Hennie R. Hoogenboom

TL;DR: These findings demonstrate for the first time the ability to transform the unique fine specificity but low intrinsic affinity of TCRs on T cells into high-affinity soluble antibody molecules endowed with a T-cell antigen receptor-like specificity.

TL;DR: The ability to isolate high-affinity human recombinant antibodies with the antigen-specific, MHC-restricted specificity of T cells is demonstrated, and this ability was demonstrated for three different epitopes of the same melanoma-derived antigen.

TL;DR: This diabody format, when combined with the power of phage display technology, allows the generation and analysis of thousands of different bispecific molecules and selection for binding presumably also selects for more stable diabodies.

TL;DR: The ability to efficiently affinity mature Fab antibodies is an important component of the antibody development pipeline and it is shown that yeast display is an efficient method for this purpose.

TL;DR: The results illustrate the feasibility of the antibody engineering technology to create and produce chimeric mouse-human immunotoxin-like molecules and demonstrate the ability of mammalian (myeloma) cells to express and secrete antibody-cytokine hybrid molecules with potential use in anticancer therapy.