Differential sirtuin expression patterns in amyotrophic lateral sclerosis (ALS) postmortem tissue: neuroprotective or neurotoxic properties of sirtuins in ALS?

Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase

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Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1

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The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms

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Negative Control of p53 by Sir2α Promotes Cell Survival under Stress

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Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase

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A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy

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Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins

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Sir2 mediates longevity in the fly through a pathway related to calorie restriction

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Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

Cheng, H.-L., Mostoslavsky, R., Saito, S., Manis, J. P., Gu, Y., Patel, P., Bronson, R., Appella, E., Alt, F. W., & Chua, K. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934713100 · Cited by 1,095 · see citing works

SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis

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Sirtuin 2 Inhibitors Rescue α-Synuclein-Mediated Toxicity in Models of Parkinson's Disease

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Nucleocytoplasmic Shuttling of the NAD+-dependent Histone Deacetylase SIRT1*

Tanno, M., Sakamoto, J., Miura, T., Shimamoto, K., & Horio, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609554200 · Cited by 784 · see citing works

Therapeutic application of histone deacetylase inhibitors for central nervous system disorders

Kazantsev, A. G., & Thompson, L. M. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2681 · Cited by 715 · see citing works

Current hypotheses for the underlying biology of amyotrophic lateral sclerosis

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Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons

Parker, J. A., Arango-Lievano, M., Abderrahmane, S., Lambert, E., Tourette, C., Catoire, H., & Néri, C. (2005) · Nature Genetics · doi:10.1038/ng1534 · Cited by 509 · see citing works

Role for Human SIRT2 NAD-Dependent Deacetylase Activity in Control of Mitotic Exit in the Cell Cycle

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Sirtuin 1 Reduction Parallels the Accumulation of Tau in Alzheimer Disease

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Sirtuins: The ‘ <i>magnificent seven</i> ’, function, metabolism and longevity

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Sodium phenylbutyrate prolongs survival and regulates expression of anti-apoptotic genes in transgenic amyotrophic lateral sclerosis mice

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Distribution of histone deacetylases 1–11 in the rat brain

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SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

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SirT1 inhibition reduces IGF-I/IRS-2/Ras/ERK1/2 signaling and protects neurons

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Differential expression of inflammation‐ and apoptosis‐related genes in spinal cords of a mutant SOD1 transgenic mouse model of familial amyotrophic lateral sclerosis

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Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington’s disease

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Sirtuin 2, a Mammalian Homolog of Yeast Silent Information Regulator-2 Longevity Regulator, Is an Oligodendroglial Protein That Decelerates Cell Differentiation through Deacetylating α-Tubulin

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Mammalian SIRT1 limits replicative life span in response to chronic genotoxic stress

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The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility

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Opposing Effects of Sirtuins on Neuronal Survival: SIRT1-Mediated Neuroprotection Is Independent of Its Deacetylase Activity

Pfister, J. A., Ma, C., Morrison, B. E., & D’Mello, S. R. (2008) · PLoS ONE · doi:10.1371/journal.pone.0004090 · Cited by 176 · see citing works

Paths of Convergence: Sirtuins in Aging and Neurodegeneration

Gan, L., & Mucke, L. (2008) · Neuron · doi:10.1016/j.neuron.2008.03.015 · Cited by 173 · see citing works

Additive neuroprotective effects of a histone deacetylase inhibitor and a catalytic antioxidant in a transgenic mouse model of amyotrophic lateral sclerosis

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Microtubule Deacetylases, SirT2 and HDAC6, in the Nervous System

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Differential Histone Deacetylase mRNA Expression Patterns in Amyotrophic Lateral Sclerosis

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Distribution of GABAAReceptor mRNA in the Motor Cortex of ALS Patients

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An in vitro screening cascade to identify neuroprotective antioxidants in ALS

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Distribution of GABAA receptor subunit mRNAs in rat lumbar spinal cord

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Differentially expressed genes in sporadic amyotrophic lateral sclerosis spinal cords – screening by molecular indexing and subsequent cDNA microarray analysis

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Sirtuin inhibition protects from the polyalanine muscular dystrophy protein PABPN1

Catoire, H., Pasco, M. Y., Abu‐Baker, A., Holbert, S., Tourette, C., Brais, B., Rouleau, G. A., Parker, J. A., & Néri, C. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn109 · Cited by 60 · see citing works

Histone Deacetylation and Motor Neuron Degeneration

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NAD+ in Brain Aging and Neurodegenerative Disorders

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Axonal Degeneration during Aging and Its Functional Role in Neurodegenerative Disorders

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Histone deacetylases (HDACs) and brain function

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Efficacy and tolerability of EH301 for amyotrophic lateral sclerosis: a randomized, double-blind, placebo-controlled human pilot study

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The role of altered protein acetylation in neurodegenerative disease

Kabir, F., Atkinson, R., Cook, A. L., Phipps, A. J., & King, A. E. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1025473 · Cited by 75 · see citing works

Could sirtuin activities modify ALS onset and progression?

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Insight into the Mechanism of Intramolecular Inhibition of the Catalytic Activity of Sirtuin 2 (SIRT2)

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Emerging Role of Sirtuin 2 in the Regulation of Mammalian Metabolism

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Sirtuins as Potential Drug Targets for Metabolic Diseases

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Sirtuins 1 and 2 Are Universal Histone Deacetylases

Hsu, W. W., Wu, B., & Liu, W. R. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00886 · Cited by 56 · see citing works

Effect of Nutritional Stress on the Expression of Sirtuin Gene Family

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