Assays for Acetylation and Other Acylations of Lysine Residues is a research paper published in Current Protocols in Protein Science (2017). On theSindex it has a DataRank of 0.421. It has been cited 6 times, with 6 citing works in its 1-hop citation network.
AbstractLysine acetylation refers to addition of an acetyl moiety to the epsilon‐amino group of a lysine residue and is important for regulating protein functions in various organisms from bacteria to humans. This is a reversible and precisely controlled covalent modification that either serves as an on/off switch or participates in a codified manner with other post‐translational modifications to regulate different cellular and developmental processes in normal and pathological states. This unit describes methods for in vitro and in vivo determination of lysine acetylation. Such methods can be easily extended for analysis of other acylations (such as propionylation, butyrylation, crotonylation, and succinylation) that are also present in histones and many other proteins. © 2017 by John Wiley & Sons, Inc.
FAIR checklist signals are shown for context only and do not affect DataRank scoring.
Base Score Contribution
0.292
From this paper's citation signal
Citation Network Contribution
0.129
From 4 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 69% comes from its base citations and 31% from the citation network (4 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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