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4 documents found
1: Title: Regulated ADAM17-dependent EGF family ligand release by substrate-selecting signaling pathways.
Authors: Dang, Michelle, .
Journal: Proceedings of the National Academy of Sciences of the United States of America (Proc Natl Acad Sci U S A), Vol. 110 (24): 9776-81, 2013 .
Snippet: Rather, inducers activate a signaling pathway using PKC-α and the PKC-regulated protein phosphatase 1 inhibitor 14D that is required for ADAM17 cleavage of TGF-α, heparin-binding EGF, and amphiregulin.
Affiliation: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA. .
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2: Title: Characterization of the brain proteome of rats with diabetes mellitus through two-dimensional electrophoresis and mass spectrometry.
Authors: Karthik, D, .
Journal: Brain research (Brain Res), Vol. 1371, 2011 .
Snippet: The identified proteins were functionally classified into two groups: (i) metabolic signalling protein (PPP1R14D) and ii) vesicle transport signalling protein (RAB18).
Affiliation: Department of Biotechnology, PRIST University, Thanjavur, Tamil Nadu-613 403, India. .
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3: Title: Regulation of cellular protein phosphatase-1 (PP1) by phosphorylation of the CPI-17 family, C-kinase-activated PP1 inhibitors.
Journal: The Journal of biological chemistry (J Biol Chem), Vol. 284 (51): 35273-7, 2009 .
Snippet: Upon phosphorylation at Thr(38), the 17-kDa PP1 inhibitor protein, CPI-17, selectively inhibits a specific form of PP1, myosin light chain phosphatase, which transduces multiple kinase signals into the phosphorylation of myosin II and other proteins.
Affiliation: Department of Molecular Physiology and Biophysics and Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA. .
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4: Title: GBPI, a novel gastrointestinal- and brain-specific PP1-inhibitory protein, is activated by PKC and inactivated by PKA.
Authors: Liu, Qing-Rong, .
Journal: The Biochemical journal (Biochem J), Vol. 377 (Pt 1): 171-81, 2004 .
Snippet: GBPI contains a consensus PP1-binding motif at residues 21-25 and consensus sites for phosphorylation by enzymes, including PKC, PKA (protein kinase A or cAMP-dependent protein kinase) and casein kinase II.
Affiliation: Molecular Neurobiology Branch, National Institute on Drug Abuse-Intramural Research Program, NIH, Department of Health and Human Services, Box 5180, Baltimore, MD 21224, USA. .
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