Patrick W. Bilder
Albert Einstein College of Medicine
7 Papers
52 Citations
Patrick W. Bilder is an academic researcher from Albert Einstein College of Medicine. The author has contributed to research in topics: Mevalonate kinase & Mycobacterium tuberculosis. The author has an hindex of 7, co-authored 7 publications. Previous affiliations of Patrick W. Bilder include Louisiana State University & Yeshiva University.
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Papers
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.
Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold.
TL;DR: The crystal packing reveals a helical assembly that is constructed from two possible tetrameric oligomers of IscA, a novel fold in which mixed beta-sheets form a compact alpha-beta sandwich domain.
Antibodies against immunodominant antigens of Mycobacterium tuberculosis in subjects with suspected tuberculosis in the United States compared by HIV status
Jacqueline M. Achkar,Elisabeth Jenny-Avital,Xian Yu,Susanne Burger,Eric Leibert,Patrick W. Bilder,Steven C. Almo,Arturo Casadevall,Suman Laal,Suman Laal +9 more
TL;DR: Serum antibody reactivity to recombinant purified MS and MPT51 was determined by enzyme-linked immunosorbent assays of samples from TB suspects and well-characterized control groups, and a positive anti-MPT51 antibody response was strongly and significantly associated with TB among U.S. HIV+ TB suspects.
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Crystal structure of the Streptococcus pneumoniae mevalonate kinase in complex with diphosphomevalonate
John Lawrence Andreassi,Patrick W. Bilder,Matthew W. Vetting,Steven L. Roderick,Thomas S. Leyh +4 more
TL;DR: Structural comparison of SpMK with other members of the GHMP kinase family reveals that DPM functions as a partial bisubstrate analog (mevalonate linked to the pyrophosphoryl moiety of ATP) in that it elicits a ternary‐complexlike form of the enzyme, except for localized disordering in a region that would otherwise interact with the missing portion of the nucleotide.
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Structure of the Ternary Complex of Phosphomevalonate Kinase: The Enzyme and Its Family
John Lawrence Andreassi,Matthew W. Vetting,Patrick W. Bilder,Steven L. Roderick,Thomas S. Leyh +4 more
TL;DR: Analysis of all available GHMP kinase ternary complex structures reveals that while their C(alpha)-scaffolds are highly conserved, their substrates bind in one of two conformations, which appear to be either reactive or nonreactive.