Evidence map›Paper›PMID 41341165›Full record

ArticlebioRxiv : the preprint server for biology2025

Aberrant cohesin function in

Gurvir Singh, Robert V Skibbens

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Gurvir SinghDepartment of Biological Sciences, Lehigh University, 111 Research Drive, Bethlehem, Pennsylvania, 18015. United States of America.
Robert V SkibbensDepartment of Biological Sciences, Lehigh University, 111 Research Drive, Bethlehem, Pennsylvania, 18015. United States of America.ORCID 0000-0003-4216-8306

Funding

Novel targets of the Roberts Syndrome acetyltransferase Esco2/Eco1R15GM139097 · NIGMS · LEHIGH UNIVERSITY · PI SKIBBENS, ROBERT · 2020 to 2020
$469k
NIGMS NIH HHS R15 GM139097
6 · The paper itself

Abstract

The cohesin complex is composed of core ring proteins (Smc1, Smc3 and Mcd1) and associated factors (Pds5, Scc3, and Rad61) that bind via Mcd1. Extrusion (looping from within a single DNA molecule) and cohesion (the tethering together of two different DNA molecules) underlie the many roles that cohesins play in chromosome segregation, gene transcription, DNA repair, chromosome condensation, replication fork progression, and genome organization. While cohesin functions flank the activities of critical cell checkpoints (including spindle assembly and DNA damage checkpoints), the extent to which checkpoints directly target cohesins, in response to aberrant cohesin function, remains unknown. Based on prior evidence that cells mutated for cohesin contain reduced Mcd1 protein, we tested whether loss of Mcd1 is based simply on cohesin instability or integrity. The results show that Mcd1 loss persists even in

Indexed as

Checkpointschromosome condensationCohesinsCornelia de Lange Syndrome (CdLS)Das1E3 ligaseEco1/Ctf7/ESCO2Mcd1/Scc1/RAD21Rad61/WAPLRoberts Syndrome (RBS)San1sister chromatid cohesion

Identifiers

PMID41341165
PMCPMC12670631

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.