Evidence map›Paper›PMID 27139824›Full record

ArticleActa crystallographica. Section F, Structural biology communications2016

Co-crystal structures of the protein kinase haspin with bisubstrate inhibitors.

Darja Lavogina, Katrin Kestav, Apirat Chaikuad, Christina Heroven, Stefan Knapp, Asko Uri

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

2 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. 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 3 institutions in 2 countries.

Darja LavoginaInstitute of Chemistry, University of Tartu, Ravila 14A, 50411 Tartu, Estonia.
Katrin KestavInstitute of Chemistry, University of Tartu, Ravila 14A, 50411 Tartu, Estonia.
Apirat ChaikuadNuffield Department of Clinical Medicine, Structural Genomics Consortium, University of Oxford, Old Road Campus Research Building, Oxford OX3 7DQ, England.
Christina HerovenNuffield Department of Clinical Medicine, Structural Genomics Consortium, University of Oxford, Old Road Campus Research Building, Oxford OX3 7DQ, England.
Stefan KnappNuffield Department of Clinical Medicine, Structural Genomics Consortium, University of Oxford, Old Road Campus Research Building, Oxford OX3 7DQ, England.
Asko UriInstitute of Chemistry, University of Tartu, Ravila 14A, 50411 Tartu, Estonia.
University of Tartu · EEUniversity of Oxford · GBGenomics England · GB

Funding

Wellcome TrustWellcome Trust 092809/Z/10/Z
6 · The paper itself

Abstract

Haspin is a mitotic protein kinase that is responsible for the phosphorylation of Thr3 of histone H3, thereby creating a recognition motif for docking of the chromosomal passenger complex that is crucial for the progression of cell division. Here, two high-resolution models of haspin with previously reported inhibitors consisting of an ATP analogue and a histone H3(1-7) peptide analogue are presented. The structures of the complexes confirm the bisubstrate character of the inhibitors by revealing the signature binding modes of the moieties targeting the ATP-binding site and the protein substrate-binding site of the kinase. This is the first structural model of a bisubstrate inhibitor targeting haspin. The presented structural data represent a model for the future development of more specific haspin inhibitors.

Indexed as

HumansIntracellular Signaling Peptides and ProteinsProtein ConformationProtein Kinase InhibitorsProtein Serine-Threonine KinasesSubstrate SpecificityHASPIN protein, humanIntracellular Signaling Peptides and ProteinsProtein Kinase InhibitorsProtein Serine-Threonine Kinasesbisubstratehaspinhistoneinhibitorlinkerprotein kinase

Identifiers

PMID27139824
PMCPMC4854560
OpenAlexW2341613060

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.