Unfolding, aggregation, and amyloid formation by the tetramerization domain from mutant p53 associated with lung cancer

Biochemistry

Volumn 45, Issue 6, 2006, Pages 1608-1619

  Higashimoto, Yuichiro ^a   Asanomi, Yuya ^b   Takakusagi, Satoru ^b   Lewis, Marc S ^c   Uosaki, Kohei ^b   Durell, Stewart R ^d   Anderson, Carl W ^e   Appella, Ettore ^d   Sakaguchi, Kazuyasu ^b  

^a KURUME UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b HOKKAIDO UNIVERSITY   (Japan)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

^d NATIONAL CANCER INSTITUTE   (United States)

^e BROOKHAVEN NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; HUMAN REHABILITATION ENGINEERING; PH EFFECTS; PHYSIOLOGY; THERMAL EFFECTS;

CANCER-DERIVED MUTANT; LUNG CANCER; MUTANT P53; TETRAMERIZATION;

TUMORS;

AMYLOID; GLYCINE; PROTEIN P53; TUMOR SUPPRESSOR PROTEIN; VALINE;

AMINO ACID SUBSTITUTION; APOPTOSIS; ARTICLE; COMPLEX FORMATION; DNA DAMAGE; ENHANCER REGION; GENE MUTATION; LUNG CANCER; OLIGOMERIZATION; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN FOLDING; TRANSCRIPTION REGULATION; TUMOR SUPPRESSOR GENE;

AMINO ACID SEQUENCE; AMYLOID; GLYCINE; GUANIDINE; HUMANS; LUNG NEOPLASMS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; TEMPERATURE; TIME FACTORS; TUMOR SUPPRESSOR PROTEIN P53; VALINE;

EID: 32344444621     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051192j     Document Type: Article

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