Zapun A - Search Results

1

Membrane topology of the Streptococcus pneumoniae FtsW division protein.

Gérard P, Vernet T, Zapun A. Gérard P, et al. Among authors: zapun a. J Bacteriol. 2002 Apr;184(7):1925-31. doi: 10.1128/JB.184.7.1925-1931.2002. J Bacteriol. 2002. PMID: 11889099 Free PMC article.

2

Expression and purification of FtsW and RodA from Streptococcus pneumoniae, two membrane proteins involved in cell division and cell growth, respectively.

Noirclerc-Savoye M, Morlot C, Gérard P, Vernet T, Zapun A. Noirclerc-Savoye M, et al. Among authors: zapun a. Protein Expr Purif. 2003 Jul;30(1):18-25. doi: 10.1016/s1046-5928(03)00051-2. Protein Expr Purif. 2003. PMID: 12821317

3

Growth and division of Streptococcus pneumoniae: localization of the high molecular weight penicillin-binding proteins during the cell cycle.

Morlot C, Zapun A, Dideberg O, Vernet T. Morlot C, et al. Among authors: zapun a. Mol Microbiol. 2003 Nov;50(3):845-55. doi: 10.1046/j.1365-2958.2003.03767.x. Mol Microbiol. 2003. PMID: 14617146 Free article.

4

The D,D-carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae.

Morlot C, Noirclerc-Savoye M, Zapun A, Dideberg O, Vernet T. Morlot C, et al. Among authors: zapun a. Mol Microbiol. 2004 Mar;51(6):1641-8. doi: 10.1046/j.1365-2958.2003.03953.x. Mol Microbiol. 2004. PMID: 15009891 Free article.

5

In vitro reconstitution of a trimeric complex of DivIB, DivIC and FtsL, and their transient co-localization at the division site in Streptococcus pneumoniae.

Noirclerc-Savoye M, Le Gouëllec A, Morlot C, Dideberg O, Vernet T, Zapun A. Noirclerc-Savoye M, et al. Among authors: zapun a. Mol Microbiol. 2005 Jan;55(2):413-24. doi: 10.1111/j.1365-2958.2004.04408.x. Mol Microbiol. 2005. PMID: 15659160 Free article.

6

Roles of pneumococcal DivIB in cell division.

Le Gouëllec A, Roux L, Fadda D, Massidda O, Vernet T, Zapun A. Le Gouëllec A, et al. Among authors: zapun a. J Bacteriol. 2008 Jul;190(13):4501-11. doi: 10.1128/JB.00376-08. Epub 2008 Apr 25. J Bacteriol. 2008. PMID: 18441058 Free PMC article.

7

The membrane anchor of penicillin-binding protein PBP2a from Streptococcus pneumoniae influences peptidoglycan chain length.

Helassa N, Vollmer W, Breukink E, Vernet T, Zapun A. Helassa N, et al. Among authors: zapun a. FEBS J. 2012 Jun;279(11):2071-81. doi: 10.1111/j.1742-4658.2012.08592.x. Epub 2012 May 8. FEBS J. 2012. PMID: 22487093 Free article.

8

Increase of the deacylation rate of PBP2x from Streptococcus pneumoniae by single point mutations mimicking the class A beta-lactamases.

Chesnel L, Zapun A, Mouz N, Dideberg O, Vernet T. Chesnel L, et al. Among authors: zapun a. Eur J Biochem. 2002 Mar;269(6):1678-83. doi: 10.1046/j.1432-1327.2002.02815.x. Eur J Biochem. 2002. PMID: 11895438 Free article.

9

The structural modifications induced by the M339F substitution in PBP2x from Streptococcus pneumoniae further decreases the susceptibility to beta-lactams of resistant strains.

Chesnel L, Pernot L, Lemaire D, Champelovier D, Croizé J, Dideberg O, Vernet T, Zapun A. Chesnel L, et al. Among authors: zapun a. J Biol Chem. 2003 Nov 7;278(45):44448-56. doi: 10.1074/jbc.M305948200. Epub 2003 Aug 15. J Biol Chem. 2003. PMID: 12923202 Free article.

10

Identical penicillin-binding domains in penicillin-binding proteins of Streptococcus pneumoniae clinical isolates with different levels of beta-lactam resistance.

Chesnel L, Carapito R, Croizé J, Dideberg O, Vernet T, Zapun A. Chesnel L, et al. Among authors: zapun a. Antimicrob Agents Chemother. 2005 Jul;49(7):2895-902. doi: 10.1128/AAC.49.7.2895-2902.2005. Antimicrob Agents Chemother. 2005. PMID: 15980366 Free PMC article.

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