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Peter Wipf

Researcher at University of Pittsburgh

Publications -  795
Citations -  27717

Peter Wipf is an academic researcher from University of Pittsburgh. The author has contributed to research in topics: Total synthesis & Transmetalation. The author has an hindex of 83, co-authored 767 publications receiving 25316 citations. Previous affiliations of Peter Wipf include University of California, Los Angeles & University of Vermont.

Papers
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Journal ArticleDOI

Separation of Cdc25 dual specificity phosphatase inhibition and DNA cleaving activities in a focused library of analogs of the antitumor antibiotic Dnacin

TL;DR: Biological evaluation of 96 analogs and synthetic intermediates of the naphthyridinomycin-type antitumor antibiotic Dnacin led to the identification of several low-micromolar inhibitors of dual specificity phosphatases, specifically Cdc25A1, CDC25B2, and VHR, as well as the tyrosine phosphatase PTP1B.
Patent

Peptidyl prodrugs and methods of making and using the same

TL;DR: In this paper, Peptidyl prodrugs of therapeutic agents having an activating function are disclosed, which include those having an amino, thiol, or hydroxyl function.
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The GS-nitroxide JP4-039 improves intestinal barrier and stem cell recovery in irradiated mice.

TL;DR: Intestinal epithelium is identified as a novel target of radiation mitigation, and potential strategies to enhance ISC recovery and regeneration after accidental or medical exposures are identified.
Journal ArticleDOI

A Screen for Modulators of Large T Antigen's ATPase Activity Uncovers Novel Inhibitors of Simian Virus 40 and BK Virus Replication

TL;DR: In this paper, small molecule inhibitors of the essential ATPase activity of TAg would inhibit viral replication, and two FDA approved compounds, bithionol and hexachlorophene, were identified as the most potent TAg inhibitors known to date.
Journal ArticleDOI

Biological evaluation of newly synthesized quinoline-5,8-quinones as Cdc25B inhibitors.

TL;DR: Results indicate that chemical modifications on the pyridine core are tolerated, providing additional sites for future structural modification of this biologically active pharmacophore.