Evidence map›Paper›PMID 26035795›Full record

ArticleScientific reports2015

Comparative study reveals better far-red fluorescent protein for whole body imaging.

K E Luker, P Pata, I I Shemiakina, A Pereverzeva, A C Stacer, D S Shcherbo, V Z Pletnev, M Skolnaja, K A Lukyanov, G D Luker and 2 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.6field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Directly adopting inverse biosensors to image live cell enzyme activities in nanodomains.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

12 authors at 3 institutions in 3 countries.

K E LukerDepartment of Radiology, University of Michigan Medical School, Ann Arbor, MI 48109-2200, USA.
P PataTallinn University of Technology, Department of Gene Technology. 15 Akadeemia St, Tallinn 12618, Estonia.
I I Shemiakina1] Shemiakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Science, Miklukho-Maklaya 16/10, 117997, Moscow, Russia [2] Evrogen JSC, Miklukho-Maklaya 16/10, 117997, Moscow, Russia.
A PereverzevaShemiakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Science, Miklukho-Maklaya 16/10, 117997, Moscow, Russia.
A C StacerDepartment of Radiology, University of Michigan Medical School, Ann Arbor, MI 48109-2200, USA.
D S Shcherbo1] Shemiakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Science, Miklukho-Maklaya 16/10, 117997, Moscow, Russia [2] Evrogen JSC, Miklukho-Maklaya 16/10, 117997, Moscow, Russia.
V Z PletnevShemiakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Science, Miklukho-Maklaya 16/10, 117997, Moscow, Russia.
M SkolnajaTallinn University of Technology, Department of Gene Technology. 15 Akadeemia St, Tallinn 12618, Estonia.
K A Lukyanov1] Shemiakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Science, Miklukho-Maklaya 16/10, 117997, Moscow, Russia [2] Nizhny Novgorod State Medical Academy, Nizhny Novgorod, Russia.
G D LukerDepartment of Radiology, University of Michigan Medical School, Ann Arbor, MI 48109-2200, USA.
I PataTallinn University of Technology, Department of Gene Technology. 15 Akadeemia St, Tallinn 12618, Estonia.
D M Chudakov1] Shemiakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Science, Miklukho-Maklaya 16/10, 117997, Moscow, Russia [2] CEITEC MU, Masaryk University, Brno, Czech republic [3] Pirogov Russian National Research Medical University, 117997 Moscow, Russia.
Institute of Bioorganic Chemistry · RUTallinn University of Technology · EEUniversity of Michigan–Ann Arbor · US

Funding

Small Animal Imaging CoreP50CA093990 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ROSS, BRIAN D. · 2002 to 2012
$19.0M
Targeted Multi-Spectral Dual Axes Confocal Imaging of In Vivo Molecular ExpressioR01CA142750 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KURABAYASHI, KATSUO, LUKER, GARY D · 2010 to 2014
$2.4M
Microfluidic Models of Metastatic CancerR01CA136829 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LUKER, GARY D · 2009 to 2013
$1.5M
Molecular Imaging of Chemokine Receptor SignalingR01CA136553 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LUKER, GARY D · 2009 to 2013
$1.5M
NCI NIH HHS P50 CA093990NCI NIH HHS P50CA093990NCI NIH HHS R01 CA136553NCI NIH HHS R01CA136553NCI NIH HHS R01 CA136829NCI NIH HHS R01CA136829NCI NIH HHS R01 CA142750NCI NIH HHS R01CA142750
6 · The paper itself

Abstract

Genetically encoded far-red and near-infrared fluorescent proteins enable efficient imaging in studies of tumorigenesis, embryogenesis, and inflammation in model animals. Here we report comparative testing of available GFP-like far-red fluorescent proteins along with a modified protein, named Katushka2S, and near-infrared bacterial phytochrome-based markers. We compare fluorescence signal and signal-to-noise ratio at various excitation wavelength and emission filter combinations using transiently transfected cell implants in mice, providing a basis for rational choice of optimal marker(s) for in vivo imaging studies. We demonstrate that the signals of various far-red fluorescent proteins can be spectrally unmixed based on different signal-to-noise ratios in different channels, providing the straightforward possibility of multiplexed imaging with standard equipment. Katushka2S produced the brightest and fastest maturing fluorescence in all experimental setups. At the same time, signal-to-noise ratios for Katushka2S and near-infrared bacterial phytochrome, iRFP720 were comparable in their optimal channels. Distinct spectral and genetic characteristics suggest this pair of a far-red and a near-infrared fluorescent protein as an optimal combination for dual color, whole body imaging studies in model animals.

Indexed as

Whole Body ImagingAlternative SplicingAnimalsHEK293 CellsHeterograftsHumansLuminescent ProteinsMiceModels, AnimalMolecular ImagingRed Fluorescent ProteinRNA Splice SitesSignal-To-Noise RatioLuminescent ProteinsRed Fluorescent ProteinRNA Splice Sites

Identifiers

PMID26035795
PMCPMC4603699
OpenAlexW2268116636

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.