Evidence map›Paper›PMID 30570821›Full record

ArticleAngewandte Chemie (International ed. in English)2019

Ion Mobility Mass Spectrometry Measures the Conformational Landscape of p27 and its Domains and how this is Modulated upon Interaction with Cdk2/cyclin A.

Rebecca Beveridge, Lukasz G Migas, Richard W Kriwacki, Perdita E Barran

Open access · greenAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

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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

4 authors at 2 institutions in 2 countries.

Rebecca BeveridgeThe Michael Barber Centre for Collaborative Mass Spectrometry, The School of Chemistry, Manchester Institute for Biotechnology, University of Manchester, Manchester, UK.ORCID 0000-0003-0320-6496
Lukasz G MigasThe Michael Barber Centre for Collaborative Mass Spectrometry, The School of Chemistry, Manchester Institute for Biotechnology, University of Manchester, Manchester, UK.
Richard W KriwackiStructural Biology, MS 311, Room D1024F, St. Jude Children's Research Hospital, 262 Danny Thomas Place, Memphis, TN, 38105-3678, USA.ORCID 0000-0002-9798-6018
Perdita E BarranThe Michael Barber Centre for Collaborative Mass Spectrometry, The School of Chemistry, Manchester Institute for Biotechnology, University of Manchester, Manchester, UK.ORCID 0000-0002-7720-586X
University of Manchester · GBSt. Jude Children's Research Hospital · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
Biotechnology and Biological Sciences Research Council BB/K017802/1Biotechnology and Biological Sciences Research Council BB/L015048/1Biotechnology and Biological Sciences Research Council BB/M017702/1NCI NIH HHS P30 CA021765NCI NIH HHS P30CA21765
6 · The paper itself

Abstract

Intrinsically disordered proteins have been reported to undergo disorder-to-order transitions upon binding to their partners in the cell. The extent of the ordering upon binding and the lack of order prior to binding is difficult to visualize with classical structure determination methods. Binding of p27 to the Cdk2/cyclin A complex is accompanied by partial folding of p27 in the KID domain, with the retention of dynamic behavior for function, particularly in the C-terminal half of the protein. Herein, native ion mobility mass spectrometry (IM-MS) is employed to measure the intrinsic dynamic properties of p27, both in isolation and within the trimeric complex with Cdk2/cyclin A. The trimeric Cdk2/cyclin A/p27-KID complex possesses significant structural heterogeneity compared to Cdk2/cyclin A. These findings support the formation of a fuzzy complex in which both the N- and C-termini of p27 interact with Cdk2/cyclin A in multiple, closely associated states.

Indexed as

Cyclin ACyclin-Dependent Kinase 2Cyclin-Dependent Kinase Inhibitor p27HumansIntrinsically Disordered ProteinsIon Mobility SpectrometryMass SpectrometryProtein BindingProtein ConformationProtein FoldingProtein Interaction Domains and MotifsProtein Interaction MapsProtein MultimerizationCDK2 protein, humanCyclin ACyclin-Dependent Kinase 2Cyclin-Dependent Kinase Inhibitor p27Intrinsically Disordered Proteinsintrinsically disordered proteinsion mobility mass spectrometryprotein structure

Identifiers

PMID30570821
PMCPMC7122115
OpenAlexW2906668607

What OpenQuestion holds

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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.