A COPII subunit acts with an autophagy receptor to target endoplasmic reticulum for degradation is a research paper published in Science (2019). On theSindex it has a DataRank of 4.7. It has been cited 159 times, with 140 citing works in its 1-hop citation network.
ER-phagy keeps cells healthy In eukaryotic cells, about one-third of all proteins are targeted to the endoplasmic reticulum (ER), which serves as a hub for secretory protein traffic and quality control. Cui et al. studied a protein known as Lst1 in yeast and SEC24C in mammalian cells that is involved in loading secretory cargo into vesicles that are delivered to the Golgi complex. In response to stress caused by starvation or misfolded aggregate-prone secretory proteins, Lst1 acted to promote an additional function—ER-phagy. Together with autophagy receptors on the ER, Lst1 targeted ER domains for degradation to avert protein aggregation, thus preserving cellular health. Science , this issue p. 53
FAIR checklist signals are shown for context only and do not affect DataRank scoring.
Base Score Contribution
0.761
From this paper's citation signal
Citation Network Contribution
4.0
From 121 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 16% comes from its base citations and 84% from the citation network (121 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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