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A Knight

Researcher at Imperial College London

Publications -  7
Citations -  762

A Knight is an academic researcher from Imperial College London. The author has contributed to research in topics: Gene delivery & Peptide. The author has an hindex of 5, co-authored 7 publications receiving 754 citations.

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An RGD-oligolysine peptide: a prototype construct for integrin-mediated gene delivery.

TL;DR: The ability to produce an efficient gene delivery system using small, easily modified, and well-defined constructs that have no constraint of particle size demonstrates the advantages of integrin-targeting peptides for gene transfer.
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Cell binding and internalization by filamentous phage displaying a cyclic Arg-Gly-Asp-containing peptide.

TL;DR: The results indicate that cyclic integrin-binding peptides can be used to target and enter cells and that it should be possible to exploit such peptides for the introduction of DNA, drugs, or other macromolecules.
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Lipid-mediated enhancement of transfection by a nonviral integrin-targeting vector.

TL;DR: It is reported that lipofectin (L) incorporated into the ID complexes enhances integrin-mediated transfection, increasing luciferase expression by more than 100-fold, and the mechanism of enhancement is likely to involve a reduction in the extent of endosomal degradation of DNA.
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Liposomes enhance delivery and expression of an RGD-oligolysine gene transfer vector in human tracheal cells

TL;DR: The results show that an integrin-binding ligand can deliver genetic material to airway cells and that a cationic liposome can enhance the efficacy of this nonviral vector system.
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Recombinant HMG1 Protein Produced in Pichia pastoris: A Nonviral Gene Delivery Agent

TL;DR: HMG1-mediated gene delivery was as efficient as calcium phosphate-mediated transfection but without associated cell damage, and stable transfectants obtained after selection for G418 resistance usually integrated only one copy of the transfected DNA in contrast to the high unpredictable number obtained by the calcium phosphate method.