Launch of the Space experiment PAMELA

PAMELA is a satellite borne experiment designed to study with great accuracy cosmic rays of galactic, solar, and trapped nature in a wide energy range protons: 80 MeV-700 GeV, electrons 50 MeV-400 GeV). Main objective is the study of the antimatter component: antiprotons (80 MeV-190 GeV), positrons (50 MeV-270 GeV) and search for antimatter with a precision of the order of 10^-8). The experiment, housed on board the Russian Resurs-DK1 satellite, was launched on June, 15, 2006 in a 350*600 km orbit with an inclination of 70 degrees. The detector is composed of a series of scintillator counters arranged at the extremities of a permanent magnet spectrometer to provide charge, Time-of-Flight and rigidity information. Lepton/hadron identification is performed by a Silicon-Tungsten calorimeter and a Neutron detector placed at the bottom of the device. An Anticounter system is used offline to reject false triggers coming from the satellite. In self-trigger mode the Calorimeter, the neutron detector and a shower tail catcher are capable of an independent measure of the lepton component up to 2 TeV. In this work we describe the experiment, its scientific objectives and the performance in the first months after launch.Comment: Accepted for publication on Advances in Space Researc

Parameter-Hiding Order Revealing Encryption

Order-revealing encryption (ORE) is a popular primitive for outsourcing encrypted databases, as it allows for efficiently performing range queries over encrypted data. Unfortunately, a series of works, starting with Naveed et al. (CCS 2015), have shown that when the adversary has a good estimate of the distribution of the data, ORE provides little protection. In this work, we consider the case that the database entries are drawn identically and independently from a distribution of known shape, but for which the mean and variance are not (and thus the attacks of Naveed et al. do not apply). We define a new notion of security for ORE, called parameter-hiding ORE, which maintains the secrecy of these parameters. We give a construction of ORE satisfying our new definition from bilinear maps

Function-Hiding Inner Product Encryption is Practical

In a functional encryption scheme, secret keys are associated with functions and ciphertexts are associated with messages. Given a secret key for a function f, and a ciphertext for a message x, a decryptor learns f(x) and nothing else about x. Inner product encryption is a special case of functional encryption where both secret keys and ciphertext are associated with vectors. The combination of a secret key for a vector x and a ciphertext for a vector y reveal and nothing more about y. An inner product encryption scheme is function- hiding if the keys and ciphertexts reveal no additional information about both x and y beyond their inner product. In the last few years, there has been a flurry of works on the construction of function-hiding inner product encryption, starting with the work of Bishop, Jain, and Kowalczyk (Asiacrypt 2015) to the more recent work of Tomida, Abe, and Okamoto (ISC 2016). In this work, we focus on the practical applications of this primitive. First, we show that the parameter sizes and the run-time complexity of the state-of-the-art construction can be further reduced by another factor of 2, though we compromise by proving security in the generic group model. We then show that function privacy enables a number of applications in biometric authentication, nearest-neighbor search on encrypted data, and single-key two-input functional encryption for functions over small message spaces. Finally, we evaluate the practicality of our encryption scheme by implementing our function-hiding inner product encryption scheme. Using our construction, encryption and decryption operations for vectors of length 50 complete in a tenth of a second in a standard desktop environment

Rho Family GTPase modification and dependence on CAAX motif-signaled posttranslational modification: J.Biol.Chem

Rho GTPases (20 human members) comprise a major branch of the Ras superfamily of small GTPases, and aberrant Rho GTPase function has been implicated in oncogenesis and other human diseases. Although many of our current concepts of Rho GTPases are based on the three classical members (RhoA, Rac1, and Cdc42), recent studies have revealed the diversity of biological functions mediated by other family members. A key basis for the functional diversity of Rho GTPases is their association with distinct subcellular compartments, which is dictated in part by three posttranslational modifications signaled by their carboxyl-terminal CAAX (where C represents cysteine, A is an aliphatic amino acid, and X is a terminal amino acid) tetrapeptide motifs. CAAX motifs are substrates for the prenyltransferase-catalyzed addition of either farnesyl or geranylgeranyl isoprenoid lipids, Rce1-catalyzed endoproteolytic cleavage of the AAX amino acids, and Icmt-catalyzed carboxyl methylation of the isoprenylcysteine. We utilized pharmacologic, biochemical, and genetic approaches to determine the sequence requirements and roles of CAAX signal modifications in dictating the subcellular locations and functions of the Rho GTPase family. Although the classical Rho GTPases are modified by geranylgeranylation, we found that a majority of the other Rho GTPases are substrates for farnesyltransferase. We found that the membrane association and/or function of Rho GTPases are differentially dependent on Rce1- and Icmt-mediated modifications. Our results further delineate the sequence requirements for prenyltransferase specificity and functional roles for protein prenylation in Rho GTPase function. We conclude that a majority of Rho GTPases are targets for pharmacologic inhibitors of farnesyltransferase, Rce1, and IcmtNRC publication: Ye