Molecular chaperone properties of serum amyloid P component is a research paper published in FEBS Letters (2000). On theSindex it has a DataRank of 2.4. It has been cited 56 times, with 51 citing works in its 1-hop citation network.
The selective binding of serum amyloid P component (SAP) to proteins in the pathological amyloid cross‐β fold suggests a possible chaperone role. Here we show that human SAP enhances the refolding yield of denatured lactate dehydrogenase and protects against enzyme inactivation during agitation of dilute solutions. These effects are independent of calcium ions and are not inhibited by compounds that block the amyloid recognition site on the B face of SAP, implicating the A face and/or the edges of the SAP pentamer. We discuss the possibility that the chaperone property of SAP, or its failure, may contribute to the pathogenesis of amyloidosis.
FAIR checklist signals are shown for context only and do not affect DataRank scoring.
Base Score Contribution
0.606
From this paper's citation signal
Citation Network Contribution
1.8
From 45 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 25% comes from its base citations and 75% from the citation network (45 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.