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Tony Ng

Researcher at King's College London

Publications -  181
Citations -  9335

Tony Ng is an academic researcher from King's College London. The author has contributed to research in topics: Cancer & Fluorescence-lifetime imaging microscopy. The author has an hindex of 46, co-authored 176 publications receiving 8237 citations. Previous affiliations of Tony Ng include St Thomas' Hospital & North Manchester General Hospital.

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Journal ArticleDOI

Imaging biomarker roadmap for cancer studies.

James P B O'Connor, +78 more
TL;DR: Experts assembled to review, debate and summarize the challenges of IB validation and qualification produced 14 key recommendations for accelerating the clinical translation of IBs, which highlight the role of parallel (rather than sequential) tracks of technical validation, biological/clinical validation and assessment of cost-effectiveness.
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The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress

TL;DR: It is reported that BRCA1 is modified by small ubiquitin-like modifier (SUMO) in response to genotoxic stress, and co-localizes at sites of DNA damage with SUMO1, SUMO2/3 and the SUMO-conjugating enzyme Ubc9.
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PKCα regulates β1 integrin‐dependent cell motility through association and control of integrin traffic

TL;DR: Protein kinase C (PKC) has been implicated in integrin‐mediated spreading and migration in mammary epithelial cells there is a partial co‐localization between β1 integrin and PKCα and this PKC α‐enhanced migratory response is inhibited by blockade of endocytosis.
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Ezrin is a downstream effector of trafficking PKC-integrin complexes involved in the control of cell motility.

TL;DR: It is provided the first evidence that PKCα or a PKC α‐associated serine/threonine kinase can phosphorylate the ERM C‐terminal threonine residue within a kinase–ezrin molecular complex in vivo.
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Imaging Protein Kinase Cα Activation in Cells

TL;DR: Spatially resolved fluorescence resonance energy transfer measured by fluorescence lifetime imaging microscopy (FLIM), provides a method for tracing the catalytic activity of fluorescently tagged proteins inside live cell cultures and enables determination of the functional state of proteins in fixed cells and tissues.