Principles of chaperone-mediated protein folding is a research paper published in Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences (1995). On theSindex it has a DataRank of 1.1. It has been cited 14 times, with 14 citing works in its 1-hop citation network.
Abstract The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo. Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediated by chaperone proteins. Different classes of molecular chaperones, such as the members of the Hsp70 and Hsp60 families of heat-shock proteins, cooperate in a coordinated pathway of cellular protein folding.
FAIR checklist signals are shown for context only and do not affect DataRank scoring.
Base Score Contribution
0.406
From this paper's citation signal
Citation Network Contribution
0.694
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 37% comes from its base citations and 63% 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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