Plexins: making links to the cytoskeleton and reducing the GAPs in our knowledge.
Bagnard
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D000199:Actins / Q000378:metabolism; D001120:Arginine / Q000235:genetics; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D020439:Growth Cones / Q000378:metabolism; D016297:Mutagenesis, Site-Directed / Q000235:genetics; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism*; D039942:Neuropilin-1; D040121:Semaphorin-3A; D017385:Sequence Homology; D015398:Signal Transduction / Q000502:physiology; D020744:rac GTP-Binding Proteins / Q000378:metabolism; D020703:ras GTPase-Activating Proteins / Q000737:chemistry / Q000378:metabolism*; D020741:rho GTP-Binding Proteins / Q000737:chemistry / Q000378:metabolism*
D000199:Actins; D015815:Cell Adhesion Molecules; D006023:Glycoproteins; D009419:Nerve Tissue Proteins; D040121:Semaphorin-3A; C091529:plexin; D020703:ras GTPase-Activating Proteins; D039942:Neuropilin-1; D001120:Arginine; D020744:rac GTP-Binding Proteins; D020741:rho GTP-Binding Proteins