Heterologous stacking of prion protein peptides reveals structural details of fibrils and facilitates complete inhibition of fibril growth

Journal of Biological Chemistry

Volumn 284, Issue 19, 2009, Pages 12809-12820

  Boshuizen, Ronald S ^a   Schulz, Veronica ^a   Morbin, Michela ^b   Mazzoleni, Glulia ^b   Meloen, Rob H ^a,c   Langedijk, Johannes P M ^a  

^a Pepscan Systems   (Netherlands)

^b DEPARTMENT OF NEUROSURGERY   (Italy)

^c UTRECHT UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

FIBRIL FORMATION; FIBRIL GROWTH; FIBRIL STRUCTURE; GROWTH PROCESS; IN-VITRO; INHIBITORY PEPTIDES; NEW APPROACHES; PREDICTIVE VALUES; PRION PROTEIN; PRION PROTEIN FIBRILS; STRUCTURAL DETAILS; STRUCTURAL MODELS; UNDERLYING MECHANISM;

MODEL STRUCTURES; MONOMERS; OCEAN STRUCTURES; PEPTIDES; SCANDIUM; STRATEGIC PLANNING;

AMINES;

MEMBRANE ENZYME; N ACETYLGLUCOSEAMINE 1 PHOSPHATE URIDYLTRANSFERASE; PRION PROTEIN; PROLINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; DIMERIZATION; DISULFIDE BOND; GROWTH INHIBITION; HETEROLOGOUS STACKING; HOMOLOGOUS STACKING; MOLECULAR DYNAMICS; NEUROFILAMENT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; ULTRASTRUCTURE;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CYCLIZATION; DIMERIZATION; HUMANS; MODELS, MOLECULAR; MOLECULAR MIMICRY; MOLECULAR SEQUENCE DATA; NUCLEOTIDYLTRANSFERASES; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PRPSC PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 67649770235     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M809151200     Document Type: Article

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