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Biochemical and Biophysical Research Communications|June 27, 1998
pp120, a substrate of the insulin receptor tyrosine kinase, is associated with phosphatase activityS M Najjar
The American Journal of Physiology|November 14, 1997
Differential effect of pp120 on insulin endocytosis by two variant insulin receptor isoformsS Li Calzi, C V Choice, S M Najjar
The American Journal of Physiology|February 1, 1991
Sucrase-alpha-dextrinase in diabetic BioBreed rats: reversible alteration of subunit structureS M Najjar, L T Hampp, R Rabkin, et al.
Metabolism: Clinical and Experimental|January 1, 1992
Altered intestinal and renal brush border amino-oligopeptidase structure in diabetes and metabolic acidosis: normal and biobreed (BB) ratsS M Najjar, L T Hampp, R Rabkin, et al.
American Journal of Physiology. Gastrointestinal and Liver Physiology|December 21, 2000
Intestinal aminooligopeptidase in diabetic BioBreed rat: altered posttranslational processing and traffickingS M Najjar, J P Broyart, L T Hampp, et al.
Molecular Cell Biology Research Communications : MCBRC|November 30, 1999
Cell adhesion properties and effects on receptor-mediated insulin endocytosis are independent properties of pp120, a substrate of the insulin receptor tyrosine kinaseP Soni, K A Al-Hosaini, M A Fernström, et al.
Journal of Cellular Biochemistry|March 10, 2001
Sucrase-alpha-dextrinase in the spontaneously diabetic BioBreed Wistar rat: altered intracellular carbohydrate processingS M Najjar, J P Broyart, L T Hampp, et al.
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