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Polyamines and heparin do not appreciably influence phosphorylation of chromatin proteins HMG 14 and HMG 17 by nuclear protein kinase II

Data up to Jan 2025

Published1984
Citations11
References29

Total Citations Per Year

Abstract

References (29)

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1978 • 57 citations

Phosphorylation of high mobility group 14 protein by cyclic nucleotide-dependent protein kinases.

1982 • 53 citations

Identity of the in vivo phosphorylation site in high mobility group 14 protein in HeLa cells with the site phosphorylated by casein kinase II in vitro.

1983 • 50 citations

Reversal of heparin inhibition of nuclear protein kinase NII by polyamines and histones

1981 • 44 citations

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1982 • 42 citations

Phosphorylation of HMG 17 by protein kinase NII from rat liver cell nuclei

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Polyamines alter the substrate preference of nuclear protein kinase NII

1982 • 35 citations

Effects of polyamines and histone on the phosphorylation of non-histone proteins in isolated rat liver nuclei

1978 • 32 citations

Heparin inhibition and polyamine stimulation of a glycogen synthase kinase (PC0.7) from rabbit skeletal muscle

1982 • 28 citations

Occurrence of NI and NII type protein kinases in the nuclei from various tissues of the rat

1982 • 25 citations

Polyamines alter the phosphorylation pattern of chromatin proteins by endogenous protein kinases

1982 • 19 citations

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1981 • 16 citations

Differential phosphorylation of high mobility group protein HMG 14 from calf thymus and avian erythrocytes by a cyclic GMP-dependent protein kinase

1983 • 16 citations

Phosphorylation of high mobility group proteins 14 and 17 by nuclear protein kinase NII in rat C6 glioma cells

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1981 • 10 citations

Stimulatory Effect of Histones on Phosphorylation of Nuclear Phosphoproteins

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Polyamines and heparin do not appreciably influence phosphorylation of chromatin proteins… (1984) – Biochimica et Biophysica Acta (BBA) - General Subjects | Metascience Observatory Explorer