A single replacement of histidine to arginine in EGFR-lytic hybrid peptide demonstrates the improved anticancer activity

Biochemical and Biophysical Research Communications

Volumn 407, Issue 2, 2011, Pages 383-388

  Tada, Noriko ^a   Horibe, Tomohisa ^a   Haramoto, Mari ^a   Ohara, Koji ^a   Kohno, Masayuki ^a,b   Kawakami, Koji ^a  

^a KYOTO UNIVERSITY   (Japan)

^b Upstream Infinity Inc   (Japan)

Author keywords

Drug delivery; Drug resistance; EGFR; Hybrid peptide; Molecular targeting

Indexed keywords

ARGININE; EPIDERMAL GROWTH FACTOR RECEPTOR; HISTIDINE; HYBRID PROTEIN;

AMINO ACID SUBSTITUTION; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTINEOPLASTIC ACTIVITY; ARTICLE; BREAST CANCER; CANCER MODEL; CIRCULAR DICHROISM; CONJUGATION; CONTROLLED STUDY; DRUG CYTOTOXICITY; DRUG RECEPTOR BINDING; FEMALE; HUMAN; HUMAN CELL; IN VIVO STUDY; MOLECULAR INTERACTION; MOUSE; MUTATION; NONHUMAN; PRIORITY JOURNAL; RECEPTOR AFFINITY; TUMOR XENOGRAFT;

AMINO ACID SUBSTITUTION; ANIMALS; ANTINEOPLASTIC AGENTS; ARGININE; BREAST NEOPLASMS; CELL LINE, TUMOR; FEMALE; HISTIDINE; HUMANS; MICE; MICE, NUDE; MUTATION; PEPTIDES; RECEPTOR, EPIDERMAL GROWTH FACTOR; RECOMBINANT FUSION PROTEINS; XENOGRAFT MODEL ANTITUMOR ASSAYS;

EID: 79953675436     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.03.030     Document Type: Article

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