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Janet E. Lovett

Researcher at University of St Andrews

Publications -  36
Citations -  1369

Janet E. Lovett is an academic researcher from University of St Andrews. The author has contributed to research in topics: Electron paramagnetic resonance & Chemistry. The author has an hindex of 16, co-authored 31 publications receiving 1109 citations. Previous affiliations of Janet E. Lovett include University of Edinburgh & University of Oxford.

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Neisseria Meningitidis Recruits Factor H Using Protein Mimicry of Host Carbohydrates.

TL;DR: The structure of a complement regulator in complex with its pathogen surface-protein ligand reveals how the important human pathogen Neisseria meningitidis subverts immune responses by mimicking the host, using protein instead of charged-carbohydrate chemistry to recruit the host complement regulator, fH.
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Detergent-Free Incorporation of a Seven-Transmembrane Receptor Protein into Nanosized Bilayer Lipodisq Particles for Functional and Biophysical Studies

TL;DR: The structural and dynamic integrity of bR was retained when compared with data for bR obtained in the native membrane and in detergents and then with crystal data, indicating the potential of Lipodisq nanoparticles as a useful membrane mimetic.
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Structural information from orientationally selective DEER spectroscopy

TL;DR: A general method is presented to analyze the dipolar interaction between two paramagnetic spin centres from a series of DEER traces recorded so that different orientations of the spin-spin vector are sampled.
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Advances in the synthesis of nitroxide radicals for use in biomolecule spin labelling

TL;DR: The most practical methods for the synthesis of nitroxides are discussed, focusing on the tunability of their structures, the manipulation of their sidechains into spin labelling handles, and their installation into biomolecules.
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The Short-Lived Signaling State of the Photoactive Yellow Protein Photoreceptor Revealed by Combined Structural Probes

TL;DR: Direct structural observation of the transient signaling state by combining double electron electron resonance spectroscopy, NMR, and time-resolved pump-probe X-ray solution scattering (TR-SAXS/WAXS) indicates the transient formation of an ordered and rearranged conformation.