Evidence map›Paper›PMID 30942588›Full record

ArticleThe journal of physical chemistry. B2019

Intramolecular Fluorescent Protein Association in a Class of Zinc FRET Sensors Leads to Increased Dynamic Range.

Joshua D Slocum, Amy E Palmer, Ralph Jimenez

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2019. 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. Review
  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

3 authors.

Funding

Regulation of Cell Signaling by Transition Metal DynamicsDP1GM114863 · NIGMS · UNIVERSITY OF COLORADO · PI PALMER, AMY E · 2014 to 2018
$3.8M
Genetically Encoded Sensors Shed Light on Zinc HomeostasisR01GM084027 · NIGMS · UNIVERSITY OF COLORADO · PI PALMER, AMY E · 2008 to 2016
$2.6M
NIGMS NIH HHS DP1 GM114863NIGMS NIH HHS R01 GM084027
6 · The paper itself

Abstract

Genetically encoded Förster resonance energy transfer (FRET) sensors enable the visualization of ions, molecules, and processes in live cells. However, despite their widespread use, the molecular states that determine sensor performance are usually poorly understood, which limits efforts to improve them. We used dynamic light scattering (DLS) and time-resolved fluorescence anisotropy to uncover the sensing mechanism of ZifCV1.173, a Zn

Indexed as

Fluorescence Resonance Energy TransferDimerizationDynamic Light ScatteringLuminescent ProteinsZincLuminescent ProteinsZinc

Identifiers

PMID30942588
PMCPMC8492229

What OpenQuestion holds

Textmetadata
LicenceTDM
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.