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Rosen, O M
author Stadtmauer, L
Rosen, O M
spellingShingle Stadtmauer, L
Rosen, O M
Journal of Biological Chemistry
Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.
Cell Biology
Molecular Biology
Biochemistry
author_sort stadtmauer, l
spelling Stadtmauer, L Rosen, O M 0021-9258 Elsevier BV Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1016/s0021-9258(18)67614-8 Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo. Journal of Biological Chemistry
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series Journal of Biological Chemistry
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title Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.
title_unstemmed Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.
title_full Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.
title_fullStr Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.
title_full_unstemmed Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.
title_short Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.
title_sort phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing tyr-1150 is phosphorylated in vivo.
topic Cell Biology
Molecular Biology
Biochemistry
url http://dx.doi.org/10.1016/s0021-9258(18)67614-8
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imprint Elsevier BV, 1986
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spelling Stadtmauer, L Rosen, O M 0021-9258 Elsevier BV Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1016/s0021-9258(18)67614-8 Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo. Journal of Biological Chemistry
spellingShingle Stadtmauer, L, Rosen, O M, Journal of Biological Chemistry, Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo., Cell Biology, Molecular Biology, Biochemistry
title Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.
title_full Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.
title_fullStr Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.
title_full_unstemmed Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.
title_short Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.
title_sort phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing tyr-1150 is phosphorylated in vivo.
title_unstemmed Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.
topic Cell Biology, Molecular Biology, Biochemistry
url http://dx.doi.org/10.1016/s0021-9258(18)67614-8