SIRT1 Protects against Microglia-dependent Amyloid-β Toxicity through Inhibiting NF-κB Signaling

THE NF-κB AND IκB PROTEINS: New Discoveries and Insights

Baldwin, A. S. (1996) · Annual Review of Immunology · doi:10.1146/annurev.immunol.14.1.649 · Cited by 5,882

Inflammation and Alzheimer’s disease

Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514

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

Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase

Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., & Mayo, M. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600244 · Cited by 2,750

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 2,690

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

RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease

Yan, S. D., Chen, X., Fu, J., Chen, M., Zhu, H., Roher, A., Slattery, T., Zhao, L., Nagashima, M., Morser, J., et al. (1996) · Nature · doi:10.1038/382685a0 · Cited by 2,012

Germline Transmission and Tissue-Specific Expression of Transgenes Delivered by Lentiviral Vectors

Lois, C., Hong, E. J., Pease, S., Brown, E. J., & Baltimore, D. (2002) · Science · doi:10.1126/science.1067081 · Cited by 1,992

Control of IκB-α Proteolysis by Site-Specific, Signal-Induced Phosphorylation

Brown, K., Gerstberger, S., Carlson, L., Franzoso, G., & Siebenlist, U. (1995) · Science · doi:10.1126/science.7878466 · Cited by 1,434

Mammalian SIRT1 Represses Forkhead Transcription Factors

Motta, M. C., Divecha, N., Lemieux, M. E., Kamel, C., Chen, D., Gu, W. J., Bultsma, Y., McBurney, M. W., & Guarente, L. (2004) · Cell · doi:10.1016/s0092-8674(04)00126-6 · Cited by 1,366

Impact of neural stem cell-derived extracellular vesicles on mitochondrial dysfunction, sirtuin 1 level, and synaptic deficits in Alzheimer’s disease

Li, B., Liu, J., Gu, G., Han, X., Zhang, Q., & Zhang, W. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15001 · Cited by 110

Age-associated decrease of SIRT1 expression in rat hippocampus

Quintas, A., de Solís, A. J., Díez-Guerra, F. J., Carrascosa, J. M., & Bogónez, E. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2011.11.010 · Cited by 110

Microglia and inflammation: conspiracy, controversy or control?

Fernandes, A., Miller-Fleming, L., & Pais, T. F. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1670-8 · Cited by 103

ADDLs and the signaling web that leads to Alzheimer’s disease

Krafft, G. A., & Klein, W. L. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.07.012 · Cited by 113

Sirtuins, resveratrol and the intertwining cellular pathways connecting them

Ungurianu, A., Zanfirescu, A., & Margina, D. M. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101936 · Cited by 114

Caloric restriction blocks neuropathology and motor deficits in Machado-Joseph disease mouse models through SIRT1 pathway

Cunha-Santos, J., Duarte-Neves, J., Carmona, V., Guarente, L., Pereira de Almeida, L., & Cavadas, C. (2016) · Nature Communications · doi:10.1038/ncomms11445 · Cited by 109

Sirtuins in Neuroendocrine Regulation and Neurological Diseases

Fujita, Y., & Yamashita, T. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00778 · Cited by 110

Icariin enhances neuronal survival after oxygen and glucose deprivation by increasing SIRT1

Wang, L., Zhang, L., Chen, Z., Wu, J., Zhang, X., & Xu, Y. (2009) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2009.03.033 · Cited by 108

Microglia Polarization in Alzheimer’s Disease: Mechanisms and a Potential Therapeutic Target

Wang, Q., Yao, H., Liu, W., Ya, B., Cheng, H., Xing, Z., & Wu, Y. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.772717 · Cited by 111

Design and synthesis of compounds that extend yeast replicative lifespan

Yang, H., Baur, J. A., Chen, A. Y., Miller, C. M., & Sinclair, D. A. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00259.x · Cited by 108

Reactive Oxygen Species, Redox Signaling and Neuroinflammation in Alzheimer's Disease: The NF-κB Connection

Kaur, U., Banerjee, P., Bir, A., Sinha, M. S., Biswas, A., & Chakrabarti, S. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150114160543 · Cited by 108

Role of dietary fatty acids in microglial polarization in Alzheimer’s disease

Desale, S. E., & Chinnathambi, S. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01742-3 · Cited by 112

Evaluation of potential pro‐survival pathways regulated by melatonin in a murine senescence model

Cuesta, J., Tajes, M., Jiménez, A., Coto‐Montes, A. M., Camins, A., & Pallàs, M. (2008) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2008.00626.x · Cited by 104

Microglial Activation in Alzheimers Disease

Schlachetzki, J. C. M., & Hüll, M. (2009) · Current Alzheimer Research · doi:10.2174/156720509790147179 · Cited by 105

Sirtuin 1 attenuates oxidative stress via upregulation of superoxide dismutase 2 and catalase in astrocytes

Cheng, Y., Takeuchi, H., Sonobe, Y., Jin, S., Wang, Y., Horiuchi, H., Parajuli, B., Kawanokuchi, J., Mizuno, T., & Suzumura, A. (2014) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2014.02.001 · Cited by 102

Sirt1 inhibition promotes in vivo arterial thrombosis and tissue factor expression in stimulated cells

Breitenstein, A., Stein, S., Holy, E. W., Camici, G. G., Lohmann, C., Akhmedov, A., Spescha, R. D., Elliott, P. J., Westphal, C. H., Matter, C. M., et al. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq339 · Cited by 106

Emerging roles of SIRT1 activator, SRT2104, in disease treatment

Chang, N., Li, J., Lin, S., Zhang, J., Zeng, W.-Q., Ma, G., & Wang, Y. (2024) · Scientific Reports · doi:10.1038/s41598-024-55923-8 · Cited by 107

Interactions between Sirt1 and MAPKs regulate astrocyte activation induced by brain injury in vitro and in vivo

Li, D., Liu, N., Zhao, H., Zhang, X., Kawano, H., Liu, L., Zhao, L., & Li, H.-P. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-017-0841-6 · Cited by 102

Anti‐aging properties of melatonin in an in vitro murine senescence model: involvement of the sirtuin 1 pathway

Tajes, M., Gutierrez‐Cuesta, J., Ortuño‐Sahagún, D., Camins, A., & Pallàs, M. (2009) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2009.00706.x · Cited by 100

AMPK and SIRT1 activation contribute to inhibition of neuroinflammation by thymoquinone in BV2 microglia

Velagapudi, R., El‐Bakoush, A., Lepiarz‐Raba, I., Ogunrinade, F., & Olajide, O. A. (2017) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-017-3064-3 · Cited by 99

Reversal of aging by NFκB blockade

Adler, A. S., Kawahara, T. L. A., Segal, E., & Chang, H. Y. (2008) · Cell Cycle · doi:10.4161/cc.7.5.5490 · Cited by 103

Molecular Bases of Caloric Restriction Regulation of Neuronal Synaptic Plasticity

Fontán‐Lozano, Á., López‐Lluch, G., Delgado-Garcia, J. M., Navas, P., & Carrión, Á. M. (2008) · Molecular Neurobiology · doi:10.1007/s12035-008-8040-1 · Cited by 104

Analysis of sirtuin 1 expression reveals a molecular explanation of IL-2-mediated reversal of T-cell tolerance

Gao, B., Kong, Q., Kemp, K., Zhao, Y.-S., & Fang, D. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118462109 · Cited by 98

The acetylation of RelA in Lys310 dictates the NF-κB-dependent response in post-ischemic injury

Lanzillotta, A., Sarnico, I., Ingrassia, R., Boroni, F., Branca, C., Benarese, M., Faraco, G., Blasi, F., Chiarugi, A., Spano, P., et al. (2010) · Cell Death and Disease · doi:10.1038/cddis.2010.76 · Cited by 98

Strong cardioprotective effect of resveratrol, a red wine polyphenol, on isolated rat hearts after ischemia/reperfusion injury

Mokni, M., Limam, F., Elkahoui, S., Amri, M., & Aouani, E. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.10.015 · Cited by 97

Targeting tissue oxidative damage by means of cell signaling modulators: The antioxidant concept revisited

Leonarduzzi, G., Sottero, B., & Poli, G. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.08.003 · Cited by 100

Chapter 24 NF‐KappaB Dimers in the Regulation of Neuronal Survival

Sarnico, I., Lanzillotta, A., Benarese, M., Alghisi, M., Baiguera, C., Battistin, L., Spano, P., & Pizzi, M. (2009) · International review of neurobiology · doi:10.1016/s0074-7742(09)85024-1 · Cited by 97

Review of the anti-inflammatory effect of SIRT1 and SIRT2 modulators on neurodegenerative diseases

Zhang, Y., Anoopkumar‐Dukie, S., Arora, D. S., & Davey, A. K. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172847 · Cited by 95

Control of Inflammation by Calorie Restriction Mimetics: On the Crossroad of Autophagy and Mitochondria

Gabandé‐Rodríguez, E., Heras, M. M. G. D. L., & Mittelbrunn, M. (2019) · Cells · doi:10.3390/cells9010082 · Cited by 101

Inhibition of transcriptional activity of c-JUN by SIRT1

Gao, Z., & Ye, J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.09.079 · Cited by 95

Therapeutic effects of resveratrol during acute periods following experimental ischemic stroke

Shin, J. A., Lee, H.-A., Lim, Y.-K., Koh, Y., Choi, J. H., & Park, E. (2010) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2010.06.017 · Cited by 95

Sirtuins as Important Factors in Pathological States and the Role of Their Molecular Activity Modulators

Kratz, E. M., Sołkiewicz, K., Kubis-Kubiak, A., & Piwowar, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020630 · Cited by 97

Comparative analysis of the effects of resveratrol in two apoptotic models: Inhibition of complex I and potassium deprivation in cerebellar neurons

Alvira, D., Yeste‐Velasco, M., Folch, J., Verdaguer, E., Canudas, A. M., Pallàs, M., & Camins, A. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.04.029 · Cited by 96

Anti-amyloid Aggregation Activity of Natural Compounds: Implications for Alzheimer’s Drug Discovery

Bu, X., Rao, P. P. N., & Wang, Y. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9301-4 · Cited by 97

Immunotoxins Constructed with Ribosome-Inactivating Proteins and their Enhancers: A Lethal Cocktail with Tumor Specific Efficacy

Gilabert‐Oriol, R., Weng, A., von Mallinckrodt, B., Melzig, M. F., Fuchs, H., & Thakur, M. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140826153913 · Cited by 92

Chronic Silymarin, Quercetin and Naringenin Treatments Increase Monoamines Synthesis and Hippocampal Sirt1 Levels Improving Cognition in Aged Rats

Sarubbo, F., Ramis, M. R., Kienzer, C., Aparicio, S., Esteban, S., Miralles, A., & Moranta, D. (2017) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-017-9759-0 · Cited by 95

NF-κB in Innate Neuroprotection and Age-Related Neurodegenerative Diseases

Lanzillotta, A., Porrini, V., Bellucci, A., Benarese, M., Branca, C., Parrella, E., Spano, P., & Pizzi, M. (2015) · Frontiers in Neurology · doi:10.3389/fneur.2015.00098 · Cited by 92

Specific Plasma Membrane Binding Sites for Polyphenols, Including Resveratrol, in the Rat Brain

Han, Y.-S., Bastianetto, S., Dumont, Y., & Quirion, R. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.102319 · Cited by 92

Activation of Nrf2 Pathway Contributes to Neuroprotection by the Dietary Flavonoid Tiliroside

Velagapudi, R., El-Bakoush, A., & Olajide, O. A. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0975-2 · Cited by 91

Brain Activation of SIRT1: Role in Neuropathology

Paraíso, A. F., Mendes, K. L., & Santos, S. H. S. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8459-x · Cited by 91

Research Progress on Alzheimer's Disease and Resveratrol

Yan, Y., Yang, H., Xie, Y., Ding, Y., Kong, D., & Yu, H. (2020) · Neurochemical Research · doi:10.1007/s11064-020-03007-0 · Cited by 93

Intercellular interplay between Sirt1 signalling and cell metabolism in immune cell biology

Chen, X., Lu, Y., Zhang, Z., Wang, J., Yang, H., & Liu, G. (2015) · Immunology · doi:10.1111/imm.12473 · Cited by 91

Melatonin reverses H2O2‐induced senescence in SH ‐ SY 5Y cells by enhancing autophagy via sirtuin 1 deacetylation of the RelA/p65 subunit of NF ‐κB

Nopparat, C., Sinjanakhom, P., & Govitrapong, P. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12407 · Cited by 89

Pre-B cell colony enhancing factor (PBEF), a cytokine with multiple physiological functions

Sun, Z., Lei, H., & Zhang, Z. (2013) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2013.05.006 · Cited by 91

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

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

Dietary Polyphenols: A Multifactorial Strategy to Target Alzheimer’s Disease

Dhakal, S., Kushairi, N., Phan, C., Adhikari, B., Sabaratnam, V., & Macreadie, I. G. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20205090 · Cited by 92

Sirtuin 1 activator SRT1720 suppresses inflammation in an ovalbumin‐induced mouse model of asthma

Ichikawa, T., Hayashi, R., Suzuki, K., Imanishi, S., Kambara, K., Okazawa, S., Inomata, M., YAMADA, T., YAMAZAKI, Y., Koshimizu, Y., et al. (2012) · Respirology · doi:10.1111/j.1440-1843.2012.02284.x · Cited by 88

Sirtuins: from metabolic regulation to brain aging

Duan, W. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00036 · Cited by 89

Sirt2 suppresses inflammatory responses in collagen-induced arthritis

Lin, J., Sun, B., Jiang, C., Hong, H., & Zheng, Y. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.10.153 · Cited by 90

Current Perspectives on Role of Chromatin Modifications and Deacetylases in Lung Inflammation in COPD

Rajendrasozhan, S., Yao, H., & Rahman, I. (2009) · COPD Journal of Chronic Obstructive Pulmonary Disease · doi:10.1080/15412550903049132 · Cited by 86

Sirtuins in Alzheimer’s Disease: SIRT2-Related GenoPhenotypes and Implications for PharmacoEpiGenetics

Cacabelos, R., Carril, J. C., Cacabelos, N., Kazantsev, A. G., Vostrov, A. A., Corzo, L., Cacabelos, P., & Goldgaber, D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20051249 · Cited by 87

Ginsenoside Rg1 ameliorates chronic social defeat stress-induced depressive-like behaviors and hippocampal neuroinflammation

Jiang, N., Lv, J., Wang, H., Huang, H. M., Wang, Q., Lü, C., Zeng, G., & Liu, X. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117669 · Cited by 86

Neuron-Glia Interactions as Therapeutic Targets in Neurodegeneration

Salmina, A. B. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0988 · Cited by 88

Valproic Acid Alleviates Memory Deficits and Attenuates Amyloid-β Deposition in Transgenic Mouse Model of Alzheimer’s Disease

Xuan, A., Xue-bing, P., Wei, P., Ji, W., Zhang, W.-J., Liu, J., Hong, L.-P., Chen, W., & Long, D. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8751-4 · Cited by 91

Effects of resveratrol and its derivatives on lipopolysaccharide-induced microglial activation and their structure–activity relationships

Meng, X., Yang, J., Chen, G., Wang, L., Zhang, L., Wang, S., Li, J., & Wu, C. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.04.015 · Cited by 87

Sirtuin 1 and Alzheimer's disease: An up-to-date review

Rizzi, L., & Roriz‐Cruz, M. (2018) · Neuropeptides · doi:10.1016/j.npep.2018.07.001 · Cited by 84

Dietary nutrition for neurological disease therapy: Current status and future directions

Mao, X., Yin, X., Guan, Q.-W., Xia, Q., Yang, N., Zhou, H., Liu, Z., & Jin, W. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107861 · Cited by 85

Oxygen metabolism abnormality and Alzheimer's disease: An update

Liu, G., Yang, C., Wang, X., Chen, X., Wang, Y., & Le, W. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102955 · Cited by 87

Cellular Links between Neuronal Activity and Energy Homeostasis

Shetty, P. K., Galeffi, F., & Turner, D. A. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00043 · Cited by 81

Apoptosis of oligodendrocytes in the central nervous system results in rapid focal demyelination

Caprariello, A. V., Mangla, S., Miller, R. H., & Selkirk, S. M. (2012) · Annals of Neurology · doi:10.1002/ana.23606 · Cited by 87

1,4-Dihydropyridines Active on the SIRT1/AMPK Pathway Ameliorate Skin Repair and Mitochondrial Function and Exhibit Inhibition of Proliferation in Cancer Cells

Valente, S., Mellini, P., Spallotta, F., Carafa, V., Nebbioso, A., Polletta, L., Carnevale, I., Saladini, S., Trisciuoglio, D., Gabellini, C., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01117 · Cited by 80

Epigenetic regulation of BACE1 in Alzheimer’s disease patients and in transgenic mice

Marques, S., Lemos, R., Ferreiro, E. B., Martins, M., de Mendonça, A., Santana, I. J., Outeiro, T. F., & Pereira, C. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.06.029 · Cited by 84

Roles of NAD / NADH and NADP+ / NADPH in Cell Death

Xia, W., Wang, Z., Wang, Q., Han, J., Zhao, C., Hong, Y., Zeng, L., Tang, L., & Ying, W. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209787185832 · Cited by 82

Resveratrol Boosts Cognitive Function by Targeting SIRT1

Cao, W., Dou, Y., & Li, A. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2586-8 · Cited by 80

Sirt1 interacts with transducin-like enhancer of split-1 to inhibit nuclear factor κB-mediated transcription

Ghosh, H. S., Spencer, J. V., Ng, B. G., McBurney, M. W., & Robbins, P. D. (2007) · Biochemical Journal · doi:10.1042/bj20070817 · Cited by 84

Selective targeting of microglia by quantum dots

Minami, S., Sun, B., Popat, K. C., Kauppinen, T. M., Pleiss, M., Zhou, Y., Ward, M. E., Floreancig, P. E., Mucke, L., Desai, T. A., et al. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-22 · Cited by 79

IKK2/NF‐κB signaling protects neurons after traumatic brain injury

Mettang, M., Reichel, S. N., Lattke, M., Palmer, A., Abaei, A., Rasche, V., Huber-Lang, M. S., Baumann, B., & Wirth, T. (2017) · The FASEB Journal · doi:10.1096/fj.201700826r · Cited by 78

Sirt1 ameliorates monosodium urate crystal–induced inflammation by altering macrophage polarization via the PI3K/Akt/STAT6 pathway

Liu, L., Zhu, X., Zhao, T., Yu, Y., Xue, Y., & Zou, H. (2019) · Lara D. Veeken · doi:10.1093/rheumatology/kez165 · Cited by 79

Neuroprotection by Histone Deacetylase-7 (HDAC7) Occurs by Inhibition of c-jun Expression through a Deacetylase-independent Mechanism

Ma, C., & D’Mello, S. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.146860 · Cited by 83

Sirtuins in cognitive ageing and Alzheimer's disease

Braidy, N., Jayasena, T., Poljak, A., & Sachdev, P. S. (2012) · Current Opinion in Psychiatry · doi:10.1097/yco.0b013e32835112c1 · Cited by 81

Microglial CX3CR1 promotes adult neurogenesis by inhibiting Sirt 1/p65 signaling independent of CX3CL1

Sellner, S., Paricio-Montesinos, R., Spieß, A., Masuch, A., Erny, D., Harsan, L. A., von Elverfeldt, D., Schwabenland, M., Biber, K. P. H., Staszewski, O., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0374-8 · Cited by 82

Histone Deacetylase Inhibitors and Neurodegenerative Disorders: Holding the Promise

Mai, A., Rotili, D., Valente, S., & Kazantsev, A. G. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209789649349 · Cited by 79

Dietary polyphenols and neurogenesis: Molecular interactions and implication for brain ageing and cognition

Sarubbo, F., Moranta, D., & Pani, G. (2018) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2018.05.011 · Cited by 77

Sporadic inclusion-body myositis: Conformational multifactorial ageing-related degenerative muscle disease associated with proteasomal and lysosomal inhibition, endoplasmic reticulum stress, and accumulation of amyloid-β42 oligomers and phosphorylated tau

Askanas, V., & Engel, W. K. (2011) · La Presse Médicale · doi:10.1016/j.lpm.2010.11.024 · Cited by 78

HIV TAT-mediated microglial senescence: Role of SIRT3-dependent mitochondrial oxidative stress

Thangaraj, A., Chivero, E. T., Tripathi, A., Singh, S., Niu, F., Guo, M.-L., Pillai, P., Periyasamy, P., & Buch, S. (2021) · Redox Biology · doi:10.1016/j.redox.2020.101843 · Cited by 76

Involvement of AMP‐activated protein kinase in neuroinflammation and neurodegeneration in the adult and developing brain

Saito, M., Saito, M., & Das, B. C. (2019) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2019.01.007 · Cited by 75

The Stemness of Human Ovarian Granulosa Cells and the Role of Resveratrol in the Differentiation of MSCs—A Review Based on Cellular and Molecular Knowledge

Józkowiak, M., Hutchings, G., Jankowski, M., Kulcenty, K. I., Mozdziak, P. E., Kempisty, B., Spaczyński, R., & Piotrowska‐Kempisty, H. (2020) · Cells · doi:10.3390/cells9061418 · Cited by 74

Curcuminoids and resveratrol as anti-Alzheimer agents

Villaflores, O. B., Chen, Y., Chen, C., Yeh, J., & Wu, T. (2012) · Taiwanese Journal of Obstetrics and Gynecology · doi:10.1016/j.tjog.2012.09.005 · Cited by 79

Review: NAD + : A modulator of immune functions

Grahnert, A., Grahnert, A., Klein, C., Schilling, E., Wehrhahn, J., & Hauschildt, S. (2010) · Innate Immunity · doi:10.1177/1753425910361989 · Cited by 78

SIRT3 protects cells from hypoxia via PGC-1α- and MnSOD-dependent pathways

Wang, Q., Li, L., Li, C. Y., Pei, Z., Zhou, M., & Li, N. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.11.045 · Cited by 77

Flavonoids-mediated SIRT1 signaling activation in hepatic disorders

Sayed, A. M. M., Hassanein, E. H. M., Salem, S. H., Hussein, O. E., & Mahmoud, A. M. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118173 · Cited by 77

Hippocampal Neurogenesis in Alzheimer's Disease: Is There a Role for Dietary Modulation?

Maruszak, A., Pilarski, A. M., Murphy, T., Branch, N., & Thuret, S. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-131004 · Cited by 78

Can changes in histone acetylation contribute to memory formation?

López‐Atalaya, J. P., & Barco, Á. (2014) · Trends in Genetics · doi:10.1016/j.tig.2014.09.003 · Cited by 79

SIRT1 facilitates amyloid beta peptide degradation by upregulating lysosome number in primary astrocytes

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Tripchlorolide protects neuronal cells from microglia‐mediated β‐amyloid neurotoxicity through inhibiting NF‐κB and JNK signaling

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β-Amyloid Stimulation of Microglia and Monocytes Results in TNFα-Dependent Expression of Inducible Nitric Oxide Synthase and Neuronal Apoptosis

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