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Mark Howarth

Researcher at University of Oxford

Publications -  99
Citations -  9784

Mark Howarth is an academic researcher from University of Oxford. The author has contributed to research in topics: Streptavidin & Biotinylation. The author has an hindex of 42, co-authored 90 publications receiving 7803 citations. Previous affiliations of Mark Howarth include Academia Sinica & John Radcliffe Hospital.

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Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin

TL;DR: The robust reaction conditions and irreversible linkage of SpyTag shed light on spontaneous isopeptide bond formation and should provide a targetable lock in cells and a stable module for new protein architectures.
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Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase.

TL;DR: A highly specific, robust and rapid new method for labeling cell surface proteins with biophysical probes that accepts a ketone isostere of biotin as a cofactor, ligating this probe to the AP with similar kinetics and retaining the high substrate specificity of the native reaction.
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Compact Biocompatible Quantum Dots Functionalized for Cellular Imaging

TL;DR: A family of water-soluble quantum dots (QDs) that exhibit low nonspecific binding to cells, small hydrodynamic diameter, tunable surface charge, high quantum yield, and good solution stability across a wide pH range are presented.
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Targeting quantum dots to surface proteins in living cells with biotin ligase.

TL;DR: This labeling method helps to address the two major deficiencies of antibody-based labeling, which is currently the most common method for targeting QDs to cells: the size of the QD conjugate after antibody attachment and the instability of many antibody-antigen interactions.
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Monovalent, reduced-size quantum dots for imaging receptors on living cells.

TL;DR: In this paper, a method to generate monovalent quantum dots (QDs) using agarose gel electrophoresis was described, which improved access of QD-labeled glutamate receptors to neuronal synapses, and monovalency prevented EphA3 tyrosine kinase activation.