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André Zapun
Researcher at University of Grenoble
Publications - 30
Citations - 1583
André Zapun is an academic researcher from University of Grenoble. The author has contributed to research in topics: Peptidoglycan & Penicillin binding proteins. The author has an hindex of 18, co-authored 30 publications receiving 1465 citations. Previous affiliations of André Zapun include Commissariat à l'énergie atomique et aux énergies alternatives & Joseph Fourier University.
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Journal ArticleDOI
Identification of FtsW as a transporter of lipid-linked cell wall precursors across the membrane.
Tamimount Mohammadi,Vincent van Dam,Robert Sijbrandi,Thierry Vernet,André Zapun,Ahmed Bouhss,Marlies Diepeveen-de Bruin,Martine Nguyen-Distèche,Ben de Kruijff,Eefjan Breukink +9 more
TL;DR: This study provides the first biochemical evidence for the involvement of an essential protein in the transport of lipid‐linked cell wall precursors across biogenic membranes.
Journal ArticleDOI
The different shapes of cocci.
TL;DR: The present review aims to integrate older ultra-structural data with recent localization studies, in order to clarify the relation between the mechanisms of cell wall synthesis and the determination of cell shape in various cocci.
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Cooperativity of peptidoglycan synthases active in bacterial cell elongation
Manuel Banzhaf,H. Bart van den Berg van Saparoea,Mohammed Terrak,Claudine Fraipont,Alexander J. F. Egan,Jules Philippe,Jules Philippe,André Zapun,André Zapun,Eefjan Breukink,Martine Nguyen-Distèche,Tanneke den Blaauwen,Waldemar Vollmer +12 more
TL;DR: In vitro peptidoglycan synthesis assays provide novel insights into the cooperativity of peptidglycan synthases with different activities, and provide a possible explanation for the depletion of lipid II precursors in penicillin‐treated cells.
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Growth and division of Streptococcus pneumoniae: localization of the high molecular weight penicillin‐binding proteins during the cell cycle
TL;DR: The cellular localization of all the high molecular weight PBPs of the human pathogen Streptococcus pneumoniae, for a wild type and for several PBP‐deficient strains, indicates the existence of peripheral peptidoglycan synthesis, which implies a similarity between the mechanism of cell division in bacilli and streptococci.
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The D,D-carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae.
TL;DR: The consequences of the absence of PBP3 indicate that the peptidoglycan composition is central to the co‐ordination of the division process.