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Lisa M. Jones

Researcher at University of Maryland, Baltimore

Publications -  32
Citations -  1040

Lisa M. Jones is an academic researcher from University of Maryland, Baltimore. The author has contributed to research in topics: Protein footprinting & Protein structure. The author has an hindex of 19, co-authored 32 publications receiving 856 citations. Previous affiliations of Lisa M. Jones include Washington University in St. Louis & Indiana University – Purdue University Indianapolis.

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Fast Photochemical Oxidation of Proteins for Epitope Mapping

TL;DR: This study reports the use of footprinting via fast photochemical oxidation of proteins (FPOP) with OH radicals to characterize the epitope of the serine protease thrombin, the first time oxidative labeling has been used for epitope mapping.
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Rational design of a calcium-binding protein.

TL;DR: This experiment is the first successful metalloprotein design that has a high coordination number (seven) metal-binding site constructed into a beta-sheet protein and the resulting site exhibits strong metal selectivity.
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Fast Photochemical Oxidation of Proteins for Comparing Structures of Protein−Ligand Complexes: The Calmodulin−Peptide Model System

TL;DR: The results show that the three calmodulin-peptide complexes have similar structures but also reveal those regions of the protein that became more or less solvent-accessible upon binding, which has the potential for relatively high throughput, information-dense characterization of a series of protein-ligand complexes in biochemistry and drug discovery.
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In Cell Footprinting Coupled with Mass Spectrometry for the Structural Analysis of Proteins in Live Cells.

TL;DR: An oxidative-based footprinting approach inside cells in which hydroxyl radicals are used to oxidatively modify proteins is described, marking the first time protein footprinting has been performed in live cells.
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Complementary MS Methods Assist Conformational Characterization of Antibodies with Altered S–S Bonding Networks

TL;DR: The use of complementary mass spectrometry methods that not only characterize mutant mAbs but also may provide a general framework for characterizing higher order structure of other protein therapeutics and biosimilars are described.