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Judith Murray-Rust

Researcher at London Research Institute

Publications -  50
Citations -  4060

Judith Murray-Rust is an academic researcher from London Research Institute. The author has contributed to research in topics: Receptor tyrosine kinase & Receptor. The author has an hindex of 27, co-authored 50 publications receiving 3864 citations. Previous affiliations of Judith Murray-Rust include Birkbeck, University of London & Laboratory of Molecular Biology.

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New protein fold revealed by a 2.3-Å resolution crystal structure of nerve growth factor

TL;DR: The crystal structure of the murine NGF dimer is reported, which reveals a novel protomer structure consisting of three antiparallel pairs of β strands, together forming a flat surface that provides a model for rational design of analogues of NGF and its relatives and for testing the NGF-receptor recognition determinants critical for signal transduction.
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Disruption of methylarginine metabolism impairs vascular homeostasis

TL;DR: It is shown that loss of DDAH-1 activity leads to accumulation of ADMA and reduction in NO signaling, which causes vascular pathophysiology, including endothelial dysfunction, increased systemic vascular resistance and elevated systemic and pulmonary blood pressure, and it is suggested that DDAh inhibition could be harnessed therapeutically to reduce the vascular collapse associated with sepsis.
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PKC at a glance.

TL;DR: The protein kinase C (PKC) family is represented in all eukaryotes and in Homo sapiens comprises the related PKCα through PKCι gene products and form part of the AGC kinase superfamily.
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Disruption of the low affinity receptor-binding site in NGF allows neuronal survival and differentiation by binding to the trk gene product.

TL;DR: It is shown that Lys-32, Lys-34, and Lys-95 form a positively charged interface involved in binding to p75NGFR, demonstrating a functional dissociation between the two NGF receptors.
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S-nitrosylation of dimethylarginine dimethylaminohydrolase regulates enzyme activity: Further interactions between nitric oxide synthase and dimethylarginine dimethylaminohydrolase

TL;DR: It is demonstrated that recombinant D DAH is reversibly inhibited after incubation with NO donors in vitro and mammalian DDAH in cytosolic extracts is also reversibly inhibition by NO donors.