Evidence map›Paper›PMID 24598913›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

Structure of Aurora B-INCENP in complex with barasertib reveals a potential transinhibitory mechanism.

Fabio Sessa, Fabrizio Villa

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

  1. Discovery of thieno[2,3-RSC advances · 2026
    Article
  2. Discovery of the first-in-class Aurora B kinase selective degrader.European journal of medicinal chemistry · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Aurora B Inhibitors as Cancer Therapeutics.Molecules (Basel, Switzerland) · 2023
    Review
  9. Pharmacophore Synergism in Diverse Scaffold Clinches in Aurora Kinase B.International journal of molecular sciences · 2022
    Article
  10. Review
  11. Article
  12. Cyclopenta[ACS omega · 2020
    Article
  13. Review
  14. Article
  15. Article
  16. Cells Lacking theCancer discovery · 2019
    Article
  17. Article
  18. Review
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Fabio SessaDepartment of Experimental Oncology, European Institute of Oncology, Via Adamello 16, 20139 Milan, Italy.
Fabrizio VillaDepartment of Experimental Oncology, European Institute of Oncology, Via Adamello 16, 20139 Milan, Italy.
European Institute of Oncology · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Aurora family is a well conserved and well characterized group of serine-threonine kinases involved in the normal progression of mitosis. The deregulation of Aurora kinases impairs spindle assembly, checkpoint function and cell division. To date, many small molecules that compete with ATP for binding to Aurora kinases have been developed and characterized. Here, the first structure of the Xenopus laevis Aurora B-INCENP complex bound to the clinically relevant small molecule barasertib was determined. The binding properties of this inhibitor to the Aurora B active site are analyzed and reported. An unexpected crystal-packing contact in the Aurora B-INCENP structure coordinated by an ATP analogue is also reported, in which the INCENP C-terminus occupies the substrate-binding region, resembling the protein kinase A inhibitory mechanism.

Indexed as

Adenylyl ImidodiphosphateAmino Acid SequenceAnimalsAntineoplastic AgentsAurora Kinase BCatalytic DomainChromosomal Proteins, Non-HistoneCrystallography, X-RayHumansHydrogen BondingModels, MolecularMolecular Sequence DataOrganophosphatesProtein BindingProtein Structure, QuaternaryProtein Structure, Secondary2-((3-((4-((5-(2-((3-fluorophenyl)amino)-2-oxoethyl)-1H-pyrazol-3-yl)amino)quinazolin-7-yl)oxy)propyl)(ethyl)amino)ethyl dihydrogen phosphateAdenylyl ImidodiphosphateAntineoplastic AgentsAurora Kinase BChromosomal Proteins, Non-HistoneINCENP protein, XenopusOrganophosphatesQuinazolinesXenopus ProteinsAurora kinasesbarasertibcancerPKAsmall-molecule inhibitors

Identifiers

PMID24598913
PMCPMC3944688
OpenAlexW2127252947

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.