Marcia E. Newcomer
Vanderbilt University
21 Papers
209 Citations
Marcia E. Newcomer is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Retinoic acid & Retinoic acid binding. The author has an hindex of 13, co-authored 21 publications.
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Papers
Plasma retinol binding protein: structure and function of the prototypic lipocalin.
Marcia E. Newcomer,David E. Ong +1 more
TL;DR: In terms of both structure and biological function, retinol binding protein (RBP) is one of the best characterized members of the lipocalin superfamily.
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The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme.
Patrick W. Bilder,Sandra Lightle,Graeme Bainbridge,Jeffrey F. Ohren,Barry C. Finzel,Fang Sun,Susan Holley,Loola Al-Kassim,Cindy Spessard,Michael Melnick,Marcia E. Newcomer,Grover L. Waldrop +11 more
TL;DR: The structures of the bacterial CT subunits from two prevalent nosocomial pathogens, Staphylococcus aureus and Escherichia coli, are presented and both reveal a small, independent zinc-binding domain that lacks a complement in the primary sequence or structure of the eukaryotic homologue.
The structure of retinal dehydrogenase type II at 2.7 A resolution: implications for retinal specificity.
TL;DR: The crystal structure of retinal dehydrogenase type II cocrystallized with nicotinamide adenine dinucleotide (NAD) has been determined and it appears to utilize a disordered loop in the substrate access channel to discriminate between retinaldehyde and short-chain aldehydes.
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The SH3 domain of Eps8 exists as a novel intertwined dimer
TL;DR: Co-immunoprecipitation experiments show that intact Eps8 is multimeric in vivo, and the X-ray crystallographic structure of the Eps8 SH3 domain reveals a novel variation of the canonical SH3 fold, which may represent a dimerization motif.
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Structure of the epididymal retinoic acid binding protein at 2.1 Å resolution
TL;DR: E-RABP achieves high-affinity binding of both all-trans and 9-cis isomers of retinoic acid by forcing the all- trans form to bind in a folded conformation, and the RAR family of nuclear receptors for retinoi acid also binds both isomers, and their binding sites may therefore be similar.
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