LYL1 degradation by the proteasome is directed by a N-Terminal PEST rich site in a phosphorylation-independent manner

PLoS ONE

Volumn 5, Issue 9, 2010, Pages 1-7

  Lukov, Georgi L ^a   Goodell, Margaret A ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; ASPARTIC ACID; GLUTAMIC ACID; LYMPHOBLASTIC LEUKEMIA 1; ONCOPROTEIN; PROLINE; PROTEASOME; SERINE; THREONINE; UNCLASSIFIED DRUG; BASIC HELIX LOOP HELIX TRANSCRIPTION FACTOR; LYL1 PROTEIN, HUMAN; MITOGEN ACTIVATED PROTEIN KINASE KINASE; TUMOR PROTEIN;

ACUTE LYMPHOBLASTIC LEUKEMIA; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; GENETIC VARIABILITY; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; NUCLEOTIDE SEQUENCE; PROTEIN DEGRADATION; PROTEIN DEPHOSPHORYLATION; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; SEQUENCE ALIGNMENT; T LYMPHOCYTE; TRANSCRIPTION REGULATION; UPREGULATION; CELL LINE; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR GENETICS; PHOSPHORYLATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BASIC HELIX-LOOP-HELIX TRANSCRIPTION FACTORS; CELL LINE; HUMANS; MITOGEN-ACTIVATED PROTEIN KINASE KINASES; MOLECULAR SEQUENCE DATA; NEOPLASM PROTEINS; PHOSPHORYLATION; PROTEASOME ENDOPEPTIDASE COMPLEX; SEQUENCE ALIGNMENT;

EID: 77958608378     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0012692     Document Type: Article

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