The Proline-Rich Motif of the proDer p 3 Allergen Propeptide Is Crucial for Protease-Protease Interaction

PLoS ONE

Volumn 8, Issue 9, 2013, Pages

  Dumez, Marie Eve ^a   Herman, Julie ^a   Campisi, Vincenzo ^a,b   Bouaziz, Ahlem ^a   Rosu, Frédéric ^a   Luxen, André ^a   Vandenberghe, Isabel ^c   de Pauw, Edwin ^a   Frère, Jean Marie ^a   Matagne, André ^a   Chevigné, Andy ^a,b   Galleni, Moreno ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

^b Retrovirology Laboratory Luxembourg   (Luxembourg)

^c Laboratory for Protein Biochemistry and Protein Engineering   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ALLERGEN; ENZYME PRECURSOR; PRODER P 3 PROPEPTIDE; PROTEIN PRECURSOR; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BIOASSAY; CONTROLLED STUDY; ELECTROSPRAY MASS SPECTROMETRY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME STABILITY; MOLECULAR DYNAMICS; NONHUMAN; NUCLEOTIDE SEQUENCE; PICHIA PASTORIS; PROLINE RICH PROTEIN DOMAIN; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN HYDROLYSIS; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN SECRETION; PROTEIN UNFOLDING; QUENCHED FLOW ASSAY; STEADY STATE; STRUCTURE ACTIVITY RELATION; THERMOSTABILITY;

ALLERGENS; AMINO ACID MOTIFS; ANTIGENS, DERMATOPHAGOIDES; ARTHROPOD PROTEINS; ENZYME PRECURSORS; FLUORESCENCE; MUTATION; PICHIA; PROLINE; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, TERTIARY; SERINE ENDOPEPTIDASES; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EID: 84884492024     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0068014     Document Type: Article

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