Evidence map›Paper›PMID 16100261›Full record

ArticleBiophysical journal2005

Solution AFM studies of human Swi-Snf and its interactions with MMTV DNA and chromatin.

H Wang, R Bash, S M Lindsay, D Lohr

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

6 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Architecture of the SWI/SNF-nucleosome complex.Molecular and cellular biology · 2008
    Article
  3. Article
  4. Article
  5. Article
  6. Review
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

4 authors at 1 institution in 1 country.

H WangArizona Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA.
R Bash
S M Lindsay
D Lohr
Arizona State University · US

Funding

New SPM Methods to Study Chromatin RemodelingR01CA085990 · NCI · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI LINDSAY, STUART · 2001 to 2005
$1.5M
NCI NIH HHS CA 85990
6 · The paper itself

Abstract

ATP-dependent nucleosome remodeling complexes are crucial for relieving nucleosome repression during transcription, DNA replication, recombination, and repair. Remodeling complexes can carry out a variety of reactions on chromatin substrates but precisely how they do so remains a topic of active inquiry. Here, a novel recognition atomic force microscopy (AFM) approach is used to characterize human Swi-Snf (hSwi-Snf) nucleosome remodeling complexes in solution. This information is then used to locate hSwi-Snf complexes bound to mouse mammary tumor virus promoter nucleosomal arrays, a natural target of hSwi-Snf action, in solution topographic AFM images of surface-tethered arrays. By comparing the same individual chromatin arrays before and after hSwi-Snf activation, remodeling events on these arrays can be monitored in relation to the complexes bound to them. Remodeling is observed to be: inherently heterogeneous; nonprocessive; able to occur near and far from bound complexes; often associated with nucleosome height decreases. These height decreases frequently occur near sites of DNA release from chromatin. hSwi-Snf is usually incorporated into nucleosomal arrays, with multiple DNA strands entering into it from various directions, + or - ATP; these DNA paths can change after hSwi-Snf activation. hSwi-Snf appears to interact with naked mouse mammary tumor virus DNA somewhat differently than with chromatin and ATP activation of surface-bound DNA/hSwi-Snf produces no changes detectable by AFM.

Indexed as

Adenosine TriphosphateChromatinChromosomal Proteins, Non-HistoneChromosomesDNAHeLa CellsHumansMammary Tumor Virus, MouseMicroscopy, Atomic ForceNuclear ProteinsNucleosomesProtein BindingProtein ConformationProtein Structure, TertiaryTranscription FactorsAdenosine TriphosphateChromatinChromosomal Proteins, Non-HistoneDNANuclear ProteinsNucleosomesTranscription Factors

Identifiers

PMID16100261
PMCPMC1366835
OpenAlexW2019037586

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.