Biosensor-based approach to the identification of protein kinase ligands with dual-site modes of action.
about
Selectively targeting an inactive conformation of interleukin-2-inducible T-cell kinase by allosteric inhibitorsSmall molecule substrate phosphorylation site inhibitors of protein kinases: approaches and challenges.Surface plasmon resonance as a high throughput method to evaluate specific and non-specific binding of nanotherapeutics.Synthetic strategies for the biotinylation of bioactive small molecules.Bridging the past and the future of virology: surface plasmon resonance as a powerful tool to investigate virus/host interactions.Quick evaluation of kinase inhibitors by surface plasmon resonance using single-site specifically biotinylated kinases.Novel approaches for targeting kinases: allosteric inhibition, allosteric activation and pseudokinases.Elucidation of direct competition and allosteric modulation of small-molecular-weight protein ligands using surface plasmon resonance methods.
P2860
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P2860
Biosensor-based approach to the identification of protein kinase ligands with dual-site modes of action.
description
2011 nî lūn-bûn
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name
Biosensor-based approach to th ...... ith dual-site modes of action.
@en
Biosensor-based approach to th ...... ith dual-site modes of action.
@nl
type
label
Biosensor-based approach to th ...... ith dual-site modes of action.
@en
Biosensor-based approach to th ...... ith dual-site modes of action.
@nl
prefLabel
Biosensor-based approach to th ...... ith dual-site modes of action.
@en
Biosensor-based approach to th ...... ith dual-site modes of action.
@nl
P2093
P2860
P356
P1476
Biosensor-based approach to th ...... ith dual-site modes of action.
@en
P2093
Andrew Cook
Chris Phillips
Colin Robinson
Graeme Macdonald
Iva Navratilova
John Mathias
Samantha Hughes
P2860
P304
P356
10.1177/1087057111422746
P577
2011-11-07T00:00:00Z