北海道大学・東北大学・東京工業大学・大阪大学・九州大学の共同研究ネットワーク

物質・デバイス領域共同研究拠点

新着情報

【2/23】2017有機生命・物理化学セミナー: Prof. Mark R. Chance 講演会(東北大多元研)

2018.02.23 イベント

2017有機生命・物理化学セミナー Prof. Mark R. Chance 講演会

日時: 2018年2月23日(金) 13時~14時
場所:東北大学多元物質科学研究所東1号館3階会議室

主催:物質・デバイス領域共同研究拠点、
   人・環境と物質をつなぐイノベーション創出ダイナミック・アライアンス、
   東北大学多元物質科学研究所(IMRAM) 有機・生命科学研究部門
共催:コア連携ラボセンター、東北大学多元物質科学研究所 他

題目:Network Biology for the Life Sciences
講師:Prof. Mark R. Chance, Ph.D.
(Vice Dean for Research, School of Medicine, Case Western Reserve University, Cleveland, OH, USA)

専門など:
Research Interests:The research in my laboratory is focused in the important areas of structural and cellular proteomics. High throughput methods are revolutionizing structural biology through structural genomics initiatives. We are using these advances to identify the structure and function of large macromolecular complexes in areas relevant to iron transport, mis-match repair, and actin filament assembly. New technologies in mass spectrometry are also allowing protein expression, localization, and interactions to be studied in increasing detail and on a genome wide scale. Our expertise in quantitative mass spectrometry and 2-D gel technologies are being applied to identify biomarkers and regulatory pathways in colon cancer, diabetes, radiation exposure, and HIV infection. In structural biology, structural genomics has as its goal the provision of structural models for all possible open reading frame sequences. This will be accomplished by solving the structures of 5,000-10,000 carefully selected target proteins, each one a member of a distinct protein family. The remainder of the structures will be solved by comparative modeling. Our experience in the New York Structural GenomiX Research Consortium with the 200 structures that have been solved so far is that we can model over 500 additional open reading frame sequences for each solved structure. Although structural genomics is rapidly progressing, our progress to date clearly identifies the next biological hurdle. High-throughput structural biology is optimized to examine the structure of small soluble protein domains, while critical functions of biology are controlled by larger multi-protein complexes. The availability of high resolution domain structures is critical to understanding the assemblies, the domains must "dock" with each other in a functionally relevant fashion. The long term structural goals of my laboratory are focused on understanding the structure and dynamics of these assemblies. We are using biochemical approaches, mass spectrometry, crystallography, cryo-EM, cross-linking, footprinting, and molecular modeling to understand the physiologically relevant functional states. In our expression proteomics studies, examining the post-translational modifications, amounts, and interactions of proteins are combined in integrated studies to understand the pathology of human disease. Working with investigators across the Case campus and across NE Ohio, we are developing new biomarkers to direct therapeutic approaches for patients, probing fundamental regulatory mechanisms of disease, and comparing these markers and regulatory mechanisms to those seen in normal development and normal physiology.

問合せ先:
東北大学多元物質科学研究所 教授 和田健彦( hiko[at]tohoku.ac.jp)