東京大学 · Immunology and Microbiology
Toshiyuki Shimizu 교수의 연구실은 단백질의 후성변환, 특히 유비퀴틴화와 관련된 효소들(특히 E3 리가제)의 구조 기반 기전 해석을 핵심으로 삼고 있습니다. 또한 신경섬유종증 2(NF2)과 관련된 페르민 단백질의 구조 기반 기능 해석을 통해 종양 suppressor 기전을 규명하고 있으며, 숙주 면역 반응의 핵심 수용체인 TLR 수용체의 구조 기반 작동 메커니즘 연구도 진행하고 있습니다. 이들의 연구는 질병 기전 규명과 약물 타겟 발굴에 기여하고 있습니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiquitination reaction: ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3). E3s play a pivotal role in selecting substrates. Many structural studies have been
Neurofibromatosis type 2 (NF2) is a dominantly inherited disease associated with the central nervous system. The NF2 gene product merlin is a tumor suppressor, and its mutation or inactivation causes this disease. We report here the crystal structure of the merlin FERM domain containing a 22-residue alpha-helical segment. The structure reveals that the merlin FERM domain consists of three subdomains displaying notable features of the electrostatic surface potentials, although the overall surface
Recognition of invading pathogens by the innate immune system is essential to initiate antimicrobial responses and trigger adaptive immunity. This is largely mediated by an array of pattern-recognition receptor families that are essential for recognizing conserved molecular motifs characteristic of pathogenic microbes. One such family is the Toll-like receptors (TLRs). Activation of TLRs induces production of pro-inflammatory cytokines and type I interferons: the former triggers the synthesis of
