Evidence map›Paper›PMID 30858169›Full record

ArticleThe Biochemical journal2019

Solution structures and biophysical analysis of full-length group A PAKs reveal they are monomeric and auto-inhibited in

Fiona J Sorrell, Lena Marie Kilian, Jonathan M Elkins

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

11 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Targeting p21-activated kinase 1 for development of a novel anti-arrhythmic drug class.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  5. Review
  6. Rho family GTPase signaling through type II p21-activated kinases.Cellular and molecular life sciences : CMLS · 2022
    Review
  7. Review
  8. Review
  9. Review
  10. Targeting Rho GTPase Signaling Networks in Cancer.Frontiers in cell and developmental biology · 2020
    Review
  11. 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

3 authors at 2 institutions in 2 countries.

Fiona J SorrellStructural Genomics Consortium, University of Oxford, Old Road Campus Research Building, Roosevelt Drive, Oxford OX3 7DQ, U.K.
Lena Marie KilianStructural Genomics Consortium, University of Oxford, Old Road Campus Research Building, Roosevelt Drive, Oxford OX3 7DQ, U.K.
Jonathan M ElkinsStructural Genomics Consortium, University of Oxford, Old Road Campus Research Building, Roosevelt Drive, Oxford OX3 7DQ, U.K. jon.elkins@sgc.ox.ac.uk.ORCID 0000-0003-2858-8929
University of Oxford · GBUniversidade Estadual de Campinas (UNICAMP) · BR

Funding

Wellcome Trust 106169/ZZ14/Z
6 · The paper itself

Abstract

The group A p21-activated kinases (PAKs) exist in an auto-inhibited form until activated by GTPase binding and auto-phosphorylation. In the auto-inhibited form, a regulatory domain binds to the kinase domain (KD) blocking the binding of substrates, and CDC42 or Rac binding to the regulatory domain relieves this auto-inhibition allowing auto-phosphorylation on the KD activation loop. We have determined the crystal structure of the PAK3 catalytic domain and by small angle X-ray scattering, the solution-phase structures of full-length inactive PAK1 and PAK3. The structures reveal a compact but elongated molecular shape that demonstrates that, together with multiple independent biophysical measurements and in contrast with previous assumptions, group A PAKs are monomeric both before and after activation, consistent with an activation mechanism of

Indexed as

Binding SitesBiophysical PhenomenaCatalytic Domaincdc42 GTP-Binding ProteinCrystallography, X-RayEnzyme ActivationHumansKineticsModels, Molecularp21-Activated KinasesPhosphorylationProtein ConformationRecombinant ProteinsScattering, Small AngleSolutionsX-Ray Diffractioncdc42 GTP-Binding ProteinCDC42 protein, humanp21-Activated KinasesPAK1 protein, humanPAK3 protein, humanRecombinant ProteinsSolutionskinaseSAXSstructure

Identifiers

PMID30858169
PMCPMC6448136
OpenAlexW2921363092

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.