ReviewPlant signaling & behavior2022
Structural comparison of unconventional G protein YchF with heterotrimeric G protein and small G protein.
Review in Plant signaling & behavior, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 9 citations in OpenAlex.
- Article
- From biophysical interaction to structural modeling: bi-terminal G and TGS domains drive rice OsYchF1-OsGAP1 complex formation.Botanical studies · 2025Article
- Structural Determinants ofbioRxiv : the preprint server for biology · 2024Article
- Article
- The Universally Conserved Unconventional G Protein YchF Is Critical for Growth and Stress Response.Life (Basel, Switzerland) · 2023Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Guanine nucleotide-binding (G) proteins, namely, phosphate-binding (P) loop GTPases, play a critical role in life processes among different species. Based on the structural characteristics, G proteins can be divided into heterotrimeric G proteins, small G proteins and multiple unique unconventional G proteins. The highly conserved unconventional G protein YchF is composed of a core G domain, an inserted coiled-coil domain, and a TGS domain from the N-terminus to the C-terminus. In this review, we compared the structural characteristics of the G domain in rice OsYchF1 with those of
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