Results 111 to 120 of about 362 (144)

Down's-syndrome-related kinase Dyrk1A modulates the p120-catenin-Kaiso trajectory of the Wnt signaling pathway.

J Cell Sci, 2012
Hong JY, Park JI, Lee M, Muñoz WA, Miller RK, Ji H, Gu D, Ezan J, Sokol SY, McCrea PD.   +9 more
europepmc   +1 more source

Die Proteine pp100 und pp120 als Substrate von Proteinkinasen der Zelloberfläche: Homologe der Kernproteine Nukleolin und hnRNP U

, 1998
Zipperle, Jacqueline
core  

Differential effect of pp120 on insulin endocytosis by two variant insulin receptor isoforms

American Journal of Physiology - Endocrinology and Metabolism, 1997
The insulin receptor is expressed as two variably spliced isoforms that differ by the absence (isoform A) or presence (isoform B) of a 12-amino acid sequence encoded by exon 11 at the carboxy terminus of the α-subunit. Coexpression of the A isoform and pp120, a substrate of the insulin receptor tyrosine kinase, in NIH 3T3 fibroblasts increased receptor
Sérgio Li Calzi, Sonia M Najjar
exaly   +4 more sources

PP120/C-CAM

, 1997
ppl20/C-CAM, a liver plasma membrane glycoprotein, is a substrate of the insulin receptor tyrosine kinase in cell-free and intact cell systems.1, 2, 3 The cDNA encoding the rat protein was originally cloned by Lin and Guidotti4 as a Ca2+/Mg2+ ecto-ATPase. Analysis of the deduced amino acid sequence revealed that the protein is of 519 amino acids (a.a.)
Sonia M Najjar
exaly   +3 more sources

Molecular Cloning of pp120/ ECTO-ATPase, An Endogenous Substrate of the Insulin Receptor Kinase

Advances in Experimental Medicine and Biology, 1994
In recent years, a great deal of attention has been devoted to dissecting intracellular pathways of insulin action following activation of the insulin receptor kinase (1). Several laboratories have reported the identification of protein substrates of the insulin receptor tyrosine kinase (2).
Sonia M Najjar, Simeon I Taylor, D Accili   +2 more
exaly   +4 more sources

Is the Rat Liver Ecto-ATPase Identical to C-CAM/PP120, a Cell Adhesion Molecule?

, 1997
The publication of a report on the molecular cloning of the rat liver ecto-ATPase1 in 1989 was considered a major break-through in ecto-ATPase research, especially since no other ecto-ATPase had been purified at that time. The extensive homology of the cDNA sequence of the rat liver ecto-ATPase with human biliary glycoprotein I (BGPI) also gave hope ...
Aileen F Knowles
exaly   +3 more sources

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pp120, a Substrate of the Insulin Receptor Tyrosine Kinase, Is Associated with Phosphatase Activity

Biochemical and Biophysical Research Communications, 1998
pp120, a plasma membrane glycoprotein, is phosphorylated on Tyr488 by the insulin receptor tyrosine kinase. This requires basal phosphorylation on Ser503 by cAMP-dependent serine kinase. Phe513, the other tyrosine residue in the intracellular domain, does not undergo insulin-stimulated phosphorylation.
Sonia M Najjar
exaly   +3 more sources

PP120. Hydatidiform mole as a cause of eclampsia in the first trimester: A case report

Pregnancy Hypertension: An International Journal of Women's Cardiovascular Health, 2012
The occurrence of preeclampsia before the 20th week of gestation is rare and it has been associated with hydatidiform molar pregnancy.We describe a case of first trimester eclampsia which occurred in a patient with hydatidiform mole.Case report.A 16-year-old woman came to emergency service for abdominal pain and vaginal bleeding. She had been suffering
Ottanelli S, Simeone S, Serena C, Rambaldi MP, Villanucci A, Tavella K, Amunni G, Mecacci F, Mello G   +8 more
openaire   +3 more sources

PP120 Health Technology Assessment Framework To Capture The Full Value Of Value Added Medicines

International Journal of Technology Assessment in Health Care, 2017
INTRODUCTION:Value added medicines (VAM) are medicines based on known molecules that address healthcare needs and deliver relevant improvements for patients, healthcare professionals and/or payers through drug repositioning, drug reformulation or drug combination (1-3).
Mondher Toumi, Cecile Remuzat, Adam Plich   +2 more
openaire   +2 more sources

Comparison of the intracellular trafficking of two alternatively spliced isoforms of pp120, a substrate of the insulin receptor tyrosine kinase

Journal of Cellular Biochemistry, 2000
pp120, a substrate of the insulin receptor tyrosine kinase, is a plasma membrane glycoprotein in the hepatocyte. It is expressed as two spliced isoforms differing by the presence (full length) or absence (truncated) of most of the intracellular domain including all phosphorylation sites.
Matthew N Poy, Pietro Formisano, Sonia M Najjar   +2 more
exaly   +3 more sources