Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Janice L. Countaway"'
Autor:
Harriet L. Robinson, Janice L. Countaway, Nandini Nair, Roger J. Davis, Steven J. Theroux, C Taglienti-Sian
Publikováno v:
Journal of Biological Chemistry. 267:7967-7970
The erbB oncogene encodes an altered form of the epidermal growth factor (EGF) receptor that lacks the extracellular ligand binding domain. This oncogene is exclusively leukemogenic. However, an increase in oncogenic potential and a broadening of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::31c9f5629bd61d79f61c38ad422deaf9
https://doi.org/10.1016/s0021-9258(18)42392-7
https://doi.org/10.1016/s0021-9258(18)42392-7
Publikováno v:
Journal of Biological Chemistry. 267:1129-1140
The intrinsic protein-tyrosine kinase activity of the epidermal growth factor (EGF) receptor is required for signal transduction. Increased protein-tyrosine kinase activity is observed following the binding of EGF to the receptor. However, signaling
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e37c6617eadd54f2235c7214e060455
https://doi.org/10.1016/s0021-9258(18)48406-2
https://doi.org/10.1016/s0021-9258(18)48406-2
Publikováno v:
Journal of Biological Chemistry. 265:3407-3416
The major sites of serine and threonine phosphorylation of the human epidermal growth factor (EGF) receptor observed in intact cells are Thr654, Thr669, Ser1046, and Ser1047. Phosphorylation of the EGF receptor is increased at these sites in cells tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd7e782b9bd47b603d080720b34cc03a
https://doi.org/10.1016/s0021-9258(19)39782-0
https://doi.org/10.1016/s0021-9258(19)39782-0
Publikováno v:
Journal of Biological Chemistry. 264:10828-10835
The major site of phosphorylation of the epidermal growth factor (EGF) receptor after treatment of cells with EGF is threonine 669. Phosphorylation of this site is also associated with the transmodulation of the EGF receptor caused by platelet-derive
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0994f08aafed76b6e315fbf07ca3d0be
https://doi.org/10.1016/s0021-9258(18)81695-7
https://doi.org/10.1016/s0021-9258(18)81695-7
Publikováno v:
Journal of Biological Chemistry. 264:13642-13647
Platelet-derived growth factor (PDGF) causes an acute decrease in the high affinity binding of epidermal growth factor (EGF) to cell surface receptors and an increase in the phosphorylation state of the EGF receptor at threonine654. The hypothesis th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f582656017a1f9341a58f0b085a8458c
https://doi.org/10.1016/s0021-9258(18)80045-x
https://doi.org/10.1016/s0021-9258(18)80045-x
Publikováno v:
FEBS Letters. (1):153-156
The glucose-6-phosphatase enzyme protein of the human hepatic microsomal glucose-6-phosphatase system was identified as a 36.5 kDa polypeptide. The 36.5 kDa glucose-6-phosphatase enzyme protein was shown to be absent in the microsomes isolated from a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3673c406a3db57cd9477ad5c300984d