title: Heat shock proteins and ion channels. Functional interactions and therapeutic consequences.
abstract: Screening for protein interaction partners of ion channels helps to elucidate signaling cascades to cellular targets and processes for a better understanding of the origin of diseases. Most important are the cytosolic segments of membrane-bound voltage- and ligand-gated ion channels or from ion channel regulators, which may connect to specific signaling complexes. So far, not much is known about those interactions. Molecular chaperones are proteins, which support the biosynthesis of proteins during maturation without being part of the final protein complex or which support the degradation of targeted proteins within the cellular protein quality control.
authors.affiliation: University of Cologne, Institute of Neurophysiology, Robert-Koch-Str. 39, D-50931 Köln, Germany.
authors.forename: Kayalvizhi
authors.initials: K
authors.lastname: Radhakrishnan
authors.forename: Jürgen
authors.initials: J
authors.lastname: Hescheler
authors.forename: Toni
authors.initials: T
authors.lastname: Schneider
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D055808:Drug Discovery; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007473:Ion Channels / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D025941:Protein Interaction Mapping; D016415:Sequence Alignment; D015398:Signal Transduction
chemical_list: D006360:Heat-Shock Proteins; D007473:Ion Channels