A homeostatic model of IκB metabolism to control constitutive NF-κB activity

Molecular Systems Biology

Volumn 3, Issue , 2007, Pages

  O'Dea, Ellen L ^a   Barken, Derren ^a   Peralta, Raechel Q ^a,c   Tran, Kim T ^a,d   Werner, Shannon L ^a   Kearns, Jeffrey D ^a   Levchenko, Andre ^b   Hoffmann, Alexander ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b Johns Hopkins University   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d University of California San Diego ^*  (United States)

Author keywords

Cross regulation; Homeostasis; Mathematical modeling; Robustness; Signaling module

Indexed keywords

I KAPPA B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; TRANSCRIPTION FACTOR; BENZYLOXYCARBONYLLEUCYL LEUCYL LEUCINE ALDEHYDE; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; I KAPPA B BETA; I KAPPA B KINASE; LEUPEPTIN; NF KAPPAB INHIBITOR ALPHA; NF-KAPPAB INHIBITOR ALPHA; NFKBIE PROTEIN, MOUSE; ONCOPROTEIN; PROTEASOME; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; CYTOPLASM; EMBRYO; HOMEOSTASIS; IN VIVO STUDY; MATHEMATICAL COMPUTING; MOUSE; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN METABOLISM; REGULATORY MECHANISM; SIGNAL TRANSDUCTION; STEADY STATE; STIMULUS RESPONSE; ANIMAL; BIOLOGICAL MODEL; CELL CULTURE; COMPARATIVE STUDY; COMPUTER SIMULATION; FIBROBLAST; GEL MOBILITY SHIFT ASSAY; GENETICS; HALF LIFE TIME; KINETICS; METABOLISM; MOUSE MUTANT; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN ANALYSIS; PROTEIN PROCESSING; WESTERN BLOTTING;

ANIMALS; BLOTTING, WESTERN; CELLS, CULTURED; COMPUTER SIMULATION; ELECTROPHORETIC MOBILITY SHIFT ASSAY; FIBROBLASTS; HALF-LIFE; HOMEOSTASIS; I-KAPPA B KINASE; I-KAPPA B PROTEINS; KINETICS; LEUPEPTINS; MICE; MICE, KNOCKOUT; MODELS, BIOLOGICAL; NF-KAPPA B; PHOSPHORYLATION; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; PROTEIN INTERACTION MAPPING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTO-ONCOGENE PROTEINS; SIGNAL TRANSDUCTION; TUMOR NECROSIS FACTOR-ALPHA;

EID: 34248997836     PISSN: 17444292     EISSN: 17444292     Source Type: Journal    
DOI: 10.1038/msb4100148     Document Type: Article

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