Evidence map›Paper›PMID 37540427›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Transfection and Thermotolerance Methods for Analysis of miR-570 Targeting the HSP Chaperone Network.

Yuka Okusha, Stuart K Calderwood

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 63% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

2 authors at 1 institution in 1 country.

Yuka OkushaBeth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.
Stuart K CalderwoodBeth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA. scalderw@bidmc.harvard.edu.
Harvard University · US

Funding

Complex Role of HSF1 in Breast CancerR01CA176326 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI CALDERWOOD, STUART KEITH, SHERMAN, MICHAEL Y · 2014 to 2018
$1.8M
NCI NIH HHS R01 CA176326
6 · The paper itself

Abstract

Heat shock proteins (HSPs) are key stress proteins induced in cells exposed to proteotoxic insult and are critical for thermotolerance. The dynamic network of chaperone interactions, known as the chaperome, contributes significantly to the proteotoxic cell response and the malignant phenotype in cancer. We identified a potent microRNA, miR-570 that could bind the 3'untranslated regions of multiple HSP mRNAs and inhibit HSP synthesis. Here, we will introduce the transfection and thermotolerance methods for analysis of miR-570 targeting the HSP chaperone network.

Indexed as

MicroRNAsThermotoleranceHeat-Shock ProteinsHot TemperatureMolecular ChaperonesTransfectionHeat-Shock ProteinsMicroRNAsMolecular ChaperonesBAG3Breast cancerHeat shock proteinMicroRNA570Thermotolerance

Identifiers

PMID37540427
OpenAlexW4385564396

What OpenQuestion holds

Textmetadata
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.