Evidence map›Paper›PMID 34791727›Full record

ArticleProtein science : a publication of the Protein Society2022

Reconstitution and use of highly active human CDK1:Cyclin-B:CKS1 complexes.

Pim J Huis In 't Veld, Sabine Wohlgemuth, Carolin Koerner, Franziska Müller, Petra Janning, Andrea Musacchio

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 30 citations in OpenAlex.

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  17. Reconstitution and use of highly active human CDK1:Cyclin-B:CKS1 complexes.Protein science : a publication of the Protein Society · 2022
    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

6 authors at 1 institution in 1 country.

Pim J Huis In 't VeldDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0003-0234-6390
Sabine WohlgemuthDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Carolin KoernerDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Franziska MüllerDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Petra JanningDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Andrea MusacchioDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0003-2362-8784
Max Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As dividing cells transition into mitosis, hundreds of proteins are phosphorylated by a complex of cyclin-dependent kinase 1 (CDK1) and Cyclin-B, often at multiple sites. CDK1:Cyclin-B phosphorylation patterns alter conformations, interaction partners, and enzymatic activities of target proteins and need to be recapitulated in vitro for the structural and functional characterization of the mitotic protein machinery. This requires a pure and active recombinant kinase complex. The kinase activity of CDK1 critically depends on the phosphorylation of a Threonine residue in its activation loop by a CDK1-activating kinase (CAK). We developed protocols to activate CDK1:Cyclin-B either in vitro with purified CAKs or in insect cells through CDK-CAK co-expression. To boost kinase processivity, we reconstituted a ternary complex consisting of CDK1, Cyclin-B, and CKS1. In this work, we provide and compare detailed protocols to obtain and use highly active CDK1:Cyclin-B (CC) and CDK1:Cyclin-B:CKS1 (CCC).

Indexed as

CDC2 Protein KinaseMitosisHumansPhosphorylationCDC2 Protein KinaseCDK1 protein, humanCDK1cell cycleCKS1cyclincyclin-Bcyclin dependent kinasephosphorylationphostagprocessivityrecombinant protein

Identifiers

PMID34791727
PMCPMC8819839
OpenAlexW3212990032

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.