Chaperone‐like activity and hydrophobicity of α‐crystallin is a research paper published in IUBMB Life (2006). On theSindex it has a DataRank of 4.6. It has been cited 130 times, with 117 citing works in its 1-hop citation network.
Abstractα‐Crystallin, a prominent member of small heat shock protein (sHsp) family and a major structural protein of the eye lens is a large polydisperse oligomer of two isoforms, αA‐ and αB‐crystallins. Numerous studies have demonstrated that α‐crystallin functions like a molecular chaperone in preventing the aggregation of various proteins under a wide range of stress conditions. The molecular chaperone function of α‐crystallin is thus considered to be vital in the maintenance of lens transparency and in cataract prevention. α‐Crystallin selectively interacts with non‐native proteins thereby preventing them from aggregation and helps maintain them in a folding competent state. It has been proposed and generally accepted that α‐crystallin suppresses the aggregation of other proteins through the interaction between hydrophobic patches on its surface and exposed hydrophobic sites of partially unfolded substrate protein. However, a quantifiable relationship between hydrophobicity and chaperone‐like activity remains a matter to be concerned about. On an attentive review of studies on α‐crystallin chaperone‐like activity, particularly the studies that have direct or indirect implications to hydrophobicity and chaperone‐like activity, we found several instances wherein the correlation between hydrophobicity and its chaperone‐like activity is paradoxical. We thus attempted to provide an overview on the role of hydrophobicity in chaperone‐like activity of α‐crystallin, the kind of evaluation done for the first time. iubmb Life, 58: 632 ‐ 641, 2006
FAIR checklist signals are shown for context only and do not affect DataRank scoring.
Base Score Contribution
0.731
From this paper's citation signal
Citation Network Contribution
3.8
From 102 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 (102 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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