Requirement of NAD and SIR2 for Life-Span Extension by Calorie Restriction in Saccharomyces cerevisiae

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

Oxidative Stress, Caloric Restriction, and Aging

Sohal, R. S., & Weindruch, R. H. (1996) · Science · doi:10.1126/science.273.5271.59 · Cited by 3,133

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

A new efficient gene disruption cassette for repeated use in budding yeast

Güldener, U. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.13.2519 · Cited by 1,657

Extrachromosomal rDNA circles—a cause of aging in yeast

Sinclair, D. A., & Guarente, L. (1997) · Cell · doi:10.1016/s0092-8674(00)80493-6 · Cited by 1,500

Gene expression profile of aging and its retardation by caloric restriction

Lee, C.-K., Klopp, R. G., Weindruch, R., & Prolla, T. A. (1999) · Science · doi:10.1126/science.285.5432.1390 · Cited by 1,473

The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases

Landry, J., Sutton, A., Tafrov, S. T., Heller, R. C., Stebbins, J., Pillus, L., & Sternglanz, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.110148297 · Cited by 970

Function and Regulation of Yeast Hexose Transporters

Özcan, S., & Johnston, M. (1999) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.63.3.554-569.1999 · Cited by 729

A phylogenetically conserved NAD + -dependent protein deacetylase activity in the Sir2 protein family

Smith, J. S., Brachmann, C. B., Celic, I., Kenna, M. A., Muhammad, S., Starai, V. J., Avalos, J. L., Escalante-Semerena, J. C., Grubmeyer, C., Wolberger, C., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.12.6658 · Cited by 718

Novel sensing mechanisms and targets for the cAMP–protein kinase A pathway in the yeast Saccharomyces cerevisiae

Thevelein, J. M., & WINDE, J. H. D. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01538.x · Cited by 682

Diet, energy metabolism and mitochondrial biogenesis

Civitarese, A. E., Smith, S. R., & Ravussin, É. (2007) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e3282f0ecd2 · Cited by 52

Quantitation of NAD+ biosynthesis from the salvage pathway in Saccharomyces cerevisiae

Sporty, J. L., Lin, S.-J., Kato, M., Ognibene, T. J., Stewart, B. J., Turteltaub, K. W., & Bench, G. (2009) · Yeast · doi:10.1002/yea.1671 · Cited by 51

Calorie restriction does not elicit a robust extension of replicative lifespan in Saccharomyces cerevisiae

Huberts, D. H. E. W., González, J., Lee, S. S., Litsios, A., Hubmann, G., Wit, E. C., & Heinemann, M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1410024111 · Cited by 60

Loss of Nat4 and its associated histone H4 N‐terminal acetylation mediates calorie restriction‐induced longevity

Molina‐Serrano, D., Schiza, V., Demosthenous, C., Stavrou, E., Oppelt, J., Kyriakou, D., Liu, W., Zisser, G., Bergler, H., Dang, W., et al. (2016) · EMBO Reports · doi:10.15252/embr.201642540 · Cited by 48

The integrated stress response in budding yeast lifespan extension

Postnikoff, S. D. L., Johnson, J. E., & Tyler, J. K. (2017) · Microbial Cell · doi:10.15698/mic2017.11.597 · Cited by 51

Effect of fasting on PPARγ and AMPK activity in adipocytes

Kajita, K., Mune, T., Ikeda, T., Matsumoto, M., Uno, Y., Sugiyama, C., Matsubara, K., Morita, H., Takemura, M., Seishima, M., et al. (2008) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2008.05.003 · Cited by 51

Genomic plasticity, energy allocations, and the extended longevity phenotypes of Drosophila

Arking, R. (2002) · Ageing Research Reviews · doi:10.1016/s1568-1637(01)00010-1 · Cited by 51

Murine Models of Life Span Extension

Quarrie, J. K., & Riabowol, K. T. (2004) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2004.31.re5 · Cited by 53

NADH binds and stabilizes the 26S proteasomes independent of ATP

Tsvetkov, P., Myers, N., Eliav, R., Adamovich, Y., Hagai, T., Adler, J., Navon, A., & Shaul, Y. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.537175 · Cited by 42

SIR2 Family of NAD+-Dependent Protein Deacetylases

Smith, J. S., Avalos‬, J. L., Celic, I., Muhammad, S., Wolberger, C., & Boeke, J. D. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)53056-1 · Cited by 50

Sirtuins of parasitic protozoa: In search of function(s)

Religa, A. A., & Waters, A. P. (2012) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2012.08.003 · Cited by 51

Therapeutic potential of activators and inhibitors of sirtuins

Balcerczyk, A., & Pirola, L. (2010) · BioFactors · doi:10.1002/biof.112 · Cited by 49

Deletion or Overexpression of Mitochondrial NAD + Carriers in Saccharomyces cerevisiae Alters Cellular NAD and ATP Contents and Affects Mitochondrial Metabolism and the Rate of Glycolysis

Agrimi, G., Brambilla, L., Frascotti, G., Pisano, I., Porro, D., Vai, M., & Palmieri, L. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.01703-10 · Cited by 53

Mitochondria-mediated hormetic response in life span extension of calorie-restricted Saccharomyces cerevisiae

Sharma, P. K., Agrawal, V., & Roy, N. (2010) · AGE · doi:10.1007/s11357-010-9169-1 · Cited by 50

The NAD + -Dependent Family of Sirtuins in Cerebral Ischemia and Preconditioning

Khoury, N., Koronowski, K. B., Young, J. I., & Pérez‐Pinzón, M. A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7258 · Cited by 51

The Role of Ghrelin and Ghrelin Signaling in Aging

Amitani, M. S., Amitani, H., Cheng, K., Kairupan, T. S., Sameshima, N., Shimoshikiryo, I., Mizuma, K., Rokot, N. T., Nerome, Y., Owaki, T., et al. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071511 · Cited by 53

Uncoupling protein homologs may provide a link between mitochondria, metabolism and lifespan

Wolkow, C. A., & Iser, W. B. (2006) · Ageing Research Reviews · doi:10.1016/j.arr.2006.03.007 · Cited by 50

Overexpressed Sod1p acts either to reduce or to increase the lifespans and stress resistance of yeast, depending on whether it is Cu2+‐deficient or an active Cu,Zn‐superoxide dismutase

Harris, N., Bachler, M. A., Costa, V., Mollapour, M., Moradas‐Ferreira, P., & Piper, P. W. (2005) · Aging Cell · doi:10.1111/j.1474-9726.2005.00142.x · Cited by 49

Nicotinamidase modulation of NAD+ biosynthesis and nicotinamide levels separately affect reproductive development and cell survival inC. elegans

Vrablik, T. L., Huang, L., Lange, S. E., & Hanna‐Rose, W. (2009) · Development · doi:10.1242/dev.028431 · Cited by 49

Animal Models in Biomedical Research

Maurer, K. J., & Quimby, F. W. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-409527-4.00034-1 · Cited by 51

Regulation of mRNA Translation as a Conserved Mechanism of Longevity Control

Mehta, R., Chandler-Brown, D., Ramos, F. J., Shamieh, L. S., & Kaeberlein, M. (2010) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4419-7002-2_2 · Cited by 44

Sirtuin regulation in calorie restriction

Qiu, X., Brown, K. V., Moran, Y., & Chen, D. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.09.015 · Cited by 50

Pathways Change in Expression During Replicative Aging in Saccharomyces cerevisiae

Yiu, G., McCord, A., Wise, A., Jindal, R., Hardee, J. J., Kuo, A., Shimogawa, M. M., Cahoon, L. A., Wu, M., Kloke, J., et al. (2008) · The Journals of Gerontology Series A · doi:10.1093/gerona/63.1.21 · Cited by 49

Transcription factor NFκB regulates the expression of the histone deacetylase SIRT1

Katto, J., Engel, N., Abbas, W., Herbein, G., & Mahlknecht, U. (2013) · Clinical Epigenetics · doi:10.1186/1868-7083-5-11 · Cited by 49

SIR2 and aging – the exception that proves the rule

Guarente, L. (2001) · Trends in Genetics · doi:10.1016/s0168-9525(01)02339-3 · Cited by 49

Characterization of Trypanosoma cruzi Sirtuins as Possible Drug Targets for Chagas Disease

Moretti, N. S., Augusto, L. D. S., Clemente, T. M., Antunes, R. P. P., Yoshida, N., Torrecilhas, A. C., Cano, M. I. N., & Schenkman, S. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.04694-14 · Cited by 48

Over-expression of Sirt1 contributes to chemoresistance and indicates poor prognosis in serous epithelial ovarian cancer (EOC)

Shuang, T., Wang, M., Zhou, Y., & Shi, C. (2015) · Medical Oncology · doi:10.1007/s12032-015-0706-8 · Cited by 48

At the crossroad of T cells, adipose tissue, and diabetes

Matarese, G., Procaccini, C., & Rosa, V. D. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01154.x · Cited by 47

Targeting PGC-1α to control energy homeostasis

Wu, Z., & Boss, O. (2007) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.11.10.1329 · Cited by 50

Nicotinamide-mediated inhibition of SIRT1 deacetylase is associated with the viability of cancer cells exposed to antitumor agents and apoptosis

Wang, T., Cui, H., MA, N., & Jiang, Y. (2013) · Oncology Letters · doi:10.3892/ol.2013.1400 · Cited by 49

Role of Hormesis in Life Extension by Caloric Restriction

Masoro, E. J. (2007) · Dose-Response · doi:10.2203/dose-response.06-005.masoro · Cited by 48

Genetic architecture of natural variation in visual senescence in Drosophila

Carbone, M. A., Ah, Y., Huang, W., Lyman, R. A., Meadors, T. B., Yamamoto, R., Anholt, R. R. H., & Mackay, T. F. C. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1613833113 · Cited by 48

NutrimiRAging: Micromanaging Nutrient Sensing Pathways through Nutrition to Promote Healthy Aging

Micó, V., Berninches, L., Tapia, J., & Daimiel, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18050915 · Cited by 50

Signaling Network of Forkhead Family of Transcription Factors (FOXO) in Dietary Restriction

Jiang, Y.-Z., Yan, F., Feng, Z., Lazarovici, P., & Zheng, W. (2019) · Cells · doi:10.3390/cells9010100 · Cited by 51

Cell stress response impairs de novo NAD+ biosynthesis in the kidney

Bignon, Y., Rinaldi, A. M., Nadour, Z., Poindessous, V., Nemazanyy, I., Lenoir, O., Fohlen, B., Weill-Raynal, P., Hertig, A., Karras, A., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.153019 · Cited by 50

A Functional Analysis Reveals Dependence on the Anaphase-Promoting Complex for Prolonged Life Span in Yeast

Harkness, T. A. A., Shea, K. A., Legrand, C., Brahmania, M., & Davies, G. F. (2004) · Genetics · doi:10.1534/genetics.104.027771 · Cited by 49

Hydrolase Controls Cellular NAD, Sirtuin, and Secondary Metabolites

Shimizu, M., Masuo, S., Fujita, T., Doi, Y., Kamimura, Y., & Takaya, N. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00032-12 · Cited by 48

NAD+ salvage pathway proteins suppress proteotoxicity in yeast models of neurodegeneration by promoting the clearance of misfolded/oligomerized proteins

Ocampo, A., Liu, J., & Barrientos, A. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt016 · Cited by 47

The Genomic Basis of Postponed Senescence in Drosophila melanogaster

Carnes, M. U., Campbell, T. G., Huang, W., Butler, D. G., Carbone, M. A., Duncan, L. H., Harbajan, S. V., King, E. M., Peterson, K. R., Weitzel, A. J., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0138569 · Cited by 49

The role of autophagy in the regulation of yeast life span

Tyler, J. K., & Johnson, J. E. (2018) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13549 · Cited by 49

Sirtuin 6: A potential therapeutic target for cardiovascular diseases

Xie, S., Deng, W., & Qizhu, T. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105214 · Cited by 47

Leaf Extract of Dillenia indica as a Source of Selenium Nanoparticles with Larvicidal and Antimicrobial Potential toward Vector Mosquitoes and Pathogenic Microbes

Meenambigai, K., Kokila, R., Maadhu, P., Thangavelu, P., Sivashanmugan, K., & Arjunan, N. (2020) · Coatings · doi:10.3390/coatings10070626 · Cited by 47

DetecDiv, a generalist deep-learning platform for automated cell division tracking and survival analysis

Aspert, T., Hentsch, D., & Charvin, G. (2022) · eLife · doi:10.7554/elife.79519 · Cited by 47

SIRT6 Minor Allele Genotype Is Associated with >5-Year Decrease in Lifespan in an Aged Cohort

Tennapel, M. J., Lynch, C. F., Burns, T. L., Wallace, R. B., Smith, B. J., Button, A. M., & Domann, F. E. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115616 · Cited by 46

Energy restriction and aging

Smith, J. V., Heilbronn, L. K., & Ravussin, É. (2004) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-200411000-00005 · Cited by 46

The anti-aging effects of Ludwigia octovalvis on Drosophila melanogaster and SAMP8 mice

Lin, W., Chen, J., Wang, J.-C., Chen, L.-Y., Lin, C.-H., Hsieh, T.-R., Wang, M.-F., Fu, T., & Wang, P. (2013) · AGE · doi:10.1007/s11357-013-9606-z · Cited by 47

Controlling Central Carbon Metabolism for Improved Pathway Yields in Saccharomyces cerevisiae

Tan, S. Z., Finney-Manchester, S. P., & Prather, K. L. J. (2015) · ACS Synthetic Biology · doi:10.1021/acssynbio.5b00164 · Cited by 46

Exploring the power of yeast to model aging and age-related neurodegenerative disorders

Oliveira, A. V., Vilaça, R., dos Santos, C. N., Costa, V., & Menezes, R. (2016) · Biogerontology · doi:10.1007/s10522-016-9666-4 · Cited by 50

Resveratrol stimulates the metabolic reprogramming of human CD4 + T cells to enhance effector function

Craveiro, M., Cretenet, G., Mongellaz, C., Matias, M. I., Caron, O., de Lima, M. C. P., Zimmermann, V. S., Solary, É., Dardalhon, V., Dulić, V., et al. (2017) · Science Signaling · doi:10.1126/scisignal.aal3024 · Cited by 48

Evaluation of antioxidant and neuroprotective activities of Cassia fistula (L.) using the Caenorhabditis elegans model

Thabit, S., Handoussa, H., Roxo, M., Sayed, N. S. E., de Azevedo, B. C., & Wink, M. (2018) · PeerJ · doi:10.7717/peerj.5159 · Cited by 48

Loss of Mitochondrial Control Impacts Renal Health

Srivastava, S. P., Kanasaki, K., & Goodwin, J. E. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.543973 · Cited by 48

Candida albicans, a distinctive fungal model for cellular aging study

Fu, X., Meng, F., Hu, Y., & Zhou, J. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2008.00424.x · Cited by 49

Calorie restriction reduces rDNA recombination independently of rDNA silencing

Riesen, M., & Morgan, A. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00514.x · Cited by 46

New clues to old yeast

Jazwinski, S. M. (2001) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(01)00244-5 · Cited by 46

Pathogen evolution in a vaccinated world

Read, A. F., & Mackinnon, M. J. (2007) · Oxford University Press eBooks · doi:10.1093/acprof:oso/9780199207466.003.0011 · Cited by 45

Structural biology of enzymes involved in NAD and molybdenum cofactor biosynthesis

Rizzi, M. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00385-8 · Cited by 46

Caloric restriction: implications for sarcopenia and potential mechanisms

Xie, W.-Q., Xiao, W.-F., Tang, K., Wu, Y.-X., Hu, P.-W., Li, Y.-S., Duan, Y., & Lv, S. (2020) · Aging · doi:10.18632/aging.103987 · Cited by 46

Distinct role of Sirtuin 1 (SIRT1) and Sirtuin 2 (SIRT2) in inhibiting cargo-loading and release of extracellular vesicles

Lee, B. R., Sanstrum, B. J., Liu, Y., & Kwon, S. (2019) · Scientific Reports · doi:10.1038/s41598-019-56635-0 · Cited by 45

SIRT1 inhibits proliferation of pancreatic cancer cells expressing pancreatic adenocarcinoma up-regulated factor (PAUF), a novel oncogene, by suppression of β-catenin

Cho, I.-R., Koh, S. S., Malilas, W., Srisuttee, R., Moon, J., Choi, Y. W., Horio, Y., Oh, S., & Chung, Y.-H. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.05.107 · Cited by 47

Heat-induced hormesis in longevity of two sibling Drosophila species

Scannapieco, A. C., Sørensen, J. G., Loeschcke, V., & Norry, F. M. (2006) · Biogerontology · doi:10.1007/s10522-006-9075-1 · Cited by 45

The Role of SIRT1 in Tumorigenesis

Li, K., Luo, J., & Azabdaftari, G. (2011) · North American Journal of Medicine and Science · doi:10.7156/v4i2p104 · Cited by 46

Shuttle craft: a candidate quantitative trait gene for Drosophila lifespan

PASYUKOVA, E. G., Roshina, N. V., & Mackay, T. F. C. (2004) · Aging Cell · doi:10.1111/j.1474-9728.2004.00114.x · Cited by 45

Having it all: historical energy intakes do not generate the anticipated trade-offs in fecundity

Johnston, S. L., Grune, T., Bell, L. M., Murray, S. J., Souter, D. M., Erwin, S. S., Yearsley, J. M., Gordon, I. J., Illius, A. W., Kyriazakis, I., et al. (2006) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.2005.3456 · Cited by 44

CBX8 suppresses Sirtinol-induced premature senescence in human breast cancer cells via cooperation with SIRT1

Lee, S. H., Um, S., & Kim, E.-J. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.02.051 · Cited by 44

Oxidative stress and chronological aging in glycogen-phosphorylase-deleted yeast

Favre, C., Aguilar, P. S., & Carrillo, M. C. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.08.021 · Cited by 44

Regulatory Effects of NAD + Metabolic Pathways on Sirtuin Activity

Zhang, N., & Sauve, A. A. (2018) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.11.012 · Cited by 46

Role of Sirtuins in Tumor Angiogenesis

Edatt, L., Poyyakkara, A., Raji, G. R., Ramachandran, V., Shankar, S. S., & Kumar, V. B. S. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2019.01516 · Cited by 43

Histone Acetyltransferases and Deacetylases Are Required for Virulence, Conidiation, DNA Damage Repair, and Multiple Stresses Resistance of Alternaria alternata

Ma, H., Li, L., Gai, Y., Zhang, X., Chen, Y., Zhuo, X., Cao, Y., Jiao, C., Gmitter, F. G., & Li, H. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.783633 · Cited by 45

Calorie restriction effects on silencing and recombination at the yeast rDNA

Smith, D. L., Li, C., Matecic, M., Maqani, N., Bryk, M., & Smith, J. S. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00516.x · Cited by 43

Gene regulatory changes in yeast during life extension by nutrient limitation

Wang, J., Jiang, J. C., & Jazwinski, S. M. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.02.008 · Cited by 45

Mitochondrial Metabolism Modulation: A New Therapeutic Approach for Parkinsons Disease

Arduíno, D. M., Esteves, A. R., Oliveira, C. R., & Cardoso, S. M. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710790966687 · Cited by 44

Ras: The Other Pro-Aging Pathway

Longo, V. D. (2004) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2004.39.pe36 · Cited by 45

The role of mitochondrial disturbances in Alzheimer, Parkinson and Huntington diseases

Carvalho, C., Correia, S. C., Cardoso, S., Plácido, A. I., Candeias, E., Duarte, A. I., & Moreira, P. I. (2015) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.2015.1058160 · Cited by 45

Biological significance of protein modifications in aging and calorie restriction

Nakamura, A., Kawakami, K., Kametani, F., Nakamoto, H., & Goto, S. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05374.x · Cited by 46

SIRT1 and SIRT5 activity expression and behavioral responses to calorie restriction

Geng, Y., Li, T.-T., Liu, X., Li, Z.-H., & Fu, Y. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23315 · Cited by 43

Underlying and Multiple Case Mortality Advanced Ages: United States 1980-1998

Stallard, E. (2002) · North American Actuarial Journal · doi:10.1080/10920277.2002.11073999 · Cited by 43

Characterization of physiological defects in adult SIRT6-/- mice

Peshti, V., Obolensky, A., Nahum, L., Kanfi, Y., RATHAUS, M., Avraham, M., Tinman, S., Alt, F. W., Banin, E., & Cohen, H. Y. (2017) · PLoS ONE · doi:10.1371/journal.pone.0176371 · Cited by 44

Thyroid hormone regulation of Sirtuin 1 expression and implications to integrated responses in fasted mice

Cordeiro, A., Souza, L. L., Oliveira, L. S. D., Faustino, L. C., Santiago, L. A., Bloise, F. F., Ortiga-Carvalho, T. M., Almeida, N. A. D. S., & Pazos-Moura, C. C. (2012) · Journal of Endocrinology · doi:10.1530/joe-12-0420 · Cited by 46

The ecology and evolution of antibiotic-resistant bacteria

Bergstrom, C. T., & Feldgarden, M. (2007) · Oxford University Press eBooks · doi:10.1093/acprof:oso/9780199207466.003.0010 · Cited by 44

Nicotinamide, Nicotinamide Riboside and Nicotinic Acid—Emerging Roles in Replicative and Chronological Aging in Yeast

Orlandi, I., Alberghina, L., & Vai, M. (2020) · Biomolecules · doi:10.3390/biom10040604 · Cited by 40

Reciprocal regulation between nicotinamide adenine dinucleotide metabolism and abscisic acid and stress response pathways in Arabidopsis

Hong, Y., Wang, Z., Shi, H., Yao, J., Liu, X., Wang, F., Zeng, L., Xie, Z., & Zhu, J. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1008892 · Cited by 42

The Potential of Calorie Restriction and Calorie Restriction Mimetics in Delaying Aging: Focus on Experimental Models

Giacomello, E., & Toniolo, L. (2021) · Nutrients · doi:10.3390/nu13072346 · Cited by 45

Sirtuins are not conserved longevity genes

Brenner, C. (2022) · Life Metabolism · doi:10.1093/lifemeta/loac025 · Cited by 43

SirT1—A Sensor for Monitoring Self-Renewal and Aging Process in Retinal Stem Cells

Peng, C., Chang, Y.-L., Kao, C.-L., Tseng, L.-M., Wu, C.-C., Chen, Y., Tsai, C.-Y., Woung, L., Liu, J., Chiou, S., et al. (2010) · Sensors · doi:10.3390/s100606172 · Cited by 42

Attenuation of Age-Related Metabolic Dysfunction in Mice With a Targeted Disruption of the C Subunit of Protein Kinase A

Enns, L. C., Morton, J. F., Mangalindan, R., McKnight, G. S., Schwartz, M. W., Kaeberlein, M. R., Kennedy, B. K., Rabinovitch, P. S., & Ladiges, W. (2009) · The Journals of Gerontology Series A · doi:10.1093/gerona/glp133 · Cited by 43

III. Senescent enteric nervous system: lessons from extraintestinal sites and nonmammalian species

Wiley, J. W. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00224.2002 · Cited by 42

The effect of diet, sex and mating status on longevity in Mediterranean fruit flies (), Diptera: Tephritidae

Davies, S. J., KATTEL, R., Bhatia, B., Petherwick, A. S., & Chapman, T. (2005) · Experimental Gerontology · doi:10.1016/j.exger.2005.07.009 · Cited by 42

Metabolic reprogramming: a bridge between aging and tumorigenesis

Drapela, S., Ilter, D., & Gomes, A. P. (2022) · Molecular Oncology · doi:10.1002/1878-0261.13261 · Cited by 41

The mitochondrial NAD+ transporter SLC25A51 is a fasting-induced gene affecting SIRT3 functions

Fu, Z., Kim, H., Morse, P. T., Lu, M., Hüttemann, M., Cambronne, X. A., Zhang, K., & Zhang, R. (2022) · Metabolism · doi:10.1016/j.metabol.2022.155275 · Cited by 40

Resveratrol-Induced Changes of the Human Adipocyte Secretion Profile

Rosenow, A., Noben, J., Jocken, J. W. E., Kallendrusch, S., Fischer‐Posovszky, P., Mariman, E. C. M., & Renes, J. (2012) · Journal of Proteome Research · doi:10.1021/pr300539b · Cited by 41

A critical role of SNF1A/dAMPKα (Drosophila AMP-activated protein kinase α) in muscle on longevity and stress resistance in Drosophila melanogaster

Tohyama, D., & Yamaguchi, A. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.02.126 · Cited by 41

Epigenetik – ein Epizentrum der Genregulation: Histone und histonmodifizierende Enzyme

Biel, M., Wascholowski, V., & Giannis, A. (2005) · Angewandte Chemie · doi:10.1002/ange.200461346 · Cited by 42

Modification of DBC1 by SUMO2/3 is crucial for p53-mediated apoptosis in response to DNA damage

Park, J., Lee, S. W., Yang, S. W., Yoo, H. M., Park, J. M., Seong, M. W., Ka, S. H., Oh, K. H., Jeon, Y. J., & Chung, C. H. (2014) · Nature Communications · doi:10.1038/ncomms6483 · Cited by 42

GABA metabolism pathway genes, UGA1 and GAD1, regulate replicative lifespan in Saccharomyces cerevisiae

Kamei, Y., Tamura, T., Yoshida, R., Ohta, S., Fukusaki, E., & Mukai, Y. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.02.136 · Cited by 43

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Burkewitz, K., Weir, H. J. M., & Mair, W. B. (2016) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-319-43589-3_10 · Cited by 42

Proline metabolism regulates replicative lifespan in the yeast Saccharomyces cerevisiae

Mukai, Y., Kamei, Y., Liu, X., Jiang, S., Sugimoto, Y., Nanyan, N. S. M., Watanabe, D., & Takagi, H. (2019) · Microbial Cell · doi:10.15698/mic2019.10.694 · Cited by 41

A Comprehensive Review of Biochemical and Molecular Evidences from Animal and Human Studies on the Role of Oxidative Stress in Aging: An Epiphenomenon or the Cause

Momtaz, S., & Abdollahi, M. R. (2011) · Asian Journal of Animal and Veterinary Advances · doi:10.3923/ajava.2012.1.19 · Cited by 41

Natural variation in replicative and chronological life spans of Saccharomyces cerevisiae

Qin, H. H., & Lu, M. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.01.007 · Cited by 45

Crystal Structure of the NAD Biosynthetic Enzyme Quinolinate Synthase

Sakuraba, H., Tsuge, H., Yoneda, K., Katunuma, N., & Ohshima, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500192200 · Cited by 40

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Counting the calories to immortality

Alfred, J. (2000) · Nature Reviews Genetics · doi:10.1038/35038524 · Cited by 1

Extending life – a lifestyle choice

Kendrew, S. G. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01706-0

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Lin, S.-J., Ford, E., Haigis, M. C., & Guarente, L. (2015)

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(2004) · Science s STKE · doi:10.1126/stke.2142004tw13