Synthetic agents that disrupt intracellular protein–protein interactions (PPIs) are desirable for elucidating cellular signaling networks and for development of new therapeutics. However, designing large cell-permeable molecules that are equipped with many functional groups necessary for binding to protein interfaces still remains a challenge. Recent studies of self-assembling small molecules have shed light on the robustness of approaches based on artificial synthetic platforms towards protein surface recognition with a wide range of applications, including library synthesis, protein sensing, and in situ generation of bioactive molecules. This review illustrates recently developed strategies of protein-templated assembly, in which self-assembly of small molecules is induced by binding to a targeted protein. Following chemical reactions between the fragments results in generation of a conjugated molecule, which is capable of modulating functions of water-exposed protein surfaces.

Protein ubiquitination plays indispensable roles in the regulation of cell homeostasis and pathogenesis of neoplastic, infectious, and neurodegenerative diseases. As ubiquitination is involved in diverse aspects of cellular physiology, many pathogenic bacteria use various strategies to target the cellular ubiquitin-proteasome system (UPS) to inactivate host defense systems and establish infections. Recent studies have identified several bacterial effectors that modulate the UPS during pathogenic infection. These effectors are classified into three groups: (1) effectors with UPS enzyme activity; (2) effectors that are targeted by the host ubiquitin ligases and thereby rapidly inactivated by degradation or modified by ubiquitination, thereby diversifying effector function; and (3) effectors that modulate steps of the UPS. This review will describe the most recent findings, including from structural analyses, on how pathogenic bacteria use ubiquitination of proteins to establish an infection.

Most anticancer drugs have the ability to suppress proliferation of the cancer cells. However, these drugs also induce the suppressant effect on normal cells. In contrast, the molecular target drugs that inhibit the molecules related to cell growth, permeation, metastasis of cancer cells attack only cancer cells, and are expected to reduce damage for normal cells. Small molecule compounds and monoclonal antibodies to the molecular targets have been developed. It has been found that sphingolipid metabolism participates deeply in various cell functions such as cell proliferation, cell death and metastasis of cancer cells. In addition, many studies suggest that these inhibitors enhance the apoptosis of cancer cells. This review is an overview of our understanding of the role of sphingolipid metabolism including ceramide and sphingosine 1-phosphate in cell proliferation and cell death in cancer and provides the possibility that inhibition of the sphingolipid metabolism is a candidate for the molecular target drugs of cancer.