Download Bacterial-Epithelial Cell Cross-Talk (Advances in Molecular by Beth A. McCormick PDF

By Beth A. McCormick

ISBN-10: 0521852447

ISBN-13: 9780521852449

As a result of my evolving examine, this booklet is as well timed because it is definitely written. whereas the procedure taken is predominantly a molecular genetics view to microbial adhesion, the bankruptcy authors & editor have provided the wealth of knowledge in this subject in a good prepared manner.

Each bankruptcy is definitely geared up and each concept given is then supported with examples of medical proof. on the finish of every bankruptcy are pages of references that i've got used to extra my learn (as will somebody else drawn to this topic).

For the photographs, the editor has performed a very good task culling out the easiest. From easy gene/operon diagrams to electron micrographs to paint plates and pictures, the authors and editor have judicially supplied merely sound transparent graphics.

If you will want a e-book that would offer a molecular method of bacterial adhesion, this is often a great place to begin. whereas a couple of chapters are too constrained of their applicablity to the final answer of this factor, the remainder greater than make up for those minor shortfalls.

Keep in brain, this ebook isn't for the amateur from simply any box of microbiology. nevertheless, nor is the topic. while you're occupied with this becoming box of study, this booklet might be a useful addition in your library.

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Additional resources for Bacterial-Epithelial Cell Cross-Talk (Advances in Molecular and Cellular Microbiology)

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Am. J. Pathol. 166, 409–419. , and Just, I. (2000). Recognition of RhoA by Clostridium botulinum C3 exoenzyme. J. Biol. Chem. 275, 16 478–16 483. Wolf, A. , Jobling, M. , et al. (1998). Ganglioside structure dictates signal transduction by cholera toxin and association with caveolaelike membrane domains in polarized epithelia. J. Cell Biol. 141, 917–927. Wong, V. and Gumbiner, B. M. (1997). A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier.

2000). , 2004). Advances in our understanding of the biology of and, potentially, developing therapy for these barrier defects have been limited by the lack of effective and specific inhibitors of MLCK. , 2002). This inhibitor has been used to specifically probe the role of MLCK in intestinal epithelial barrier dysfunction. As noted above, epithelial barrier dysfunction is seen in a variety of infectious diseases of the intestines. , 2002). , 2004). In this case, it is thought that barrier disruption is mediated by local release of T helper type 1 (Th1) cytokines, including IFN␥ and TNF␣.

And Galan, J. E. (1998). S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 93, 815–826. Harris, D. , Slot, J. , Geuze, H. , and James, D. E. (1992). Polarized distribution of glucose transporter isoforms in Caco-2 cells. Proc. Natl. Acad. Sci. U. S. A. 89, 7556–7560. , Wittchen, E. , and Stevenson, B. R. (1998). ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin.

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