Evidence map›Paper›PMID 37850630›Full record

ArticleeLife2023

Probing conformational dynamics to understand kinase inhibition.

Ian R Outhwaite, Markus A Seeliger

Open access · goldAbstract readEditorial
In one paragraph

Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.8field-weighted citation impact, top 26% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
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.

Ian R OuthwaiteDepartment of Pharmacological Sciences, Stony Brook University, Stony Brook, United States.ORCID 0000-0003-2037-3261
Markus A SeeligerDepartment of Pharmacological Sciences, Stony Brook University, Stony Brook, United States.ORCID 0000-0003-0990-1756
Stony Brook University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Why do some inhibitors select the on-state in ERK2, a kinase that is involved in many signaling pathways in cells, whereas others bind to more than one conformation?

Indexed as

Signal TransductionPhosphorylationProtein Conformationallosteric regulationbiochemistrychemical biologyERK2hydrogen-deuterium exchange mass spectrometryinhibitorMAP kinaseNMRnone

Identifiers

PMID37850630
PMCPMC10584368
OpenAlexW4387729019

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.