Evidence map›Paper›PMID 26956628›Full record

ArticleScientific reports2016

Dependence of fluorescent protein brightness on protein concentration in solution and enhancement of it.

Takamitsu J Morikawa, Hideaki Fujita, Akira Kitamura, Takashi Horio, Johtaro Yamamoto, Masataka Kinjo, Akira Sasaki, Hiroaki Machiyama, Keiko Yoshizawa, Taro Ichimura and 3 more

Abstract read
In one paragraph

Article in Scientific reports, 2016. 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
–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

27 citing papers in PubMed.

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  17. Enhancing fluorescent protein photostability through robot-assisted photobleaching.Integrative biology : quantitative biosciences from nano to macro · 2018
    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

13 authors.

Takamitsu J MorikawaGraduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita,Osaka 565-0871, JAPAN.
Hideaki FujitaWPI, Immunology Frontier Research Center, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, JAPAN.
Akira KitamuraFaculty of Advanced Life Science, Hokkaido University, Sapporo 001-0021, JAPAN.
Takashi HorioFaculty of Advanced Life Science, Hokkaido University, Sapporo 001-0021, JAPAN.
Johtaro YamamotoFaculty of Advanced Life Science, Hokkaido University, Sapporo 001-0021, JAPAN.
Masataka KinjoFaculty of Advanced Life Science, Hokkaido University, Sapporo 001-0021, JAPAN.
Akira SasakiBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki 305-8566, JAPAN.
Hiroaki MachiyamaWPI, Immunology Frontier Research Center, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, JAPAN.
Keiko YoshizawaRIKEN Quantitative Biology Center (QBiC), Suita, Osaka 565-0874, JAPAN.
Taro IchimuraRIKEN Quantitative Biology Center (QBiC), Suita, Osaka 565-0874, JAPAN.
Katsumi ImadaDepartment of Macromolecular Science, Graduate School of Science, Osaka University, Toyonaka, Osaka 565-0043, JAPAN.
Takeharu NagaiGraduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita,Osaka 565-0871, JAPAN.
Tomonobu M WatanabeRIKEN Quantitative Biology Center (QBiC), Suita, Osaka 565-0874, JAPAN.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorescent proteins have been widely used in biology because of their compatibility and varied applications in living specimens. Fluorescent proteins are often undesirably sensitive to intracellular conditions such as pH and ion concentration, generating considerable issues at times. However, harnessing these intrinsic sensitivities can help develop functional probes. In this study, we found that the fluorescence of yellow fluorescent protein (YFP) depends on the protein concentration in the solution and that this dependence can be enhanced by adding a glycine residue in to the YFP; we applied this finding to construct an intracellular protein-crowding sensor. A Förster resonance energy transfer (FRET) pair, involving a cyan fluorescent protein (CFP) insensitive to protein concentration and a glycine-inserted YFP, works as a genetically encoded probe to evaluate intracellular crowding. By measuring the fluorescence of the present FRET probe, we were able to detect dynamic changes in protein crowding in living cells.

Indexed as

Fluorescence Resonance Energy TransferGlycineLuminescent MeasurementsLuminescent ProteinsRecombinant ProteinsSolutionsGlycineLuminescent ProteinsRecombinant ProteinsSolutions

Identifiers

PMID26956628
PMCPMC4783657

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.