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Timothy J. Nott

Researcher at University of Oxford

Publications -  12
Citations -  2593

Timothy J. Nott is an academic researcher from University of Oxford. The author has contributed to research in topics: Peptide library & Phosphothreonine. The author has an hindex of 10, co-authored 12 publications receiving 2008 citations. Previous affiliations of Timothy J. Nott include University of Toronto & National Institute for Medical Research.

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Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles

TL;DR: It is demonstrated that the disordered tails of Ddx4, a primary constituent of nuage or germ granules, form phase-separated organelles both in live cells and in vitro, and proposed that phase separation of disordered proteins containing weakly interacting blocks is a general mechanism for forming regulated, membraneless organlles.
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Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation

TL;DR: Observation of a network of interchain interactions, as established by NOE spectroscopy, shows the importance of Phe and Arg interactions in driving the phase separation of Ddx4, while the salt dependence of both low- and high-concentration regions of phase diagrams establishes an important role for electrostatic interactions.
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Membraneless organelles can melt nucleic acid duplexes and act as biomolecular filters.

TL;DR: It is demonstrated that the solvent environment within the interior of these cellular bodies behaves more like an organic solvent than like water, revealing that cells have also evolved this capability by exploiting the interiors of membraneless organelles.
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Deciphering arginine methylation: Tudor tells the tale

TL;DR: Tudor proteins are now known to be present in PIWI complexes, where they are thought to interact with methylated PIWI proteins and regulate the PIWI-interacting RNA (piRNA) pathway in the germ line.
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Structure and Regulation of the Human Nek2 Centrosomal Kinase

TL;DR: A role for dimerization-dependent allosteric regulation that combines with autophosphorylation and proteinosphatase 1c phosphatase activity to generate the precise spatial and temporal control required for Nek2 function in centrosomal maturation is suggested.