Cited by 1,065Sirtuins and Resveratrol in MedicineHistone Deacetylase Inhibitors ResearchBiochemical and Molecular Research

The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.

Mechanism of Human SIRT1 Activation by Resveratrol

Open access

Borra, Margie T., Smith, Brian C., Denu, John M.·2005·Journal of Biological Chemistry

DOI 10.1074/jbc.m501250200

Open this paper in CoChat — free account Open PDF

Abstract

The NAD+-dependent protein deacetylase family, Sir2 (or sirtuins), is important for many cellular processes including gene silencing, regulation of p53, fatty acid metabolism, cell cycle regulation, and life span extension. Resveratrol, a polyphenol found in wines and thought to harbor major health benefits, was reported to be an activator of Sir2 enzymes in vivo and in vitro. In addition, resveratrol was shown to increase life span in three model organisms through a Sir2-dependent pathway. Here, we investigated the molecular basis for Sir2 activation by resveratrol. Among the three enzymes tested (yeast Sir2, human SIRT1, and human SIRT2), only SIRT1 exhibited significant enzyme activation ( approximately 8-fold) using the commercially available Fluor de Lys kit (BioMol). To examine the requirements for resveratrol activation of SIRT1, we synthesized three p53 acetylpeptide substrates either lacking a fluorophore or containing a 7-amino-4-methylcoumarin (p53-AMC) or rhodamine 110 (p53-R110). Although SIRT1 activation was independent of the acetylpeptide sequence, resveratrol activation was completely dependent on the presence of a covalently attached fluorophore. Substrate competition studies indicated that the fluorophore decreased the binding affinity of the peptide, and, in the presence of resveratrol, fluorophore-containing substrates bound more tightly to SIRT1. Using available crystal structures, a model of SIRT1 bound to p53-AMC peptide was constructed. Without resveratrol, the coumarin of p53-AMC peptide is solvent-exposed and makes no significant contacts with SIRT1. We propose that binding of resveratrol to SIRT1 promotes a conformational change that better accommodates the attached coumarin group.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1074/jbc.m501250200

Cites

68 of 68 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modeling
Guex, N., & Peitsch, M. C. (1997) · Electrophoresis · doi:10.1002/elps.1150181505 · Cited by 11,297
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
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
Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239
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
The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253
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
Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ
Picard, F., Kurtev, M. V., Chung, N., Topark‐Ngarm, A., Senawong, T., de Oliveira, R. M., Leid, M. E., McBurney, M. W., & Guarente, L. (2004) · Nature · doi:10.1038/nature02583 · Cited by 1,943
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

Flagged first, then by citations

Show all 68 references

Research works printed but not linked: 2

Aggarwal, 2004, Anticancer Res., 24, 2783
Gescher, 2003, Cancer Epidemiol. Biomarkers Prev., 12, 953

Sorted by citations

Items 901–1,000 of 1,000

Epigenetics and Nutrition
Raganelli, A. (2018) · MOJ Food Processing & Technology · doi:10.15406/mojfpt.2018.06.00141 · Cited by 1
Comparison of apoptosis between bovine subcutaneous and intramuscular adipocytes by resveratrol via SIRT1
Zhang, X., Wan, F., You, W., Tan, X., Liu, G., Jin, Q., Wei, C., Liu, X., Zhao, H., Liu, Y., et al. (2019) · Animal Biotechnology · doi:10.1080/10495398.2019.1636808 · Cited by 2
Introduction
Obulesu, M. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816412-9.00001-x · Cited by 3
Diet and Epigenetics: Dietary Effects on DNA Methylation, Histone Remodeling and mRNA Stability
Fratantonio, D., Virgili, F., & Benassi, B. (2020) · Elsevier eBooks · doi:10.1016/b978-0-08-100596-5.22721-2 · Cited by 2
Periodontology - New Insights
Sridharan, G. (2022) · Dentistry · doi:10.5772/intechopen.100796 · Cited by 2
Le resvératrol en complément thérapeutique : une piste pour la prévention du diabète de type 2 ?
Sérée, E., Burcelin, R., & Savouret, J. (2009) · Médecine des Maladies Métaboliques · doi:10.1016/s1957-2557(09)73295-x · Cited by 2
One feature doesn't fit all
Chua, H. E., Bhowmick, S. S., & Tucker‐Kellogg, L. (2014) · ACM International Conference on Bioinformatics, Computational Biology, and Health Informatics (ACM-BCB) · doi:10.1145/2649387.2649424 · Cited by 2
Aging Kidney: Modern Perspectives for an ‘Old’ Problem
Grosjean, F., Vlassara, H., & Striker, G. E. (2011) · Aging Health · doi:10.2217/ahe.11.63 · Cited by 2
Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis
Katen, A. L., & Roman, S. D. (2015) · Cited by 2
Epigenetic Mechanisms of Sirtuins in Dermatology
Lo, A., Serravallo, M., & Jagdeo, J. R. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800957-4.00008-4 · Cited by 3
Resveratrol Oligomers from the Stem Bark of Vatica mangachapoi
Yang, H., Song, X., Han, C., Chen, G., Wu, S., & Chen, W. (2018) · Chemistry of Natural Compounds · doi:10.1007/s10600-018-2528-3 · Cited by 2
Impact of resveratrol-containing peptide nanospheres on retinoblastoma cells
Su, F., Luan, G., Guo, M., & Wang, J. (2022) · Materials Express · doi:10.1166/mex.2022.2307 · Cited by 2
Computationally Driven Discovery and Characterization of SIRT3-Activating Compounds that Fully Recover Catalytic Activity under NAD + Depletion
Guan, X., Upadhyay, A., Dumpati, R. K., Munshi, S., Roy, S., Chall, S., Rahnamoun, A., Reverdy, C., Errasti, G., Delacroix, T., et al. (2024) · Physical Review X · doi:10.1103/physrevx.14.041019 · Cited by 2
Life-Extending Effect of Phytochemicals in Drosophila
Shin-Hae, L., & Min, K. (2015) · Healthy ageing and longevity · doi:10.1007/978-3-319-18326-8_10 · Cited by 2
Life Extension in the Short-Lived Fish Nothobranchius furzeri
Cellerino, A. (2009) · Humana Press eBooks · doi:10.1007/978-1-60327-507-1_10 · Cited by 2
Sirtuin Inhibitors and Activators
Rahnasto‐Rilla, M., Tyni, J., & Lahtela-Kakkonen, M. K. (2019) · Topics in medicinal chemistry · doi:10.1007/7355_2019_70 · Cited by 2
The bifunctional roles of sirtuins and their therapeutic potential in cancer
Lee, Y. T., Tan, Y. J., Mok, P. Y., Subramaniam, A. V., & Oon, C. E. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822467-0.00009-7 · Cited by 2
Beneficial Effects of Resveratrol on Neurological Disorders
Farooqui, A. A. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3804-5_7 · Cited by 2
Correction: Effects of Resveratrol and SIRT1 on PGC-1α Activity and Mitochondrial Biogenesis: A Reevaluation
Higashida, K., Kim, S. H., Jung, S. R., Asaka, M., Holloszy, J. O., & Han, D. (2014) · PLoS Biology · doi:10.1371/annotation/900c9397-eeb9-4d4e-9a05-ff18d657be79 · Cited by 2
Inosine ameliorates the effects of hemin induced oxidative stress in broilers
Seaman, C. (2007) · doi:10.33915/etd.4334 · Cited by 2
Metadichol® a Sirtuin Modulator for Anti-Aging TherapiesPreprint
Raghavan, P. R. (2023) · Research Square · doi:10.21203/rs.3.rs-3199226/v2 · Cited by 2
Molecular Nutritional Study on Prevention of Muscle Atrophy
Hirasaka, K. (2014) · Nippon Eiyo Shokuryo Gakkaishi · doi:10.4327/jsnfs.67.291 · Cited by 1
Harvesting Health: Phytochemicals in Cognitive Impairment Therapy
Jain, S., Mazumder, A., Das, S., Tyagi, P. K., & Chaitanya, M. (2024) · Central Nervous System Agents in Medicinal Chemistry · doi:10.2174/0118715249315826240603075900 · Cited by 1
Myosin inhibition enhances cardiomyocyte cell cycle activity through SIRT1-NFAT-mediated H3K9me3 modification
Jiang, R., Chen, J., Pei, L., Huang, S., Feng, M., Ouyang, Z., Yuan, M., Zhu, Y., Yao, S., He, F., et al. (2025) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2025.151504 · Cited by 1
Considerations of dietary bioactive compounds/postbiotics, foods, and cooking methods in stroke
Losso, J. N., & Losso, M. (2025) · Nutritional Neuroscience · doi:10.1080/1028415x.2025.2565310 · Cited by 1
Gestational fluoride exposure compromises ovarian function via SIRT1-ATF4 axis in female offspring
Gu, Y., Shi, Y., Wei, B., Zhao, Y., Huo, M., Zeng, L., Zhao, Z., Song, Y., Yu, X., Chen, Y., et al. (2026) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2026.119872 · Cited by 1
Full Transcriptome Analysis of the Liver of Rats Receiving the Complex of L-Carnitine and Resveratrol in the Composition of a Standard or Hypercaloric Diet
Вячеславович, Т. Н., Александрович, Ш. В., & Gmoshinski, I. V. (2025) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s1990750824601322 · Cited by 1
Chemical and Molecular Strategies in Restoring Autophagic Flux in TDP-43 Proteinopathy
Jamerlan, A., & Hulme, J. (2026) · Molecules · doi:10.3390/molecules31060924 · Cited by 1
Mitochondrial metabolic imbalance drives diploidization in mouse haploid embryonic stem cells via NADPH overload
Minin, G. D., Rüegg, A. B., Halter, K., Fuhrer, T., Kleele, T., Zamboni, N., & Wutz, A. (2026) · Nature Communications · doi:10.1038/s41467-026-70939-6 · Cited by 1
The Role of Nrf2 in SIRT1-Mediated RGC Neuroprotection in Traumatic Optic Neuropathy
O’Neill, N., Sarabu, N., Alhadi, S. A., Pham, J. C., Dine, K. E., Chaqour, B., Ross, A. G., & Shindler, K. S. (2026) · Translational Vision Science & Technology · doi:10.1167/tvst.15.7.2 · Cited by 1
Polydatin Alleviates APAP‐Induced Hepatotoxicity by Targeting C/EBPβ to Suppress the NLRP3 Inflammasome Signaling Pathway
Yang, T., Cb, W., Ding, Y., Zhang, W., Zheng, L., Li, Y., & Zhang, L. (2026) · iNew Medicine · doi:10.1002/inm3.70063 · Cited by 1
Still un-sirtuin
Osherovich, L. Z. (2012) · Science-Business eXchange · doi:10.1038/scibx.2012.170 · Cited by 1
Environnement périnatal : marques épigénétiques et déterminisme des maladies métaboliques de l’adulte. Preuves de concept
Portha, B., Fournier, A., Kioon, M. D. A., Mezger, V., & Movassat, J. (2013) · Cahiers de Nutrition et de Diététique · doi:10.1016/j.cnd.2013.07.002 · Cited by 2
Leucine and Resveratrol: Experimental Model of Sirtuin Pathway Activation
Bruckbauer, A., & Zemel, M. B. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1923-9_8 · Cited by 1
Resveratrol: A crossroad of enology and biomedicine
Nikolova, V. (2007) · Biomedical Reviews · doi:10.14748/bmr.v18.73 · Cited by 1
The Enzymology of SIR2 Proteins
Borra, M. T., & Denu, J. M. (2006) · Humana Press eBooks · doi:10.1385/1-59745-024-3:219 · Cited by 1
Self-citation
Elixir of immortality? Wine, resveratrol and sirtuins: an overview
Casey, D. (2012) · Journal of Wine Research · doi:10.1080/09571264.2012.690091 · Cited by 1
Screening und Charakterisierung von Protein‐modifizierenden Naturstoffen durch MALDI‐Massenspektrometrie bringen starke SIRT1‐ und p300‐Inhibitoren hervor
Holzhauser, S., Freiwald, A., Weise, C., Multhaup, G., Han, T., & Sauer, S. (2013) · Angewandte Chemie · doi:10.1002/ange.201207325 · Cited by 1
Hyperglycemia, Oxidative Stress, and Vascular Complications: Role of Epigenetic Mechanisms
Simo‐Cheyou, E. R., & Srivastava, A. K. (2013) · Springer eBooks · doi:10.1007/978-1-4614-9317-4_6 · Cited by 1
Cellular and Molecular Mechanisms of Resveratrol and Its Derivatives
Stuart, J. A., & Robb, E. L. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6968-1_3 · Cited by 1
Targeting FOXOs to slow aging
Martins, R., Dumas, K. J., & Lithgow, G. J. (2015) · Molecular inhibitors in targeted therapy · doi:10.1515/motth-2015-0003 · Cited by 1
Structural and Mechanistic Insights in Sirtuin Catalysis and Pharmacological Modulation
Moniot, S., You, W., & Steegborn, C. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813499-3.00005-8 · Cited by 1
Resveratrol Oligosaccharide Induces mRNA Expression for SIRT
Hamada, H., Shimoda, K., Saitoh, Y., Doi, S., Fujitaka, Y., Ono, T., Hamada, H., & Araki, M. (2018) · Natural Product Communications · doi:10.1177/1934578x1801300419 · Cited by 1
Use of phytochemicals for the treatment of insulin resistance–linked visceral and neurological disorders
Farooqui, A. A. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819603-8.00009-2 · Cited by 1
Neurodegenerative Diseases and Small Molecule Protein Chaperone Activator of Natural Origin
Dutta, N., Ghosh, S., & Pal, M. (2021) · Springer eBooks · doi:10.1007/978-981-15-8127-4_5 · Cited by 1
青蒿素模拟热量限制延长酵母寿命的双期响应模式全转录组谱解析
李, 思., 曾, 庆., 汪, 大., 吴, 明., & 高, 倩. (2015) · Scientia Sinica Vitae · doi:10.1360/zc2015-45-4-398
Stereochemistries of Mariannamides C and D, Two Lipohexapeptides, Isolated from Mariannaea elegans NBRC102301
Ishiuchi, K., Nagumo, A., Kawaguchi, M., Furuyashiki, H., Nakagawa, H., & Hirose, D. (2022) · Heterocycles · doi:10.3987/com-22-14728 · Cited by 1
Unexplained infertility: a fresh look at the old problem and the novel therapeutic options of its treatment
Yemeliyanova, M., Chan, M. K., Wong, M. B., & Klokol, D. (2024) · Obstetrics & Gynecology International Journal · doi:10.15406/ogij.2024.15.00726 · Cited by 1
Enzymology in drug discovery
Chowdhury, S., Kar, K., & Chakraborty, P. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-16013-4.00008-7 · Cited by 1
Biological Activities and Mechanisms of Actions of Bioactive Compounds (BACS) Identified in Pure and Ternary Blends of Cocoyam, Soya Bean and Bambara Groundnut Flour Using Gas Chromatography-Mass Spectrometry (GC-MS) Technique: A Review
Uro-Chukwu, H., Uro-Chukwu, F. C., & Uro-Chukwu, F. C. (2025) · Journal of Drug Delivery and Therapeutics · doi:10.22270/jddt.v15i1.6973 · Cited by 2
THE PHARMACOLOGICAL EFFECT OF STILBENES ISOLATED FROM KANGAROO ISLAND PROPOLIS ON SIRT-1 ENZYME ACTIVITY
Abu-Mellal, A., Ahmed, A. S., Tran, V. H., & Duke, C. C. (2016) · International Journal of Pharmacy and Pharmaceutical Sciences · Cited by 1
Development of Treatments and Therapies to Target Mitochondrial Dysfunction
Helliwell, S. B. (2016) · Springer eBooks · doi:10.1007/978-3-319-28637-2_15 · Cited by 1
Biochemistry and Enzymology of Sirtuins
Yang, Y. J., & Sauve, A. A. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_1 · Cited by 1
Dietary compounds as inhibitors of DNA methyltransferases
Rasmi, Y., Khan, J., Ghoshal, K., & Daeihassani, B. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-824412-8.00008-4 · Cited by 1
Drosophila Nicotinamidase And Sir2 In Longevity Regulation And Oxidative Stress Response, And The Implications For Aging Theory
Miller, G. S. (2010) · Human Biology · Cited by 1
Cellular Mechanisms of Resveratrol's Interaction with Mitochondrial Reactive Oxygen Species Metabolism
Robb, E. L. (2013) · Brock University Digital Repository (Brock University) · Cited by 1
Crosstalk between microRNAs and Epigenetics: From the Nutritional Perspective
Liu, Z., Tammen, S. A., Friso, S., & Choi, S. (2013) · Wiley eBooks · doi:10.1002/9781118695999.ch20 · Cited by 1
NAD‐Dependent Deacetylases as Therapeutic Targets
Li, H., Simon, J. A., & Bedalov, A. (2009) · Methods and principles in medicinal chemistry · doi:10.1002/9783527627073.ch10 · Cited by 1
Sirtuin Function in Longevity
Smith, D. L., & Smith, J. S. (2009) · Springer eBooks · doi:10.1007/978-90-481-3465-6_6 · Cited by 1
Adipose Triglyceride Lipase Mediated Regulation Of Sirtuin1 And Lipophagy
Sathyanarayan, A. (2016) · University of Minnesota Digital Conservancy (University of Minnesota) · Cited by 1
O Diabetes Mellitus induz alterações epigenéticas no gene Slc2a4 em músculo esquelético que se relacionam com a repressão do gene, e que podem ser revertidas pela insulinoterapia ou pelo resveratrol.
Yonamine, C. Y. (2018) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.42.2018.tde-21022018-172243 · Cited by 1
Stilbenes: Beneficial Effects of Resveratrol Metabolites in Obesity, Dyslipidemia, Insulin Resistance, and Inflammation
Eseberri, I., Milton‐Laskibar, I., Fernández‐Quintela, A., Gómez‐Zorita, S., & Portillo, M. P. (2020) · doi:10.1002/9781119563754.ch11 · Cited by 1
Chromatin Structure in Senescent Cells
Richards, H. W., & Medrano, E. E. (2009) · Springer eBooks · doi:10.1007/978-1-4419-1075-2_6 · Cited by 1
Mapping the genes for complex canine autoimmune diseases
Massey, J. (2012) · Research Explorer (The University of Manchester) · Cited by 1
An investigation of ageing-related genomic effects of resveratrol
Alatawi, F. S. (2013) · Cited by 1
An investigation of roles for SIRT1 and dietary polyphenols in modulating the ageing process through DNA methylation
Ions, L. J. (2011) · OpenGrey (Institut de l'Information Scientifique et Technique) · Cited by 1
Regulation of pituitary growth hormone synthesis by NAD+ dependent deacetylase Sirt1
Garcia, M. (2014) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.17112
In Vitro Assays for Histone‐Modifying Enzymes
Hauser, A., & Jung, M. (2009) · Methods and principles in medicinal chemistry · doi:10.1002/9783527627073.ch5
A Potential Tumor Suppressive Role of SIRT1 in Cancer
Kabra, N. (2010) · Digital Commons - University of South Florida (University of South Florida)
Sirtuins as Potential Drug Targets for Metabolic Diseases
Tong, Q. (2011) · Wiley eBooks · doi:10.1002/9780470910016.ch15
The role of ER stress in the pathogenesis of Kennedy’s Disease
Montague-Cardoso, K. (2012) · UCL Discovery (University College London)
The Acute And Chronic Effects Of Resveratrol On Renal Function And Blood Pressure
Gordish, K. L. (2015) · Human Biology
Therapeutic potential and challenges of targeting sirtuins in neurodegenerative diseases
Gan, L. (2010) · Frontiers in Biology · doi:10.1007/s11515-010-0700-7
Resveratrol Suppresses CD4+T Cell Activation and Differentiation in vitro
Seo, D., Yi, Y., & Lee, S. (2014) · 한국자원식물학회지 · doi:10.7732/kjpr.2014.27.5.567
Development of Fluorogenic Probes for the Detection of Histone Deacetylase Activity
Hori, Y., Baba, R., & Kikuchi, K. (2015) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.14-00202-3
Can aging be reversed?
Nabavi, N. (2014) · Postdoc Journal · doi:10.14304/surya.jpr.v2n2.4
Regulation of rat Liver Glucokinase Gene Expression by Sterol Regulatory Element Binding Protein-1a and Forkhead box classO1 Transcription factors
Ganjam, G. K. (2008) · doi:10.53846/goediss-1335
Mechanisms of environmental tobacco smoke and benzo[a]pyrene induced cardiovascular injury and the protective role of resveratrol
Al-Dissi, A. N. (2010) · University Library - University of Saskatchewan (University of Saskatchewan)
On histone deacetylases in the epigenetic regulation of neural stem and cancer cell fate
Wallenborg, K. (2008) · Figshare
Antioxidants and Skin Aging 167
Masaki, H. (2014)
Amurensin G, a Potent Natural SIRT1 Inhibitor, Rescues Doxorubicin Responsiveness via Down-Regulation of Multidrug
Oh, W. K., Cho, K. B., Hiền, T. T., Kim, T. H., Kim, H. S., Đào, T. T., Han, H., Kwon, S., Ahn, S., Yoon, J., et al. (2010)
ReviewArticle Targeting Gonadotropins: An Alternative Option for Alzheimer Disease Treatment
Casadesús, G., Puig, E. R., Webber, K. M., Atwood, C., Castell, M., Bowen, R. L., Perry, G. L., Smith, M. A., Middleton, W. S., & Veterans, M. (2006)
Attenuation of skeletal muscle FFA-induced insulin resistance by the polyphenol resveratrol. Elucidation of the mechanisms involved
Sanli, T. (2008) · Brock University Digital Repository (Brock University)
Análise de variantes polimórficas da região promotora do gene SIRT1 em pacientes com lúpus eritematoso sistêmico
Consiglio, C. R. (2013) · Americanae (AECID Library)
Aging-dependent effects of repetitive loading exercise and antioxidant supplementation on oxidative stress in skeletal muscle
Ryan, M. J. (2010) · doi:10.33915/etd.3093
Action of resveratrol analogs and hyperthermia in cancer chemoprevention and chemotherapyY
Butler, R. (2011) · Rutgers University Community Repository (Rutgers University) · doi:10.7282/t34t6j1z
Resveratrolün hücresel yaşlanmanın indüklenmesi ve sirtüinlerin aktivasyonunda rolünün insan dermal fibroblastlarında araştırılması
Kılınçlı, A. (2013) · eArsiv - Adu (Adnan Menderes University)
Functional impact of microRNA-34a on stem cell differentiation towards smooth muscle cell
Yu, X. (2014)
The Underlying Mechanisms for Resveratrol’ Superinduction Effects
Li, W. (2015) · International Journal of Health Sciences (IJHS) · doi:10.15640/ijhs.v3n1a3
ART for Antiaging
Zeng, Q.-P. (2015) · Springer briefs in molecular science · doi:10.1007/978-3-662-47688-8_6
Chemical Biology of Histone Modifications
Rose, N. R., Schofield, C. J., & Heightman, T. D. (2010) · Royal Society of Chemistry eBooks · doi:10.1039/9781849732178-00151
Marking of metabolites in the diagnostics of metabolic diseases and in the investigation of xenobiotics metabolism using NMR spectroscopy
Krawczyk, H. (2016) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2016.05.021
Proteomic approaches for identifying new mechanisms of action and pharmacodynamic biomarkers of resveratrol in colorectal cancer
Kovoor, C. J. (2015) · Figshare
An Interview with Andrew D. Napper, Ph.D.
Napper, A. D. (2008) · Assay and Drug Development Technologies · doi:10.1089/adt.2008.9985
Resveratrol and Inflammatory–Autoimmune Diseases
Petro, T. M. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-397156-2.00034-x
NAD + -Dependent Deacetylases and Medical Therapy
Kumar, A., Ben-Aderet, L., Elayyan, J., & Dvir‐Ginzberg, M. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803239-8.00035-1
Mechanisms Underlying Longevity Regulation and Extension by Genetic, Dietary and Pharmacological Interventions in the Yeast Saccharomyces Cerevisiae
Kyryakov, P. (2012) · Spectrum Research Repository (Concordia University)
Sirtuin 1 and Oxidative Stress 19
Li, H. (2014)
THE ACUTE IMPACT OF A SINGLE DOSE OF RESVERATROL ON INSULIN SENSITIVITY, WHOLE BODY FAT OXIDATION, AND INTRACELLULAR SIGNALING IN SKELETAL MUSCLE AND ADIPOSE TISSUE IN OVERWEIGHT AND OBESE MEN
Williams, C. (2013) · QSpace (Queen's University Library)
In Vitro Histone Deacetylase Activity Screening
Sodji, Q. H., Kornacki, J. R., Mrksich, M., & Oyelere, A. K. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801080-8.00015-6

Authors: Borra, M. T., Smith, B. C., & Denu, J. M.
Affiliations: University of Wisconsin–Madison (US)
Corresponding author: Denu, John M.
ORCID: Smith, Brian C.
Denu, John M.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2005-04
Volume: 280
Issue: 17
Pages: 17187-17195
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m501250200
OpenAlex: W2007842741
Cited by: 1,065
References: 68
Citations by year: 2026: 27 · 2025: 29 · 2024: 29 · 2023: 39 · 2022: 62 · 2021: 45 · 2020: 59 · 2019: 58 · 2018: 62 · 2017: 35 · 2016: 52 · 2015: 72 · 2014: 48 · 2013: 73 · 2012: 72
FWCI: 18.16
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5677 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (NIH 5 T32)
National Institute of General Medical Sciences (T32GM008349, F31GM066366, NIH 5T32 GM08349, R01GM065386)
Topics: Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Keywords: SIRT1, resveratrol, NAD+-dependent deacetylase, p53 acetylation, substrate affinity, conformational change, lifespan extension
MeSH terms: Resveratrol, Antioxidants, Binding Sites, Binding, Competitive, Cell Cycle, Chromatography, High Pressure Liquid, Coumarins, Coloring Agents, Histidine, Histone Deacetylases, Humans, Kinetics, Models, Chemical, Models, Molecular, Peptides, Protein Binding, Protein Conformation, Rhodamines, Stilbenes, Substrate Specificity, Time Factors, Tumor Suppressor Protein p53, Crystallography, X-Ray, Gene Silencing, Sirtuins, Immunoprecipitation, Sirtuin 1, Sirtuin 2

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

Mechanism of Human SIRT1 Activation by Resveratrol

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks