A 27-amino-acid synthetic peptide corresponding to the NH 2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity

Cancer Research

Volumn 65, Issue 9, 2005, Pages 3656-3663

  Sjin, Robert M Tjin Tham ^a   Satchi Fainaro, Ronit ^a   Birsner, Amy E ^a   Ramanujam, V M Sadagopa ^b   Folkman, Judah ^a   Javaherian, Kashi ^a  

^a BOSTON CHILDREN S HOSPITAL   (United States)

^b University of Texas Medical Branch School of Medicine   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENDOSTATIN; HISTIDINE; SYNTHETIC PEPTIDE; ZINC;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIANGIOGENIC ACTIVITY; ANTINEOPLASTIC ACTIVITY; ARTICLE; CELL MEMBRANE PERMEABILITY; CELL MIGRATION; CONTROLLED STUDY; DRUG PROTEIN BINDING; ESCHERICHIA COLI; GENE MUTATION; HUMAN; HUMAN CELL; MALE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN STRUCTURE;

ADENOCARCINOMA; AMINO ACID SEQUENCE; ANIMALS; CARCINOMA, LEWIS LUNG; CELL MOVEMENT; ENDOSTATINS; ENDOTHELIAL CELLS; HISTIDINE; HUMANS; MICE; MICE, INBRED C57BL; MICE, SCID; MOLECULAR SEQUENCE DATA; PANCREATIC NEOPLASMS; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; XENOGRAFT MODEL ANTITUMOR ASSAYS; ZINC;

EID: 18144419701     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-04-1833     Document Type: Article

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