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Philip A. Walker

Researcher at Francis Crick Institute

Publications -  47
Citations -  9087

Philip A. Walker is an academic researcher from Francis Crick Institute. The author has contributed to research in topics: Histone methyltransferase & Virus. The author has an hindex of 35, co-authored 46 publications receiving 8087 citations. Previous affiliations of Philip A. Walker include National Institute for Medical Research.

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Structure of mammalian AMPK and its regulation by ADP

TL;DR: It is shown that ADP binding to just one of the two exchangeable AXP (AMP/ADP/ATP) binding sites on the regulatory domain protects the enzyme from dephosphorylation, although it does not lead to allosteric activation.
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HIV-1 restriction factor SAMHD1 is a deoxynucleoside triphosphate triphosphohydrolase

TL;DR: It is proposed that SAMHD1, which is highly expressed in dendritic cells, restricts HIV-1 replication by hydrolysing the majority of cellular dNTPs, thus inhibiting reverse transcription and viral complementary DNA (cDNA) synthesis.
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Structural basis for AMP binding to mammalian AMP-activated protein kinase

TL;DR: The crystal structure of the regulatory fragment of mammalian AMPK in complexes with AMP and ATP is reported and suggests a mechanism for propagating AMP/ATP signalling whereby a phosphorylated residue from the α and/or β subunits binds to the γ subunit in the presence of AMP but not when ATP is bound.
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Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants.

TL;DR: The enzymatic properties and crystal structures of neuraminidase mutants from H5N1-infected patients are reported that explain the molecular basis of resistance and indicate that it would be prudent for pandemic stockpiles of oseltamivir to be augmented by additional antiviral drugs, including zanamivIR.