The effect of small molecules in modulating the chaperone activity of αB‐crystallin against ordered and disordered protein aggregation is a research paper published in The FEBS Journal (2008). On theSindex it has a DataRank of 2.0. It has been cited 59 times, with 38 citing works in its 1-hop citation network.
Protein aggregation can proceed via disordered or ordered mechanisms, with the latter being associated with amyloid fibril formation, which has been linked to a number of debilitating conditions including Alzheimer’s, Parkinson’s and Creutzfeldt‐Jakob diseases. Small heat‐shock proteins (sHsps), such as αB‐crystallin, act as chaperones to prevent protein aggregation and are thought to play a key role in the prevention of protein‐misfolding diseases. In this study, we have explored the potential for small molecules such as arginine and guanidine to affect the chaperone activity of αB‐crystallin against disordered (amorphous) and ordered (amyloid fibril) forms of protein aggregation. The effect of these additives is highly dependent upon the target protein undergoing aggregation. Importantly, our results show that the chaperone action of αB‐crystallin against aggregation of the disease‐related amyloid fibril forming protein α‐synucleinA53T is enhanced in the presence of arginine and similar positively charged compounds (such as lysine and guanidine). Thus, our results suggest that target protein identity plays a critical role in governing the effect of small molecules on the chaperone action of sHsps. Significantly, small molecules that regulate the activity of sHsps may provide a mechanism to protect cells from the toxic protein aggregation that is associated with some protein‐misfolding diseases.
FAIR checklist signals are shown for context only and do not affect DataRank scoring.
Base Score Contribution
0.614
From this paper's citation signal
Citation Network Contribution
1.4
From 38 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 30% comes from its base citations and 70% from the citation network (38 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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