ArticleCell adhesion & migration
Sirt1 and cell migration.
Article in Cell adhesion & migration. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 12 citations in OpenAlex.
- Optical Redox Imaging of Breast Cancer NADH Redox Status Associated with PGC1α Gene Expression.Academic radiology · 2026Article
- SIRT1 inhibits rheumatoid arthritis fibroblast-like synoviocyte aggressiveness and inflammatory response via suppressing NF-κB pathway.Bioscience reports · 2018Article
- Recreational scuba diving: negative or positive effects of oxidative and cardiovascular stress?Biochemia medica · 2014Review
- SIRT1 catalytic activity has little effect on tumor formation and metastases in a mouse model of breast cancer.PloS one · 2013Article
Corrections and comments
- Comment on
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sirt1 is a type III histone deacetylase implicated in a wide range of physiological and pathophysiological roles. Acting though a myriad of non-histone substrates, Sirt1 modulates transcriptional regulation of energy metabolism and stress response, with important consequences on cell survival and a myriad of human pathologies. Sirt1 has an apparent (albeit context- and tissue type-dependent) role in tumorigenesis, acting particularly through its deacetylation of tumor suppressor gene products such as p53 and Rb. Recent works have now revealed that cortactin, an F-actin binding protein with established roles in protrusive actin dynamics, is a Sirt1 substrate. Cortactin could be acetylated by the acetyltransferase p300, and its deacetylation by Sirt1, either directly or indirectly, retards cell migration. In conjunction with deacetylation of other oncogenic targets, Sirt1's modulation of cell migration and invasion may be an important additional aspect of its tumorigenic activity.
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.