Evidence map›Paper›PMID 26025769›Full record

ReviewBiochimica et biophysica acta2016

Subcellular functions of proteins under fluorescence single-cell microscopy.

Casey L Kohnhorst, Danielle L Schmitt, Anand Sundaram, Songon An

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

8 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Quantitative Imaging of BiochemistryACS central science · 2020
    Review
  5. Review
  6. Detecting Purinosome Metabolon Formation with Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  7. Article
  8. 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.

Casey L KohnhorstDepartment of Chemistry and Biochemistry, University of Maryland Baltimore County (UMBC), 1000 Hilltop Circle, Baltimore, MD 21250, USA.
Danielle L SchmittDepartment of Chemistry and Biochemistry, University of Maryland Baltimore County (UMBC), 1000 Hilltop Circle, Baltimore, MD 21250, USA.
Anand SundaramDepartment of Chemistry and Biochemistry, University of Maryland Baltimore County (UMBC), 1000 Hilltop Circle, Baltimore, MD 21250, USA.
Songon AnDepartment of Chemistry and Biochemistry, University of Maryland Baltimore County (UMBC), 1000 Hilltop Circle, Baltimore, MD 21250, USA. Electronic address: san@umbc.edu.
University of Maryland, Baltimore County · US

Funding

Graduate Training at The Chemistry Biology InterfaceT32GM066706 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI SELEY-RADTKE, KATHERINE L, SMITH, AARON T · 2004 to 2023
$3.3M
NIGMS NIH HHS T32 GM066706
6 · The paper itself

Abstract

A cell is a highly organized, dynamic, and intricate biological entity orchestrated by a myriad of proteins and their self-assemblies. Because a protein's actions depend on its coordination in both space and time, our curiosity about protein functions has extended from the test tube into the intracellular space of the cell. Accordingly, modern technological developments and advances in enzymology have been geared towards analyzing protein functions within intact single cells. We discuss here how fluorescence single-cell microscopy has been employed to identify subcellular locations of proteins, detect reversible protein-protein interactions, and measure protein activity and kinetics in living cells. Considering that fluorescence single-cell microscopy has been only recently recognized as a primary technique in enzymology, its potentials and outcomes in studying intracellular protein functions are projected to be immensely useful and enlightening. We anticipate that this review would inspire many investigators to study their proteins of interest beyond the conventional boundary of specific disciplines. This article is part of a Special Issue entitled: Physiological Enzymology and Protein Functions.

Indexed as

Enzyme AssaysFluorescence Resonance Energy TransferIntracellular SpaceKineticsMicroscopy, FluorescenceModels, BiologicalProtein BindingSingle-Cell AnalysisSubstrate SpecificityTime-Lapse ImagingColocalizationEnzyme kineticsFluorescence microscopyGenetically-encoded fluorescent tagProtein activityProtein–protein interactionSubcellular localization

Identifiers

PMID26025769
PMCPMC5679394
OpenAlexW364709548

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.