R
Robin J. Rosenfeld
Researcher at Scripps Research Institute
Publications - 16
Citations - 1413
Robin J. Rosenfeld is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Nitric oxide synthase & Hydrogen bond. The author has an hindex of 15, co-authored 16 publications receiving 1322 citations. Previous affiliations of Robin J. Rosenfeld include Harvey Mudd College.
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Journal ArticleDOI
Deciphering the fluorescence signature of daunomycin and doxorubicin.
TL;DR: The spectroscopic response of DXR and DNM to their surroundings in several systems, including solvents of differing dielectric constant, aqueous solutions of varying pH or fluorophore concentration, and the reverse micellar system of AOT/heptane/water with a range of doxorubicin concentrations is delineated.
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Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase.
Elsa D. Garcin,Elsa D. Garcin,Andrew S. Arvai,Robin J. Rosenfeld,Matt D. Kroeger,Matt D. Kroeger,Brian R. Crane,Brian R. Crane,Gunilla Andersson,Glen Andrews,Peter Hamley,Peter Hamley,Philip Mallinder,David J. Nicholls,Stephen A. St-Gallay,Tinker Alan,Nigel Gensmantel,Antonio Mete,David Cheshire,Stephen Connolly,Dennis J. Stuehr,Anders Åberg,Alan V. Wallace,John A. Tainer,Elizabeth D. Getzoff +24 more
TL;DR: The anchored plasticity approach, which anchor an inhibitor core in a conserved binding pocket, then extend rigid bulky substituents towards remote specificity pockets, accessible upon conformational changes of flexible residues, exemplifies general principles for the design of selective enzyme inhibitors that overcome strong active-site conservation.
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Distinct Dimer Interaction and Regulation in Nitric-oxide Synthase Types I, II, and III
Koustubh Panda,Robin J. Rosenfeld,Sanjay Ghosh,Abigail L. Meade,Elizabeth D. Getzoff,Dennis J. Stuehr +5 more
TL;DR: The results indicate that the three NOS isozymes, despite their general structural similarity, differ markedly in their strengths, interfaces, and in how l-Arg and H4B influence their formation and stability.
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Interaction of 5-methyltetrahydrofolate and tetrahydrobiopterin on endothelial function.
TL;DR: It is suggested that 5-methyltetrahydrofolate directly interacts with nitric oxide synthase to promoteNitric oxide (vs. superoxide) production and improve endothelial function and may represent an important strategy for intervention aimed at improving tetraydrobiopterin bioavailability.
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N-terminal domain swapping and metal ion binding in nitric oxide synthase dimerization.
Brian R. Crane,Brian R. Crane,Robin J. Rosenfeld,Andrew S. Arvai,Dipak K. Ghosh,Dipak K. Ghosh,Sanjay Ghosh,John A. Tainer,Dennis J. Stuehr,Elizabeth D. Getzoff +9 more
TL;DR: The correlation between three‐dimensional domain swapping of the N‐terminal hook and metal ion release with disulfide formation may impact inducible nitric oxide synthase (i)NOS stability and regulation in vivo.