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200 OK - itmol.com
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Date: Sat, 03 May 2025 16:16:41 GMT
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HTTP Code 200 OK

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        <h1>株式会社理論創薬研究所</h1>
        <h2 style="font-size: 2.1em;">Institute for Theoretical Medicine, Inc.</h2>
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<section id="message" class="section section-default point">
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        <h2>メッセージ</h2>
        <h3>「天然ペプチドから最適ペプチド、そしてペプチドミメティックへ」</h3>
        <p>当社は、独自に開発した<i>in silico</i> 創薬技術を通じてペプチドミメティックによる創薬を支援いたします。</p>
        <p>革新的な医薬品の研究開発を発展させ、人々の健康と福祉に貢献することを理念としています。</p>
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          <h4>天然ペプチド (Step 1)</h4>
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          <a><img src="img/step1a.png"></a>
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          <h6>生体内でタンパク質間相互作用に寄与しているペプチドの探索</h6>
        </div>
      </div>
      
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            <h4>最適ペプチド (Step 2)</h4>
        </div>
        <div class="thumbnail">
          <a><img src="img/step2a.png"></a>
        </div>
        <div class="caption text-center">
          <h6>天然ペプチドをもとに親和性、選択性を向上させたペプチドの設計</h6>
        </div>
      </div>
      
      <div class="col-md-4">
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          <h4>ペプチドミメティク (Step 3)</h4>
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          <a><img src="img/step3a.png"></a>
        </div>
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          <h6>最適ペプチドの特徴を医薬品ライクな低分子で擬態した化合物の設計</h6>
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          <dt>２０１８年０２月１６日 プレスリリース</dt>
          <dd>(株)京都コンステラテクノロジーズ、(株)アフィニティサイエンス、(株)理論創薬研究所の3社連携によるインシリコ創薬戦略コンサルティングサービスの開始<a href="./pdf/DrugDiscoveryConsulting_Press20180216.pdf" target="_blank"><i class="fa fa-file-pdf-o" style="color:red;"></i></a></dd>
          <br>
          <dt>２０１５年１２月９日 プレスリリース</dt>
          <dd>田辺三菱製薬株式会社、日本電気株式会社、株式会社理論創薬研究所の3社共同でインシリコ創薬での高精度かつ高速なアプローチを開発 <a href="./pdf/ITM151209.pdf" target="_blank"><i class="fa fa-file-pdf-o" style="color:red;"></i></a></dd>
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          <h4>創薬研究</h4>
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          </div>
          <p>アポトーシス関連タンパク質を中心にタンパク質間相互作用を標的としたペプチドミメティクスの創製を行っています。</p>
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          <h4>創薬支援</h4>
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            <a><img src="img/act2.png"></a>
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          <p>製薬企業、創薬ベンチャー企業との共同研究、並びに受託研究を通じてペプチドミメティクスによる創製を支援しています。</p>
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          <h4>ソフトウェア販売</h4>
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            <a><img src="img/act3.png"></a>
          </div>
          <p>化合物検索システムの販売、並びに創薬支援ソフトウェアの受託開発を行っています。</p>
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          <h4>情報提供サイト運営</h4>
          <div class="thumbnail">
            <a><img src="img/act4.png"></a>
          </div>
          <p>Chemoinformaticsに関連するプログラミングを中心に情報提供を行うCheminformist</a>を運営しています。</p>
        </div>
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<section id="company" class="section section-inverse japanese-font">
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        <h2 class="subtitle">会社概要</h2>
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        <dt>社名:</dt><dd>株式会社理論創薬研究所</dd>
        <dt>住所:</dt><dd>神奈川県藤沢市村岡東二丁目26番地の1 湘南ヘルスイノベーションパーク BW3M-20B</dd>
        <dt>設立:</dt><dd>平成16年2月</dd>
        <dt>代表取締役:</dt><dd>吉森 篤史</dd>
        <dt>顧問:</dt><dd>田沼 靖一</dd>
        <dt>問い合わせ先:</dt><dd><a><img src="img/info.png"></a></dd>
        </dl>
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</section>

<section id="research" class="section section-default japanese-font">
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        <h2 class="subtitle">研究成果</h2>
        <h5 class="subtitle">当社研究員 (下線) が学会誌、専門誌に発表した論文をご紹介いたします(共著含む)。</h5>
        <ul>
          <li>New Insights into the Roles of NAD+-Poly(ADP-ribose) Metabolism and Poly(ADP-ribose) Glycohydrolase. Tanuma SI, Sato A, Oyama T, <u>Yoshimori A</u>, Abe H, Uchiumi F. <i>Curr Protein Pept Sci.</i> 2016 [in press]</li>
          <li>Structure-activity relationships of the thujaplicins for inhibition of human tyrosinase. <u>Yoshimori A</u>, Oyama T, <u>Takahashi S</u>, Abe H, Kamiya T, Abe T, Tanuma S. <i>Bioorg Med Chem.</i> 2014;22(21):6193-200.</li>
          <li>Structure-based design of dipeptide derivatives for the human neutral endopeptidase. Misawa K, Suzuki Y, <u>Takahashi S</u>, <u>Yoshimori A</u>, Takasawa R, Shibuya Y, Tanuma S. <i>Bioorg Med Chem.</i> 2011;19(20):5935-47.</li>
          <li>Discovery of a new type inhibitor of human glyoxalase I by myricetin-based 4-point pharmacophore. Takasawa R, Tao A, Saeki K, Shionozaki N, Tanaka R, Uchiro H, <u>Takahashi S</u>, <u>Yoshimori A</u>, Tanuma S. <i>Bioorg Med Chem Lett.</i> 2011 ;21(14):4337-42.</li>
          <li>Structural insights into the hot spot amino acid residues of mushroom tyrosinase for the bindings of thujaplicins. <u>Takahashi S</u>, Kamiya T, Saeki K, Nezu T, Takeuchi S, Takasawa R, Sunaga S, <u>Yoshimori A</u>, Ebizuka S, Abe T, Tanuma S. <i>Bioorg Med Chem.</i> 2010;18(22):8112-8. </li>
          <li>A new small molecule that directly inhibits the DNA binding of NF-kappaB. Kobayashi T, <u>Yoshimori A</u>, Kino K, Komori R, Miyazawa H, Tanuma S. <i>Bioorg Med Chem.</i> 2009;17(14):5293-7.</li>
          <li>Structure-based discovery of a novel non-peptidic small molecular inhibitor of caspase-3. Sakai J, <u>Yoshimori A</u>, Nose Y, Mizoroki A, Okita N, Takasawa R, Tanuma S. <i>Bioorg Med Chem.</i> 2008;16(9):4854-9. </li>
          <li>Structure-activity relationship of human GLO I inhibitory natural flavonoids and their growth inhibitory effects. Takasawa R, <u>Takahashi S</u>, Saeki K, Sunaga S, <u>Yoshimori A</u>, Tanuma S. <i>Bioorg Med Chem.</i> 2008;16(7):3969-75.</li>
          <li>Structural and functional definition of the specificity of a novel caspase-3 inhibitor, Ac-DNLD-CHO. <u>Yoshimori A</u>, Sakai J, Sunaga S, Kobayashi T, <u>Takahashi S</u>, Okita N, Takasawa R, Tanuma S. <i>BMC Pharmacol.</i> 2007;7:8.</li>
          <li>Structure basis for the inhibitory mechanism of a novel DNase gamma-specific inhibitor, DR396. Sunaga S, <u>Yoshimori A</u>, Shiokawa D, Tanuma S. <i>Bioorg Med Chem.</i> 2006;14(12):4217-26.</li>
          <li>A novel inhibitor that protects apoptotic DNA fragmentation catalyzed by DNase gamma. Sunaga S, Kobayashi T, <u>Yoshimori A</u>, Shiokawa D, Tanuma S. <i>Biochem Biophys Res Commun.</i> 2004;325(4):1292-7.</li>
          <li>A novel method for evaluation and screening of caspase inhibitory peptides by the amino acid positional fitness score. <u>Yoshimori A</u>, Takasawa R, Tanuma S. <i>BMC Pharmacol.</i> 2004;4:7.</li>
        </ul>
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