Role of N-terminal residues in the ubiquitin-independent degradation of human thymidylate synthase

Biochemical Journal

Volumn 394, Issue 1, 2006, Pages 355-363

  Peña, Maria Marjorette O ^a   Xing, Yang Yang ^a   Koli, Sangita ^a   Berger, Franklin G ^a  

^a UNIVERSITY OF SOUTH CAROLINA   (United States)

Author keywords

Enzyme degradation; Fluoropyrimidine; Proteasome; Proteolysis; Thymidylate synthase; Ubiquitin independent

Indexed keywords

AMINO ACIDS; CELL CULTURE; CHEMOTHERAPY; DEGRADATION; TUMORS;

ENZYME DEGRADATION; FLUOROPYRIMIDINE; PROTEASOME; PROTEOLYSIS; THYMIDYLATE SYNTHASE; UBIQUITIN-INDEPENDENT;

ENZYMES;

ARGININE; PROTEASOME; THYMIDINE; THYMIDYLATE SYNTHASE; UBIQUITIN;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME DEGRADATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; ANIMALS; CRICETINAE; CRICETULUS; HUMANS; LYSINE; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; SIGNAL TRANSDUCTION; THYMIDYLATE SYNTHASE; UBIQUITIN;

ANIMALIA;

EID: 32944460570     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051479     Document Type: Article

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