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Volumn 62, Issue 1, 2000, Pages 120-133
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Prion peptide fragment PrP[106-126] forms distinct cation channel types
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Author keywords
Cation channels; Channel forming peptides; Heterogeneous channels; Prions; Signal transduction
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Indexed keywords
CATION CHANNEL;
GLUTATHIONE DISULFIDE;
LIPOSOME;
OXIDIZING AGENT;
PHOSPHATIDYLCHOLINE;
PHOSPHATIDYLETHANOLAMINE;
PHOSPHATIDYLSERINE;
POTASSIUM CHANNEL BLOCKING AGENT;
PRION PROTEIN;
PRP[106-126]PROTEIN;
TETRYLAMMONIUM CHLORIDE;
UNCLASSIFIED DRUG;
ARTICLE;
CHANNEL GATING;
CONTROLLED STUDY;
DRUG SYNTHESIS;
ION CONDUCTANCE;
ION CURRENT;
ION TRANSPORT;
KINETICS;
LIPID BILAYER;
MEMBRANE TRANSPORT;
NEUROPATHOLOGY;
PATHOGENESIS;
PEPTIDE ANALYSIS;
PRION DISEASE;
PRIORITY JOURNAL;
PROTEIN STRUCTURE;
SIGNAL TRANSDUCTION;
CATIONS, MONOVALENT;
DITHIOTHREITOL;
ELECTRIC CONDUCTIVITY;
GLUTATHIONE DISULFIDE;
ION CHANNELS;
KINETICS;
LIPID BILAYERS;
LIPOSOMES;
MEMBRANE POTENTIALS;
OXIDANTS;
PEPTIDE FRAGMENTS;
POTASSIUM CHANNEL BLOCKERS;
PRIONS;
SUBSTRATE SPECIFICITY;
SUPPORT, NON-U.S. GOV'T;
TETRAETHYLAMMONIUM;
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EID: 0033774525
PISSN: 03604012
EISSN: None
Source Type: Journal
DOI: 10.1002/1097-4547(20001001)62:1<120::AID-JNR13>3.0.CO;2-2 Document Type: Article |
Times cited : (60)
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References (30)
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