Evidence map›Paper›PMID 18481156›Full record

ArticleJournal of fluorescence2009

Nucleosome dynamics as studied by single-pair fluorescence resonance energy transfer: a reevaluation.

Miroslav Tomschik, Ken van Holde, Jordanka Zlatanova

Abstract read
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In one paragraph

Article in Journal of fluorescence, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
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  4. Review
  5. Article
  6. Nucleosomes undergo slow spontaneous gaping.Nucleic acids research · 2015
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  11. Review
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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

3 authors.

Miroslav TomschikDepartment of Molecular Biology, College of Agriculture, University of Wyoming, Laramie, WY 82071, USA. mitom@uwyo.edu
Ken van Holde
Jordanka Zlatanova

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Accessibility of nucleosomal DNA to protein factor binding is ensured by at least three mechanisms: post-synthetic modifications to the histones, chromatin remodeling, and spontaneous unwrapping of the DNA from the histone core. We have previously used single-pair fluorescence resonance energy transfer (spFRET) experiments to investigate long-range conformational fluctuations in nucleosomal DNA (Tomschik M, Zheng H, van Holde K, Zlatanova J, Leuba SH in Proc Natl Acad Sci USA 102(9):3278-3283, 2005). Recent work has drawn attention to a major artifact in such studies due to photoblinking of the acceptor fluorophore. We have now used formaldehyde-crosslinked nucleosomes and imaging in the presence of Trolox, an efficient triplet-state quencher that suppresses photoblinking, to reevaluate our previous conclusions. Careful analysis of the data indicates that most of the events previously characterized as nucleosome 'opening' must have corresponded to photoblinking. There is, nevertheless, evidence for the existence of infrequent, rapid opening events.

Indexed as

Fluorescence Resonance Energy TransferChromansDNAFormaldehydeMercaptoethanolNucleic Acid ConformationNucleosomesTime Factors6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acidChromansDNAFormaldehydeMercaptoethanolNucleosomes

Identifiers

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.