Pathogenesis of bacterial infections and immunity

@article{samori_enhanced_2010,

title = {Enhanced anticancer activity of multi-walled carbon nanotube-methotrexate conjugates using cleavable linkers},

author = {Cristian Samorì and Hanene Ali-Boucetta and Raquel Sainz and Chang Guo and Francesca Maria Toma and Chiara Fabbro and Tatiana da Ros and Maurizio Prato and Kostas Kostarelos and Alberto Bianco},

doi = {10.1039/b923560d},

issn = {1364-548X},

year  = {2010},

date = {2010-03-01},

journal = {Chemical Communications (Cambridge, England)},

volume = {46},

number = {9},

pages = {1494--1496},

abstract = {Methotrexate was tethered to multi-walled carbon nanotubes through different cleavable linkers exploiting the ammonium functionalities introduced by 1,3-dipolar cycloaddition reaction of azomethine ylides to the nanotubes. The new nanobio-hybrid conjugates were internalized into human breast cancer cells and it was shown that the cytotoxic activity was strongly dependent on the presence and type of linker.},

keywords = {Antineoplastic Agents, Azo Compounds, carbon, Cell Line, Cross-Linking Reagents, Humans, I2CT, Methotrexate, Nanotubes, Team-Bianco, Thiosemicarbazones, tumor},

pubstate = {published},

tppubtype = {article}

}

@article{weber_ligand-receptor_2005,

title = {Ligand-receptor and receptor-receptor interactions act in concert to activate signaling in the Drosophila toll pathway},

author = {Alexander N R Weber and Martin C Moncrieffe and Monique Gangloff and Jean-Luc Imler and Nicholas J Gay},

doi = {10.1074/jbc.M502074200},

issn = {0021-9258},

year  = {2005},

date = {2005-01-01},

journal = {The Journal of Biological Chemistry},

volume = {280},

number = {24},

pages = {22793--22799},

abstract = {In Drosophila, the signaling pathway mediated by the Toll receptor is critical for the establishment of embryonic dorso-ventral pattern and for innate immune responses to bacterial and fungal pathogens. Toll is activated by high affinity binding of the cytokine Spätzle, a dimeric ligand of the cystine knot family. In vertebrates, a related family of Toll-like receptors play a critical role in innate immune responses. Despite the importance of this family of receptors, little is known about the biochemical events that lead to receptor activation and signaling. Here, we show that Spätzle binds to the N-terminal region of Toll and, using biophysical methods, that the binding is complex. The two binding events that cause formation of the cross-linked complex are non-equivalent: the first Toll ectodomain binds Spätzle with an affinity 3-fold higher than the second molecule suggesting that pathway activation involves negative cooperativity. We further show that the Toll ectodomains are able to form low affinity dimers in solution and that juxtamembrane sequences of Toll are critical for the activation or derepression of the pathway. These results, taken together, suggest a mechanism of signal transduction that requires both ligand-receptor and receptor-receptor interactions.},

keywords = {Amino Acid, Animals, Biophysical Phenomena, Biophysics, Body Patterning, Calorimetry, Cell Line, Cell Surface, Cross-Linking Reagents, Cytokines, dimerization, Electrophoresis, Humans, imler, ligands, Luciferases, M3i, Membrane Glycoproteins, Polyacrylamide Gel, Protein Binding, Protein Structure, Receptors, Recombinant Proteins, Sequence Homology, Signal Transduction, Tertiary, Time Factors, Toll-Like Receptors, Ultracentrifugation},

pubstate = {published},

tppubtype = {article}

}