ReviewThe Journal of biological chemistry2012
Structural basis for sirtuin activity and inhibition.
Review in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
73 citing papers in PubMed, 155 citations in OpenAlex.
- Naphthalene-based hydroxamate HDAC inhibitors with anti-breast tumor activity.Molecular diversity · 2026Article
- MeSRT1 Interacts with MeNF-YC15 and Negatively Mediates Resistance to Cassava Bacterial Blight via Regulation of Gibberellin Metabolism inPlants (Basel, Switzerland) · 2026Article
- Comparative Structure-Based Analysis of Predicted BZD9L1 Binding Modes Across Human Sirtuins.International journal of molecular sciences · 2026Article
- Physical interactions within the SIR heterochromatin complex potentiate inter-subunit communication and gene repression.Cell reports · 2026Article
- Carba-NAD binding activates SIR2 by reshaping conformational plasticity and rewiring long-range allosteric networks.PLoS computational biology · 2026Article
- SIRT1 as a Key Regulator in Rheumatic Diseases: Integrating Molecular Insights with Traditional Chinese Medicine Approaches.Journal of inflammation research · 2026Review
- Elucidating binding hot spots and structural stability in sirtuin family proteins for selective inhibitors: a computational approach.Frontiers in bioinformatics · 2026Article
- Filament formation and NAD processing by noncanonical human FAM118 sirtuins.Nature structural & molecular biology · 2025Article
- The role of succinylation-mediated metabolic reprogramming in tumor progression.Molecular biology reports · 2025Review
- Impact of sirtuin‑1 expression on progression‑free survival in non‑endometrioid endometrial cancer: A retrospective cohort study.Oncology letters · 2025Article
- Tetramerization-dependent activation of the Sir2-associated short prokaryotic Argonaute immune system.Nature communications · 2024Article
- Sirtuins in kidney health and disease.Nature reviews. Nephrology · 2024Review
- Structural basis for phage-mediated activation and repression of bacterial DSR2 anti-phage defense system.Nature communications · 2024Article
- Sirtuins in kidney diseases: potential mechanism and therapeutic targets.Cell communication and signaling : CCS · 2024Review
- Impact of Lysine Succinylation on the Biology of Fungi.Current issues in molecular biology · 2024Review
- Bacterial protein acetylation: mechanisms, functions, and methods for study.Frontiers in cellular and infection microbiology · 2024Review
- Sirtuins in kidney homeostasis and disease: where are we now?Frontiers in endocrinology · 2024Review
- Structure and Function of Kdac1, a Class II Deacetylase from the Multidrug-Resistant PathogenBiochemistry · 2023Article
- Sirtuin-3-Mediated Cellular Metabolism Links Cardiovascular Remodeling with Hypertension.Biology · 2023Review
- Macrocyclic Octapeptide Binding and Inferences on Protein Substrate Binding to Histone Deacetylase 6.ACS chemical biology · 2023Article
13 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Sir2 proteins, or sirtuins, are a family of enzymes that catalyze NAD(+)-dependent deacetylation reactions and can also process ribosyltransferase, demalonylase, and desuccinylase activities. More than 40 crystal structures of sirtuins have been determined, alone or in various liganded forms. These high-resolution architectural details lay the foundation for understanding the molecular mechanisms of catalysis, regulation, substrate specificity, and inhibition of sirtuins. In this minireview, we summarize these structural features and discuss their implications for understanding sirtuin function.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.