ArticleThe FEBS journal2014
A knot in the protein structure - probing the near-infrared fluorescent protein iRFP designed from a bacterial phytochrome.
Article in The FEBS journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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
13 citing papers in PubMed, 28 citations in OpenAlex.
- Bright monomeric fluorescent protein elite-niRFP704 for two-channel near-infrared STED nanoscopy.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Impact of Double Covalent Binding of BV in NIR FPs on Their Spectral and Physicochemical Properties.International journal of molecular sciences · 2022Article
- A set of monomeric near-infrared fluorescent proteins for multicolor imaging across scales.Nature communications · 2020Article
- The unfolding of iRFP713 in a crowded milieu.PeerJ · 2019Article
- The Pathways of the iRFP713 Unfolding Induced by Different Denaturants.International journal of molecular sciences · 2018Article
- Designing brighter near-infrared fluorescent proteins: insights from structural and biochemical studies.Chemical science · 2017Article
- Tolerance of a Knotted Near-Infrared Fluorescent Protein to Random Circular Permutation.Biochemistry · 2016Article
- Allosteric effects of chromophore interaction with dimeric near-infrared fluorescent proteins engineered from bacterial phytochromes.Scientific reports · 2016Article
- Article
- Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms.PeerJ · 2016Article
- Minimal domain of bacterial phytochrome required for chromophore binding and fluorescence.Scientific reports · 2015Article
- Near-infrared fluorescent proteins engineered from bacterial phytochromes.Current opinion in chemical biology · 2015Review
- Natural photoreceptors as a source of fluorescent proteins, biosensors, and optogenetic tools.Annual review of biochemistry · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
The possibility of engineering near-infrared fluorescent proteins and biosensors from bacterial phytochrome photoreceptors (BphPs) has led to substantial interest in this family of proteins. The near-infrared fluorescent proteins have allowed non-invasive bio-imaging of deep tissues and whole organs in living animals. BphPs and derived near-infrared fluorescent proteins contain a structural element, called a knot, in their polypeptide chains. The formation of knot structures in proteins was refuted for a long time. Here, we studied the denaturation and renaturation processes of the near-infrared fluorescent probe iRFP, engineered from RpBphP2, which utilizes a heme-derived tetrapyrrole compound biliverdin as a chromophore. iRFP contains a unique figure-of-eight knot. The denaturation and renaturation curves of the iRFP apoform coincided well, suggesting efficient refolding. However, the iRFP holoform exhibited irreversible unfolding and aggregation associated with the bound chromophore. The knot structure in the apoform did not prevent subsequent binding of biliverdin, resulting in the functional iRFP holoform. We suggest that the irreversibility of protein unfolding is caused by post-translational protein modifications, such as chromophore binding, rather than the presence of the knot. These results are essential for future design of BphP-based near-infrared probes, and add important features to our knowledge of protein 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.