Zobrazeno 1 - 7
of 7
pro vyhledávání: '"R C Hresko"'
Publikováno v:
Journal of Biological Chemistry. 265:21075-21085
It was established previously that the 15-kDa protein phosphorylated in 3T3-L1 adipocytes treated with insulin and phenylarsine oxide is O-phospho-Tyr19 422(aP2) protein, a fatty acid-binding protein. To assess its capacity to serve as substrate of t
Autor:
R D Hoffman, K H Kaestner, K Liao, R C Hresko, J R Flores-Riveros, T Kastelic, J C McLenithan, Robert J. Christy, M Janicot, M D Lane
Publikováno v:
Diabetes Care. 13:565-575
We identified the earliest events in autophosphorylation of the insulin receptor after insulin addition. Insulinstimulated autophosphorylation at specific sites in the tyrosine kinase domain of the receptor's β-subunit is correlated kinetically with
Publikováno v:
The Journal of biological chemistry. 269(51)
The rate of movement of the glucose transporter isoforms Glut1 and Glut4 from the endoplasmic reticulum (ER) to the Golgi apparatus was investigated by pulse labeling and monitoring endoglycosidase H resistance in mRNA-injected Xenopus oocytes and in
Publikováno v:
The Journal of biological chemistry. 269(32)
The erythrocyte glucose transporter (Glut 1) is predicted to contain 12 membrane-spanning domains based on the hydropathy plot of its deduced amino acid sequence. The membrane topology of Glut 1 was analyzed by a scanning mutagenesis procedure in whi
Publikováno v:
The Journal of biological chemistry. 268(35)
The Glut4 glucose transporter is poorly functional compared with other glucose transporter isoforms when expressed in Xenopus oocytes. To investigate the molecular basis for this poor functionality, we compared the biosynthesis and targeting of Glut1
Publikováno v:
The Journal of biological chemistry. 265(34)
It was established previously that the 15-kDa protein phosphorylated in 3T3-L1 adipocytes treated with insulin and phenylarsine oxide is O-phospho-Tyr19 422(aP2) protein, a fatty acid-binding protein. To assess its capacity to serve as substrate of t
Publikováno v:
Scopus-Elsevier
[32P]pp15, the [32P]phosphorylated form of a specific cytosolic substrate of the insulin receptor tyrosine kinase, was purified to homogeneity from mouse 3T3-L1 adipocytes incubated with 32Pi. Evidence presented here and previously indicates that pp1