Leonard R. Johnson
Affiliations: | University of Tennessee Health Science Center, Memphis, TN, United States |
Area:
Cell BiologyGoogle:
"Leonard Johnson"
BETA: Related publications
See more...
Publications
|
You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect. |
| Tigyi GJ, Johnson LR, Lee SC, et al. (2019) Lysophosphatidic acid type 2 receptor agonists in targeted drug development offer broad therapeutic potential. Journal of Lipid Research |
| Thompson KE, Ray RM, Alli S, et al. (2018) Prevention and treatment of secretory diarrhea by the lysophosphatidic acid analog Rx100. Experimental Biology and Medicine (Maywood, N.J.). 1535370218803349 |
| Ray RM, Bavaria M, Johnson LR. (2015) Interaction of polyamines and mTOR signaling in the synthesis of antizyme (AZ). Cellular Signalling |
| Ray RM, Bhattacharya S, Bavaria MN, et al. (2014) Antizyme (AZ) regulates intestinal cell growth independent of polyamines. Amino Acids. 46: 2231-9 |
| Ray RM, Bhattacharya S, Bavaria MN, et al. (2014) Spermidine, a sensor for antizyme 1 expression regulates intracellular polyamine homeostasis. Amino Acids. 46: 2005-13 |
| Bavaria MN, Jin S, Ray RM, et al. (2014) The mechanism by which MEK/ERK regulates JNK and p38 activity in polyamine depleted IEC-6 cells during apoptosis. Apoptosis : An International Journal On Programmed Cell Death. 19: 467-79 |
| Bhattacharya S, Ray RM, Johnson LR. (2014) Cyclin-dependent kinases regulate apoptosis of intestinal epithelial cells. Apoptosis : An International Journal On Programmed Cell Death. 19: 451-66 |
| Ray RM, Johnson LR. (2014) Regulation of intestinal mucosal growth by amino acids. Amino Acids. 46: 565-73 |
| Ray RM, Li C, Bhattacharya S, et al. (2012) Spermine, a molecular switch regulating EGFR, integrin β3, Src, and FAK scaffolding. Cellular Signalling. 24: 931-42 |
| Ray RM, Viar MJ, Johnson LR. (2012) Amino acids regulate expression of antizyme-1 to modulate ornithine decarboxylase activity. The Journal of Biological Chemistry. 287: 3674-90 |