title: Bacterial mimics of eukaryotic GTPase-activating proteins (GAPs).
abstract: Bacterial GTPase-activating proteins (GAPs) subvert their host's eukaryotic Rho GTPases to their own advantage. Studies of bacterial GAPs extend our understanding of the action of eukaryotic GAPs, provide new tools for studies of cytoskeletal dynamics and offer new targets for anti-bacterial drugs.
authors.affiliation: Department of Biological Chemistry and the Kuhne Minerva Center, Institute of Life Sciences, The Hebrew University of Jerusalem, 91904, Jerusalem, Israel.
authors.forename: Yael
authors.initials: Y
authors.lastname: Litvak
authors.forename: Zvi
authors.initials: Z
authors.lastname: Selinger
mesh_terms: D000595:Amino Acid Sequence; D001120:Arginine / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002384:Catalysis; D005057:Eukaryotic Cells / Q000378:metabolism; D020690:GTPase-Activating Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D017510:Protein Folding; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D001426:Bacterial Proteins; D020690:GTPase-Activating Proteins; D001120:Arginine