Phosphorylation of the stress protein HSP27 is an early event in murine myelomonocytic leukemic cell differentiation induced by leukemia inhibitory factor/D-factor
- 15 May 1991
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 176 (3) , 979-984
- https://doi.org/10.1016/0006-291x(91)90378-k
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Regulation of the expression of vimentin gene during the differentiation of mouse myeloid leukemia cells.The Journal of cell biology, 1990
- The respective 27 kDa and 28 kDa protein kinase C substrates in vascular endothelial and MCF-7 cells are most probably heat shock proteinsBiochemical and Biophysical Research Communications, 1990
- Tumor necrosis factor-α induces the phosphorylation of 28kDa stress proteins in endothelial cells: Possible role in protection against cytotoxicity?Biochemical and Biophysical Research Communications, 1989
- Purification of a lipoprotein lipase-inhibiting protein produced by a melanoma cell line associated with cancer cachexiaBiochemical and Biophysical Research Communications, 1989
- Combined Effects of Differentiation-inducing Factor and Other Cytokines on Induction of Differentiation of Mouse Myeloid Leukemic CellsJapanese Journal of Cancer Research, 1989
- Interleukin 1 and tumour necrosis factor increase phosphorylation of fibroblast proteinsFEBS Letters, 1988
- THE HEAT-SHOCK PROTEINSAnnual Review of Genetics, 1988
- Leukaemia inhibitory factor is identical to the myeloid growth factor human interleukin for DA cellsNature, 1988
- Rapid phosphorylation of a 27 kDa protein induced by tumor necrosis factorFEBS Letters, 1988
- Thrombin-induced protein phosphorylation in resting platelets and fibroblasts: Evidence for common post-receptor molecular eventsBiochemical and Biophysical Research Communications, 1983