Keio University · 의학
히라시 후미유키 교수의 연구실은 암의 정밀의료를 위한 유전자 기반 진단과 치료 전략 개발에 초점을 맞추고 있습니다. 특히 췌장암을 비롯한 다양한 암에서의 드라이버 유전자 변이, 미세위성 불안정성(MSI-H) 및 복합 유전자 프로파일링을 위한 NGS 기반 분석 기술 개발이 핵심 연구 분야입니다. 임상 적용에 적합한 고정밀 유전자 검사 시스템 구축과 함께, 약물 반응성 및 부작용에 대한 분자 기반 연구도 병행하고 있습니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
The number of mutated driver genes assessed using a targeted deep sequencing assay was a promising prognostic biomarker for pancreatic cancer.
Various malignancies exhibit high microsatellite instability (MSI-H) or mismatch repair deficiency (dMMR). The MSI-IVD kit, a polymerase chain reaction (PCR)-based method, was the first tumor-agnostic companion diagnostic to detect MSI status in MSI-H solid tumors. Recently, next-generation sequencing (NGS), which can also detect MSI-H/dMMR, has been made clinically available; however, its real-world concordance with PCR-based testing of MSI-H/dMMR remains to be investigated. The co-primary end
Precision medicine is a promising strategy for cancer treatment. In this study, we developed an in-house clinical sequencing system to perform a comprehensive cancer genomic profiling test as a clinical examination and analyzed the utility of this system. Genomic DNA was extracted from tumor tissues and peripheral blood cells collected from 161 patients with different stages and types of cancer. A comprehensive targeted amplicon exome sequencing for 160 cancer-related genes was performed using n
When carefully managed, FOLFIRINOX is acceptably safe and efficacious in Japanese patients with unresectable pancreatic cancer.
Journal Article Multiple fixed drug eruption caused by acetaminophen Get access H. Hayashi, H. Hayashi Department of Dermatology, Hokkaido University Graduate School of Medicine, Kita‐ku, Sapporo 060‐8638, Japan Search for other works by this author on: Oxford Academic Google Scholar T. Shimizu, T. Shimizu Department of Dermatology, Hokkaido University Graduate School of Medicine, Kita‐ku, Sapporo 060‐8638, Japan Search for other works by this author on: Oxford Academic Google Scholar H. Shimizu
The reaction of Escherichia coli aspartate aminotransferase (AspAT) with L-erythro-3-hydroxyaspartate (HOAsp) produces an intense absorption at 494 nm (epsilon = 13,650 M-1 cm-1), which is ascribed to the quinonoid intermediate. However, when Tyr70 of AspAT has been replaced by Phe, the enzyme shows only a faint absorption at 494 nm (epsilon = 522 M-1 cm-1) on the reaction with HOAsp. This indicates the involvement of the hydroxy group of Tyr70 in stabilizing the quinonoid intermediate formed fr
Journal Article Epidermotropic metastatic malignant melanoma with a pedunculated appearance Get access H. Hayashi, H. Hayashi Department of Dermatology, Hokkaido University Graduate School of Medicine, N15, W7, Sapporo 060‐8638, Japan Search for other works by this author on: Oxford Academic Google Scholar T. Kawashima, T. Kawashima Department of Dermatology, Hokkaido University Graduate School of Medicine, N15, W7, Sapporo 060‐8638, Japan Search for other works by this author on: Oxford Academi
