In Silico tilted properties of the 67-78 fragment of α-synuclein are responsible for membrane destabilization and neurotoxicity

Proteins: Structure, Function and Genetics

Volumn 68, Issue 4, 2007, Pages 936-947

  Crowet, Jean Marc ^a   Lins, Laurence ^a   Dupiereux, Ingrid ^b   Elmoualija, Benaissa ^b   Lorin, Aurélien ^a   Charloteaux, Benoit ^a   Stroobant, Vincent ^c   Heinen, Ernst ^b   Brasseur, Robert ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

^b Institut de Pharmacie CHU   (Belgium)

^c LUDWIG INSTITUTE FOR CANCER RESEARCH   (Belgium)

Author keywords

Hydrophobicity; Lipid interacting peptides; Molecular modelling; Parkinson; Tilted peptides

Indexed keywords

ALPHA SYNUCLEIN; NEUROTOXIN; PEPTIDE FRAGMENT; PHOSPHOLIPID;

ARTICLE; CIRCULAR DICHROISM; COMPUTER MODEL; CONTROLLED STUDY; CYTOTOXICITY; HUMAN; HUMAN CELL; HYDROPHOBICITY; IN VITRO SELECTION; MATHEMATICAL MODEL; MOLECULAR MODEL; NEUROBLASTOMA CELL; NEUROTOXICITY; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; LEWY BODY; MECHANICAL STRESS; PARKINSON DISEASE; PATHOLOGY; PROTEIN CONFORMATION;

ALPHA-SYNUCLEIN; CIRCULAR DICHROISM; HUMANS; LEWY BODIES; MODELS, MOLECULAR; NEUROTOXINS; PARKINSON DISEASE; PEPTIDE FRAGMENTS; PHOSPHOLIPIDS; PROTEIN CONFORMATION; STRESS, MECHANICAL;

EID: 34548753401     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21483     Document Type: Article

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