Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
3.1field-weighted citation impact, top 9% 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
1 citing paper in PubMed, 5 citations in OpenAlex.
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 at 3 institutions in 3 countries.
Nora Lisa BitzenhoferInstitute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf, Forschungszentrum Jülich, Jülich, Germany.
Fabienne HilgersInstitute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf, Forschungszentrum Jülich, Jülich, Germany.
Gabriela N BosioInstitute of Biological Information Processing IBI-1: Molecular and Cellular Physiology, Forschungszentrum Jülich GmbH, Jülich, Germany.ORCID 0000-0001-7279-264X
Joaquim TorraInstitut Químic de Sarrià, Universitat Ramon Llull, Barcelona, Spain.ORCID 0000-0002-7562-6986
Giorgia CasiniInstitute of Biological Information Processing IBI-1: Molecular and Cellular Physiology, Forschungszentrum Jülich GmbH, Jülich, Germany.
Felix R M BeinlichInstitute of Biological Information Processing IBI-1: Molecular and Cellular Physiology, Forschungszentrum Jülich GmbH, Jülich, Germany.ORCID 0000-0002-6411-0909
Esther Knieps-GrünhagenInstitute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf, Forschungszentrum Jülich, Jülich, Germany.
Karl-Erich JaegerInstitute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf, Forschungszentrum Jülich, Jülich, Germany.
Santi NonellInstitut Químic de Sarrià, Universitat Ramon Llull, Barcelona, Spain. santi.nonell@iqs.url.edu.ORCID 0000-0002-8900-5291
Ulrich KraussInstitute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf, Forschungszentrum Jülich, Jülich, Germany. u.krauss@fz-juelich.de.
Thomas GenschInstitute of Biological Information Processing IBI-1: Molecular and Cellular Physiology, Forschungszentrum Jülich GmbH, Jülich, Germany. t.gensch@fz-juelich.de.ORCID 0000-0002-3903-4705
Thomas DrepperInstitute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf, Forschungszentrum Jülich, Jülich, Germany. t.drepper@fz-juelich.de.
Forschungszentrum Jülich · DEInstitut Químic de Sarrià · ESCentre National de la Recherche Scientifique · FR
Funding
No grant is acknowledged in the PubMed record.
6 · The paper itself
Abstract
Flavin-based fluorescent proteins (FbFPs), a class of small fluorescent proteins derived from light-oxygen-voltage (LOV) domains, bind ubiquitous endogenous flavins as chromophores. Due to their unique properties, they can be used as versatile in vivo reporter proteins under aerobic and anaerobic conditions. This chapter presents methodologies for in-depth characterization of the biochemical, spectroscopic, photophysical, and photochemical properties of FbFPs.
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.
Development and Characterization of Flavin-Binding Fluorescent Proteins, Part II: Advanced Characterization. · full record | OpenQuestion