Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: The role of dangerous unchaperoned molecules

Clinical and Experimental Pharmacology and Physiology

Volumn 29, Issue 9, 2002, Pages 741-753

  Kourie, Joseph I ^a   Henry, Christine L ^a  

^a AUSTRALIAN NATIONAL UNIVERSITY   (Australia)

Author keywords

Amyloid forming proteins; Antimicrobial proteins; Ion channel formation; Membrane destabilization; Membrane linked pathologies; Misfolded hydrophobic proteins; Unchaperoned proteins; Viral proteins

Indexed keywords

ALAMETHICIN; ALPHA SARCIN; AMYLIN; AMYLOID BETA PROTEIN; AMYLOID PROTEIN; CALCITONIN; CATHELICIDIN; CECROPIN; CHAPERONE; DIPHTHERIA TOXIN; GALANIN; GRAMICIDIN; GRAMICIDIN A; INDOLICIDIN; LACTOFERRICIN B; MAGAININ; MELITTIN; NATRIURETIC PEPTIDE TYPE C; PARDAXIN; POLYPEPTIDE ANTIBIOTIC AGENT; PRION PROTEIN; PROTEIN; SYNAPSIN I; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ANTIMICROBIAL ACTIVITY; CELL DAMAGE; CELL FUNCTION; CHANNEL GATING; CYTOTOXICITY; DEGENERATIVE DISEASE; HYDROPHOBICITY; ION TRANSPORT; LIPID MEMBRANE; MEMBRANE DAMAGE; MEMBRANE STABILIZATION; NONHUMAN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; REVIEW;

ANIMALS; CELL MEMBRANE; HUMANS; HYDROPHOBICITY; ION CHANNELS; MEMBRANE PROTEINS; MOLECULAR CHAPERONES; PROTEIN FOLDING;

EID: 0036381074     PISSN: 03051870     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1440-1681.2002.03737.x     Document Type: Review

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