Evidence map›Paper›PMID 22191901›Full record

ArticleThe Journal of chemical physics2011

Fluorescent protein barrel fluctuations and oxygen diffusion pathways in mCherry.

Prem P Chapagain, Chola K Regmi, William Castillo

Abstract read
In one paragraph

Article in The Journal of chemical physics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. PEG-mCherry interactions beyond classical macromolecular crowding.Protein science : a publication of the Protein Society · 2025
    Article
  3. Article
  4. Article
  5. Nitric Oxide Sensing by a Blue Fluorescent Protein.Antioxidants (Basel, Switzerland) · 2022
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Microfluidics-based selection of red-fluorescent proteins with decreased rates of photobleaching.Integrative biology : quantitative biosciences from nano to macro · 2015
    Article
  13. Review
  14. Article
  15. Article
  16. 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.

Prem P ChapagainDepartment of Physics, Florida International University, Miami, Florida 33199, USA. chapagap@fiu.edu
Chola K Regmi
William Castillo

Funding

Computational Investigations of Monomeric Variants of Red Fluorescent ProteinsSC3GM096903 · NIGMS · FLORIDA INTERNATIONAL UNIVERSITY · PI CHAPAGAIN, PREM P · 2011 to 2014
$425k
NIGMS NIH HHS SC3 GM096903NIGMS NIH HHS SC3GM096903
6 · The paper itself

Abstract

Fluorescent proteins (FPs) are valuable tools as biochemical markers for studying cellular processes. Red fluorescent proteins (RFPs) are highly desirable for in vivo applications because they absorb and emit light in the red region of the spectrum where cellular autofluorescence is low. The naturally occurring fluorescent proteins with emission peaks in this region of the spectrum occur in dimeric or tetrameric forms. The development of mutant monomeric variants of RFPs has resulted in several novel FPs known as mFruits. Though oxygen is required for maturation of the chromophore, it is known that photobleaching of FPs is oxygen sensitive, and oxygen-free conditions result in improved photostabilities. Therefore, understanding oxygen diffusion pathways in FPs is important for both photostabilites and maturation of the chromophores. In this paper, we use molecular dynamics calculations to investigate the protein barrel fluctuations in mCherry, which is one of the most useful monomeric mFruit variant. We employ implicit ligand sampling to determine oxygen pathways from the bulk solvent into the mCherry chromophore in the interior of the protein. We also show that these pathways can be blocked or altered and barrel fluctuations can be reduced by strategic amino acid substitutions.

Indexed as

Molecular Dynamics SimulationDiffusionFluorescenceLuminescent ProteinsMutagenesis, Site-DirectedMutant ProteinsOxygenPhotobleachingProtein EngineeringProtein Structure, TertiaryRed Fluorescent ProteinLuminescent ProteinsMutant ProteinsOxygenRed Fluorescent Protein

Identifiers

PMID22191901
PMCPMC3248888

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.