Flexible regions within IκBα create the ubiquitin-independent degradation signal

Journal of Biological Chemistry

Volumn 285, Issue 43, 2010, Pages 32927-32936

  Mathes, Erika ^a   Wang, Lily ^a   Komives, Elizabeth ^a   Ghosh, Gourisankar ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; C TERMINUS; CONTINUOUS SYNTHESIS; DEGRADATION RATE; HOMEOSTATIC REGULATIONS; HYDROPHOBIC CHARACTER; HYDROPHOBIC RESIDUES; INHERENT FLEXIBILITY; POLYPROLINE II; POLYPROLINE II HELIX; PROTEASOMES; RAPID DEGRADATION; UBIQUITIN;

AMINO ACIDS; HYDROPHOBICITY;

DEGRADATION;

ANKYRIN; I KAPPA B ALPHA; TYROSINE; UBIQUITIN;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN METABOLISM;

3T3 CELLS; ANIMALS; I-KAPPA B PROTEINS; MICE; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; UBIQUITIN;

EID: 77958506556     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.107326     Document Type: Article

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