ArticleThe Journal of biological chemistry2017
Sirtuin 2 mutations in human cancers impair its function in genome maintenance.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 38 citations in OpenAlex.
- MRE11 deacetylation by SIRT2 promotes DNA binding to facilitate DNA end resection and ATM-dependent signaling.The Journal of clinical investigation · 2026Article
- BubR1 and SIRT2: Insights into aneuploidy, aging, and cancer.Seminars in cancer biology · 2024Review
- Emerging role of sirtuins in non‑small cell lung cancer (Review).Oncology reports · 2024Review
- Multifaceted regulation of sirtuin 2 (Sirt2) deacetylase activity.The Journal of biological chemistry · 2024Article
- DNA-PK is activated by SIRT2 deacetylation to promote DNA double-strand break repair by non-homologous end joining.Nucleic acids research · 2023Article
- Why Is Longevity Still a Scientific Mystery? Sirtuins-Past, Present and Future.International journal of molecular sciences · 2022Review
- SAMHD1 deacetylation by SIRT1 promotes DNA end resection by facilitating DNA binding at double-strand breaks.Nature communications · 2022Article
- Protocol forSTAR protocols · 2022Article
- Fueling genome maintenance: On the versatile roles of NADThe Journal of biological chemistry · 2022Review
- Quantitative proteomic analysis of the lysine acetylome reveals diverse SIRT2 substrates.Scientific reports · 2022Article
- Emerging role of SIRT2 in non-small cell lung cancer.Oncology letters · 2021Review
- Protein Acetylation at the Interface of Genetics, Epigenetics and Environment in Cancer.Metabolites · 2021Review
- SIRT2 promotes BRCA1-BARD1 heterodimerization through deacetylation.Cell reports · 2021Article
- NADSignal transduction and targeted therapy · 2021Review
- Active nuclear import of the deacetylase Sirtuin-2 is controlled by its C-terminus and importins.Scientific reports · 2020Article
- Subcellular compartmentalization of NADPharmacology & therapeutics · 2019Review
- Acetylation regulates ribonucleotide reductase activity and cancer cell growth.Nature communications · 2019Article
- Article
- DNA Repair: Translation to the Clinic.Clinical oncology (Royal College of Radiologists (Great Britain)) · 2019Review
- Sirtuins in B lymphocytes metabolism and function.World journal of experimental medicine · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Sirtuin 2 (SIRT2) is a sirtuin family deacetylase, which maintains genome integrity and prevents tumorigenesis. Although
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.