Versatility of ARD1/NAA10-mediated protein lysine acetylation is a research paper published in Experimental & Molecular Medicine (2018). On theSindex it has a DataRank of 0.703. It has been cited 16 times, with 13 citing works in its 1-hop citation network.
AbstractPost-translational modifications (PTMs) are chemical alterations that occur in proteins that play critical roles in various cellular functions. Lysine acetylation is an important PTM in eukaryotes, and it is catalyzed by lysine acetyltransferases (KATs). KATs transfer acetyl-coenzyme A to the internal lysine residue of substrate proteins. Arrest defective 1 (ARD1) is a member of the KAT family. Since the identification of its KAT activity 15 years ago, many studies have revealed that diverse cellular proteins are acetylated by ARD1. ARD1-mediated lysine acetylation is a key switch that regulates the enzymatic activities and biological functions of proteins and influences cell biology from development to pathology. In this review, we summarize protein lysine acetylation mediated by ARD1 and describe the biological meanings of this modification.
FAIR checklist signals are shown for context only and do not affect DataRank scoring.
Base Score Contribution
0.425
From this paper's citation signal
Citation Network Contribution
0.278
From 12 citing papers with measurable signal
Ranked by citation count — the same ordering the engine uses when summing log1p(Cq) over citers.
DataRank blends this paper's own citation count with the influence of the papers that cite it. Here, roughly 60% comes from its base citations and 40% from the citation network (12 citing papers contributed measurable signal).
Citers are pulled from OpenAlex sorted by cited_by_count:descand capped per paper, so when the cap binds we keep the highest-signal references and the score is reproducible across reruns.
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