Evidence map›Paper›PMID 31453255›Full record

ArticleJournal of biological methods2018

High resolution measurement of membrane receptor endocytosis.

Zhihui Zhang, David K Heidary, Christopher I Richards

Open access · diamondAbstract read
In one paragraph

Article in Journal of biological methods, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 24% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. 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.

Zhihui ZhangDepartment of Chemistry, University of Kentucky, 505 Rose Street, Lexington, KY 40506, USA.
David K HeidaryDepartment of Chemistry, University of Kentucky, 505 Rose Street, Lexington, KY 40506, USA.
Christopher I RichardsDepartment of Chemistry, University of Kentucky, 505 Rose Street, Lexington, KY 40506, USA.
University of Kentucky · US

Funding

Protein CoreP30GM110787 · NIGMS · UNIVERSITY OF KENTUCKY · PI WHITEHEART, SIDNEY WALDO · 2014 to 2018
$5.7M
NIGMS NIH HHS P30 GM110787
6 · The paper itself

Abstract

We present a new approach to quantify the half-life of membrane proteins on the cell surface, through tagging the protein with the photoconvertible fluorescent protein, Dendra2. Upon exposure to 405 nm light, Dendra2 is photoconverted from green to red emission. Total internal reflection fluorescence microscopy (TIRF) is applied to limit visualization of fluorescence to proteins located on the plasma membrane. Conversion of Dendra2 works as a pulse chase experiment through monitoring only the population of protein that has been photoconverted. As the protein is endocytosed the red emission decreases due to the protein leaving the TIRF field of view. This method is not impacted by the insertion of new protein into the plasma membrane as newly synthesized protein only exhibits green emission. We used this approach to determine the half-life of ENaC on the plasma membrane illustrating the high temporal resolution capability of this technique compared to current methods.

Indexed as

Dendra2fluorescence microscopymembrane protein half-lifeTIRF

Identifiers

PMID31453255
PMCPMC6706155
OpenAlexW2903764203

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.