Zobrazeno 1 - 10
of 87
pro vyhledávání: '"Z, Damuni"'
Publikováno v:
The Biochemical journal. 341
Transient expression of I2PP2A, a potent inhibitor of protein phosphatase 2A (PP2A), in HEK-293 cells increased the concentration and DNA binding of the proto-oncogene c-Jun. In contrast, expression of the catalytic subunit of PP2A (PP2AC) markedly d
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 93
Publikováno v:
The Journal of biological chemistry. 268(20)
Two myelin basic protein kinases designated MBPK-1 and MBPK-2 were purified to apparent homogeneity from extracts of bovine kidney cortex. The purified preparations exhibited an apparent M(r) approximately 40,000 by sodium dodecyl sulfate-polyacrylam
Publikováno v:
Journal of Biological Chemistry. 262:5129-5132
The catalytic subunit of the branched-chain alpha-keto acid dehydrogenase (BCKDH) phosphatase (Damuni, Z., Merryfield, M.L., Humphreys, J.S., and Reed, L.J., (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 4335-4338) has been purified over 50,000-fold from
Publikováno v:
Journal of Biological Chemistry. 262:5133-5138
A divalent cation-independent and spermine-stimulated phosphatase (protein phosphatase SP) that is active toward the phosphorylated pyruvate dehydrogenase complex has been purified about 15,000-fold to near homogeneity from extracts of bovine kidney
Publikováno v:
Journal of Biological Chemistry. 264:6412-6416
A protamine kinase has been purified to apparent homogeneity from extracts of the cytosol of bovine kidney cortex. This protamine kinase exhibited an apparent Mr = 43,000 as estimated by gel permeation chromatography on Sephacryl S-200 and an apparen
Publikováno v:
The Journal of biological chemistry. 262(11)
A divalent cation-independent and spermine-stimulated phosphatase (protein phosphatase SP) that is active toward the phosphorylated pyruvate dehydrogenase complex has been purified about 15,000-fold to near homogeneity from extracts of bovine kidney
Autor:
Peter J. Parker, Alastair Aitken, Nicholas K. Tonks, Therese J. Resink, Colin Picton, Thomas S. Ingebritsen, Z. Damuni, Brian A. Hemmings, James R. Woodgett, Philip Cohen, Alexander A. Stewart
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d6849a8b3fec35a3c93f605183043b32
https://doi.org/10.1016/b978-0-12-387560-0.50010-4
https://doi.org/10.1016/b978-0-12-387560-0.50010-4
Publikováno v:
Methods in enzymology. 166
Publikováno v:
The Journal of biological chemistry. 262(11)
The catalytic subunit of the branched-chain alpha-keto acid dehydrogenase (BCKDH) phosphatase (Damuni, Z., Merryfield, M.L., Humphreys, J.S., and Reed, L.J., (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 4335-4338) has been purified over 50,000-fold from