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Yujing-MS-Thesis-2015-final.pdf (949.56 KB)

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Specificty and Inhibition of Protein Tyrosine Phosphatases

Zhai, Yujing
http://rave.ohiolink.edu/etdc/view?acc_num=osu1429223068

Abstract Details

2015, Master of Science, Ohio State University, Chemistry.
Protein tyrosine phosphatases (PTPs) are proteins which are responsible for removing phosphate group on tyrosine. Although the reaction mechanism of dephosphorylation has been well estabilished, the substrate specificity and physiological roles of PTPs still remain undefined. In this work, modified PTP substrates were utilized to investigate their interactions with PTPs. Moreover, PTPs have been shown to be closely related to many disease including diabetes, obesity and cancer. Therefore development of PTP inhibitors for therapeutic purpose is of great significance. In this work, a One-bead-one-compound library was built to screen for potential PTP1B inhibitors. The positive hits were distinct from the negative ones and they have shown sequence consensus. The hits showed decant inhibition on PTP1B and they will be promising inhibitors after further improvement.
Dehua Pei, Dr. (Advisor)
Ross Dalbey, Dr. (Committee Member)
45 p.
Chemistry

Recommended Citations

Citations

  • Zhai, Y. (2015). Specificty and Inhibition of Protein Tyrosine Phosphatases [Master's thesis, Ohio State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=osu1429223068

    APA Style (7th edition)

  • Zhai, Yujing. Specificty and Inhibition of Protein Tyrosine Phosphatases. 2015. Ohio State University, Master's thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=osu1429223068.

    MLA Style (8th edition)

  • Zhai, Yujing. "Specificty and Inhibition of Protein Tyrosine Phosphatases." Master's thesis, Ohio State University, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=osu1429223068

    Chicago Manual of Style (17th edition)

osu1429223068
211
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This open access ETD is published by The Ohio State University and OhioLINK.