Evidence map›Paper›PMID 20730082›Full record

ArticlePloS one2010

Structural comparison of human mammalian ste20-like kinases.

Christopher J Record, Apirat Chaikuad, Peter Rellos, Sanjan Das, Ashley C W Pike, Oleg Fedorov, Brian D Marsden, Stefan Knapp, Wen Hwa Lee

Open access · goldAbstract readComparative Study
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

26 citing papers in PubMed, 51 citations in OpenAlex.

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  17. Cdk5-dependent Mst3 phosphorylation and activity regulate neuronal migration through RhoA inhibition.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  18. Article
  19. Article
  20. Structural insights into the activation of MST3 by MO25.Biochemical and biophysical research communications · 2013
    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

9 authors at 2 institutions in 1 country.

Christopher J RecordStructural Genomics Consortium, University of Oxford, Oxford, United Kingdom.
Apirat Chaikuad
Peter Rellos
Sanjan Das
Ashley C W Pike
Oleg Fedorov
Brian D Marsden
Stefan Knapp
Wen Hwa Lee
University of Oxford · GBGenomics (United Kingdom) · GB

Funding

CIHRWellcome Trust
6 · The paper itself

Abstract

backgroundThe serine/threonine mammalian Ste-20 like kinases (MSTs) are key regulators of apoptosis, cellular proliferation as well as polarization. Deregulation of MSTs has been associated with disease progression in prostate and colorectal cancer. The four human MSTs are regulated differently by C-terminal regions flanking the catalytic domains. PRINCIPAL

findingsWe have determined the crystal structure of kinase domain of MST4 in complex with an ATP-mimetic inhibitor. This is the first structure of an inactive conformation of a member of the MST kinase family. Comparison with active structures of MST3 and MST1 revealed a dimeric association of MST4 suggesting an activation loop exchanged mechanism of MST4 auto-activation. Together with a homology model of MST2 we provide a comparative analysis of the kinase domains for all four members of the human MST family. SIGNIFICANCE: The comparative analysis identified new structural features in the MST ATP binding pocket and has also defined the mechanism for autophosphorylation. Both structural features may be further explored for inhibitors design. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.

Indexed as

Adenosine TriphosphateAmino Acid SequenceBinding SitesBiomimetic MaterialsCrystallography, X-RayEnzyme ActivationHumansModels, MolecularMolecular Sequence DataPhosphorylationProtein ConformationProtein Kinase InhibitorsProtein MultimerizationProtein Serine-Threonine KinasesQuinazolinesSequence Homology, Amino AcidAdenosine TriphosphateProtein Kinase InhibitorsProtein Serine-Threonine KinasesQuinazolines

Identifiers

PMID20730082
PMCPMC2920948
OpenAlexW1991110933

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.