Evidence map›Paper›PMID 24005907›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2013

Visualization of human Bloom's syndrome helicase molecules bound to homologous recombination intermediates.

Máté Gyimesi, Ricardo H Pires, Neil Billington, Kata Sarlós, Zsuzsa S Kocsis, Károly Módos, Miklós S Z Kellermayer, Mihály Kovács

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In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

14 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
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  4. The convergence of head-on DNA unwinding forks induces helicase oligomerization and activity transition.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Mechanism of Bloom syndrome complex assembly required for double Holliday junction dissolution and genome stability.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

8 authors at 3 institutions in 2 countries.

Máté Gyimesi3Department of Biochemistry, Eötvös University, Pázmány P. s. 1/c, H-1117 Budapest, Hungary. kovacsm@elte.hu.
Ricardo H Pires
Neil Billington
Kata Sarlós
Zsuzsa S Kocsis
Károly Módos
Miklós S Z Kellermayer
Mihály Kovács
Eötvös Loránd University · HUSemmelweis University · HUNational Heart Lung and Blood Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Homologous recombination (HR) is a key process in the repair of double-stranded DNA breaks (DSBs) that can initiate cancer or cell death. Human Bloom's syndrome RecQ-family DNA helicase (BLM) exerts complex activities to promote DSB repair while avoiding illegitimate HR. The oligomeric assembly state of BLM has been a key unresolved aspect of its activities. In this study we assessed the structure and oligomeric state of BLM, in the absence and presence of key HR-intermediate DNA structures, by using single-molecule visualization (electron microscopic and atomic force microscopic single-particle analysis) and solution biophysical (dynamic light scattering, kinetic and equilibrium binding) techniques. Besides full-length BLM, we used a previously characterized truncated construct (BLM(642-1290)) as a monomeric control. Contrary to previous models proposing a ring-forming oligomer, we found the majority of BLM molecules to be monomeric in all examined conditions. However, BLM showed a tendency to form dimers when bound to branched HR intermediates. Our results suggest that HR activities requiring single-stranded DNA translocation are performed by monomeric BLM, while complex DNA structures encountered and dissolved by BLM in later stages of HR induce partial oligomerization of the helicase.

Indexed as

Homologous RecombinationAdenosine TriphosphateAmino Acid SequenceDNA, Single-StrandedHumansHydrolysisMolecular Sequence DataProtein BindingProtein MultimerizationRecQ HelicasesAdenosine TriphosphateBloom syndrome proteinDNA, Single-StrandedRecQ Helicasesatomic force microscopyDNA repairelectron microscopyoligomerizationstructure

Identifiers

PMID24005907
PMCPMC3834772
OpenAlexW2074143935

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.