D
David H. Russell
Researcher at Texas A&M University
Publications - 503
Citations - 18391
David H. Russell is an academic researcher from Texas A&M University. The author has contributed to research in topics: Mass spectrometry & Ion. The author has an hindex of 66, co-authored 477 publications receiving 17172 citations. Previous affiliations of David H. Russell include University of Oxford & University of North Carolina at Chapel Hill.
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Bacterial resistance to silver in wound care.
TL;DR: The purpose of this review is to assess the likelihood of widespread resistance to silver and the potential for silver to induce cross-resistance to antibiotics, in light of its increasing usage within the healthcare setting.
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Size-Selected (2−10 nm) Gold Nanoparticles for Matrix Assisted Laser Desorption Ionization of Peptides
TL;DR: First use of size-selected gold nanoparticles (AuNPs) as matrixes for matrix assisted laser desorption/ionization (MALDI) is described for peptides and proteins, with significant differences in the relative abundances of the ions observed in positive and negative mode MALDI-time-of-flight mass spectrometry (TOFMS).
Journal Article
Prolactin receptors on human T and B lymphocytes: antagonism of prolactin binding by cyclosporine.
TL;DR: The presence ofPRL receptors on T and B lymphocytes suggests that PRL may be involved in the regulation of humoral and cell-mediated immunity, and that one effect of CsA on immune function may be its ability to inhibit the effects of PRL action on these lymphocytes.
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Anion template effect on the self-assembly and interconversion of metallacyclophanes.
Cristian S. Campos-Fernández,Brandi L. Schottel,Helen T. Chifotides,Jitendra K. Bera,John Bacsa,John M. Koomen,David H. Russell,Kim R. Dunbar +7 more
TL;DR: Reactions of 3,6-bis(2-pyridyl)-1,2,4,5-tetrazine with solvated first-row transition metals M(II) have been explored with emphasis on the factors that influence the identity of the resulting cyclic products for Ni (II) and Zn(II).
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Ion mobility–mass spectrometry: a new paradigm for proteomics
TL;DR: New avenues for enhancing the figures of merit (e.g., sensitivity, limits of detection, dynamic range, and analyte selectivity) and optimizing IM–MS experimental parameters are described in the context of deriving new information at the forefront of proteomics research.