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http://hub.abes.fr/acs/periodical/bichaw/1980/volume_19/issue_1/101021bi00542a010/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1987/volume_26/issue_8/101021bi00382a044/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1988/volume_27/issue_1/101021bi00401a071/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/2004/volume_43/issue_49/101021bi049221y/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/1990/volume_29/issue_15/101021bi00467a010/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_3/101021bi00003a029/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1992/volume_31/issue_42/101021bi00157a023/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/1991/volume_30/issue_31/101021bi00245a010/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1992/volume_31/issue_41/101021bi00156a012/authorship/2
http://hub.abes.fr/springer/periodical/125/1996/volume_39/issue_2/B9267F136D9D5090E053120B220A1D5D/authorship/2
http://hub.abes.fr/springer/periodical/125/1990/volume_33/issue_2/B9267F1368B65090E053120B220A1D5D/authorship/3
http://hub.abes.fr/springer/periodical/125/1992/volume_35/issue_2/B9267F1367C55090E053120B220A1D5D/authorship/2
http://hub.abes.fr/springer/periodical/12035/1996/volume_13/issue_2/B8DC8E3F124B2847E053120B220A5C1F/authorship/4
http://hub.abes.fr/springer/periodical/125/1996/volume_39/issue_5/B9267F136CD25090E053120B220A1D5D/authorship/12
http://hub.abes.fr/springer/periodical/592/1996/volume_33/issue_3/B8E9244026D53944E053120B220A7E9F/authorship/3
http://hub.abes.fr/springer/periodical/11010/1995/volume_153/issue_1_2/B8ED752B9D3B0BE4E053120B220A160B/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/1984/volume_23/issue_14/101021bi00309a028/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/1988/volume_27/issue_9/101021bi00409a015/authorship/3
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Subunit structure of the insulin receptor of the human lymphocyte
Phosphorylation and dephosphorylation of the insulin receptor: evidence against an intrinsic phosphatase activity
Separate domains of the insulin receptor contain sites of autophosphorylation and tyrosine kinase activity
Autophosphorylation within insulin receptor .beta.-subunits can occur as an intramolecular process
Insulin induces the phosphorylation of DNA-binding nuclear proteins including lamins in 3T3-F442A
Transcriptional and posttranscriptional regulation of tyrosine aminotransferase by insulin in rat hepatoma cells
Insulin Substrates 1 and 2 Are Corequired for Activation ofAtypical Protein Kinase C and Cbl-Dependent Phosphatidylinositol 3-Kinase duringInsulin Action in Immortalized Brown Adipocytes
The early intracellular signaling pathway for the insulin/insulin-like growth factor receptor family in the mammalian central nervous system
In vivo andin vitro studies of vanadate in human and rodent diabetes mellitus
Insulin differentially regulates protein phosphotyrosine phosphatase activity in rat hepatoma cells
A family of polypeptide substrates and inhibitors of insulin receptor kinase
Transmembrane Domain Inversion Blocks ER Release and Insulin Receptor Signaling
Insulin receptor/IRS-1/PI 3-kinase signaling system in corticosteroid-induced insulin resistance
Molecular scanning of the insulin receptor substrate-1 (IRS-1) gene in Japanese patients with NIDDM: identification of five novel polymorphisms
Effect of phospholipase treatment on insulin receptor signal transduction
Activation of liver and muscle insulin receptor tyrosine kinase activity during in vivo insulin administration in rats
Expression of the gene encoding glycogen phosphorylase is elevated in diabetic rat skeletal muscle and is regulated by insulin and cyclic AMP
Phosphorylation of insulin-like growth factor I receptor by the insulin receptor tyrosine kinase in intact cultured skeletal muscle cells
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