Functional analysis of propeptide as an intramolecular chaperone for in vivo folding of subtilisin nattokinase is a research paper published in FEBS Letters (2010). On theSindex it has a DataRank of 1.0. It has been cited 20 times, with 18 citing works in its 1-hop citation network.
Here, we show that during in vivo folding of the precursor, the propeptide of subtilisin nattokinase functions as an intramolecular chaperone (IMC) that organises the in vivo folding of the subtilisin domain. Two residues belonging to β‐strands formed by conserved regions of the IMC are crucial for the folding of the subtilisin domain through direct interactions. An identical protease can fold into different conformations in vivo due to the action of a mutated IMC, resulting in different kinetic parameters. Some interfacial changes involving conserved regions, even those induced by the subtilisin domain, blocked subtilisin folding and altered its conformation. Insight into the interaction between the subtilisin and IMC domains is provided by a three‐dimensional structural model.
FAIR checklist signals are shown for context only and do not affect DataRank scoring.
Base Score Contribution
0.457
From this paper's citation signal
Citation Network Contribution
0.588
From 13 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 44% comes from its base citations and 56% from the citation network (13 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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