By Andreas Luch

ISBN-10: 3764383372

ISBN-13: 9783764383374

Scientific Toxicology is the second one quantity of a three-volume set on molecular, scientific and environmental toxicology that provides a entire and in-depth reaction to the expanding significance and abundance of chemicals of way of life. via delivering exciting insights some distance right down to the molecular point, this three-volume paintings covers the full diversity of contemporary toxicology with targeted emphasis on contemporary advancements and achievements. it's written for college kids and pros in drugs, technological know-how, public wellbeing and fitness or engineering who're tough trustworthy details on poisonous or very likely destructive brokers and their hostile results at the human physique.

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Extra resources for Molecular, Clinical and Environmental Toxicology: Volume 2: Clinical Toxicology (Experientia Supplementum)

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FEMS Microbiol Lett 255: 175–186 80 Henderson IR, Navarro-Garcia F, Desvaux M, Fernandez RC, Ala’Aldeen D (2004) Type V protein secretion pathway: The autotransporter story. Microbiol Mol Biol Rev 68: 692–744 81 Martoglio B, Dobberstein B (1998) Signal sequences: More than just greasy peptides. Trends Cell Biol 8: 410–415 82 Yanez ME, Korotkov KV, Abendroth J, Hol WG (2008) Structure of the minor pseudopilin EpsH from the Type 2 secretion system of Vibrio cholerae. J Mol Biol 377: 91–103 83 Bachert C, Zhang N, Patou J, van Zele T, Gevaert P (2008) Role of staphylococcal superantigens in upper airway disease.

Biochemical studies showed that LC/A3 had similar kinetic properties to LC/A1, and amino acids that differed with LC/A1 within the binding site did not change the binding or catalytic activity of LC/A3 for SNAP25, while LC/A4 showed a ~80-fold decrease in catalytic activity compared to LC/A1, suggesting a defect in SNAP25 cleavage. This change in catalytic activity is believed to be due to a single residue substitution indirectly causing a loss of coordination with the catalytic zinc in the active site, as a point mutation to LC/A4 restores catalytic activity to the level of LC/A1 [192].

Curr Opin Struct Biol 7: 566–573 25 Lesieur C, Vecsey-Semjen B, Abrami L, Fivaz M, van der Goot FG (1997) Membrane insertion: The strategy of toxins. Mol Membr Biol 14: 45–64 26 Kurisu G, Zakharov SD, Zhalnina MV, Bano S, Eroukova VY, Rokitskaya TI, Antonenko YN, Wiener MC, Cramer WA (2003) The structure of BtuB with bound colicin E3 R-domain implies a translocon. Nat Struct Biol 10: 948–954 27 Yamashita E, Zhalnina MV, Zakharov SD, Sharma O, Cramer WA (2008) Crystal structures of the OmpF porin: Function in a colicin translocon.

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Molecular, Clinical and Environmental Toxicology: Volume 2: Clinical Toxicology (Experientia Supplementum) by Andreas Luch


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