ArticlePlant physiology2017
Chloroplast Preproteins Bind to the Dimer Interface of the Toc159 Receptor during Import.
Article in Plant physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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
3 citing papers in PubMed.
- Deciphering the Molecular Mechanisms of Chilling Tolerance inInternational journal of molecular sciences · 2022Article
- Origins, function, and regulation of the TOC-TIC general protein import machinery of plastids.Journal of experimental botany · 2020Article
- Targeted Control of Chloroplast Quality to Improve Plant Acclimation: From Protein Import to Degradation.Frontiers in plant science · 2019Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most chloroplast proteins are synthesized in the cytosol as higher molecular weight preproteins and imported via the translocons in the outer (TOC) and inner (TIC) envelope membranes of chloroplasts. Toc159 functions as a primary receptor and directly binds preproteins through its dimeric GTPase domain. As a first step toward a molecular understanding of how Toc159 mediates preprotein import, we mapped the preprotein-binding regions on the Toc159 GTPase domain (Toc159G) of pea (
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