Evidence map›Paper›PMID 28273169›Full record

ArticlePloS one2017

Reversible modulation of SIRT1 activity in a mouse strain.

Katherine V Clark-Knowles, Xiaohong He, Karen Jardine, Josée Coulombe, Danielle Dewar-Darch, Annabelle Z Caron, Douglas A Gray, Michael W McBurney

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 30% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Calcitonin Gene-Related Peptide Attenuates LPS-Induced Acute Kidney Injury by Regulating Sirt1.Medical science monitor : international medical journal of experimental and clinical research · 2020
    Article
  4. Article
  5. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Katherine V Clark-KnowlesProgram in Cancer Therapeutics, Ottawa Hospital Research Institute, Ottawa, Canada.
Xiaohong HeProgram in Cancer Therapeutics, Ottawa Hospital Research Institute, Ottawa, Canada.
Karen JardineProgram in Cancer Therapeutics, Ottawa Hospital Research Institute, Ottawa, Canada.
Josée CoulombeProgram in Cancer Therapeutics, Ottawa Hospital Research Institute, Ottawa, Canada.
Danielle Dewar-DarchProgram in Cancer Therapeutics, Ottawa Hospital Research Institute, Ottawa, Canada.
Annabelle Z CaronProgram in Cancer Therapeutics, Ottawa Hospital Research Institute, Ottawa, Canada.
Douglas A GrayProgram in Cancer Therapeutics, Ottawa Hospital Research Institute, Ottawa, Canada.ORCID http://orcid.org/0000-0002-8634-4984
Michael W McBurneyProgram in Cancer Therapeutics, Ottawa Hospital Research Institute, Ottawa, Canada.ORCID http://orcid.org/0000-0001-6096-3659
Ottawa Hospital · CAUniversity of Ottawa · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SIRT1 protein deacetylase is reported to have a remarkably wide spectrum of biological functions affecting such varied processes as aging, cancer, metabolism, neurodegeneration and immunity. However, the SIRT1 literature is also full of contradictions. To help establish the role(s) of SIRT1 in these and other biological processes, we set out to create a mouse in which the SIRT1 activity could be toggled between on and off states by fusing the estrogen receptor ligand-binding domain (ER) to the C terminus of the SIRT1 protein. We found that the catalytic activity of the SIRT1-ER fusion protein increased 4-5 fold in cells treated with its ligand, 4-hydroxy-tamoxifen (4OHT). The 4OHT-induced activation of SIRT1-ER was due in large part to a 2 to 4-fold increase in abundance of the SIRT1-ER protein in cells in culture and in tissues in vivo. This increase is reversible and is a consequence of 4OHT-induced stabilization of the SIRT1-ER protein. Since changes in SIRT1 level or activity of 2-4 fold are frequently reported to be sufficient to affect its biological functions, this mouse should be helpful in establishing the causal relationships between SIRT1 and the diseases and processes it affects.

Indexed as

AllelesAnimalsBlood GlucoseCatalysisCell LineEnzyme ActivationFemaleGene ExpressionGenotypeMaleMiceMice, KnockoutMice, TransgenicPhenotypeReceptors, EstrogenRecombinant Fusion ProteinsBlood GlucoseReceptors, EstrogenRecombinant Fusion ProteinsSirtuin 1Tamoxifen

Identifiers

PMID28273169
PMCPMC5342236
OpenAlexW2593495535

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.