On the substrate specificity of <i>α</i>-crystallin as a molecular chaperone is a research paper published in Biochemical Journal (1995). On theSindex it has a DataRank of 4.1. It has been cited 76 times, with 66 citing works in its 1-hop citation network.
alpha-Crystallin, the major protein of the ocular lens, acts as a molecular chaperone by preventing the thermal aggregation of proteins. However, in contrast with many other heat shock proteins, alpha-crystallin fails to protect proteins from aggregation during refolding reactions. Our results indicate that alpha-crystallin has substrate specificity different from other chaperones and recognizes specific non-native intermediates formed on the denaturation pathway only, with no affinity for intermediates formed on the refolding pathway.
FAIR checklist signals are shown for context only and do not affect DataRank scoring.
Base Score Contribution
0.652
From this paper's citation signal
Citation Network Contribution
3.5
From 63 citing papers with measurable signal
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 (63 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.
Click a node to highlight its connections. Use scroll to zoom. Drag to pan.