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Michal Bohdanowicz et al.
Molecular biology of the cell, 24(11), 1700-1712 (2013-04-12)
Macrophages and dendritic cells continuously survey their environment in search of foreign particles and soluble antigens. Such surveillance involves the ongoing extension of actin-rich protrusions and the consequent formation of phagosomes and macropinosomes. The signals inducing this constitutive cytoskeletal remodeling
Phosphatidic acid induces conformational changes in Sec18 protomers that prevent SNARE priming
Starr ML, et al.
Test, 294(9), 3100-3116 (2019)
Regulation of human monocyte surface antigen expression. I. Up-modulation of Mo3e antigen expression on U-937 and HL-60 cells stimulated by pharmacologic activators of protein kinase C
Todd RF, et al.
Blood, 68(5), 1154-1161 (1986)
J G Ebeling et al.
Proceedings of the National Academy of Sciences of the United States of America, 82(3), 815-819 (1985-02-01)
Activation of cellular protein kinase C appears to be involved in the mechanism by which phorbol diesters induce differentiation of human myeloid leukemia cells (HL-60). Protein kinase C is thought to be physiologically activated by diacylglycerol derived from receptor-mediated phosphatidylinositol
1, 2-dioctanoyl-sn-glycerol can stimulate neutrophils by different mechanisms. Evidence for a pathway that does not involve phosphorylation of the 47-kDa protein.
Badwey JA, et al.
The Journal of biological chemistry, 264(34), 20676-20682 (1989)
R J Davis et al.
The Journal of biological chemistry, 260(3), 1562-1566 (1985-02-10)
The cell-permeable diacylglycerol, sn-1,2-dioctanoylglycerol (DiC8), is shown to mimic the effect of tumor promoting phorbol diesters on epidermal growth factor (EGF) binding and action in intact cells. DiC8 inhibited the binding of [3H]phorbol dibutyrate to A431 cell monolayers indicating that
sn-1, 2-Dioctanoylglycerol. A cell-permeable diacylglycerol that mimics phorbol diester action on the epidermal growth factor receptor and mitogenesis.
Davis RJ, et al.
The Journal of biological chemistry, 260(3), 1562-1566 (1985)
E G Lapetina et al.
The Journal of biological chemistry, 260(3), 1358-1361 (1985-02-10)
The ability of exogenous sn-1,2-diacylglycerols and analogs to function as bioregulators of protein kinase C in human platelets was investigated. The activation of protein kinase C in platelets is indicated by specific phosphorylation of a 40,000-dalton protein. Dihexanoylglycerol, dioctanoylglycerol (diC8)
Specificity and Mechanism of Protein Kinase C Activation by sn-1,2-diacylglycerols.
Ganong BR, et al.
Proceedings of the National Academy of Sciences of the USA, 83, 1184-1188 (1986)
S P Soltoff
The Journal of biological chemistry, 276(41), 37986-37992 (2001-08-11)
Protein kinase Cdelta (PKCdelta) is activated by stimuli that increase its tyrosine phosphorylation, including neurotransmitters that initiate fluid secretion in salivary gland (parotid) epithelial cells. Rottlerin, a compound reported to be a PKCdelta-selective inhibitor, rapidly increased the rate of oxygen
Rottlerin is a mitochondrial uncoupler that decreases cellular ATP
Soltoff SP
Test, 276(41), 37986-37992 (1986)
Protein Kinase Calpha (PKCalpha) Is Resistant to Long Term Desensitization/Down-regulation by Prolonged Diacylglycerol Stimulation
Lum MA, et al.
The Journal of biological chemistry, 291(12), 6331-6346 (2016)
Vineet Choudhary et al.
The Journal of cell biology, 219(7) (2020-04-30)
Lipid droplets (LDs) are fat storage organelles that originate from the endoplasmic reticulum (ER). Relatively little is known about how sites of LD formation are selected and which proteins/lipids are necessary for the process. Here, we show that LDs induced
B R Ganong et al.
Proceedings of the National Academy of Sciences of the United States of America, 83(5), 1184-1188 (1986-03-01)
The specificity of protein kinase C activation by sn-1,2-diacylglycerols and analogues was investigated by using a Triton X-100 mixed micellar assay [Hannun, Y. A., Loomis, C. R. & Bell, R. M. (1985) J. Biol. Chem. 260, 10039-10043]. Analogues containing acyl
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