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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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Preliminary X-ray crystallographic investigation of human parvovirus B19.

TL;DR: Crystals that diffract X rays to at least 8 A resolution have been grown from human B19 parvovirus empty capsids, possibly the first time that a self-assembled empty viral capsid, grown in other than normal host cells, has been crystallized.
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AAV6 K531 serves a dual function in selective receptor and antibody ADK6 recognition.

TL;DR: This study expands the available repertoire of AAV-antibody information that can guide the design of host immune escaping AAV vectors able to maintain capsid functionality through identification of residues on the virus capsid important for these interactions and changing them.
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Crystallographic and molecular modeling studies on 3-ethyl-3-(4-pyridyl)piperidine-2,6-dione and its butyl analogue, inhibitors of mammalian aromatase. Comparison with natural substrates: prediction of enantioselectivity for N-alkyl derivatives.

TL;DR: Inhibitors of the cytochrome P450 enzyme aromatase, which is involved in the biosynthesis of estrogens from androgens, are of proven utility in the treatment of hormone-dependent breast cancer and the determination of the crystal structure of one such inhibitor is described.
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Atomic structure of a rationally engineered gene delivery vector, AAV2.5.

TL;DR: AAV2.5 represents the first structure-guided in-silico designed Adeno-associated virus (AAV) gene delivery vector and adopts the AAV1 conformation indicating the importance of amino acid residues in dictating VP structure.
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Recombinant plasmepsin 1 from the human malaria parasite Plasmodium falciparum: Enzymatic characterization, active site inhibitor design, and structural analysis

TL;DR: A mutated form of truncated proplasmepsin 1 from the human malaria parasite Plasmodium falciparum, proPfPM1 K110pN, was generated and overexpressed in Escherichia coli, and this mature PfPM1 showed comparable binding affinity to peptide substrates and inhibitors with the naturally occurring form isolated from parasites.