Phosphorylation of FADD at serine 194 by CKIalpha regulates its nonapoptotic activities. [electronic resource]
Producer: 20051101Description: 321-32 p. digitalISSN:- 1097-2765
- Adaptor Proteins, Signal Transducing -- genetics
- Amino Acid Sequence
- Animals
- Apoptosis
- Binding Sites -- genetics
- Casein Kinase Ialpha -- genetics
- Cell Cycle -- drug effects
- Cell Line
- Cell Nucleus -- metabolism
- Concanavalin A -- pharmacology
- Cytosol -- metabolism
- Enzyme Inhibitors -- pharmacology
- Fas-Associated Death Domain Protein
- HeLa Cells
- Humans
- Isoquinolines -- pharmacology
- Jurkat Cells
- Lymphocyte Activation
- Mice
- Mice, Inbred C57BL
- Mice, Mutant Strains
- Mitosis -- drug effects
- Molecular Sequence Data
- Mutation -- genetics
- Paclitaxel -- pharmacology
- Phosphorylation
- Protein Binding
- Protein Transport -- genetics
- RNA, Small Interfering -- genetics
- Sequence Homology, Amino Acid
- Serine -- metabolism
- Spindle Apparatus -- metabolism
- T-Lymphocytes -- metabolism
- Tetradecanoylphorbol Acetate -- pharmacology
- Transfection
No physical items for this record
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
There are no comments on this title.
Log in to your account to post a comment.