Evidence map›Paper›PMID 25162908›Full record

ArticleJournal of biomedical optics2014

Re-evaluation of biotin-streptavidin conjugation in Förster resonance energy transfer applications.

Bahar Saremi, Ming-Yuan Wei, Yuan Liu, Bingbing Cheng, Baohong Yuan

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of biomedical optics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. 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

5 authors at 3 institutions in 1 country.

Bahar SaremiUniversity of Texas at Arlington, Department of Bioengineering, Ultrasound and Optical Imaging Laboratory, Arlington, 500 UTA Boulevard, Texas 76010, United StatesbUniversity of Texas at Arlington and University of Texas Southwestern Medical Center at Dal.
Ming-Yuan WeiUniversity of Texas at Arlington, Department of Bioengineering, Ultrasound and Optical Imaging Laboratory, Arlington, 500 UTA Boulevard, Texas 76010, United StatesbUniversity of Texas at Arlington and University of Texas Southwestern Medical Center at Dal.
Yuan LiuUniversity of Texas at Arlington, Department of Bioengineering, Ultrasound and Optical Imaging Laboratory, Arlington, 500 UTA Boulevard, Texas 76010, United StatesbUniversity of Texas at Arlington and University of Texas Southwestern Medical Center at Dal.
Bingbing ChengUniversity of Texas at Arlington, Department of Bioengineering, Ultrasound and Optical Imaging Laboratory, Arlington, 500 UTA Boulevard, Texas 76010, United StatesbUniversity of Texas at Arlington and University of Texas Southwestern Medical Center at Dal.
Baohong YuanUniversity of Texas at Arlington, Department of Bioengineering, Ultrasound and Optical Imaging Laboratory, Arlington, 500 UTA Boulevard, Texas 76010, United StatesbUniversity of Texas at Arlington and University of Texas Southwestern Medical Center at Dal.
Southwestern Medical Center · USThe University of Texas at Arlington · USThe University of Texas Southwestern Medical Center · US

Funding

FRET-based Ultrasound-Switchable Fluorescence ImagingR15EB012312 · NIBIB · UNIVERSITY OF TEXAS ARLINGTON · PI YUAN, BAOHONG · 2010 to 2010
$397k
NIBIB NIH HHS 7R15EB012312-02NIBIB NIH HHS R15 EB012312
6 · The paper itself

Abstract

Bioaffinity conjugation between streptavidin (SA) and biotin has been widely used to link donors and acceptors for investigating the distance-dependent Förster resonance energy transfer (FRET). When studying a commonly used FRET system of (QD-SA)-(biotin-DNA-dye) [donor: quantum dot (QD); acceptor: small organic fluorescent dye; and linker: deoxyribose nucleic acid (DNA) molecule via SA-biotin conjugation], however, a contradictory finding was recently reported in the literature. It was found that the FRET lost its dependence on the number of DNA base pairs when using a phosphate-buffered saline (PBS) solution. We found that the conflicted results were caused by the ionic strength of the adopted buffer solutions. Our results suggest that the dependent FRET on the number of DNA bases is favorable in a low-ionic-strength buffer, whereas in relatively high-ionic-strength buffers, the FRET loses the DNA length dependence. We propose that the independence is mainly caused by the conformational change of DNA molecules from a stretched to a coiled mode when the cations in the high-ionic-strength buffer neutralize the negatively charged backbone of DNA molecules, thereby bringing the acceptors close to the donors.

Indexed as

ArtifactsQuantum DotsBiotinDNAFluorescence Resonance Energy TransferImmunoassayProtein Interaction MappingReproducibility of ResultsSensitivity and SpecificityStaining and LabelingStreptavidinBiotinDNAStreptavidin

Identifiers

PMID25162908
PMCPMC4145247
OpenAlexW1982517203

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.