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Volumn 306, Issue 5694, 2004, Pages 271-275
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Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase itch
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Author keywords
[No Author keywords available]
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Indexed keywords
CHEMICAL ACTIVATION;
DEGRADATION;
LIGASES;
PHOSPHORYLATION;
PROTEOLYSIS;
PROTEINS;
F BOX PROTEIN;
LIGASE;
MITOGEN ACTIVATED PROTEIN KINASE;
STRESS ACTIVATED PROTEIN KINASE INHIBITOR;
TRANSCRIPTION FACTOR;
UBIQUITIN;
BIOCHEMISTRY;
ANIMAL CELL;
ARTICLE;
CELL STIMULATION;
CYTOKINE PRODUCTION;
EFFECTOR CELL;
ENZYME ACTIVITY;
MOUSE;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DEGRADATION;
PROTEIN METABOLISM;
PROTEIN PHOSPHORYLATION;
T LYMPHOCYTE;
UBIQUITINATION;
ANIMALS;
ANTIGENS, CD28;
CD4-POSITIVE T-LYMPHOCYTES;
INTERFERON TYPE II;
INTERLEUKINS;
LYMPHOCYTE ACTIVATION;
MAP KINASE KINASE KINASE 1;
MAP KINASE KINASE KINASES;
MICE;
MITOGEN-ACTIVATED PROTEIN KINASE 8;
MITOGEN-ACTIVATED PROTEIN KINASE 9;
MITOGEN-ACTIVATED PROTEIN KINASES;
PHOSPHORYLATION;
PROTO-ONCOGENE PROTEINS C-JUN;
RECEPTORS, ANTIGEN, T-CELL;
RECOMBINANT FUSION PROTEINS;
RNA, MESSENGER;
T-LYMPHOCYTES;
TH2 CELLS;
UBIQUITIN;
UBIQUITIN-PROTEIN LIGASES;
ANIMALIA;
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EID: 5044225158
PISSN: 00368075
EISSN: None
Source Type: Journal
DOI: 10.1126/science.1099414 Document Type: Article |
Times cited : (343)
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References (27)
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