Evidence map›Paper›PMID 24712386›Full record

ArticleThe journal of physical chemistry. B2014

Chromophore photoreduction in red fluorescent proteins is responsible for bleaching and phototoxicity.

Russell B Vegh, Ksenia B Bravaya, Dmitry A Bloch, Andreas S Bommarius, Laren M Tolbert, Michael Verkhovsky, Anna I Krylov, Kyril M Solntsev

Open access · bronzeAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
11.2field-weighted citation impact, top 2% 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

19 citing papers in PubMed, 68 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Light-induced oxidant production by fluorescent proteins.Free radical biology & medicine · 2018
    Review
  10. Engineering molecular imaging strategies for regenerative medicine.Bioengineering & translational medicine · 2018
    Review
  11. Article
  12. Review
  13. A Guide to Fluorescent Protein FRET Pairs.Sensors (Basel, Switzerland) · 2016
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

8 authors at 3 institutions in 2 countries.

Russell B VeghSchool of Chemistry and Biochemistry, Georgia Institute of Technology , Atlanta, Georgia 30332-0400, United States.
Ksenia B Bravaya
Dmitry A Bloch
Andreas S Bommarius
Laren M Tolbert
Michael Verkhovsky
Anna I Krylov
Kyril M Solntsev
Georgia Institute of Technology · USUniversity of Helsinki · FIUniversity of Southern California · US

Funding

Optically Modulated Fluorescent ProteinsR21EB009976 · NIBIB · GEORGIA INSTITUTE OF TECHNOLOGY · PI DICKSON, ROBERT M, TOLBERT, LAREN MALCOLM · 2009 to 2010
$398k
NIBIB NIH HHS R21 EB009976NIBIB NIH HHS R21EB009976-01
6 · The paper itself

Abstract

Red fluorescent proteins (RFPs) are indispensable tools for deep-tissue imaging, fluorescence resonance energy transfer applications, and super-resolution microscopy. Using time-resolved optical spectroscopy this study investigated photoinduced dynamics of three RFPs, KillerRed, mRFP, and DsRed. In all three RFPs, a new transient absorption intermediate was observed, which decays on a microsecond-millisecond time scale. This intermediate is characterized by red-shifted absorption at 1.68-1.72 eV (λmax = 720-740 nm). On the basis of electronic structure calculations, experimental evidence, and published literature, the chemical nature of the intermediate is assigned to an unusual open-shell dianionic chromophore (dianion-radical) formed via photoreduction. A doubly charged state that is not stable in the isolated (gas phase) chromophore is stabilized by the electrostatic field of the protein. Mechanistic implications for photobleaching, blinking, and phototoxicity are discussed.

Indexed as

LightPhotobleachingKineticsLuminescent ProteinsModels, MolecularProtein ConformationRed Fluorescent ProteinThermodynamicsLuminescent ProteinsRed Fluorescent Protein

Identifiers

PMID24712386
PMCPMC4010289
OpenAlexW2335047098

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.