Download Bioorganometallic Chemistry: Applications in Drug Discovery, by Gérard Jaouen, Michèle Salmain PDF

By Gérard Jaouen, Michèle Salmain

An updated reference reflecting the numerous advances and critical breakthroughs made during this rising self-discipline during the last decade.
As such, the booklet presents an outline of the newest advancements and destiny developments within the box, concentrating on such purposes because the improvement of doubtless lively organometallic medicines opposed to incurable illnesses, in addition to in such components as catalysis, power, analytical chemistry, and imaging.
The popular editor, who verified the time period "bioorganometallics", and his foreign staff of specialists have prepare a invaluable source for researchers in organometallic, inorganic, medicinal, and biochemistry.

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Additional resources for Bioorganometallic Chemistry: Applications in Drug Discovery, Biocatalysis, and Imaging

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And 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 Marmorstein, R. (2008) ACS Chem. , 3, 305–316. , and Meggers, E. (2004) Org. , 6, 521–523. , and Meggers, E. (2010) Angew. , Int. , 49, 3839–3842. , and Meggers, E. (2012) Chem. , 48, 1863–1865. , and Meggers, E. , 41, 9337–9348. S. (2012) Inorg. Chim. Acta, 393, 84–102. , and Meggers, E. (2007) Inorg. , 46, 2944–2946. , and Meggers, E. (2012) Eur. J. Inorg. , 2012, 813–821. , and Meggers, E. (2012) Inorg. Chim. Acta, 393, 261–268. , and Meggers, E.

Copyright  2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. In summary, Co-ASS 31 leads to acetylation of COX, however, at different sites than ASS. Nevertheless, these acetylations are certainly involved in the inactivation of the COX enzymes. Interestingly, 32, which lacks the acetyl moiety present in Co-ASS 31 and ASS and, thus, cannot acetylate COX, is still inhibiting COX [118]. However, the presence of the organometallic moiety in Co-ASS enables to postulate several alternative modes of COX inhibition.

2009) PLoS One, 4, e7112. , and Meggers, E. (2011) J. Biol. Inorg. , 16, 45–50. , and Marmorstein, R. (2009) J. Med. , 52, 1602–1611. , and Meggers, E. (2008) ChemBioChem, 9, 2933–2936. , and Meggers, E. (2006) J. Am. Chem. , 128, 877–884. Bregman, H. and Meggers, E. (2006) Org. , 8, 5465–5468. , and Prokop, A. , 10882–10888. , and Meggers, E. (2007) Org. Biomol. , 5, 1218–1227. , and Meggers, E. (2011) Inorg. Chim. Acta, 377, 34–41. , and Marmorstein, R. (2009) Biochemistry, 48, 5187–5198. , and 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 Marmorstein, R.

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