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Peter N. Lowe

Researcher at GlaxoSmithKline

Publications -  50
Citations -  2564

Peter N. Lowe is an academic researcher from GlaxoSmithKline. The author has contributed to research in topics: GTPase-activating protein & Small G Protein. The author has an hindex of 28, co-authored 50 publications receiving 2486 citations. Previous affiliations of Peter N. Lowe include The Hertz Corporation & University of Cambridge.

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Effect of detergent on "promiscuous" inhibitors.

TL;DR: It is demonstrated that promiscuous inhibitors can be differentiated from classical 1:1 inhibitors by the judicious use of detergents, making it possible to configure assays that significantly reduce this undesirable mechanism of inhibition without compromising assay performance.
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Evidence for the Presence of Three Distinct Binding Sites for the Thioflavin T Class of Alzheimer's Disease PET Imaging Agents on β-Amyloid Peptide Fibrils *

TL;DR: An in-depth characterization of the binding of seven previously described ligands to in vitro generated Aβ-(1–40) polymers finds that these compounds display a more complex binding pattern than described previously and are consistent with three classes of binding sites on the Aβ fibrils.
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Structure of Cdc42 bound to the GTPase binding domain of PAK.

TL;DR: The solution structure of CDC42 bound to the GTPase binding domain of αPAK, an effector of both Cdc42 and Rac, is reported, suggesting reasons for the specificity of these interactions and providing insight into the mechanism of PAK activation.
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Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK

TL;DR: The solution structure of the complex of Cdc42 with the GTPase-binding domain of ACK is reported, where both proteins undergo significant conformational changes on binding, to form a new type of G-protein/effector complex.
Journal Article

Cloning and characterisation of cDNAs encoding a novel non-receptor tyrosine kinase, brk, expressed in human breast tumours

TL;DR: Sequencing of brk cDNAs isolated from T-47D and MCF-7 human breast tumour cell lines indicate that they encode a protein with the features of a novel nonreceptor tyrosine kinase, including amino terminal SH3 and SH2 domains.