{"doi":"10.1039/c0mb00033g","title":"Sirtuin mechanism and inhibition: explored with Nε-acetyl-lysine analogs","abstract":"<jats:title>Abstract</jats:title>\n                  <jats:p>Silent information regulator 2 (Sir2) enzymes or sirtuins are a family of intracellular protein deacetylases that can catalyze the β-nicotinamide adenine dinucleotide (β-NAD+)-dependent deacetylation of Nε-acetyl-lysine on protein substrates, with the formation of lysine Nε-deacetylated protein species and small molecule products, i.e.nicotinamide and 2′-O-acetyl-ADP-ribose (2′-O-AADPR). These enzymes are evolutionarily conserved among all the three kingdoms of life, with the yeast Sir2 being the founding family member. In humans, seven sirtuins, i.e. SIRT1-7, have been identified. The past a few years have witnessed a tremendous interest in investigating the unique mechanism for the sirtuin-catalyzed deacetylation reaction. We have also seen a lot of research employing different strategies to identify different types of the inhibitors for this enzymatic deacetylation reaction. These inhibitors hold great potential toward a fuller exploration of sirtuin biology and pharmacology as well as toward developing novel therapeutics for metabolic and age-related diseases and cancer. Here we would like to review the significant contributions that the judicious use of a variety of Nε-acetyl-lysine analogs has been able to make toward our enhanced mechanistic understanding and capability of pharmacological exploitation of the sirtuin-catalyzed deacetylation reaction.</jats:p>\n                  <jats:p/>","journal":"Molecular BioSystems","year":2010,"id":15414,"datarank":1.2805308494594192,"base_score":3.4339872044851463,"endowment":3.4339872044851463,"self_citation_contribution":0.515098080672772,"citation_network_contribution":0.7654327687866472,"self_endowment_contribution":0.515098080672772,"citer_contribution":0.7654327687866472,"corpus_percentile":null,"corpus_rank":null,"citation_count":30,"citer_count":26,"citers_with_citation_signal":22,"citers_with_endowment":22,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":117696,"name":"Weiping Zheng","orcid":null,"position":1,"is_corresponding":false},{"id":117695,"name":"Brett M Hirsch","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":3.4339872044851463,"endowment":3.4339872044851463,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"20842312","pmcid":null,"openalex_id":"https://openalex.org/W2097713324","authors":[],"funders":[],"total_grants":0,"fwci":1.381,"citation_percentile":0.82448778,"influential_citations":0,"citation_trend":[{"year":2012,"count":6},{"year":2013,"count":2},{"year":2014,"count":1},{"year":2015,"count":2},{"year":2016,"count":3},{"year":2018,"count":3},{"year":2019,"count":3},{"year":2021,"count":1},{"year":2022,"count":1},{"year":2023,"count":4},{"year":2024,"count":2}],"oa_status":"closed","license":"https://academic.oup.com/pages/standard-publication-reuse-rights","oa_locations":[{"url":"https://academic.oup.com/molecular-omics/article-pdf/7/1/16/66203680/c0mb00033g.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1039/c0mb00033g","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/20842312","host_type":"repository"}],"fields_of_study":["Sirtuins and Resveratrol in Medicine","Autophagy in Disease and Therapy","Adenosine and Purinergic Signaling","Biology","Medicine","Chemistry","Humans","Lysine","Molecular Structure","Sirtuins"],"mesh_terms":["Humans","Lysine","Molecular Structure","Sirtuins"],"keywords":["Sirtuin","NAD+ kinase","Acetylation","Lysine","SIRT2","Nicotinamide adenine dinucleotide","Biochemistry","Enzyme","Sirtuin 1","Regulator","Biology","Nicotinamide","Small molecule","Yeast","Chemistry","Amino acid","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-01T17:37:08.399226Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}