ArticleNature plants2021
The cryo-EM structure of the chloroplast ClpP complex.
Article in Nature plants, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- Estimation of chloroplast macromolecular complex copy numbers and subunit stoichiometries during the Chlamydomonas reinhardtii cell cycle.The Plant journal : for cell and molecular biology · 2026Article
- A chaperonin complex regulates organelle proteostasis in malaria parasites.PLoS pathogens · 2025Article
- Genome-wide association study reveals the genetic basis of vitamin C content in rapeseed (Frontiers in plant science · 2025Article
- Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants.The Plant cell · 2024Review
- Intra-chloroplast proteases: A holistic network view of chloroplast proteolysis.The Plant cell · 2024Review
- A proteostasis network safeguards the chloroplast proteome.Essays in biochemistry · 2022Review
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein homoeostasis in plastids is strategically regulated by the protein quality control system involving multiple chaperones and proteases, among them the Clp protease. Here, we determined the structure of the chloroplast ClpP complex from Chlamydomonas reinhardtii by cryo-electron microscopy. ClpP contains two heptameric catalytic rings without any symmetry. The top ring contains one ClpR6, three ClpP4 and three ClpP5 subunits while the bottom ring is composed of three ClpP1
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Registered trials
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