Evidence map›Paper›PMID 33877599›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Indirect Detection of Ligand Binding by Thermal Melt Analysis.

Joseph Shaw, Christopher Stubbs

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.1field-weighted citation impact, top 21% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Review
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.

Joseph ShawDiscovery Biology, Discovery Sciences, IMED Biotech Unit, AstraZeneca, Cambridge, UK. joseph.shaw@astrazeneca.com.
Christopher StubbsDiscovery Biology, Discovery Sciences, IMED Biotech Unit, AstraZeneca, Cambridge, UK.
AstraZeneca (United Kingdom) · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A thermal shift assay (TSA) involves measuring the effect of a compound on the thermal stability of a protein as an indirect measure of ligand binding. In this chapter, we provide a protocol for a conventional TSA with recombinant/purified proteins using differential scanning fluorimetry (DSF), followed by a protocol for a Cellular Thermal Shift Assay (CETSA

Indexed as

Biophysical PhenomenaFluorometryHigh-Throughput Screening AssaysLigandsProtein BindingProtein StabilityRecombinant ProteinsLigandsRecombinant ProteinsCellular Thermal Shift AssayCETSADifferential scanning fluorimetryDSFLigand bindingTarget engagementThermal shift assayTSA

Identifiers

PMID33877599
OpenAlexW3153696296

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.