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Recently, several practical attacks raised serious concerns over the security of searchable encryption. The attacks have brought emphasis on forward privacy, which is the key concept behind solutions to the adaptive leakage-exploiting attacks, and will very likely to become mandatory in the design of new searchable encryption schemes. For a long time, forward privacy implies inefficiency and thus most existing searchable encryption schemes do not support it. Very recently, Bost (CCS 2016) showed that forward privacy can be obtained without inducing a large communication overhead. However, Bost's scheme is constructed with a relatively inefficient public key cryptographic primitive, and has a poor I/O performance. Both of the deficiencies significantly hinder the practical efficiency of the scheme, and prevent it from scaling to large data settings. To address the problems, we first present FAST, which achieves forward privacy and the same communication efficiency as Bost's scheme, but uses only symmetric cryptographic primitives. We then present FASTIO, which retains all good properties of FAST, and further improves I/O efficiency. We implemented the two schemes and compared their performance with Bost's scheme. The experiment results show that both our schemes are highly efficient, and FASTIO achieves a much better scalability due to its optimized I/O.

Senescence is a result of cellular stress and is a potential mechanism for regulating cancer. As a member of the mitogen-activated protein kinase family, ERK1/2 (extracellular signal-regulated protein kinase) has an important role in delivering extracellular signals to the nucleus, and these signals regulate the cell cycle, cell proliferation and cell development. Previous studies demonstrated that ERK1/2 is closely associated with cell aging; however other previous studies suggested that ERK1/2 exerts an opposite effect on aging models and target proteins, even within the same cell model. Recent studies demonstrated that the effect of ERK1/2 on aging is likely associated with its target proteins and regulators, negative feedback loops, phosphorylated ERK1/2 factors and ERK1/2 translocation from the cytoplasm to the nucleus. The present review aims to examine the mechanism of ERK1/2 and discuss its role in cellular outcomes and novel drug development.

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