An American in Japan : William Merrell Vories (Hitotsuyanagi), 1905-1964

論説application/pdfdepartmental bulletin pape

1980年代のイギリス産業の資本蓄積と産業政策

Articledepartmental bulletin pape

SBML Level 3: an extensible format for the exchange and reuse of biological models

Abstract Systems biology has experienced dramatic growth in the number, size, and complexity of computational models. To reproduce simulation results and reuse models, researchers must exchange unambiguous model descriptions. We review the latest edition of the Systems Biology Markup Language (SBML), a format designed for this purpose. A community of modelers and software authors developed SBML Level 3 over the past decade. Its modular form consists of a core suited to representing reaction‐based models and packages that extend the core with features suited to other model types including constraint‐based models, reaction‐diffusion models, logical network models, and rule‐based models. The format leverages two decades of SBML and a rich software ecosystem that transformed how systems biologists build and interact with models. More recently, the rise of multiscale models of whole cells and organs, and new data sources such as single‐cell measurements and live imaging, has precipitated new ways of integrating data with models. We provide our perspectives on the challenges presented by these developments and how SBML Level 3 provides the foundation needed to support this evolution

SBML Level 3: an extensible format for the exchange and reuse of biological models

Systems biology has experienced dramatic growth in the number, size, and complexity of computational models. To reproduce simulation results and reuse models, researchers must exchange unambiguous model descriptions. We review the latest edition of the Systems Biology Markup Language (SBML), a format designed for this purpose. A community of modelers and software authors developed SBML Level 3 over the past decade. Its modular form consists of a core suited to representing reaction-based models and packages that extend the core with features suited to other model types including constraint-based models, reaction-diffusion models, logical network models, and rule-based models. The format leverages two decades of SBML and a rich software ecosystem that transformed how systems biologists build and interact with models. More recently, the rise of multiscale models of whole cells and organs, and new data sources such as single-cell measurements and live imaging, has precipitated new ways of integrating data with models. We provide our perspectives on the challenges presented by these developments and how SBML Level 3 provides the foundation needed to support this evolution.journal articl

有害化学物質を考える

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An Overview of Igbo Oral Literature

departmental bulletin pape

A New Scheme for Information Systems Design

departmental bulletin pape

第二次世界大戦中のイギリスのギリシャ政策(一) : 1939-1944

2000-12-25departmental bulletin pape

Inhibition of PRIMA-1 mediated transcriptional reactivation function of p53 with pifithrin-α (PFTα)

<p><b>Copyright information:</b></p><p>Taken from "Proteomic identification of heat shock protein 90 as a candidate target for p53 mutation reactivation by PRIMA-1 in breast cancer cells"</p><p>Breast Cancer Research 2005;7(5):R765-R774.</p><p>Published online 27 Jul 2005</p><p>PMCID:PMC1242148.</p><p>Copyright © 2005 Rehman et al.; licensee BioMed Central Ltd.</p> MCF-7 (p53) and GI-101A (mut p53) cells were treated with 100 μM PRIMA-1 for 2, 4 and 8 hours (lanes 1, 2 and 3, respectively). Cells were treated with 20 μM PFTα for 6 hours (lane 4) or with 20 μM PFTα for 2 hours followed by PRIMA-1 for 4 hours (lane 5). 20 μg of protein samples of cell lysates were separated by SDS-PAGE (4 to 20% polyacrylamide) and subjected to Western blot analysis with p53 and p21 primary antibodies. The reactive bands were revealed and detected with the Odyssey™ Infrared Imaging System. β-Actin was used as a loading control for protein samples

Protein-protein interaction analysis of p53 and the α isoform of heat shock protein 90 (Hsp90α)

<p><b>Copyright information:</b></p><p>Taken from "Proteomic identification of heat shock protein 90 as a candidate target for p53 mutation reactivation by PRIMA-1 in breast cancer cells"</p><p>Breast Cancer Research 2005;7(5):R765-R774.</p><p>Published online 27 Jul 2005</p><p>PMCID:PMC1242148.</p><p>Copyright © 2005 Rehman et al.; licensee BioMed Central Ltd.</p> MDA-231 cell lysates from untreated cells (lanes 1 and 3) and cells treated for 4 hours with 100 μM PRIMA-1 (lanes 2 and 4) were immunoprecipitated (IP) with anti-Hsp90α monoclonal antibody and subjected to Western blotting (WB) with anti-p53 (DO-1) monoclonal antibody (lanes 1 and 2) in addition to reciprocal immunoprecipitation with DO-1 and Western blotting with anti-Hsp90α (lanes 3 and 4). GI-101A cell lysates from untreated cells (lanes 1 and 3) and cells treated for 4 hours with 100 μM PRIMA-1 (lanes 2 and 4) were immunoprecipitated with anti-Hsp90α monoclonal antibody and subjected to Western blotting with anti-p53 (DO-1) monoclonal antibody (lanes 1 and 2) in addition to reciprocal immunoprecipitation with DO-1 and Western blotting with anti-Hsp90α (lanes 3 and 4)