytes expressing ALS-linked mutated SOD1 release factors selectively toxic to motor neurons
Nagai, M., Re, D. B., Nagata, T., Chalazonitis, A., Jessell, T. M., Wichterle, H., & Przedborski, S. (2007) · Nature Neuroscience · doi:10.1038/nn1876 · Cited by 1,220 · see citing works
Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
Deng, H.-X., Chen, W., Hong, S.-T., Boycott, K. M., Gorrie, G. H., Siddique, N., Yang, Y., Fecto, F., Shi, Y., Zhai, H., et al. (2011) · Nature · doi:10.1038/nature10353 · Cited by 1,174 · see citing works
Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150 · see citing works
Astrocytes as determinants of disease progression in inherited amyotrophic lateral sclerosis
Yamanaka, K., Chun, S. J., Boillee, S., Fujimori-Tonou, N., Yamashita, H., Gutmann, D. H., Takahashi, R., Misawa, H., & Cleveland, D. W. (2008) · Nature Neuroscience · doi:10.1038/nn2047 · Cited by 1,140 · see citing works
SIRT1 and other sirtuins in metabolism
Chang, H.-C., & Guarente, L. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.12.001 · Cited by 1,138 · see citing works
Regulation of autophagy by cytoplasmic p53
Tasdemir, E., Maiuri, M. C., Galluzzi, L., Vitale, I., Djavaheri-Mergny, M., D'Amelio, M., Criollo, A., Morselli, E., Zhu, C., Harper, F., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1730 · Cited by 1,132 · see citing works
Riluzole for amyotrophic lateral sclerosis (ALS)/motor neuron disease (MND)
Miller, R. G., Mitchell, J. D., & Moore, D. H. (2012) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd001447.pub3 · Cited by 1,123 · see citing works
Wild-Type Nonneuronal Cells Extend Survival of SOD1 Mutant Motor Neurons in ALS Mice
Clement, A. M., Nguyen, M. D., Roberts, E. A., Garcia, M. L., Boillée, S., Rule, M., McMahon, A. P., Doucette, W. T., Siwek, D. F., Ferrante, R. J., et al. (2003) · Science · doi:10.1126/science.1086071 · Cited by 1,101 · see citing works
Kim, D., Nguyen, M. D., Dobbin, M. M., Fischer, A., Sananbenesi, F., Rodgers, J. T., Delalle, I., Baur, J. A., Sui, G., Armour, S. M., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601758 · Cited by 1,074 · see citing works
Sirtuin 2 Inhibitors Rescue α-Synuclein-Mediated Toxicity in Models of Parkinson's Disease
Outeiro, T. F., Kontopoulos, E., Altmann, S. M., Kufareva, I., Strathearn, K. E., Amore, A. M., Volk, C. B., Maxwell, M. M., Rochet, J., McLean, P. J., et al. (2007) · Science · doi:10.1126/science.1143780 · Cited by 1,066 · see citing works
SIRT1 Functionally Interacts with the Metabolic Regulator and Transcriptional Coactivator PGC-1α
Nemoto, S., Fergusson, M. M., & Finkel, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501485200 · Cited by 1,047 · see citing works
Nishimura, A. L., Mitne‐Neto, M., da Silva, H. C. A., Richieri‐Costa, A., Middleton, S., Cascio, D., Kok, F., de Oliveira, J. R. M., Gillingwater, T. H., Webb, J., et al. (2004) · The American Journal of Human Genetics · doi:10.1086/425287 · Cited by 995 · see citing works
Mackenzie, I. R. A., Bigio, E. H., Ince, P. G., Geser, F., Neumann, M., Cairns, N. J., Kwong, L. K., Forman, M. S., Ravits, J., Stewart, H., et al. (2007) · Annals of Neurology · doi:10.1002/ana.21147 · Cited by 992 · see citing works
Stress granules as crucibles of ALS pathogenesis
Li, Y. R., King, O. D., Shorter, J., & Gitler, A. D. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201302044 · Cited by 913 · see citing works
The many faces of insulin-like peptide signalling in the brain
Fernandez, A. M., & Torres-Alemán, I. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3209 · Cited by 872 · see citing works
Slowing ageing by design: the rise of NAD+ and sirtuin-activating compounds
Bonkowski, M. S., & Sinclair, D. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.93 · Cited by 834 · see citing works
Wong, Y. C., & Holzbaur, E. L. F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405752111 · Cited by 812 · see citing works
Non–cell autonomous effect of glia on motor neurons in an embryonic stem cell–based ALS model
Di Giorgio, F. P., Carrasco, M. A., Siao, M. C., Maniatis, T., & Eggan, K. (2007) · Nature Neuroscience · doi:10.1038/nn1885 · Cited by 799 · see citing works
Johnson, B. S., Snead, D., Lee, J. J., McCaffery, J. M., Shorter, J., & Gitler, A. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.010264 · Cited by 790 · see citing works
Mitochondria, oxidative stress and neurodegeneration
Federico, A., Cardaioli, E., Pozzo, P. D., Formichi, P., Gallus, G. N., & Radi, E. (2012) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2012.05.030 · Cited by 790 · see citing works
Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia
Freischmidt, A., Wieland, T., Richter, B., Ruf, W., Schaeffer, V., Müller, K., Marroquin, N., Nordin, F., Hübers, A., Weydt, P., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4000 · Cited by 786 · see citing works
Astrocytes from familial and sporadic ALS patients are toxic to motor neurons
Haidet-Phillips, A. M., Hester, M. E., Miranda, C. J., Meyer, K., Braun, L., Frakes, A., Song, S., Likhite, S., Murtha, M. J., Foust, K. D., et al. (2011) · Nature Biotechnology · doi:10.1038/nbt.1957 · Cited by 782 · see citing works
Richter, B., Sliter, D. A., Herhaus, L., Stolz, A., Wang, C., Beli, P., Zaffagnini, G., Wild, P., Martens, S., Wagner, S. A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523926113 · Cited by 755 · see citing works
A randomized, double-blind, placebo-controlled trial of resveratrol for Alzheimer disease
Turner, R. S., Thomas, R. G., Craft, S., van Dyck, C. H., Mintzer, J. E., Reynolds, B., Brewer, J. B., Rissman, R. A., Raman, R., Aisen, P. S. S., et al. (2015) · Neurology · doi:10.1212/wnl.0000000000002035 · Cited by 753 · see citing works
Luen Tang, B. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.2318 · Cited by 740 · see citing works
Self-citationA comprehensive review of amyotrophic lateral sclerosis
Zarei, S., Carr, K., Reiley, L. E., Diaz, K., Guerra, O., Altamirano, P., Pagani, W., Lodin, D., Orozco, G., & Chinea, A. R. (2015) · Surgical Neurology International · doi:10.4103/2152-7806.169561 · Cited by 737 · see citing works
Resveratrol stimulates AMP kinase activity in neurons
Dasgupta, B., & Milbrandt, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610068104 · Cited by 723 · see citing works
Stress-Inducible Regulation of Heat Shock Factor 1 by the Deacetylase SIRT1
Westerheide, S. D., Anckar, J., Stevens, S. M., Sistonen, L., & Morimoto, R. I. (2009) · Science · doi:10.1126/science.1165946 · Cited by 722 · see citing works
Kong, X., Wang, R., Xue, Y., Liu, X., Zhang, H., Chen, Y., Fang, F., & Chang, Y. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011707 · Cited by 718 · see citing works
Sirtuin 1 and Sirtuin 3: Physiological Modulators of Metabolism
Nogueiras, R., Habegger, K. M., Chaudhary, N., Finan, B., Banks, A. S., Dietrich, M. O., Horváth, T. L., Sinclair, D. A., Pfluger, P. T., & Tschöp, M. H. (2012) · Physiological Reviews · doi:10.1152/physrev.00022.2011 · Cited by 712 · see citing works
Hariharan, N., Maejima, Y., Nakae, J., Paik, J., DePinho, R. A., & Sadoshima, J. (2010) · Circulation Research · doi:10.1161/circresaha.110.227371 · Cited by 688 · see citing works
Fecto, F. (2011) · Archives of Neurology · doi:10.1001/archneurol.2011.250 · Cited by 650 · see citing works
Stoica, R., Vos, K. J. D., Paillusson, S., Mueller, S., Sancho, R. M., Lau, K., Vizcay‐Barrena, G., Lin, W.-L., Xu, Y.-F., Lewis, J. M., et al. (2014) · Nature Communications · doi:10.1038/ncomms4996 · Cited by 623 · see citing works
Evidence for a Common Mechanism of SIRT1 Regulation by Allosteric Activators
Hubbard, B. P., Gomes, A. P., Dai, H., Li, J., Case, A. W., Considine, T., Riera, T. V., Lee, J. E., Yen, E. S., Lamming, D. W., et al. (2013) · Science · doi:10.1126/science.1231097 · Cited by 618 · see citing works
Molecular pathways of motor neuron injury in amyotrophic lateral sclerosis
Ferraiuolo, L., Kirby, J., Grierson, A. J., Sendtner, M., & Shaw, P. J. (2011) · Nature Reviews Neurology · doi:10.1038/nrneurol.2011.152 · Cited by 615 · see citing works
VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis
Vos, K. J. D., Mórotz, G. M., Stoica, R., Tudor, E. L., Lau, K., Ackerley, S., Warley, A., Shaw, C. E., & Miller, C. C. J. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr559 · Cited by 573 · see citing works
Small molecule SIRT1 activators for the treatment of aging and age-related diseases
Hubbard, B. P., & Sinclair, D. A. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.12.004 · Cited by 572 · see citing works
SIRT1 Is Essential for Normal Cognitive Function and Synaptic Plasticity
Michan, S., Li, Y., Chou, M. M.-H., Parrella, E., Ge, H., Long, J. M., Allard, J. S., Lewis, K., Miller, M., Xu, W., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0027-10.2010 · Cited by 541 · see citing works
Wen, X., Tan, W., Westergard, T., Krishnamurthy, K., Markandaiah, S. S., Shi, Y., Lin, S., Shneider, N. A., Monaghan, J., Pandey, U. B., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.12.010 · Cited by 513 · see citing works
Redox regulation of SIRT1 in inflammation and cellular senescence
Hwang, J.-W., Yao, H., Caito, S., Sundar, I. K., & Rahman, I. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.03.015 · Cited by 503 · see citing works
Resveratrol-Activated AMPK/SIRT1/Autophagy in Cellular Models of Parkinson’s Disease
Wu, Y., Li, X., Zhu, J. X., Xie, W., Le, W., Fan, Z., Jankovic, J. J., & Pan, T. (2011) · Neurosignals · doi:10.1159/000328516 · Cited by 495 · see citing works
Giorgio, F. P. D., Boulting, G. L., Bobrowicz, S., & Eggan, K. C. (2008) · Cell stem cell · doi:10.1016/j.stem.2008.09.017 · Cited by 488 · see citing works
Shimazu, T., Hirschey, M. D., Hua, L., Dittenhafer-Reed, K. E., Schwer, B., Lombard, D. B., Li, Y., Bunkenborg, J., Alt, F. W., Denu, J. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.003 · Cited by 484 · see citing works
Bannwarth, S., Ait-El-Mkadem, S., Chaussenot, A., Genin, E. C., Lacas‐Gervais, S., Fragaki, K., Berg-Alonso, L., Kageyama, Y., Serre, V., Moore, D. G., et al. (2014) · Brain · doi:10.1093/brain/awu138 · Cited by 482 · see citing works
Sirtuin 1 Reduction Parallels the Accumulation of Tau in Alzheimer Disease
Julien, C., Tremblay, C., Émond, V., Lebbadi, M., Salem, N., Bennett, D. A., & Calon, F. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181922348 · Cited by 467 · see citing works
Calorie restriction and sirtuins revisited
Guarente, L. (2013) · Genes & Development · doi:10.1101/gad.227439.113 · Cited by 464 · see citing works
ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS
Ling, S., de Albuquerque, C. P., Han, J. S., Lagier‐Tourenne, C., Tokunaga, S., Zhou, H., & Cleveland, D. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008227107 · Cited by 450 · see citing works
Sun, Z., Diaz, Z., Fang, X., Hart, M. P., Chesi, A., Shorter, J., & Gitler, A. D. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000614 · Cited by 448 · see citing works
SIRT3 deacetylates FOXO3 to protect mitochondria against oxidative damage.
Tseng, A. H., Shieh, S., & Wang, D. (2013) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2013.05.002 · Cited by 445 · see citing works
Watanabe, M., Dykes‐Hoberg, M., Culotta, V., Price, D. L., Wong, P. C., & Rothstein, J. D. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0443 · Cited by 432 · see citing works
FoxO Transcription Factors Promote Autophagy in Cardiomyocytes
Sengupta, A., Molkentin, J. D., & Yutzey, K. E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.024406 · Cited by 428 · see citing works
Marchetto, M. C. N., Muotri, A. R., Mu, Y., Smith, A. M., Cezar, G. G., & Gage, F. H. (2008) · Cell Stem Cell · doi:10.1016/j.stem.2008.10.001 · Cited by 424 · see citing works
Sellier, C., Campanari, M., Julie Corbier, C., Gaucherot, A., Kolb‐Cheynel, I., Oulad‐Abdelghani, M., Ruffenach, F., Page, A., Ciura, S., Kabashi, E., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593350 · Cited by 414 · see citing works
Necroptosis Drives Motor Neuron Death in Models of Both Sporadic and Familial ALS
Ré, D. B., Verche, V. L., Yu, C., Amoroso, M. W., Politi, K. A., Phani, S., Ikiz, B., Hoffmann, L., Koolen, M., Nagata, T., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.01.011 · Cited by 404 · see citing works
The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate initiation of autophagy
Webster, C. P., Smith, E. F., Bauer, C. S., Moller, A., Hautbergue, G. M., Ferraiuolo, L., Myszczynska, M. A., Higginbottom, A., Walsh, M. J., Whitworth, A. J., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201694401 · Cited by 404 · see citing works
The three ‘P’s of mitophagy: PARKIN.; PINK1.; and post-translational modifications
Durcan, T. M., & Fon, E. A. (2015) · Genes & Development · doi:10.1101/gad.262758.115 · Cited by 400 · see citing works
Hamacher‐Brady, A., & Brady, N. R. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2087-8 · Cited by 396 · see citing works
The role of sirtuins in cardiac disease
Matsushima, S., & Sadoshima, J. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00053.2015 · Cited by 378 · see citing works
Sirtuins in Aging and DiseasePreprint
Guarente, L. (2007) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2007.72.024 · Cited by 371 · see citing works
C9orf72 BAC Mouse Model with Motor Deficits and Neurodegenerative Features of ALS/FTD
Liu, Y., Pattamatta, A., Zu, T., Reid, T. S., Bardhi, O., Borchelt, D., Yachnis, A. T., & Ranum, L. P. W. (2016) · Neuron · doi:10.1016/j.neuron.2016.04.005 · Cited by 368 · see citing works
SIRT3-SOD2-mROS-dependent autophagy in cadmium-induced hepatotoxicity and salvage by melatonin
Pi, H., Xu, S., Reiter, R. J., Guo, P., Zhang, L., Li, Y., Li, M., Cao, Z., Tian, L., Xie, J., et al. (2015) · Autophagy · doi:10.1080/15548627.2015.1052208 · Cited by 363 · see citing works
Barbee, S. A., Estes, P. S., Cziko, A.-M., Hillebrand, J., Luedeman, R. A., Coller, J. M., Johnson, N., Howlett, I. C., Geng, C., Ueda, R., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.10.028 · Cited by 359 · see citing works
Jaarsma, D., Haasdijk, E. D., Grashorn, J., Hawkins, R. K., van Duijn, W., Verspaget, H. W., London, J., & Holstege, J. C. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0299 · Cited by 351 · see citing works
Meyer, K., Ferraiuolo, L., Miranda, C. J., Likhite, S., McElroy, S., Renusch, S., Ditsworth, D., Lagier-Tourenne, C., Smith, R. A., Ravits, J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314085111 · Cited by 345 · see citing works
Deregulation of Cdk5 in a Mouse Model of ALS
Nguyen, M. D., Larivière, R., & Julien, J. (2001) · Neuron · doi:10.1016/s0896-6273(01)00268-9 · Cited by 339 · see citing works
SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis
Luthi‐Carter, R., Taylor, D. M., Pallos, J., Lambert, E., Amore, A. M., Parker, J. A., Moffitt, H., Smith, D. L., Runne, H., Gökçe, Ö., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002924107 · Cited by 338 · see citing works
Song, Y. M., Lee, Y.-H., Kim, J.-W., Ham, D.-S., Kang, E.-S., Cha, B. S., Lee, H. C., & Lee, B.-W. (2015) · Autophagy · doi:10.4161/15548627.2014.984271 · Cited by 332 · see citing works
Regulation of SIRT1 in aging: Roles in mitochondrial function and biogenesis
Yuan, Y., Cruzat, V. F., Newsholme, P., Cheng, J., Chen, Y., & Lu, Y. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.02.003 · Cited by 301 · see citing works
The IKK complex contributes to the induction of autophagy
Criollo, A., Senovilla, L., Authier, H., Maiuri, M. C., Morselli, E., Vitale, I., Kepp, O., Tasdemir, E., Galluzzi, L., Shen, S., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.364 · Cited by 296 · see citing works
Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43
Nonaka, T., Kametani, F., Arai, T., Akiyama, H., & Hasegawa, M. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp275 · Cited by 295 · see citing works
Sullivan, P. M., Zhou, X., Robins, A. M., Paushter, D. H., Kim, D., Smolka, M. B., & Hu, F. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0324-5 · Cited by 295 · see citing works
Mitsumoto, H., Brooks, B. R., & Silani, V. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70129-2 · Cited by 291 · see citing works
SirT3 Regulates the Mitochondrial Unfolded Protein Response
Papa, L., & Germain, D. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01337-13 · Cited by 282 · see citing works
Pallos, J., Bodai, L., Lukácsovich, T., Purcell, J. M., Steffan, J. S., Thompson, L. M., & Marsh, J. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn273 · Cited by 265 · see citing works
Nicotinamide-induced Mitophagy
Jang, S., Kang, H. T., & Hwang, E. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.363747 · Cited by 259 · see citing works
Tubulin acetylation: responsible enzymes, biological functions and human diseases
Li, L., & Yang, X. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2000-5 · Cited by 257 · see citing works
Stoica, R., Paillusson, S., Gómez‐Suaga, P., Mitchell, J. C., Lau, D. H. W., Gray, E. H., Sancho, R. M., Vizcay‐Barrena, G., Vos, K. J. D., Shaw, C. E., et al. (2016) · EMBO Reports · doi:10.15252/embr.201541726 · Cited by 254 · see citing works
Dual control of mitochondrial biogenesis by sirtuin 1 and sirtuin 3
Brenmoehl, J., & Hoeflich, A. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.04.002 · Cited by 240 · see citing works
A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in autophagy
Yang, M., Liang, C., Swaminathan, K., Herrlinger, S., Lai, F., Shiekhattar, R., & Chen, J.-F. (2016) · Science Advances · doi:10.1126/sciadv.1601167 · Cited by 238 · see citing works
Sirtuin regulation in aging and injury
Poulose, N., & Raju, R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.017 · Cited by 236 · see citing works
Sirtuin deacetylases in neurodegenerative diseases of aging
Herskovits, A. Z., & Guarente, L. (2013) · Cell Research · doi:10.1038/cr.2013.70 · Cited by 222 · see citing works
Song, W., Song, Y., Kincaid, B., Bossy, B., & Bossy‐Wetzel, E. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.07.004 · Cited by 215 · see citing works
The Sirtuin 2 Inhibitor AK-7 Is Neuroprotective in Huntington’s Disease Mouse Models
Chopra, V., Quinti, L., Kim, J., Vollor, L., Narayanan, K. L., Edgerly, C. K., Cipicchio, P. M., Lauver, M. A., Choi, S. H., Silverman, R. B., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.11.001 · Cited by 214 · see citing works
Kim, S. H., Shanware, N. P., Bowler, M. J., & Tibbetts, R. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.154831 · Cited by 213 · see citing works
Fang, Y.-S., Tsai, K., Chang, Y.-J., Kao, P. F., Woods, R., Kuo, P. H., Wu, C., Liao, J., Chou, S.-C., Lin, V., et al. (2014) · Nature Communications · doi:10.1038/ncomms5824 · Cited by 211 · see citing works
Giralt, A., Hondares, E., Villena, J. A., Ribas, F., Díaz-Delfín, J., Giralt, M., Iglesias, R., & Villarroya, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.202390 · Cited by 210 · see citing works
Resveratrol Improves Motoneuron Function and Extends Survival in SOD1G93A ALS Mice
Mancuso, R., del Valle, J., Mòdol, L., Martínez‐Muriana, A., Granado‐Serrano, A. B., Ramírez‐Núñez, O., Pallàs, M., Portero‐Otín, M., Osta, R., & Navarro, X. (2014) · Neurotherapeutics · doi:10.1007/s13311-013-0253-y · Cited by 206 · see citing works
Transcriptional targets of sirtuins in the coordination of mammalian physiology
Feige, J. N., & Auwerx, J. H. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.012 · Cited by 202 · see citing works
Ferraiuolo, L., Heath, P. R., Holden, H. M., Kasher, P. R., Kirby, J., & Shaw, P. J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1470-07.2007 · Cited by 198 · see citing works
Sirtuins' modulation of autophagy
Ng, F., & Tang, B. L. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24399 · Cited by 194 · see citing works
Self-citationFUS Interacts with HSP60 to Promote Mitochondrial Damage
Deng, J., Yang, M., Chen, Y., Chen, X., Liu, J., Sun, S., Cheng, H., Li, Y., Bigio, E. H., Mesulam, M. M., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005357 · Cited by 188 · see citing works
Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin‐independent mechanism
Gal, J., Ström, A., Kwinter, D. M., Kilty, R., Zhang, J., Shi, P., Fu, W., Wooten, M. W., & Zhu, H. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06388.x · Cited by 187 · see citing works
SIRT1 in the brain—connections with aging-associated disorders and lifespan
Ng, F. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00064 · Cited by 185 · see citing works
Heat Shock Factor 1 as a Coordinator of Stress and Developmental Pathways
Anckar, J., & Sistonen, L. (2007) · Springer eBooks · doi:10.1007/978-0-387-39975-1_8 · Cited by 181 · see citing works
Chen, H.-J., Mitchell, J. C., Novoselov, S. S., Miller, J. W., Nishimura, A. L., Scotter, E. L., Vance, C. A., Cheetham, M. E., & Shaw, C. E. (2016) · Brain · doi:10.1093/brain/aww028 · Cited by 181 · see citing works
Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities
Magrané, J., Hervías, I., Henning, M. S., Damiano, M. G., Kawamata, H., & Manfredi, G. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp421 · Cited by 171 · see citing works
SIRT1 suppresses the senescence-associated secretory phenotype through epigenetic gene regulation
Hayakawa, T., Iwai, M., Aoki, S., Takimoto, K., Maruyama, M., Maruyama, W., & Motoyama, N. (2015) · PLOS ONE · doi:10.1371/journal.pone.0116480 · Cited by 170 · see citing works
SOD1 misplacing and mitochondrial dysfunction in amyotrophic lateral sclerosis pathogenesis
Tafuri, F., Ronchi, D., Magri, F., Comi, G. P., & Corti, S. P. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00336 · Cited by 162 · see citing works
Nomura, T., Watanabe, S., Kaneko, K., Yamanaka, K., Nukina, N., & Furukawa, Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.516492 · Cited by 160 · see citing works
Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones
Udan-Johns, M., Bengoechea, R., Bell, S., Shao, J., Diamond, M. I., True, H. L., Weihl, C. C., & Baloh, R. H. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt408 · Cited by 149 · see citing works
Repeat-associated non-ATG (RAN) translation in neurological disease
Cleary, J. D., & Ranum, L. P. W. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt371 · Cited by 143 · see citing works
Hdac6 deletion delays disease progression in the SOD1G93A mouse model of ALS
Taes, I., Timmers, M., Hersmus, N., Bento‐Abreu, A., Bosch, L. V. D., Damme, P. V., Auwerx, J. H., & Robberecht, W. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt028 · Cited by 139 · see citing works
Pathogenesis of FUS-associated ALS and FTD: insights from rodent models
Nolan, M., Talbot, K., & Ansorge, O. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0358-8 · Cited by 139 · see citing works
Zhao, W., Varghese, M., Vempati, P., Dzhun, A., Cheng, A., Wang, J., Lange, D. J., Bilski, A. E., Faravelli, I., & Pasinetti, G. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049191 · Cited by 135 · see citing works
Zhao, Y., Luo, P., Guo, Q., Li, S., Zhang, L., Zhao, M., Xu, H., Yang, Y., Poon, W. S., & Fei, Z. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.07.004 · Cited by 134 · see citing works
Gifondorwa, D. J., Robinson, M., Hayes, C. D., Taylor, A. R., Prevette, D. M., Oppenheim, R. W., Caress, J. B., & Milligan, C. E. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4057-07.2007 · Cited by 134 · see citing works
Zhao, W., Varghese, M., Yemul, S., Pan, Y., Cheng, A., Marano, P., Hassan, S., Vempati, P., Chen, F., Qian, X., et al. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-51 · Cited by 134 · see citing works
Sirtuin‐dependent epigenetic regulation in the maintenance of genome integrity
Bosch‐Presegué, L., & Vaquero, A. (2015) · The FEBS Journal · doi:10.1111/febs.13053 · Cited by 132 · see citing works
Distinct Patterns of Sirtuin Expression During Progression of Alzheimer’s Disease
Lutz, M. I., Milenković, I., Regelsberger, G., & Kovács, G. G. (2014) · NeuroMolecular Medicine · doi:10.1007/s12017-014-8288-8 · Cited by 131 · see citing works
The expanding syndrome of amyotrophic lateral sclerosis: a clinical and molecular odyssey
Turner, M. R., & Swash, M. (2015) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2014-308946 · Cited by 130 · see citing works
Nicotinamide enhances mitochondria quality through autophagy activation in human cells
Kang, H. T., & Hwang, E. S. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00487.x · Cited by 125 · see citing works
Sirtuins in neurodegenerative diseases: an update on potential mechanisms
Min, S., Sohn, P., Cho, S.-H., Swanson, R. A., & Gan, L. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00053 · Cited by 123 · see citing works
Sirtuins and Their Relevance to the Kidney
Hao, C., & Haase, V. H. (2010) · Journal of the American Society of Nephrology · doi:10.1681/asn.2010010046 · Cited by 117 · see citing works
Amyotrophic lateral sclerosis: Current perspectives from basic research to the clinic
Mancuso, R., & Navarro, X. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.07.004 · Cited by 116 · see citing works
Modulation of SIRT1 expression in different neurodegenerative models and human pathologies
Pallàs, M., Pizarro, J. G., Cuesta, J., Crespo‐Biel, N., Alvira, D., Tajes, M., Yeste‐Velasco, M., Folch, J., Canudas, A. M., Sureda, F. X., et al. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.04.065 · Cited by 112 · see citing works
Protein folding alterations in amyotrophic lateral sclerosis
Parakh, S., & Atkin, J. D. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.010 · Cited by 111 · see citing works
Distribution Analysis of Deacetylase SIRT1 in Rodent and Human Nervous Systems
Zakhary, S. M., Ayubcha, D., Dileo, J. N., Jose, R., Leheste, J. R., Horowitz, J. M., & Torres, G. (2010) · The Anatomical Record · doi:10.1002/ar.21116 · Cited by 110 · see citing works
Autophagy induced by the class III histone deacetylase Sirt1 prevents prion peptide neurotoxicity
Jeong, J., Moon, M., Lee, Y.-J., Seol, J., & Park, S. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.04.002 · Cited by 102 · see citing works
Restricted mitochondrial protein acetylation initiates mitochondrial autophagy
Webster, B. R., Scott, I., Han, K., Li, J. H., Lu, Z., Stevens, M. V., Malide, D. A., Chen, Y., Samsel, L., Connelly, P. S., et al. (2013) · Journal of Cell Science · doi:10.1242/jcs.131300 · Cited by 101 · see citing works
Properties of sea urchin embryo messenger RNA containing and lacking poly(A)
Nemer, M. J., Dubroff, L. M., & Graham, M. (1975) · Cell · doi:10.1016/0092-8674(75)90007-0 · Cited by 97 · see citing works
Pathogenesis/genetics of frontotemporal dementia and how it relates to ALS
Callister, J. B., & Pickering-Brown, S. M. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.06.001 · Cited by 96 · see citing works
Duan, W., Li, Y.-F., Liu, F., Deng, J., Wu, Y., Yuan, W., Tsoi, B., Chen, J., Wang, Q., Cai, S., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.03.022 · Cited by 94 · see citing works
Harlan, B. A., Pehar, M., Sharma, D. R., Beeson, G., Beeson, C. C., & Vargas, M. R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.698779 · Cited by 94 · see citing works
Watanabe, S., Ageta‐Ishihara, N., Nagatsu, S., Takao, K., Komine, O., Endo, F., Miyakawa, T., Misawa, H., Takahashi, R., Kinoshita, M., et al. (2014) · Molecular Brain · doi:10.1186/s13041-014-0062-1 · Cited by 90 · see citing works
Pathways to mitochondrial dysfunction in ALS pathogenesis
Carrı̀, M. T., D’Ambrosi, N., & Cozzolino, M. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.07.055 · Cited by 90 · see citing works
Recent advances in amyotrophic lateral sclerosis
Riva, N., Agosta, F., Lunetta, C., Filippi, M., & Quattrini, A. (2016) · Journal of Neurology · doi:10.1007/s00415-016-8091-6 · Cited by 88 · see citing works
Resveratrol upregulated heat shock proteins and extended the survival of G93A-SOD1 mice
Han, S.-Y., Choi, J.-R., Shin, K. S., & Kang, S. J. (2012) · Brain Research · doi:10.1016/j.brainres.2012.09.022 · Cited by 83 · see citing works
Wang, J., Zhang, Y., Tang, L., Zhang, N., & Fan, D. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.08.047 · Cited by 83 · see citing works
Proteostasis impairment in ALS
Ruegsegger, C., & Saxena, S. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.032 · Cited by 82 · see citing works
From molecule to molecule and cell to cell: Prion-like mechanisms in amyotrophic lateral sclerosis
Grad, L. I., Fernando, S. M., & Cashman, N. R. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.02.009 · Cited by 77 · see citing works
SIRT1, a histone deacetylase, regulates prion protein-induced neuronal cell death
Seo, J., Moon, M., Jeong, J., Seol, J., Lee, Y.-J., Park, B., & Park, S. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.09.019 · Cited by 75 · see citing works
Resveratrol: New Avenues for a Natural Compound in Neuroprotection
Pallàs, M., Porquet, D., Vicente, A., & Sanfeliu, C. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319380005 · Cited by 75 · see citing works
Using mitochondrial sirtuins as drug targets: disease implications and available compounds
Gertz, M., & Steegborn, C. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2180-7 · Cited by 71 · see citing works
Srivastava, S., & Haigis, M. C. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211798072526 · Cited by 69 · see citing works
Pérez‐Pinzón, M. A., & Koronowski, K. B. (2015) · Brain Circulation · doi:10.4103/2394-8108.162532 · Cited by 69 · see citing works
Yu, Z., Fan, D., Gui, B., Shi, L., Xuan, C., Shan, L., Wang, Q., Shang, Y., & Wang, Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.357582 · Cited by 67 · see citing works
Schirmer, H., Pereira, T. C. B., Rico, E. P., Rosemberg, D. B., Bonan, C. D., Bogo, M. R., & Souto, A. A. (2011) · Molecular Biology Reports · doi:10.1007/s11033-011-1096-4 · Cited by 66 · see citing works
Körner, S., Böselt, S., Thau, N., Rath, K. J., Dengler, R., & Petri, S. (2013) · Neurodegenerative Diseases · doi:10.1159/000338048 · Cited by 64 · see citing works
Novoselov, S. S., Mustill, W. J., Gray, A. L., Dick, J. R. T., Kanuga, N., Kalmár, B., Greensmith, L., & Cheetham, M. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073944 · Cited by 63 · see citing works
Cell death in amyotrophic lateral sclerosis: interplay between neuronal and glial cells
Ferri, A., Nencini, M., Casciati, A., Cozzolino, M., Angelini, D. F., Longone, P., Spalloni, A., Rotilio, G., & Carrı̀, M. T. (2004) · The FASEB Journal · doi:10.1096/fj.03-1199fje · Cited by 62 · see citing works
SIRT1 as a therapeutic target for Alzheimer’s disease
Wong, S. Y., & Tang, B. L. (2016) · Reviews in the Neurosciences · doi:10.1515/revneuro-2016-0023 · Cited by 59 · see citing works
Self-citationLiang, Q., Benavides, G. A., Vassilopoulos, A., Gius, D. R., Darley-Usmar, V. M., & Zhang, J. (2013) · Biochemical Journal · doi:10.1042/bj20130414 · Cited by 57 · see citing works
Amyotrophic lateral sclerosis: an update on recent genetic insights
Iguchi, Y., Katsuno, M., Ikenaka, K., Ishigaki, S., & Sobue, G. (2013) · Journal of Neurology · doi:10.1007/s00415-013-7112-y · Cited by 55 · see citing works
Yamashita, H., Kawamata, J., Okawa, K., Kanki, R., Nakamizo, T., Hatayama, T., Yamanaka, K., Takahashi, R., & Shimohama, S. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04534.x · Cited by 54 · see citing works
Krey, L., Lühder, F., Kusch, K., Czech-Zechmeister, B., Könnecke, B., Outeiro, T. F., & Trendelenburg, G. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2015.178 · Cited by 52 · see citing works
A Single-Dose Resveratrol Treatment in a Mouse Model of Amyotrophic Lateral Sclerosis
Markert, C. D., Kim, E., Gifondorwa, D. J., Childers, M. K., & Milligan, C. (2010) · Journal of Medicinal Food · doi:10.1089/jmf.2009.0243 · Cited by 52 · see citing works
Valle, C., Salvatori, I., Gerbino, V., Rossi, S., Palamiuc, L., René, F., & Carrı̀, M. T. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.247 · Cited by 52 · see citing works
Old versus New Mechanisms in the Pathogenesis of ALS
Rossi, S., Cozzolino, M., & Carrı̀, M. T. (2016) · Brain Pathology · doi:10.1111/bpa.12355 · Cited by 52 · see citing works
The central role of heat shock factor 1 in synaptic fidelity and memory consolidation
Hooper, P. L., Durham, H. D., Török, Z., Hooper, P. L., Crul, T., & Vı́gh, L. (2016) · Cell Stress and Chaperones · doi:10.1007/s12192-016-0709-1 · Cited by 47 · see citing works
Sirt1's systemic protective roles and its promise as a target in antiaging medicine
Tang, B. L. (2010) · Translational research · doi:10.1016/j.trsl.2010.11.006 · Cited by 45 · see citing works
Self-citationBizat, N., Peyrin, J., Haı̈k, S., Cochois, V., Beaudry, P., Laplanche, J., & Néri, C. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5831-09.2010 · Cited by 45 · see citing works
Bartus, R. T., Bétourné, A., Basile, A. S., Peterson, B. L., Glass, J. D., & Boulis, N. M. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.006 · Cited by 43 · see citing works
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Lev, N., Ickowicz, D., Barhum, Y., Melamed, E., & Offen, D. (2008) · Journal of Molecular Neuroscience · doi:10.1007/s12031-008-9138-7 · Cited by 42 · see citing works
Koistinen, H. K., Prinjha, R. K., Soden, P. E., Harper, A. J., Banner, S. J., Pradat, P., Loeffler, J., & Dingwall, C. (2006) · Muscle & Nerve · doi:10.1002/mus.20612 · Cited by 42 · see citing works
Schipper, L. J., Raaphorst, J., Aronica, E., Baas, F., de Haan, R. J., de Visser, M., & Troost, D. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12284 · Cited by 41 · see citing works
de Oliveira, G. P., Alves, C. J., & Chadi, G. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00216 · Cited by 40 · see citing works
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Self-citationMazzini, L., Vescovi, A. L., Cantello, R. M., Gelati, M., & Vercelli, A. (2015) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2016.1116516 · Cited by 38 · see citing works
Jonsson, P. A., Bergemalm, D., Andersen, P. M., Gredal, O., Brännström, T., & Marklund, S. L. (2008) · Annals of Neurology · doi:10.1002/ana.21356 · Cited by 34 · see citing works
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Lee, J. C., Shin, J.-H., Park, B.-W., Kim, G. S., Kim, J. C., Kang, K.-S., & Cha, C. I. (2012) · Brain Research · doi:10.1016/j.brainres.2011.11.019 · Cited by 32 · see citing works
Porta, S., Kwong, L. K., Trojanowski, J. Q., & Lee, V. M. ‐. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000182 · Cited by 32 · see citing works
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Petegnief, V., & Planas, A. M. (2013) · Translational Stroke Research · doi:10.1007/s12975-013-0277-y · Cited by 31 · see citing works
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Cragnaz, L., Klima, R., Skoko, N., Budini, M., Feiguin, F. M., & Baralle, F. E. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.07.009 · Cited by 29 · see citing works
Franco, J. G., de Moura, E. G., Koury, J. C., Trotta, P. A., Cordeiro, A., Souza, L. L., Almeida, N. A. D. S., Lima, N. D. S., Pazos-Moura, C. C., Lisboa, P. C., et al. (2010) · Journal of Endocrinology · doi:10.1677/joe-10-0124 · Cited by 26 · see citing works
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Knippenberg, S., Sipos, J., Thau‐Habermann, N., Körner, S., Rath, K. J., Dengler, R., & Petri, S. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000004 · Cited by 25 · see citing works
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Chen, L., Smith, A. P., Ben, Y., Zukic, B., Ignacio, S., Moore, D. H., & Lee, N. M. (2004) · Amyotrophic Lateral Sclerosis and Other Motor Neuron Disorders · doi:10.1080/14660820410017091 · Cited by 25 · see citing works
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Sirtuins as therapeutic targets of ALS
Pasinetti, G. M., Bilski, A. E., & Zhao, W. (2013) · Cell Research · doi:10.1038/cr.2013.94 · Cited by 22 · see citing works
Mutant SOD1 Increases APP Expression and Phosphorylation in Cellular and Animal Models of ALS
Rabinovich‐Toidman, P., Rabinovich-Nikitin, I., Ezra, A., Barbiro, B., Fogel, H., Slutsky, I., & Solomon, B. (2015) · PLoS ONE · doi:10.1371/journal.pone.0143420 · Cited by 22 · see citing works
Age-related Changes in Tau Expression in Transgenic Mouse Model of Amyotrophic Lateral Sclerosis
Barańczyk‐Kuźma, A., Usarek, E., Kuźma‐Kozakiewicz, M., Kaźmierczak, B., Gajewska, B., Schwalenstöcker, B., & Ludolph, A. C. (2007) · Neurochemical Research · doi:10.1007/s11064-006-9242-4 · Cited by 11 · see citing works
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Research works printed but not linked: 1
- Fecto F, Yan J, Vemula SP, Liu E, Yang Y, Chen W, Zheng JG, Shi Y, Siddique N, Arrat H, Donkervoort S, Ajroud-Driss S, Sufit RL, Heller SL, Deng HX, Siddique T (2011) SQSTM1 mutations in familial and sporadic amyotrophic lateral sclerosis. Arch Neurol 68:1440–1446 [DOI] [PubMed] [Google Scholar]
Cited by
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- Authors
- Tang, B. L.
- Affiliations
- National University of Singapore (SG)
- Corresponding author
- Tang, Bor Luen
- ORCID
- Tang, Bor Luen
- Venue
- Cellular and Molecular Neurobiology
- Published
- 2016-12-10
- Volume
- 37
- Issue
- 7
- Pages
- 1147-1160
- ISSN
- 0272-4340 (ISSN-L)
- 1573-6830
- PMC
- PMC11482121
- OpenAlex
- W2560651871
- Cited by
- 24
- References
- 201
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 4 · 2022: 3 · 2021: 2 · 2020: 5 · 2019: 2 · 2018: 1 · 2017: 4
- FWCI
- 0.32
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Cellular and Molecular Neurobiology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National University of Singapore (C-183-000-102-091)
- Topics
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Keywords
- amyotrophic lateral sclerosis, sirtuins, disease-modifying therapy, neuroprotection, SOD1 mutations, TDP-43, FUS, C9orf72
- MeSH terms
- Superoxide Dismutase-1, Amyotrophic Lateral Sclerosis, Animals, Humans, Motor Neurons, Disease Progression, Sirtuins
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