ArticleProtein science : a publication of the Protein Society2026
Absolute quantification of fluorescent protein fusions by mass spectrometry.
Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
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.
Who cites it
1 citing paper in PubMed.
- Absolute quantification of fluorescent protein fusions by mass spectrometry.Protein science : a publication of the Protein Society · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fusions with fluorescent proteins (FPs) play a pivotal role in experimental biology because of their sensitive and spatially precise visualization by spectroscopy. However, observed fluorescence is not always proportional to their molar concentration. Only a fraction of the fusion protein that contains the mature fluorescence chromophore is detectable by spectroscopy and there is no accurate and generic method for estimating its molar abundance. We have developed a fluorescence-independent mass spectrometry-based method for absolute (molar) sub-femtomole quantification of FP-fusions that also estimates the fraction of fully matured chromophore. The method exploits an isotopically labeled 68 kDa recombinant protein standard expressed in E. coli and used without further purification. This chimeric protein contains multiple peptide proxies for six prototypical FPs (mCherry, mScarlet-I, mKate2, EGFP, mNeonGreen, and Dendra2) and two self-labelling (Halo- and SNAP-) tags and supports the quantification of proteins fused to any of 615 common FPs and tags. The method can be used broadly for the absolute quantification of fluorescent fusions in vivo and in vitro and is complementary to fluorescence measurements. We further combined mass spectrometry with fluorescence spectroscopy to study expression kinetics of FP fusions in cell-free systems. Molar concentrations of the expressed fusion, its fraction with mature chromophore, and of the fluorescing protein were integrated into a mathematical model to obtain kinetic rates of translation, chromophore maturation, and folding.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.