Fully distributed identity-based threshold signatures with identifiable aborts

Identity-based threshold signature(IDTS)is a forceful primitive to protect identity and data privacy,in which parties can collaboratively sign a given message as a signer without reconstructing a signing key.Nevertheless,most IDTS schemes rely on a trusted key generation center(KGC).Recently,some IDTS schemes can achieve escrow-free security against corrupted KGC,but all of them are vulnerable to denial-of-service attacks in the dishonest majority setting,where cheaters may force the protocol to abort without providing any feedback.In this work,we present a fully decentralized IDTS scheme to resist corrupted KGC and denialof-service attacks.To this end,we design threshold protocols to achieve distributed key generation,private key extraction,and signing generation which can withstand the collusion between KGCs and signers,and then we propose an identification mechanism that can detect the identity of cheaters during key generation,private key extraction and signing generation.Finally,we formally prove that the proposed scheme is threshold unforgeability against chosen message attacks.The experimental results show that the computation time of both key generation and signing generation is<1 s,and private key extraction is about 3 s,which is practical in the distributed environment.

The novel SLC40A1(T419I)variant results in a loss-of-function phenotype and may provide insights into the mechanism of large granular lymphocytic leukemia and pure red cell aplasia

Variants in the solute carrier family 40 member 1(SLC40A1)gene are the molecular basis of ferroportin disease,which is an autosomal dominant hereditary hemochromatosis.Here,we present a patient with pure red cell aplasia(PRCA)and large granular lymphocytic leukemia(LGLL)associated with an extremely high levels of serum ferritin and iron overload syndrome.Whole exon sequencing revealed a novel heterozygous variant in SLC40A1(p.T419I),which was found in his daughter as well.A series of functional studies in vitro of the T419I variant in ferroportin were conducted and the results revealed a reduced capacity of iron export from cells without changes in protein localization and its sensitivity to hepcidin.Intracellular iron storage in mutated cells was significantly higher than that of wild-type.These findings suggest that the novel variant p.T419I can cause the classical form of ferroportin disease and an elevated intracellular iron level indicates a potential novel pathogenic mechanism underlying PRCA and LGLL.