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Paul J. Hergenrother

Researcher at University of Illinois at Urbana–Champaign

Publications -  248
Citations -  11457

Paul J. Hergenrother is an academic researcher from University of Illinois at Urbana–Champaign. The author has contributed to research in topics: Cancer & Cancer cell. The author has an hindex of 51, co-authored 231 publications receiving 9767 citations. Previous affiliations of Paul J. Hergenrother include Urbana University & University of Texas at Austin.

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DNA as a target for anticancer compounds: methods to determine the mode of binding and the mechanism of action.

TL;DR: This review provides a summary of the assays that should be performed when it is suspected that DNA may be a target for a given small molecule, and a battery of in vitro assays readily distinguishes between DNA intercalation, DNA groove binding, and the inhibition of topoisomerases.
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Targeting RNA with small molecules

TL;DR: A comparison study of RNA binding in NMR-based and electrospray Ionization Mass Spectrometry-Based methods found that the former showed superior results while the latter showed better results in relation to the latter.
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Predictive compound accumulation rules yield a broad-spectrum antibiotic

TL;DR: These guidelines were then applied to convert deoxynybomycin, a natural product that is active only against Gram-positive organisms, into an antibiotic with activity against a diverse panel of multi-drug-resistant Gram-negative pathogens.
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How many human proteoforms are there

Ruedi Aebersold, +53 more
TL;DR: This work frames central issues regarding determination of protein-level variation and PTMs, including some paradoxes present in the field today, and uses this framework to assess existing data and ask the question, "How many distinct primary structures of proteins (proteoforms) are created from the 20,300 human genes?"
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Dissecting glucose signalling with diversity-oriented synthesis and small-molecule microarrays

TL;DR: It is demonstrated that diversity-oriented synthesis and small-molecule microarrays can be used to identify small molecules that bind to a protein of interest, and that these small molecules can regulate specific functions of the protein.