Evidence map›Paper›PMID 41111108›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Bulk FRET Analysis of the Conformation of the Cohesin Ring.

Torahiko L Higashi

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. 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

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.

Torahiko L HigashiResearch Division, Chugai Pharmaceutical Co. Ltd., Yokohama, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cohesin is a member of the SMC protein family that exerts its chromosome functions by holding district DNA segments together using the ring structure. Topological cohesin loading involves complex, dynamic structural changes; these transitions are tightly linked to the initial cohesin association with DNA and subsequent DNA entrapment, which occurs through the transient opening of the ring at the interfaces between subunits. This chapter describes a method of monitoring the conformational changes of fission yeast cohesin that combines biochemical reconstitution and fluorescence resonance energy transfer (FRET). This method is useful for studying the structural dynamics and protein-protein interactions of not only cohesin but also other SMC proteins.

Indexed as

Cell Cycle ProteinsChromosomal Proteins, Non-HistoneFluorescence Resonance Energy TransferSchizosaccharomycesSchizosaccharomyces pombe ProteinsCohesinsProtein BindingProtein ConformationCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsSchizosaccharomyces pombe ProteinsATP hydrolysisCohesin structureFRETIn vitro reconstitutionS. pombe

Identifiers

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.