Bacterial proteostasis balances energy and chaperone utilization efficiently is a research paper published in Proceedings of the National Academy of Sciences (2017). On theSindex it has a DataRank of 2.1. It has been cited 71 times, with 64 citing works in its 1-hop citation network.
Significance A cell’s proteins must be properly folded. Therefore, cells have chaperones that help other proteins, their clients, fold and not aggregate. The machinery is like a hospital: it assesses the “sickness” of the patient (finds improperly folded proteins), sends the patient to the right doctor (sorts the protein to the right chaperone), and cures the disease (folds or disaggregates the protein). How are sick proteins recognized and routed to the right chaperone? How does the machine handle different growth rates? Here, we model proteostasis. We find that it can handle any arbitrary client protein, that it spends the least energy on least sick proteins, and that the cell produces just enough chaperone to keep the proteome folded but no more.
FAIR checklist signals are shown for context only and do not affect DataRank scoring.
Base Score Contribution
0.641
From this paper's citation signal
Citation Network Contribution
1.4
From 52 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 31% comes from its base citations and 69% from the citation network (52 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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