J
Jacqueline K. Barton
Researcher at California Institute of Technology
Publications - 430
Citations - 45235
Jacqueline K. Barton is an academic researcher from California Institute of Technology. The author has contributed to research in topics: DNA & Base pair. The author has an hindex of 100, co-authored 429 publications receiving 43349 citations. Previous affiliations of Jacqueline K. Barton include City University of New York & University of North Carolina at Chapel Hill.
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Journal ArticleDOI
Chiral discrimination in the covalent binding of bis(phenanthroline)dichlororuthenium(II) to B-DNA
Jacqueline K. Barton,Elias Lolis +1 more
Journal ArticleDOI
(Ru(bpy)2(L))Cl2: Luminescent Metal Complexes That Bind DNA Base Mismatches
TL;DR: Results with these novel luminescent complexes support the concept of using a structurally demanding ligand to obtain selectivity in targeting single base mismatches in DNA.
Journal ArticleDOI
Redox signaling between DNA repair proteins for efficient lesion detection
Amie K. Boal,Joseph C. Genereux,Pamela A. Sontz,Jeffrey A. Gralnick,Dianne K. Newman,Jacqueline K. Barton +5 more
TL;DR: Examination of the proposed DNA repair glycosylases model for CT scanning shows how repair proteins might efficiently locate DNA lesions and point to a biological role for DNA-mediated CT within the cell.
Journal ArticleDOI
1H NMR studies of tris(phenanthroline) metal complexes bound to oligonucleotides: characterization of binding modes.
TL;DR: The NMR chemical shift variations appear particularly sensitive to this surface-bound interaction, which, on the basis of a comparison of binding and photophysical parameters for Ru(phen)3(2+), appears more prominant in binding to oligonucleotide than that to polynucleotides.
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Targeting a ruthenium complex to the nucleus with short peptides
TL;DR: Evaluating the nuclear entry of a series of luminescent ruthenium peptide conjugates of shorter sequence and lower charge shows that fluorescein conjugation is not a general strategy for modulating the distribution of cell-penetrating peptides.