Evidence map›Paper›PMID 39700017›Full record

ReviewBiochemical Society transactions2024

Adding a twist to the loops: the role of DNA superhelicity in the organization of chromosomes by SMC protein complexes.

Antonio Valdés, Christian H Haering

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2024. 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
–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

2 citing papers in PubMed.

  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

2 authors.

Antonio ValdésChair of Biochemistry and Cell Biology, Biocenter, Julius-Maximilians-Universität of Würzburg, Wurzburg, Germany.ORCID 0000-0002-9119-3092
Christian H HaeringChair of Biochemistry and Cell Biology, Biocenter, Julius-Maximilians-Universität of Würzburg, Wurzburg, Germany.ORCID 0000-0001-8301-1722

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural maintenance of chromosomes (SMC) protein complexes, including cohesin, condensin, and the Smc5/6 complex, are integral to various processes in chromosome biology. Despite their distinct roles, these complexes share two key properties: the ability to extrude DNA into large loop structures and the capacity to alter the superhelicity of the DNA double helix. In this review, we explore the influence of eukaryotic SMC complexes on DNA topology, debate its potential physiological function, and discuss new structural insights that may explain how these complexes mediate changes in DNA topology.

Indexed as

Cell Cycle ProteinsChromosomal Proteins, Non-HistoneChromosomesCohesinsDNA-Binding ProteinsMultiprotein ComplexesAdenosine TriphosphatasesAnimalsDNADNA, SuperhelicalHumansNucleic Acid ConformationAdenosine TriphosphatasesCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinscondensin complexesDNADNA-Binding ProteinsDNA, SuperhelicalMultiprotein ComplexescohesincondensinDNA loop extrusionDNA topologySMC complextopoisomerase

Identifiers

PMID39700017
PMCPMC11668287

What Socratic 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 Socratic graph.