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PBP active site flexibility as the key mechanism for beta-lactam resistance in pneumococci.
Contreras-Martel C, Dahout-Gonzalez C, Martins Ados S, Kotnik M, Dessen A. Contreras-Martel C, et al. J Mol Biol. 2009 Apr 10;387(4):899-909. doi: 10.1016/j.jmb.2009.02.024. Epub 2009 Feb 20. J Mol Biol. 2009. PMID: 19233207
In Streptococcus pneumoniae, a major human pathogen, the surge in resistance to such antibiotics is a direct consequence of the proliferation of mosaic PBP-encoding genes, which give rise to proteins containing tens of mutations. ...In this work, we have solved the …
In Streptococcus pneumoniae, a major human pathogen, the surge in resistance to such antibiotics is a direct consequence of th …
Primary structure and crystallization of orotate phosphoribosyltransferase from Salmonella typhimurium.
Scapin G, Sacchettini JC, Dessen A, Bhatia M, Grubmeyer C. Scapin G, et al. J Mol Biol. 1993 Apr 20;230(4):1304-8. doi: 10.1006/jmbi.1993.1244. J Mol Biol. 1993. PMID: 8487307
The space group is P4(1)2(1)2 (or P4(3)2(1)2) with unit cell dimensions of a = b = 48.5 A, c = 210.5 A, and alpha = beta = gamma = 90 degrees. A crystalline form of the selenomethionine derivative of the protein is also reported....
The space group is P4(1)2(1)2 (or P4(3)2(1)2) with unit cell dimensions of a = b = 48.5 A, c = 210.5 A, and alpha = bet …
Structural basis for membrane fusion by enveloped viruses.
Weissenhorn W, Dessen A, Calder LJ, Harrison SC, Skehel JJ, Wiley DC. Weissenhorn W, et al. Mol Membr Biol. 1999 Jan-Mar;16(1):3-9. doi: 10.1080/096876899294706. Mol Membr Biol. 1999. PMID: 10332732 Review.
Their structural organization suggests that they have all evolved to use a similar strategy to promote fusion of viral and cellular membranes. This observation led to the proposal of a general model for viral membrane fusion, which will be discussed in detail....
Their structural organization suggests that they have all evolved to use a similar strategy to promote fusion of viral and cellular m …
Structural characterization and membrane binding properties of the matrix protein VP40 of Ebola virus.
Ruigrok RW, Schoehn G, Dessen A, Forest E, Volchkov V, Dolnik O, Klenk HD, Weissenhorn W. Ruigrok RW, et al. J Mol Biol. 2000 Jun 30;300(1):103-12. doi: 10.1006/jmbi.2000.3822. J Mol Biol. 2000. PMID: 10864502
The matrix protein VP40 of Ebola virus is believed to play a central role in viral assembly as it targets the plasma membrane of infected cells and subsequently forms a tightly packed layer on the inner side of the viral envelope. ...Membrane association of truncate …
The matrix protein VP40 of Ebola virus is believed to play a central role in viral assembly as it targets the plasma membrane of infe …
Crystal structure of the matrix protein VP40 from Ebola virus.
Dessen A, Volchkov V, Dolnik O, Klenk HD, Weissenhorn W. Dessen A, et al. EMBO J. 2000 Aug 15;19(16):4228-36. doi: 10.1093/emboj/19.16.4228. EMBO J. 2000. PMID: 10944105 Free PMC article.
Here we report the X-ray crystal structure of VP40 from Ebola virus at 2.0 A resolution. The crystal structure reveals that Ebola virus VP40 is topologically distinct from all other known viral matrix proteins, consisting of two domains with unique folds, connected by a
Here we report the X-ray crystal structure of VP40 from Ebola virus at 2.0 A resolution. The crystal structure reveals that Ebola vir …
Structure and mechanism of human cytosolic phospholipase A(2).
Dessen A. Dessen A. Biochim Biophys Acta. 2000 Oct 31;1488(1-2):40-7. doi: 10.1016/s1388-1981(00)00108-6. Biochim Biophys Acta. 2000. PMID: 11080675 Review.
cPLA(2) is an 85-kDa enzyme whose primary function, the release of arachidonic acid from phospholipid membranes, is a crucial reaction in the metabolism of lipid mediators of inflammation. cPLA(2) consists of two domains: an N-terminal, C2-type unit analogous to those pres …
cPLA(2) is an 85-kDa enzyme whose primary function, the release of arachidonic acid from phospholipid membranes, is a crucial reactio …
Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: a mosaic framework containing 83 mutations.
Dessen A, Mouz N, Gordon E, Hopkins J, Dideberg O. Dessen A, et al. J Biol Chem. 2001 Nov 30;276(48):45106-12. doi: 10.1074/jbc.M107608200. Epub 2001 Sep 11. J Biol Chem. 2001. PMID: 11553637
To understand such a resistance mechanism at an atomic level, we have solved the x-ray crystal structure of PBP2x from a highly penicillin-resistant clinical isolate of S. pneumoniae, Sp328, which harbors 83 mutations in the soluble region. ...In addition, the Ser(3 …
To understand such a resistance mechanism at an atomic level, we have solved the x-ray crystal structure of PBP2x from a highl …
Bifunctional penicillin-binding proteins: focus on the glycosyltransferase domain and its specific inhibitor moenomycin.
Di Guilmi AM, Dessen A, Dideberg O, Vernet T. Di Guilmi AM, et al. Curr Pharm Biotechnol. 2002 Jun;3(2):63-75. doi: 10.2174/1389201023378436. Curr Pharm Biotechnol. 2002. PMID: 12022260 Review.
Moenomycin, a well studied glycosyltransferase activity inhibitor has provided useful informations about lipid binding properties and about cellular role of bifunctional PBPs. These enzymes were shown to be a part of the multienzymatic complex involved in peptidogly …
Moenomycin, a well studied glycosyltransferase activity inhibitor has provided useful informations about lipid binding properties and …
Molecular mechanisms of antibiotic resistance in gram-positive pathogens.
Dessen A, Di Guilmi AM, Vernet T, Dideberg O. Dessen A, et al. Curr Drug Targets Infect Disord. 2001 May;1(1):63-77. doi: 10.2174/1568005013343272. Curr Drug Targets Infect Disord. 2001. PMID: 12455234 Review.
The widespread and uncontrolled use of antibiotics, both for human consumption and animal feed, has encouraged the development of drug resistance in a variety of pathogenic bacteria. ...
The widespread and uncontrolled use of antibiotics, both for human consumption and animal feed, has encouraged the development of drug resis …
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