title: Self-assembly of okadaic acid as a pathway to the cell.
abstract: The polyether toxin okadaic acid (OA) inhibits several protein serine/threonine phosphatases that play central roles in the regulation of many essential cellular processes. The use of scanning tunneling microscopy (STM) shows that dimerization of such toxins is crucial to understand the mechanism of toxin transport across model membranes.
authors.affiliation: Instituto Universitario de Bio-OrgAnica Antonio GonzAlez, Astrofísico Francisco SAnchez 2, Universidad de La Laguna, 38206 La Laguna, Tenerife, Spain.
authors.forename: Antonio Hernández
authors.initials: AH
authors.lastname: Daranas
authors.forename: Patricia G
authors.initials: PG
authors.lastname: Cruz
authors.forename: Alberto Hernández
authors.initials: AH
authors.lastname: Creus
authors.forename: Manuel
authors.initials: M
authors.lastname: Norte
authors.forename: José J
authors.initials: JJ
authors.lastname: Fernández
mesh_terms: D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D008387:Marine Toxins / Q000494:pharmacology*; D016252:Microscopy, Scanning Tunneling / Q000379:methods; D008954:Models, Biological; D015394:Molecular Structure; D019319:Okadaic Acid / Q000737:chemistry / Q000494:pharmacology*; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors*
chemical_list: D004791:Enzyme Inhibitors; D008387:Marine Toxins; D019319:Okadaic Acid; D010749:Phosphoprotein Phosphatases