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Volumn 19, Issue 20, 2000, Pages 5324-5331
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Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo
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Author keywords
4 hydroxyproline; Polyproline II helix; Post translational modifications; Prion protein; Prolyl 4 hydroxylase
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Indexed keywords
CATION;
HYDROXYPROLINE;
POLYMER;
PRION PROTEIN;
PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE;
PROLINE;
RECOMBINANT PROTEIN;
AMINO ACID SEQUENCE;
AMINO TERMINAL SEQUENCE;
ANIMAL CELL;
ANIMAL MODEL;
ANIMAL TISSUE;
ARTICLE;
CIRCULAR DICHROISM;
ENZYME SUBSTRATE;
HYDROXYLATION;
MASS SPECTROMETRY;
MOUSE;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN MODIFICATION;
PROTEIN PROCESSING;
PROTEIN STRUCTURE;
SCRAPIE;
STRUCTURE ACTIVITY RELATION;
AMINO ACID SEQUENCE;
ANIMAL;
CHO CELLS;
CIRCULAR DICHROISM;
GUANIDINE;
HAMSTERS;
HYDROXYLATION;
MICE;
MOLECULAR SEQUENCE DATA;
OSMOLAR CONCENTRATION;
OXIDATION-REDUCTION;
PEPTIDE FRAGMENTS;
PEPTIDES;
PRIONS;
PROLINE;
PROTEIN DENATURATION;
PROTEIN PROCESSING, POST-TRANSLATIONAL;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
PRPSC PROTEINS;
RECOMBINANT PROTEINS;
SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;
SUPPORT, NON-U.S. GOV'T;
TEMPERATURE;
TRANSFECTION;
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EID: 0034676088
PISSN: 02614189
EISSN: None
Source Type: Journal
DOI: 10.1093/emboj/19.20.5324 Document Type: Article |
Times cited : (57)
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References (48)
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