Sandra Lightle
Pfizer
11 Papers
99 Citations
Sandra Lightle is an academic researcher from Pfizer. The author has contributed to research in topics: Pyruvate carboxylase & Lipid A. The author has an hindex of 11, co-authored 11 publications. Previous affiliations of Sandra Lightle include Vanderbilt University.
Chat about Author
Papers
Discovery of Antibacterial Biotin Carboxylase Inhibitors by Virtual Screening and Fragment-Based Approaches.
Igor Mochalkin,J. Richard Miller,Lakshmi Narasimhan,Venkataraman Thanabal,Paul Erdman,Philip B. Cox,J.V.N. Vara Prasad,Sandra Lightle,Michael D. Huband,C. Kendall Stover +9 more
TL;DR: This work employed a unique combination of two emergent lead discovery strategies that used both de novo fragment-based drug discovery and virtual screening, which employs 3D shape and electrostatic property similarity searching to identify novel antibacterial agents.
105
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.
Structural evidence for substrate‐induced synergism and half‐sites reactivity in biotin carboxylase
Igor Mochalkin,J. Richard Miller,Artem G. Evdokimov,Sandra Lightle,Chunhong Yan,Charles Ken Stover,Grover L. Waldrop +6 more
TL;DR: A series of structures of BC from several bacteria crystallized in the presence of various ATP analogs is described that addresses three major questions concerning the catalytic mechanism and provides the first structural evidence for half‐sites reactivity in BC.
85
Characterization of substrate binding and catalysis in the potential antibacterial target N‐acetylglucosamine‐1‐phosphate uridyltransferase (GlmU)
Igor Mochalkin,Sandra Lightle,Yaqi Zhu,Jeffrey F. Ohren,Cindy Spessard,Nickolay Y. Chirgadze,Nickolay Y. Chirgadze,Nickolay Y. Chirgadze,Craig Banotai,Michael Melnick,Laura McDowell +10 more
TL;DR: The new data strongly suggest that the mechanism of phosphotransfer in the uridyltransferase reaction in GlmU is primarily through an associative mechanism with a pentavalent phosphate intermediate and an inversion of stereochemistry.
46
Mutations within a human IgG2 antibody form distinct and homogeneous disulfide isomers but do not affect Fc gamma receptor or C1q binding
Sandra Lightle,Serdar Aykent,Nathan A. Lacher,Vesselin Mitaksov,Kristine Wells,James F. Zobel,Oliphant Theodore Lawrence +6 more
TL;DR: There was no observed difference in binding to any of the Fc gamma receptors or C1q between the mutants and the wild‐type IgG2, however, differences were seen in the apparent binding affinity of these antibodies that were dependent on the selection of the secondary detection antibody used.
46