scispace - formally typeset
R

Randy Hoffman

Researcher at Invitrogen

Publications -  6
Citations -  927

Randy Hoffman is an academic researcher from Invitrogen. The author has contributed to research in topics: Signal transduction & Protein kinase B. The author has an hindex of 6, co-authored 6 publications receiving 872 citations. Previous affiliations of Randy Hoffman include Life Technologies.

Papers
More filters
Journal ArticleDOI

Targeted polypharmacology: discovery of dual inhibitors of tyrosine and phosphoinositide kinases

TL;DR: It is shown that one compound, PP121, blocks the proliferation of tumor cells by direct inhibition of oncogenic tyrosine kinases and PI3-Ks, and demonstrates the feasibility of accessing a chemical space that intersects two families ofoncogenes.
Journal ArticleDOI

Inhibitor Hijacking of Akt Activation

TL;DR: It is concluded that ATP-competitive Akt inhibitors impart regulatory phosphorylation of their target kinase Akt providing new insights into both natural regulation of Akt activation andAkt inhibitors entering the clinic.
Journal ArticleDOI

Discovery of Dual Inhibitors of the Immune Cell PI3Ks p110δ and p110γ: a Prototype for New Anti-inflammatory Drugs

TL;DR: It is found selective inhibition of only PI3Kdelta is weakly anti-inflammatory, but PI3kdelta/gamma inhibitors show superior inflammatory marker suppression through suppression of lipopolysaccharide-induced TNFalpha production and T cell activation.
Journal ArticleDOI

Overcoming compound interference in fluorescence polarization-based kinase assays using far-red tracers.

TL;DR: The PanVera PolarScreen far- red fluorescence polarization assay format is described, which mitigates assay interference from autofluorescent compounds or scattered light through the use of a far-red tracer.
Journal ArticleDOI

A fragment-based approach for the discovery of isoform-specific p38alpha inhibitors.

TL;DR: It is demonstrated that a pharmacophore-based search guided by experimental binding data of weakly in- teracting fragments can be rapidly and efficiently used to identify (or synthesize) high-affinity, selective ligands.