Nuclear Protein Kinases

2018 ◽  
pp. 131-171
Author(s):  
Samuel J. Mitchell* ◽  
Lewis J. Kleinsmith
Life Sciences ◽  
1976 ◽  
Vol 19 (1) ◽  
pp. 85-90 ◽  
Author(s):  
James Hirsch ◽  
Orlando J. Martelo

1981 ◽  
Vol 14 (4) ◽  
pp. 260-276 ◽  
Author(s):  
Doriano Fabbro ◽  
Richard A. Jungmann ◽  
Urs Eppenberger

2018 ◽  
pp. 131-171
Author(s):  
Samuel J. Mitchell ◽  
Lewis J. Kleinsmith

Author(s):  
Max Costa ◽  
David J.M. Fuller ◽  
Diane Haddock Russell ◽  
Eugene W. Gerner

1974 ◽  
Vol 249 (3) ◽  
pp. 750-760
Author(s):  
Valerie M. Kish ◽  
Lewis J. Kleinsmith

1984 ◽  
Vol 59 (1-2) ◽  
Author(s):  
HarryR. Matthews ◽  
VerenaD. Huebner

1985 ◽  
Vol 232 (3) ◽  
pp. 767-771 ◽  
Author(s):  
K Ahmed ◽  
S A Goueli ◽  
H G Williams-Ashman

The extent of direct stimulation by spermine of reactions catalysed by nuclear N1 and N2 protein kinases purified from liver and prostate depends critically on the nature of the protein substrate. The chemically inert Co(NH3)36+ ion exerts effects on protein kinase reactions similar to those of spermidine or spermine. This enhancement of the phosphorylation of various protein substrates by polyamines or Co(NH3)63+ by purified nuclear protein kinase preparations was studied in relation to effects of temperature, pH and other factors. The results provide further support for our hypothesis [Ahmed, Wilson, Goueli & Williams-Ashman (1978) Biochem. J. 176, 739-750] that the enhancement of certain protein kinase reactions by polycations relates primarily to their interaction with the protein substrate, yielding more favourable conformations for phosphorylation by the protein kinase, rather than a direct effect on its catalytic activity.


1991 ◽  
Vol 195 (1) ◽  
pp. 255-262 ◽  
Author(s):  
A.M. Martelli ◽  
C. Carini ◽  
S. Marmiroli ◽  
M. Mazzoni ◽  
P.J. Barker ◽  
...  

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