Evidence map›Paper›PMID 23351712›Full record

ReviewInternational review of cell and molecular biology2013

Beta-barrel scaffold of fluorescent proteins: folding, stability and role in chromophore formation.

Olesya V Stepanenko, Olga V Stepanenko, Irina M Kuznetsova, Vladislav V Verkhusha, Konstantin K Turoverov

Abstract readReview
In one paragraph

Review in International review of cell and molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing 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

54 citing papers in PubMed.

  1. Article
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  8. PEG-mCherry interactions beyond classical macromolecular crowding.Protein science : a publication of the Protein Society · 2025
    Article
  9. Article
  10. Review
  11. Review
  12. An arginine-rich nuclear localization signal (ArgiNLS) strategy for streamlined image segmentation of single cells.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Article
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  19. Bleaching-Resistant Super-Resolution Fluorescence Microscopy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Review
  20. 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

5 authors.

Olesya V StepanenkoInstitute of Cytology of Russian Academy of Sciences, St. Petersburg, Russia.
Olga V Stepanenko
Irina M Kuznetsova
Vladislav V Verkhusha
Konstantin K Turoverov

Funding

In Vivo Multiphoton Based Imaging of Complex Cancer Cell BehaviorR01CA164468 · NCI · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI VERKHUSHA, VLADISLAV · 2011 to 2015
$3.8M
Molecular Fluorescent ToolkitR01GM073913 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI VERKHUSHA, VLADISLAV · 2006 to 2014
$2.4M
NCI NIH HHS CA164468NCI NIH HHS R01 CA164468NIGMS NIH HHS GM073913NIGMS NIH HHS R01 GM073913
6 · The paper itself

Abstract

This review focuses on the current view of the interaction between the β-barrel scaffold of fluorescent proteins and their unique chromophore located in the internal helix. The chromophore originates from the polypeptide chain and its properties are influenced by the surrounding protein matrix of the β-barrel. On the other hand, it appears that a chromophore tightens the β-barrel scaffold and plays a crucial role in its stability. Furthermore, the presence of a mature chromophore causes hysteresis of protein unfolding and refolding. We survey studies measuring protein unfolding and refolding using traditional methods as well as new approaches, such as mechanical unfolding and reassembly of truncated fluorescent proteins. We also analyze models of fluorescent protein unfolding and refolding obtained through different approaches, and compare the results of protein folding in vitro to co-translational folding of a newly synthesized polypeptide chain.

Indexed as

Models, MolecularProtein RefoldingProtein UnfoldingLuminescent ProteinsProtein StabilityProtein Structure, SecondaryLuminescent Proteins

Identifiers

PMID23351712
PMCPMC3739439

What OpenQuestion holds

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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.