Evidence map›Paper›PMID 29791843›Full record

ArticleCell reports2018

Cell-Cycle Regulation of Dynamic Chromosome Association of the Condensin Complex.

Rahul Thadani, Julia Kamenz, Sebastian Heeger, Sofía Muñoz, Frank Uhlmann

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 48 citations in OpenAlex.

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  7. Targeting RAD52 overcomes PARP inhibitor resistance in preclinicalbioRxiv : the preprint server for biology · 2025
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  8. Mitotic genome folding.The Journal of cell biology · 2025
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  16. Role and mechanism ofFrontiers in pharmacology · 2024
    Article
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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

5 authors at 1 institution in 2 countries.

Rahul ThadaniChromosome Segregation Laboratory, The Francis Crick Institute, London NW1 1AT, UK; Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Julia KamenzChromosome Segregation Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
Sebastian HeegerChromosome Segregation Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
Sofía MuñozChromosome Segregation Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
Frank UhlmannChromosome Segregation Laboratory, The Francis Crick Institute, London NW1 1AT, UK. Electronic address: frank.uhlmann@crick.ac.uk.
The Francis Crick Institute · GB

Funding

Cancer Research UKMedical Research CouncilWellcome Trust
6 · The paper itself

Abstract

Eukaryotic cells inherit their genomes in the form of chromosomes, which are formed from the compaction of interphase chromatin by the condensin complex. Condensin is a member of the structural maintenance of chromosomes (SMC) family of ATPases, large ring-shaped protein assemblies that entrap DNA to establish chromosomal interactions. Here, we use the budding yeast Saccharomyces cerevisiae to dissect the role of the condensin ATPase and its relationship with cell-cycle-regulated chromosome binding dynamics. ATP hydrolysis-deficient condensin binds to chromosomes but is defective in chromosome condensation and segregation. By modulating the ATPase, we demonstrate that it controls condensin's dynamic turnover on chromosomes. Mitosis-specific phosphorylation of condensin's Smc4 subunit reduces the turnover rate. However, reducing turnover by itself is insufficient to compact chromosomes. We propose that condensation requires fine-tuned dynamic condensin interactions with more than one DNA. These results enhance our molecular understanding of condensin function during chromosome condensation.

Indexed as

Cell CycleAdenosine TriphosphatasesCell ProliferationChromosome SegregationChromosomes, FungalDNA-Binding ProteinsDNA, RibosomalHydrolysisMultiprotein ComplexesMutationPhosphorylationProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine Triphosphatasescondensin complexesDNA-Binding ProteinsDNA, RibosomalMultiprotein ComplexesSaccharomyces cerevisiae ProteinsABC ATPasecell cyclechromosome condensationcondensinmitosisphosphorylationSaccharomyces cerevisiae

Identifiers

PMID29791843
PMCPMC5986713
OpenAlexW2803563092

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.