Evidence map›Paper›PMID 38114484›Full record

ArticleNature communications2023

Blue-shift photoconversion of near-infrared fluorescent proteins for labeling and tracking in living cells and organisms.

Francesca Pennacchietti, Jonatan Alvelid, Rodrigo A Morales, Martina Damenti, Dirk Ollech, Olena S Oliinyk, Daria M Shcherbakova, Eduardo J Villablanca, Vladislav V Verkhusha, Ilaria Testa

Abstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. The near-infrared bacteriophytochrome-derived fluorescent protein PENELOPE enables RESOLFT superresolution microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
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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

10 authors.

Francesca PennacchiettiDepartment of Applied Physics and SciLifeLab, KTH Royal Institute of Technology, Stockholm, 17165, Sweden. frapen@kth.se.ORCID 0000-0003-1769-972X
Jonatan AlvelidDepartment of Applied Physics and SciLifeLab, KTH Royal Institute of Technology, Stockholm, 17165, Sweden.ORCID 0000-0002-3554-9322
Rodrigo A MoralesDivision of Immunology and Allergy, Department of Medicine Solna, Karolinska Institutet and University Hospital, Stockholm, 17176, Sweden.ORCID 0000-0003-4382-5777
Martina DamentiDepartment of Applied Physics and SciLifeLab, KTH Royal Institute of Technology, Stockholm, 17165, Sweden.ORCID 0000-0002-4209-5381
Dirk OllechDepartment of Applied Physics and SciLifeLab, KTH Royal Institute of Technology, Stockholm, 17165, Sweden.ORCID 0000-0002-9490-7070
Olena S OliinykMedicum, University of Helsinki, Helsinki, 00290, Finland.
Daria M ShcherbakovaDepartment of Genetics, and Gruss-Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY, 10461, USA.
Eduardo J VillablancaDivision of Immunology and Allergy, Department of Medicine Solna, Karolinska Institutet and University Hospital, Stockholm, 17176, Sweden.ORCID 0000-0001-9522-9729
Vladislav V VerkhushaMedicum, University of Helsinki, Helsinki, 00290, Finland.
Ilaria TestaDepartment of Applied Physics and SciLifeLab, KTH Royal Institute of Technology, Stockholm, 17165, Sweden. testa@kth.se.ORCID 0000-0003-4005-4997

Funding

Near-Infrared Fluorescent Proteins, Biosensors and Optogenetic ToolsR35GM122567 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI Vladislav Verkhusha · 2017 to 2026
$4.3M
NIGMS NIH HHS R35 GM122567
6 · The paper itself

Abstract

Photolabeling of intracellular molecules is an invaluable approach to studying various dynamic processes in living cells with high spatiotemporal precision. Among fluorescent proteins, photoconvertible mechanisms and their products are in the visible spectrum (400-650 nm), limiting their in vivo and multiplexed applications. Here we report the phenomenon of near-infrared to far-red photoconversion in the miRFP family of near infrared fluorescent proteins engineered from bacterial phytochromes. This photoconversion is induced by near-infrared light through a non-linear process, further allowing optical sectioning. Photoconverted miRFP species emit fluorescence at 650 nm enabling photolabeling entirely performed in the near-infrared range. We use miRFPs as photoconvertible fluorescent probes to track organelles in live cells and in vivo, both with conventional and super-resolution microscopy. The spectral properties of miRFPs complement those of GFP-like photoconvertible proteins, allowing strategies for photoconversion and spectral multiplexed applications.

Indexed as

Fluorescent DyesHeLa CellsHumansLuminescent ProteinsMicroscopy, FluorescenceFluorescent DyesLuminescent Proteins

Identifiers

PMID38114484
PMCPMC10730883

What OpenQuestion holds

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Registered trials

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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.