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Mads Gabrielsen

Researcher at University of Glasgow

Publications -  55
Citations -  1589

Mads Gabrielsen is an academic researcher from University of Glasgow. The author has contributed to research in topics: Protein structure & Membrane protein. The author has an hindex of 20, co-authored 51 publications receiving 1343 citations. Previous affiliations of Mads Gabrielsen include Ninewells Hospital & University of Dundee.

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Distinct Binding Determinants for ERK2/p38α and JNK MAP Kinases Mediate Catalytic Activation and Substrate Selectivity of MAP Kinase Phosphatase-1

TL;DR: The yeast two-hybrid assay is used to demonstrate that MKP-1 is able to interact selectively with the extracellular signal-regulated kinase 1/2 (ERK1/2), p38α, and c-Jun NH2-terminal kinase (JNK) MAP kinase isoforms, indicating that there are distinct binding determinants for these MAP kinases.
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Activation of a Primed RING E3-E2–Ubiquitin Complex by Non-Covalent Ubiquitin

TL;DR: Backside bound Ub (Ub(B) serves as an allosteric activator of RING E3-mediated Ub transfer, thereby improving the catalytic efficiency of Ub transfer.
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Instantaneous mapping of coherently coupled electronic transitions and energy transfers in a photosynthetic complex using angle-resolved coherent optical wave-mixing.

TL;DR: A novel nonlinear optical method is demonstrated, angle-resolved coherent wave mixing, that separates out coherently coupled electronic transitions and energy transfers in an instantaneous two-dimensional mapping.
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Identification of Bacterial Target Proteins for the Salicylidene Acylhydrazide Class of Virulence-blocking Compounds

TL;DR: This work provides the first identification of bacterial proteins that are targeted by a class of anti-virulence compounds and provides evidence that their mode of action is likely to result from a synergistic effect arising from a perturbation of the function of several conserved proteins.
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Calicivirus VP2 forms a portal-like assembly following receptor engagement

TL;DR: Cryo-electron microscopy structures of feline calicivirus and its cellular receptor show that twelve copies of the minor capsid protein VP2 form a portal-like assembly arranged about a pore in the capsid shell, hypothesized to function as a channel for the delivery of the calicvirus genome through the endosomal membrane, into the cytoplasm of a host cell, thereby initiating infection.