E
Emir Berkane
Researcher at Centre national de la recherche scientifique
Publications - 4
Citations - 162
Emir Berkane is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Maltoporin & Vesicle. The author has an hindex of 4, co-authored 4 publications receiving 149 citations. Previous affiliations of Emir Berkane include University of Würzburg.
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Interaction between quinolones antibiotics and bacterial outer membrane porin OmpF.
TL;DR: It is possible to conclude that some of the quinolones associate preferably with the protein than with simpler biomembrane models (liposomes), which suggests that an interaction drug/porin is, probably, the preferentially used for the latest fluoroquinolones.
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Modes of membrane interaction of a natural cysteine-rich peptide: viscotoxin A3.
TL;DR: An interaction model is proposed in which the embedding of VA3 in the membrane induces membrane defects leading to the gradual release of encapsulated dye, and when the surfaces of the vesicles are saturated with the viscotoxin, complete vesicle destabilization is induced which leads to bilayer disruption, all-or-none encapsulated dyed release and rearrangement of theVesicles.
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Interaction of bacteriophage lambda with its cell surface receptor: an in vitro study of binding of the viral tail protein gpJ to LamB (Maltoporin).
Emir Berkane,Frank Orlik,Johannes F. Stegmeier,Alain Charbit,Mathias Winterhalter,Roland Benz +5 more
TL;DR: The interaction of the MBP-gpJ chimera protein with reconstituted LamB and its mutants LamB Y118G and the loop deletion mutant LamB Delta4+Delta6+Delta9v was studied and revealed that phage Lambda binding includes not only the extracellular loops.
Journal ArticleDOI
Nanopores: maltoporin channel as a sensor for maltodextrin and lambda-phage
Emir Berkane,Frank Orlik,Alain Charbit,Christophe Danelon,Didier Fournier,Roland Benz,Mathias Winterhalter,Mathias Winterhalter +7 more
TL;DR: This work could demonstrate the asymmetry of the bacterial phage Lambda binding to its natural receptor maltoporin and suggests that this type of measurement can be used as a new type of biosensors.