Evidence map›Paper›PMID 41501934›Full record

ArticleBiology direct2026

A phospho-switch to trigger mitotic chromosome condensation.

Alessandro Borsellini

Abstract read
In one paragraph

Article in Biology direct, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Review
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

1 author.

Alessandro BorselliniHuman Technopole, Viale Rita Levi-Montalcini 1, Milan, Italy. alessandro.borsellini@fht.org.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of the most eye-catching events in cell biology is the condensation of chromosomes. During mitosis, the diffuse interphase chromatin rearranges into compact, rod-shaped chromosomes that can be precisely segregated between the daughter cells. This drastic reorganization of the DNA relies on condensin I and II complexes, large ring-shaped ATPases that extrude and stabilize loops of DNA. Since condensin II is always present in the nucleous its activity is repressed by the protein MCPH1 during interphase. But what are the molecular mechanisms regulating the activation of condensin II? New evidence suggests that this activation depends on the interaction between the condensin II subunit CAP-G2 with the centromeric protein M18BP1. Both the repressor and the activator bind on the same subunit of condensin II and their alternative binding is regulated by phosphorylation, which acts as the signal to trigger DNA condensation by condensin II.

Indexed as

Adenosine TriphosphatasesChromosomesDNA-Binding ProteinsMitosisMultiprotein ComplexesAnimalsBiomolecular CondensatesHumansPhosphorylationAdenosine Triphosphatasescondensin complexesDNA-Binding ProteinsMultiprotein ComplexesChromosome condensationCondensin IIM18BP1MitosisSMC complexes

Identifiers

PMID41501934
PMCPMC12781423

What OpenQuestion holds

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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.