Mutational analysis of the cleavage of the cancer-associated laminin receptor by stromelysin-3 reveals the contribution of flanking sequences to site recognition and cleavage efficiency

International Journal of Molecular Medicine

Volumn 23, Issue 3, 2009, Pages 389-397

  Fiorentino, Maria ^a   Fu, Liezhen ^a   Shi, Yun Bo ^a  

^a Section on Molecular Morphogenesis   (United States)

Author keywords

Extracellular matrix; Laminin receptor; Matrix metallo proteinase; Stromelysin 3; Tumor invasion; Xenopus laevis

Indexed keywords

ALANINE; LAMININ RECEPTOR; STROMELYSIN 3; MMP11 PROTEIN, HUMAN; TUMOR PROTEIN; XENOPUS PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL EXPERIMENT; ARTICLE; CANCER GROWTH; CANCER INHIBITION; CELL FATE; CONTROLLED STUDY; DNA FLANKING REGION; HUMAN; METASTASIS INHIBITION; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CLEAVAGE; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN PURIFICATION; XENOPUS; ANIMAL; BIOLOGICAL MODEL; GENETICS; METABOLISM; METAMORPHOSIS; MUTATION; NEOPLASM; PHYSIOLOGY; XENOPUS LAEVIS;

AMINO ACID SUBSTITUTION; ANIMALS; HUMANS; MATRIX METALLOPROTEINASE 11; METAMORPHOSIS, BIOLOGICAL; MODELS, BIOLOGICAL; MUTATION; NEOPLASM PROTEINS; NEOPLASMS; RECEPTORS, LAMININ; XENOPUS LAEVIS; XENOPUS PROTEINS;

EID: 64249169015     PISSN: 11073756     EISSN: 1791244X     Source Type: Journal    
DOI: 10.3892/ijmm_00000143     Document Type: Article

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