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Anthony R. Rees

Researcher at University of Bath

Publications -  100
Citations -  7198

Anthony R. Rees is an academic researcher from University of Bath. The author has contributed to research in topics: Peptide sequence & Medicine. The author has an hindex of 37, co-authored 83 publications receiving 7055 citations. Previous affiliations of Anthony R. Rees include Western General Hospital & ImmunoGen, Inc..

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A peptide mimetic of an anti-CD4 monoclonal antibody by rational design

TL;DR: Using peptide mapping to determine 'active' antigen recognition residues, molecular modeling, and a molecular dynamics trajectory analysis, a peptide mimic of an anti-CD4 antibody is developed, containing antigen contact residues from multiple CDRs.
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Studies on the Internalization Mechanism of Cationic Cell-penetrating Peptides *

TL;DR: In vitro study of the cellular uptake of peptides, originally deriving from protegrin (the SynB peptide vectors), that have also been shown to enhance the transport of drugs across the blood-brain barrier suggest that SynB and pAntp-(43–58) peptides penetrate into cells by an adsorptive-mediated endocytosis process rather than temperature-independent translocation.
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Humanization of murine monoclonal antibodies through variable domain resurfacing

TL;DR: Resurfaced N901 and anti-B4 antibodies had apparent affinities for their cell surface ligands that were identical to those of their respective parent murine antibodies, suggesting that, despite the differences in the surfaces of mouse and human Fv regions, it is possible to substitute one for the other while retaining full antigen binding affinity.
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A new family of mouse homeo box-containing genes: molecular structure, chromosomal location, and developmental expression of Hox-7.1.

TL;DR: The isolation of a homeo box-containing gene that belongs to a new family of which there are at least three related genes in the mouse genome, and the homeobox of this new gene shows remarkable similarity to the Drosophila MshHomeo box that is designated as the prototype for this family.
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Epidermal growth factor receptors.

TL;DR: There is ample evidence that EGF binds to the receptor; that ligand-receptor complexes cluster or aggregate; and then are internalized and degraded, but evidence for a direct connection between internalization and the subsequent mitogenic response is lacking, and an alternative model is suggested.