Evidence map›Paper›PMID 17196924›Full record

ArticleAnalytical biochemistry2007

Two-component atomic force microscopy recognition imaging of complex samples.

H Wang, R Bash, D Lohr

Open access · greenAbstract read
In one paragraph

Article in Analytical biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

1 citing paper in PubMed, 9 citations in OpenAlex.

  1. AFM of biological complexes: what can we learn?Current opinion in colloid & interface science · 2008
    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

3 authors at 1 institution in 1 country.

H WangBiodesign Institute, Arizona State University, Tempe, AZ 85287-1604, USA.
R Bash
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 R01 CA-085990NCI NIH HHS R01 CA085990
6 · The paper itself

Abstract

Biological complexes are typically multisubunit in nature and the processes in which they participate often involve protein compositional changes in themselves and/or their target substrates. Being able to identify more than one type of protein in complex samples and to track compositional changes during processes would thus be very useful. Toward this goal, we describe here a single-molecule technique that can simultaneously identify two types of proteins in compositionally complex samples. It is an adaptation of the recently developed atomic force microscopy (AFM) recognition imaging technique but involves the tethering of two different types of antibodies to the AFM tip and sequential blocking with appropriate antigenic peptides to distinguish the recognition from each antibody. The approach is shown to be capable of simultaneously identifying in a single AFM image two specific components, BRG1 and beta-actin, of the human Swi-Snf ATP-dependent nucleosome remodeling complex and two types of histones, H2A and H3, in chromatin samples.

Indexed as

ActinsChromatinChromosomal Proteins, Non-HistoneDNADNA HelicasesHistonesHumansMicroscopy, Atomic ForceMultiprotein ComplexesNuclear ProteinsProteinsTranscription FactorsActinsChromatinChromosomal Proteins, Non-HistoneDNADNA HelicasesHistonesMultiprotein ComplexesNuclear ProteinsProteinsSMARCA4 protein, humanSWI-SNF-B chromatin-remodeling complexTranscription Factors

Identifiers

PMID17196924
PMCPMC2071926
OpenAlexW2009093446

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.