ArticleNature communications2021
Plant LHC-like proteins show robust folding and static non-photochemical quenching.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- The role of far-red fluorescing chlorophylls in the quenching of LHCII.Photosynthesis research · 2026Article
- Suppression of miR426 enhances photoprotection and chlorophyll stability via upregulation of ELIP2 in Arabidopsis thaliana.Molecular biology reports · 2026Article
- High-light-inducible proteins control associations between chlorophyll synthase and the Photosystem II biogenesis factor Ycf39.Plant physiology · 2025Article
- LHC-like Proteins: The Guardians of Photosynthesis.International journal of molecular sciences · 2023Review
- Protein Changes in Shade and SunPlants (Basel, Switzerland) · 2023Article
- Coevolution of tandemly repeatedProceedings of the National Academy of Sciences of the United States of America · 2022Article
- High-light-inducible proteins HliA and HliB: pigment binding and protein-protein interactions.Photosynthesis research · 2022Article
- High-resolution dissection of photosystem II electron transport reveals differential response to water deficit and heat stress in isolation and combination in pearl millet [Frontiers in plant science · 2022Article
- Moderate Temperature Reduction Changes the High-Light Acclimation Strategy of Lettuce Plants.Physiologia plantarumArticle
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 4 institutions in 4 countries.
Funding
Abstract
Life on Earth depends on photosynthesis, the conversion of light energy into chemical energy. Plants collect photons by light harvesting complexes (LHC)-abundant membrane proteins containing chlorophyll and xanthophyll molecules. LHC-like proteins are similar in their amino acid sequence to true LHC antennae, however, they rather serve a photoprotective function. Whether the LHC-like proteins bind pigments has remained unclear. Here, we characterize plant LHC-like proteins (LIL3 and ELIP2) produced in the cyanobacterium Synechocystis sp. PCC 6803 (hereafter Synechocystis). Both proteins were associated with chlorophyll a (Chl) and zeaxanthin and LIL3 was shown to be capable of quenching Chl fluorescence via direct energy transfer from the Chl Q
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Registered trials
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