Hepatitis C virus NS3 serine protease interacts with the serpin C1 inhibitor is a research paper published in FEBS Letters (1999). On theSindex it has a DataRank of 1.0. It has been cited 16 times, with 15 citing works in its 1-hop citation network.
Both NS3 protein (1007–1657) and its protease moiety (NS3p, 1027–1207) were able to interact in vitro with C1 Inhibitor (C1Inh) to give a 95‐kDa M r C1Inh cleavage product similar to that obtained upon proteolysis by complement protease C1s. High‐M r reaction products were also detected after incubation of C1Inh with NS3 but not with NS3p; they correspond to ester‐bonded complexes from their hydroxylamine lability. Similar reactivity of NS3 was observed upon incubation with α2‐antiplasmin. Serpin cleavage was prevented by treatment of NS3 with synthetic serine protease inhibitors. This interaction between viral NS3 and host serpins suggests that NS3 is likely to be controlled by infected cell protease inhibitors.
FAIR checklist signals are shown for context only and do not affect DataRank scoring.
Base Score Contribution
0.425
From this paper's citation signal
Citation Network Contribution
0.615
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 41% comes from its base citations and 59% 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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