ArticleJournal of molecular biology2014
Structural and functional analysis of human SIRT1.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.
What it found
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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
104 citing papers in PubMed, 163 citations in OpenAlex.
- SIRT1 Exon 2-Encoded IDR Gates CREB-Dependent Transcriptional Timing During Fasting.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Factors Determining Sirtuin-1 Target Engagement.Advanced biology · 2026Review
- Article
- Computational Insights into SIRT1: Elucidating Mutational Impact on SIRT1-RECQL4 Structural Dynamics.Cell biochemistry and biophysics · 2026Article
- Expression and Transcriptional Response of sirt1 in Yellow Catfish (Pelteobagrus fulvidraco) Under Acute Hypoxia Stress.Animals : an open access journal from MDPI · 2026Article
- Evaluation of Sirtuin 1 (SIRT1) and Sirtuin 3 (SIRT3) in serum and cerebrospinal fluid following fatal traumatic brain injury.International journal of legal medicine · 2026Article
- In Silico Identification of Natural SIRT1 Inhibitors through Molecular Docking, Dynamics Simulation, and MM/PBSA.Cell biochemistry and biophysics · 2026Article
- Lactylation in cancer: molecular mechanisms and advances in clinical study.Molecular cancer · 2026Review
- Computational and experimental analysis of oleanolic acid as an allosteric activator of SIRT1.Turkish journal of chemistry · 2026Article
- Berbamine sensitizes hepatocellular carcinoma to chemotherapy by inhibiting autophagyFrontiers in pharmacology · 2026Article
- Elucidating binding hot spots and structural stability in sirtuin family proteins for selective inhibitors: a computational approach.Frontiers in bioinformatics · 2026Article
- Influence of Certain Natural Bioactive Compounds on Glycemic Control: A Narrative Review.Nutrients · 2025Review
- Article
- SIRT1 as a potential target for age-related eye diseases: mechanisms and therapeutic strategies.Human cell · 2025Review
- Article
- Sirtuins in Central Nervous System Tumors-Molecular Mechanisms and Therapeutic Targeting.Cells · 2025Review
- Structural and enzymatic plasticity of SIRT6 deacylase activity.The Journal of biological chemistry · 2025Article
- SIRT5: a potential target for discovering bioactive natural products.Journal of natural medicines · 2025Review
- Insights Into the Therapeutic Potential of SIRT1-modifying Compounds for Alzheimer's Disease: A Focus on Molecular Mechanisms.Journal of molecular neuroscience : MN · 2025Review
- Article
44 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
3 authors at 1 institution in 1 country.
Funding
Abstract
SIRT1 is a NAD(+)-dependent deacetylase that plays important roles in many cellular processes. SIRT1 activity is uniquely controlled by a C-terminal regulatory segment (CTR). Here we present crystal structures of the catalytic domain of human SIRT1 in complex with the CTR in an open apo form and a closed conformation in complex with a cofactor and a pseudo-substrate peptide. The catalytic domain adopts the canonical sirtuin fold. The CTR forms a β hairpin structure that complements the β sheet of the NAD(+)-binding domain, covering an essentially invariant hydrophobic surface. The apo form adopts a distinct open conformation, in which the smaller subdomain of SIRT1 undergoes a rotation with respect to the larger NAD(+)-binding subdomain. A biochemical analysis identifies key residues in the active site, an inhibitory role for the CTR, and distinct structural features of the CTR that mediate binding and inhibition of the SIRT1 catalytic domain.
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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.