Analysis of Protein Lysine Acetylation In Vitro and In Vivo is a research paper published in Current Protocols in Protein Science (2008). On theSindex it has a DataRank of 0.224. It has been cited 3 times, with 1 citing works in its 1-hop citation network.
AbstractProtein lysine acetylation, referring to acetylation of the ɛ‐amino group of a lysine residue, has recently emerged as an important post‐translational modification for regulating protein functions in various organisms. Like phosphorylation, lysine acetylation is a rapidly reversible and precisely controlled covalent modification that serves as a simple on/off switch or participates in a codified manner with other post‐translational modifications to regulate protein functions in different cellular and developmental processes. This unit describes and discusses methods used for in vitro and in vivo determination of lysine acetylation. Curr. Protoc. Protein Sci. 54:14.11.1‐14.11.17. © 2008 by John Wiley & Sons, Inc.
FAIR checklist signals are shown for context only and do not affect DataRank scoring.
Base Score Contribution
0.208
From this paper's citation signal
Citation Network Contribution
0.0156
From 1 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 93% comes from its base citations and 7% from the citation network (1 citing paper 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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