Communication between sink and source organs is crucial for normal plant development. The synthesis of assimilates during photosynthesis must be adapted to the demand in sink tissues. Surplus of carbon dioxide assimilation in source leaves leads to the accumulation of soluble sugars in mesophyll cells and thereby to the inhibition of photosynthesis. The underlying mechanism of the so called ”si...

PurposeThe immunocytokine L19-IL2 delivers interleukin-2 to the tumor by exploiting selective L19-dependent binding of extradomain B fibronectin on blood vessels. In preclinical models, has been shown enhance local and abscopal effects radiation therapy. The clinical safety monotherapy established previously. this study, tolerability after stereotactic body therapy (SBRT) was assessed.Methods M...

Eight ribosomal proteins, L9, L11, L15, L17, L18, L19, L23, and L29, have been localized on the surface of the 50S subunit from Escherichia coli by immunoelectron microscopy. The specificity of the antibody binding site was demonstrated by stringent absorption experiments. For each protein, the antibody attachment site was localized on the two characteristic views of the 50S subunit. Thus, each...

The formation of new blood vessels (angiogenesis) is an important step in tumor progression. Molecules capable of selectively targeting markers of angiogenesis may offer opportunities for the in vivo imaging of aggressive tumors and for the delivery of toxic agents to the tumoral vasculature. Using antibody phage display libraries and combinatorial mutagenesis, we isolated single-chain Fv antib...

L19-tumor necrosis factor alpha (L19mTNF-α; L), a fusion protein consisting of mouse TNFα and the human antibody fragment L19 directed to the extra domain-B (ED-B) of fibronectin, is able to selectively target tumor vasculature and to exert a long-lasting therapeutic activity in combination with melphalan (M) in syngeneic mouse tumor models. We have studied the antitumor activity of single L19m...

Specific binding of purified proteins from the large ribosomal subunits of Saccharomyces cerevisiae to 5.8 S rRNA was examined by three different methods: nitrocellulose membrane filtration, sucrose density gradient centrifugation, and RNA-Sepharose column chromatography. RNA-protein complex formation was proportional to the amount of proteins added to the reaction mixture. The binding of prote...