ArticleTrends in biochemical sciences2019
Formylation of Eukaryotic Cytoplasmic Proteins: Linking Stress to Degradation.
Article in Trends in biochemical sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 11 citations in OpenAlex.
- Regulation of Neurodegeneration-associated Protein Fragments by the N-degron Pathways.Neurotoxicity research · 2022Review
- Mitochondrial DNA variants modulate N-formylmethionine, proteostasis and risk of late-onset human diseases.Nature medicine · 2021Article
- The Experimental Proteome ofGenes · 2020Article
- How does protein degradation regulate TOM machinery-dependent mitochondrial import?Current genetics · 2020Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Unlike prokaryotes, N-terminal formylation has been confined to a handful of mitochondrial proteins in eukaryotes. A recent study unveils a new role for eukaryotic cytoplasmic N-terminal formylation linking diverse cellular stresses to N-terminal-dependent protein degradation. These findings suggest broad cellular implications in higher eukaryotes for N-terminal methionine formylation.
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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.