ArticleThe Journal of biological chemistry2019
CpeF is the bilin lyase that ligates the doubly linked phycoerythrobilin on β-phycoerythrin in the cyanobacterium
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 18 citations in OpenAlex.
- Phycoerythrin from algae: functional properties, bioactivities, production challenges, and industrial prospects.Archives of microbiology · 2026Review
- Partial photoswitching of rod-shaped phycobilisome production in the cyanobacterium Synechocystis sp. PCC 6803.Plant & cell physiology · 2025Article
- Responding to light signals: a comprehensive update on photomorphogenesis in cyanobacteria.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023Review
- The Unique Light-Harvesting System of the Algal Phycobilisome: Structure, Assembly Components, and Functions.International journal of molecular sciences · 2023Review
- The increasing role of structural proteomics in cyanobacteria.Essays in biochemistry · 2023Review
- Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic Cyanobacteria.International journal of molecular sciences · 2023Article
- A hybrid type of chromatic acclimation regulated by the dual green/red photosensory systems in cyanobacteria.Plant physiology · 2022Article
- Phycobiliproteins-A Family of Algae-Derived Biliproteins: Productions, Characterization and Pharmaceutical Potentials.Marine drugs · 2022Review
- The phycoerythrobilin isomerization activity of MpeV inFrontiers in microbiology · 2022Article
- Patterning of the Autotrophic, Mixotrophic, and Heterotrophic Proteomes of Oxygen-Evolving CyanobacteriumFrontiers in microbiology · 2022Article
- Phycobiliproteins: Structural aspects, functional characteristics, and biotechnological perspectives.Computational and structural biotechnology journal · 2022Review
- MpeV is a lyase isomerase that ligates a doubly linked phycourobilin on the β-subunit of phycoerythrin I and II in marine Synechococcus.The Journal of biological chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phycoerythrin (PE) is a green light-absorbing protein present in the light-harvesting complex of cyanobacteria and red algae. The spectral characteristics of PE are due to its prosthetic groups, or phycoerythrobilins (PEBs), that are covalently attached to the protein chain by specific bilin lyases. Only two PE lyases have been identified and characterized so far, and the other bilin lyases are unknown. Here, using
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.