Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy

International Journal of Nanomedicine

Volumn 6, Issue 1, 2011, Pages 3011-3019

  Bizzarri, Anna Rita ^a   Santini, Simona ^a   Coppari, Emilia ^a   Bucciantini, Monica ^b   Di Agostino, Silvia ^c   Yamada, Tohru ^d   Beattie, Craig W ^d   Cannistraro, Salvatore ^a  

^a UNIVERSITY OF TUSCIA   (Italy)

^b UNIVERSITY OF FLORENCE   (Italy)

^c REGINA ELENA NATIONAL CANCER INSTITUTE   (Italy)

^d UNIVERSITY OF ILLINOIS   (United States)

Author keywords

AFS; Cancer physics; Unbinding forces

Indexed keywords

AZURIN; PEPTIDE FRAGMENT; PROTEIN MDM2; PROTEIN P53; UBIQUITIN PROTEIN LIGASE; ANTINEOPLASTIC AGENT; IMMOBILIZED PROTEIN; TP53 PROTEIN, HUMAN;

ANTINEOPLASTIC ACTIVITY; ARTICLE; ATOMIC FORCE MICROSCOPY; BINDING AFFINITY; BINDING SITE; COMPLEX FORMATION; DISSOCIATION CONSTANT; DRUG PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; CHEMISTRY; HUMAN; METABOLISM; PROTEIN BINDING; PSEUDOMONAS AERUGINOSA; SPECTROSCOPY;

ANTINEOPLASTIC AGENTS; AZURIN; HUMANS; IMMOBILIZED PROTEINS; MICROSCOPY, ATOMIC FORCE; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PSEUDOMONAS AERUGINOSA; SPECTRUM ANALYSIS; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84862618583     PISSN: 11769114     EISSN: 11782013     Source Type: Journal    
DOI: 10.2147/IJN.S26155     Document Type: Article

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