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Department: search.filters.department.Department of Chemical and Biological EngineeringSubject: search.filters.subject.Medicinal

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Now showing 1 - 2 of 2
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    Discovery of novel CYP17 inhibitors for the treatment of prostate cancer with structure-based drug design
    (Bentham Science Publ Ltd, 2009) N/A; N/A; N/A; Department of Chemical and Biological Engineering; Department of Industrial Engineering; Armutlu, Pelin; Özdemir, Muhittin Emre; Özdaş, Şule Beyhan; Kavaklı, İbrahim Halil; Türkay, Metin; Master Student; Master Student; Researcher; Faculty Member; Faculty Member; Department of Chemical and Biological Engineering; Department of Industrial Engineering; Graduate School of Sciences and Engineering; Graduate School of Sciences and Engineering; Graduate School of Sciences and Engineering; College of Engineering; College of Engineering; N/A; N/A; N/A; 40319; 24956
    It has been shown that prostate cancer is associated with elevated androgen biosynthesis; therefore, inhibiting the activity of Cytochrome P450 17 (CYP17) may prevent progression of prostate cancer. In this study we identified, using in silico and experimental methods, two novel steroidal and non-steroidal lead compounds that inhibit the activity CYP17.
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    Taming oncogenic signaling at protein interfaces: challenges and opportunities
    (Bentham Science Publ Ltd, 2015) N/A; N/A; Department of Chemical and Biological Engineering; Department of Computer Engineering; Cavga, Ayşe Derya; Karahan, Nilay; Keskin, Özlem; Gürsoy, Attila; PhD Student; PhD Student; Faculty Member; Faculty Member; Department of Chemical and Biological Engineering; Department of Computer Engineering; Graduate School of Sciences and Engineering; Graduate School of Sciences and Engineering; College of Engineering; College of Engineering; N/A; N/A; 26605; 8745
    Many key cellular events determining the thin line between healthy and oncogenic behavior rely on the proper functioning of protein-protein interactions (PPIs). Alterations that affect the affinity of a protein-protein binding site may destabilize a desired healthy interaction, or stabilize an oncogenic interaction. The understanding that there are a few key hot-spot residues that are mainly responsible for the binding energy of an interaction greatly widened the prospects of targeting oncogenic protein-protein interfaces enabling the use of small ligands in addition to biological molecules such as peptides and antibodies. Taming oncogenic signaling requires a deep understanding of protein interactions and their networks. Traditional representation of PPIs in signaling pathways as nodes and edges falls short of expressing interaction specific modulation of signals. Structural networks, deciphering which sites on a protein structure are responsible for each of the many interactions it may carry out, help understanding specific oncogenic mutations on signaling. We describe the key features of PPIs and their targeting, together with the advantages of structural networks, and provide four case studies demonstrating different opportunities for the aim of modulating oncogenic interactions.