Ronald Henry Jackson

TL;DR: In this paper, a member of a specific binding pair (sbp) is identified by expressing DNA encoding a genetically diverse population of such sbp members in recombinant host cells in which the sbps members are displayed in functional form at the surface of a secreted recombinant genetic display package (rgdp) containing DNA encoding the sbp member or a polypeptide component thereof.

TL;DR: In this article, specific binding members comprising human antibody antigen binding domains specific for human transforming growth factor beta (TGF.beta.) bind specifically isoforms TGF.β.2 and TGF,82, neutralising its activity, but does not bind the latent form.

TL;DR: It is demonstrated that an active enzyme can be expressed on the surface of a bacteriophage and the functional enzyme is co-purified with the DNA encoding it, which may permit a novel approach to enzyme engineering based on affinity chromatography of mutant enzymes expressing on the phage surface.

TL;DR: The findings suggest that such synthetic anti‐fibrotic TGF‐β antibodies are potentially applicable to a number of human CNS fibrotic diseases to arrest the deposition of excessive extracellular matrix components, and maintain and/or restore functional integrity.

TL;DR: Affinity maturation of phage antibody populations using ribosome display is a valuable method of rapidly generating diverse, high affinity antibodies to antigen and should be readily applicable to the isolation of antibodies for the detection and assay of biomarkers.