Evidence map›Paper›PMID 17150039›Full record

ArticleThe Biochemical journal2007

A sharper instrument for dissecting signalling events: a specific AGC kinase inhibitor.

Christopher G Proud

Abstract readComment
In one paragraph

Article in The Biochemical journal, 2007. 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
–field-weighted citation impact
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.

  1. ROCK and Rho: biochemistry and neuronal functions of Rho-associated protein kinases.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2007
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

Christopher G ProudDepartment of Biochemistry and Molecular Biology, Life Sciences Institute, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, Canada V6T 1Z3. cgpr@interchange.ubc.ca

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small-molecule inhibitors are now widely used to try to dissect regulatory signalling events. Many of these interfere with the function of protein kinases, often as part of signalling cascades. In addition to their utility as tools for the researcher, the long-term aspiration is that certain of these compounds may be useful as therapeutic agents for the treatment of conditions that arise from the dysregulation of specific signalling pathways. In this issue of the Biochemical Journal, Sapkota and colleagues report the identification and initial validation of a compound that inhibits the RSK (p90 ribosomal S6 kinase) group of protein kinases, which are members of an important family of kinases (the 'AGC kinases') that have overlapping specificities.

Indexed as

Signal TransductionCell LineEnzyme InhibitorsGenome, HumanHumansMitogen-Activated Protein Kinase KinasesMutationPhosphoric Triester HydrolasesPhosphoserinePhosphothreonineProtein KinasesRibosomal Protein S6 Kinases, 90-kDaTOR Serine-Threonine KinasesEnzyme InhibitorsMitogen-Activated Protein Kinase Kinasesmitogen and stress-activated protein kinase 1MTOR protein, humanPhosphoric Triester HydrolasesPhosphoserinePhosphothreonineProtein KinasesRibosomal Protein S6 Kinases, 90-kDaTOR Serine-Threonine Kinases

Identifiers

PMID17150039
PMCPMC1698685

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.