ArticleStructure (London, England : 1993)2021
Molecular mechanism of N-terminal acetylation by the ternary NatC complex.
Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Acetyltransferase in cardiovascular disease and aging.The journal of cardiovascular aging · 2024Article
- N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity.Nature communications · 2023Article
- Molecular role of NAA38 in thermostability and catalytic activity of the human NatC N-terminal acetyltransferase.Structure (London, England : 1993) · 2023Article
- System analysis based on the T cell exhaustion‑related genes identifies CD38 as a novel therapy target for ovarian cancer.Oncology research · 2023Article
- Charting the N-Terminal Acetylome: A Comprehensive Map of Human NatA Substrates.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Protein N-terminal acetylation is predominantly a ribosome-associated modification, with NatA-E serving as the major enzymes. NatC is the most unusual of these enzymes, containing one Naa30 catalytic subunit and two auxiliary subunits, Naa35 and Naa38; and substrate selectivity profile that overlaps with NatE. Here, we report the cryoelectron microscopy structure of S. pombe NatC with a NatE/C-type bisubstrate analog and inositol hexaphosphate (IP
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