352 research outputs found
Noninteractive Verifiable Outsourcing Algorithm for Bilinear Pairing with Improved Checkability
It is well known that the computation of bilinear pairing is the most expensive operation in pairing-based cryptography. In this paper, we propose a noninteractive verifiable outsourcing algorithm of bilinear pairing based on two servers in the one-malicious model. The outsourcer need not execute any expensive operation, such as scalar multiplication and modular exponentiation. Moreover, the outsourcer could detect any failure with a probability close to 1 if one of the servers misbehaves. Therefore, the proposed algorithm improves checkability and decreases communication cost compared with the previous ones. Finally, we utilize the proposed algorithm as a subroutine to achieve an anonymous identity-based encryption (AIBE) scheme with outsourced decryption and an identity-based signature (IBS) scheme with outsourced verification
Metamagnetic transitions and anomalous magnetoresistance in EuAgAs single crystal
In this paper, the magnetic and transport properties were systematically
studied for EuAgAs single crystals, crystallizing in a centrosymmetric
trigonal CaCuP type structure. It was confirmed that two magnetic
transitions occur at = 10 K and = 15 K,
respectively. With the increasing field, the two transitions are noticeably
driven to lower temperature. At low temperatures, applying a magnetic field in
the plane induces two successive metamagnetic transitions. For
both and
, EuAgAs shows a positive, unexpected large
magnetoresistance (up to 202\%) at low fields below 10 K, and a large negative
magnetoresistance (up to -78\%) at high fields/intermediate temperatures. Such
anomalous field dependence of magnetoresistance may have potential application
in the future magnetic sensors. Finally, the magnetic phase diagrams of
EuAgAs were constructed for both
and
Structure of TAR RNA Complexed with a Tat-TAR Interaction Nanomolar Inhibitor that Was Identified by Computational Screening
AbstractHIV-1 TAR RNA functions critically in viral replication by binding the transactivating regulatory protein Tat. We recently identified several compounds that experimentally inhibit the Tat-TAR interaction completely at a 100 nM concentration. We used computational screening of the 181,000-compound Available Chemicals Directory against the three-dimensional structure of TAR [1]. Here we report the NMR-derived structure of TAR complexed with acetylpromazine. This structure represents a new class of compounds with good bioavailability and low toxicity that bind with high affinity to TAR. NMR data unambiguously show that acetylpromazine binds only to the unique 5β² bulge site to which the Tat protein binds. Specificity and affinity of binding are conferred primarily by a network of base stacking and hydrophobic interactions. Acetylpromazine alters the structure of free TAR less than Tat peptides and neomycin do
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