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Juan A. Ayala

Researcher at Spanish National Research Council

Publications -  95
Citations -  5301

Juan A. Ayala is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Peptidoglycan & Escherichia coli. The author has an hindex of 31, co-authored 93 publications receiving 4787 citations. Previous affiliations of Juan A. Ayala include University of Extremadura & Autonomous University of Madrid.

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The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis

Eric Sauvage, +4 more
- 01 Mar 2008 - 
TL;DR: An overview of the content in PBPs of some bacteria is provided with an emphasis on comparing the biochemical properties of homologous PBPs (orthologues) belonging to different bacteria.
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CTX-M: changing the face of ESBLs in Europe

David M. Livermore, +11 more
- 06 Dec 2006 - 
TL;DR: Dramatic shifts have occurred in the prevalence and types of extended-spectrum beta-lactamases (ESBLs) in Europe, and changing patterns present major therapeutic and infection control challenges, with the public health intervention points unclear.
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Morphogenesis of rod‐shaped sacculi

Tanneke den Blaauwen, +3 more
- 01 Mar 2008 - 
TL;DR: In this article, the authors describe a protein complex, the elongase that inserts disaccharidepentapeptide units at a limited number of discrete sites while using the cytoskeletal MreB helix as a tracking device.
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Relationship between β-lactamase production, outer membrane protein and penicillin-binding protein profiles on the activity of carbapenems against clinical isolates of Acinetobacter baumannii

Felipe Fernández-Cuenca, +5 more
- 01 Mar 2003 - 
TL;DR: It is concluded that production of beta-lactamases of pI 6.3 and 7.0 and reduced expression of PBP 2 are the most frequently observed mechanisms of resistance to carbapenems.
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The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli.

Mohammed Terrak, +8 more
- 01 Oct 1999 - 
TL;DR: In in vitro assays with the lipid precursor and in the presence of penicillin at concentrations sufficient to derivatize the active‐site serine 510 of the acyl transferase, the rate of glycan chain synthesis is unmodified, showing that the functioning of the glycosyl transfer enzyme is acyltransferase independent.