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Robert McKenna

Researcher at University of Florida

Publications -  481
Citations -  23708

Robert McKenna is an academic researcher from University of Florida. The author has contributed to research in topics: Carbonic anhydrase & Carbonic anhydrase II. The author has an hindex of 78, co-authored 457 publications receiving 21349 citations. Previous affiliations of Robert McKenna include University of South Carolina & Florida State University College of Arts and Sciences.

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Structural Insights into Human Bocaparvoviruses.

TL;DR: Comparisons at the strain and genus levels identified differences in surface loops that are functionally important in host/tissue tropism, pathogenicity, and antigenicity in other parvoviruses and likely play similar roles in these viruses.
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CAIX forms a transport metabolon with monocarboxylate transporters in human breast cancer cells.

TL;DR: The study shows that carbonic anhydrases form transport metabolons with acid/base transporters in human tumor tissue and that these interactions can be exploited to interfere with tumor metabolism and proliferation.
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Structural insights and functional implications of choline acetyltransferase

TL;DR: The crystal structure of rat ChAT (rChAT) is a monomer and consists of two domains with an interfacial active site tunnel that provides critical insights into the molecular basis for the production of acetylcholine and may further the understanding of disease causing mutations.
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Structure of the unbound form of HIV-1 subtype A protease: comparison with unbound forms of proteases from other HIV subtypes.

TL;DR: The crystal structure of the unbound form of HIV-1 subtype A protease (PR) has been determined to 1.7 A resolution and refined as a homodimer in the hexagonal space group P6(1) to an R(cryst) of 20.5%.
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Joint neutron crystallographic and NMR solution studies of Tyr residue ionization and hydrogen bonding: Implications for enzyme-mediated proton transfer

TL;DR: Detailed interrogation of tyrosines in HCA II by NMR and neutron crystallography revealed a significantly lowered pKa of Tyr7 and how pH and Tyr proximity to Zn affect hydrogen-bonding interactions, which have broad implications for understanding of proton transfer.