Evidence map›Paper›PMID 25827873›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2015

Chromatin imaging with time-lapse atomic force microscopy.

Yuri L Lyubchenko, Luda S Shlyakhtenko

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2015. 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.

Yuri L LyubchenkoDepartment of Pharmaceutical Sciences, University of Nebraska Medical Center, 986025, Nebraska Medical Center, Omaha, NE, 68198-6025, USA, ylyubchenko@unmc.edu.
Luda S Shlyakhtenko

Funding

Structural Characterization of APOBECS's Atomic interactionsP01GM091743 · NIGMS · UNIVERSITY OF MINNESOTA · PI KOTLER, MOSHE · 2011 to 2015
$10.1M
Protein Self-Assembly into NanoaggregatesR01GM096039 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI LYUBCHENKO, YURI L · 2011 to 2018
$2.9M
NIGMS NIH HHS 1R01 GM096039NIGMS NIH HHS P01 GM091743NIGMS NIH HHS R01 GM096039
6 · The paper itself

Abstract

Time-lapse atomic force microscopy (AFM) is widely used for direct visualization of the nanoscale dynamics of various biological systems. The advent of high-speed AFM instrumentation made it possible to image the dynamics of proteins and protein-DNA complexes within millisecond time range. This chapter describes protocols for studies of structure and dynamics of nucleosomes with time-lapse AFM including the high-speed AFM instrument. The necessary specifics for the preparation of chromatin samples for imaging with AFM including the protocols for the surface preparation are provided.

Indexed as

Microscopy, Atomic ForceTime-Lapse ImagingChromatinChromatin Assembly and DisassemblyHistonesNucleosomesProtein MultimerizationChromatinHistonesNucleosomes

Identifiers

PMID25827873
PMCPMC4930652

What OpenQuestion holds

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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.