An improved preimage attack on MD2

This paper describes an improved preimage attack on the cryptographic hash function MD2. The attack has complexity equivalent to about $2^{73}$ evaluations of the MD2 compression function. This is to be compared with the previous best known preimage attack, which has complexity about $2^{97}$

On hash functions using checksums

We analyse the security of iterated hash functions that compute an input dependent checksum which is processed as part of the hash computation. We show that a large class of such schemes, including those using non-linear or even one-way checksum functions, is not secure against the second preimage attack of Kelsey and Schneier, the herding attack of Kelsey and Kohno and the multicollision attack of Joux. Our attacks also apply to a large class of cascaded hash functions. Our second preimage attacks on the cascaded hash functions improve the results of Joux presented at Crypto’04. We also apply our attacks to the MD2 and GOST hash functions. Our second preimage attacks on the MD2 and GOST hash functions improve the previous best known short-cut second preimage attacks on these hash functions by factors of at least 226 and 254, respectively. Our herding and multicollision attacks on the hash functions based on generic checksum functions (e.g., one-way) are a special case of the attacks on the cascaded iterated hash functions previously analysed by Dunkelman and Preneel and are not better than their attacks. On hash functions with easily invertible checksums, our multicollision and herding attacks (if the hash value is short as in MD2) are more efficient than those of Dunkelman and Preneel

Induced activation in accelerator components

The residual activity induced in particle accelerators is a serious issue from the point of view of radiation safety as the long-lived radionuclides produced by fast or moderated neutrons and impact protons cause problems of radiation exposure for staff involved in the maintenance work and when decommissioning the facility. This paper presents activation studies of the magnets and collimators in the High Energy Beam Transport line of the European Spallation Source due to the backscattered neutrons from the target and also due to the direct proton interactions and their secondaries. An estimate of the radionuclide inventory and induced activation are predicted using the GEANT4 code

ER stress induces caspase-2-tBID-GSDME-dependent cell death in neurons lytically infected with herpes simplex virus type 2

Neurotropic viruses, including herpes simplex virus (HSV) types 1 and 2, have the capacity to infect neurons and can cause severe diseases. This is associated with neuronal cell death, which may contribute to morbidity or even mortality if the infection is not controlled. However, the mechanistic details of HSV-induced neuronal cell death remain enigmatic. Here, we report that lytic HSV-2 infection of human neuron-like SH-SY5Y cells and primary human and murine brain cells leads to cell death mediated by gasdermin E (GSDME). HSV-2-induced GSDME-mediated cell death occurs downstream of replication-induced endoplasmic reticulum stress driven by inositol-requiring kinase 1α (IRE1α), leading to activation of caspase-2, cleavage of the pro-apoptotic protein BH3-interacting domain death agonist (BID), and mitochondria-dependent activation of caspase-3. Finally, necrotic neurons released alarmins, which activated inflammatory responses in human iPSC-derived microglia. In conclusion, lytic HSV infection in neurons activates an ER stress-driven pathway to execute GSDME-mediated cell death and promote inflammation.</p

Peptide-oligonucleotide conjugates as nanoscale building blocks for assembly of an artificial three-helix protein mimic

Peptide-based structures can be designed to yield artificial proteins with specific folding patterns and functions. Template-based assembly of peptide units is one design option, but the use of two orthogonal self-assembly principles, oligonucleotide triple helix and a coiled coil protein domain formation have never been realized for de novo protein design. Here, we show the applicability of peptide–oligonucleotide conjugates for self-assembly of higher-ordered protein-like structures. The resulting nano-assemblies were characterized by ultraviolet-melting, gel electrophoresis, circular dichroism (CD) spectroscopy, small-angle X-ray scattering and transmission electron microscopy. These studies revealed the formation of the desired triple helix and coiled coil domains at low concentrations, while a dimer of trimers was dominating at high concentration. CD spectroscopy showed an extraordinarily high degree of α-helicity for the peptide moieties in the assemblies. The results validate the use of orthogonal self-assembly principles as a paradigm for de novo protein design