Tripartite degrons confer diversity and specificity on regulated protein degradation in the ubiquitin-proteasome system

Nature Communications

Volumn 7, Issue , 2016, Pages

  Guharoy, Mainak ^a   Bhowmick, Pallab ^a   Sallam, Mohamed ^a   Tompa, Peter ^a,b  

^a VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^b INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME; UBIQUITIN PROTEIN LIGASE E3; PROTEIN; UBIQUITIN;

AMINO ACID; CELLS AND CELL COMPONENTS; CHEMICAL CUE; DISEASE; ENZYME ACTIVITY; PEPTIDE; PROTEIN; SUBSTRATE;

AMINO ACID COMPOSITION; AMINO TERMINAL SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; DNA FLANKING REGION; ENZYME SPECIFICITY; MOLECULAR RECOGNITION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN UNFOLDING; UBIQUITINATION; ANIMAL; GENE EXPRESSION REGULATION; GENETICS; HUMAN; MAMMAL; METABOLISM; MOLECULAR MODEL;

ANIMALS; GENE EXPRESSION REGULATION; HUMANS; MAMMALS; MODELS, MOLECULAR; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN CONFORMATION; PROTEINS; PROTEOLYSIS; UBIQUITINS;

EID: 84954288558     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms10239     Document Type: Article

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