The metabolic turnover of the major proteins of the postsynaptic density

1986 ◽  
Vol 1 (3) ◽  
pp. 221-230 ◽  
Author(s):  
G.L. Sedman ◽  
P.L. Jeffrey ◽  
L. Austin ◽  
J.A.P. Rostas
Keyword(s):  
Postsynaptic Density ◽  
Metabolic Turnover

scholarly journals Metabolic Turnover Studies on the Two Major Forms of Rat and Rabbit Plasminogen

1974 ◽  
Vol 249 (5) ◽  
pp. 1434-1438
Author(s):  
Gerald E. Siefring ◽  
Francis J. Castellino
Keyword(s):  
Metabolic Turnover

scholarly journals Studies on the Metabolic Turnover of Muscle Proteins. Part I

1965 ◽  
Vol 39 (3) ◽  
pp. 109-113
Author(s):  
Ryuhei FUNABIKI ◽  
Makoto KANDATSU
Keyword(s):  
Muscle Proteins ◽  
Metabolic Turnover

scholarly journals Differential Control of Postsynaptic Density Scaffolds via Actin-Dependent and -Independent Mechanisms

2006 ◽  
Vol 26 (29) ◽  
pp. 7693-7706 ◽  
Author(s):  
T. Kuriu ◽  
A. Inoue ◽  
H. Bito ◽  
K. Sobue ◽  
S. Okabe
Keyword(s):  
Postsynaptic Density ◽  
Differential Control

scholarly journals Mass of the postsynaptic density and enumeration of three key molecules

2005 ◽  
Vol 102 (32) ◽  
pp. 11551-11556 ◽  
Author(s):  
X. Chen ◽  
L. Vinade ◽  
R. D. Leapman ◽  
J. D. Petersen ◽  
T. Nakagawa ◽  
...  
Keyword(s):  
Postsynaptic Density

Selective localization of amyloid precursor-like protein 1 in the cerebral cortex postsynaptic density

1995 ◽  
Vol 32 (1) ◽  
pp. 36-44 ◽  
Author(s):  
Tae-Wan Kim ◽  
Kuo Wu ◽  
Jia-Ling Xu ◽  
Geoff McAuliffe ◽  
Rudolph E. Tanzi ◽  
...  
Keyword(s):  
Cerebral Cortex ◽  
Postsynaptic Density ◽  
Selective Localization

scholarly journals Metabolic turnover of human c-rasH p21 protein of EJ bladder carcinoma and its normal cellular and viral homologs.

1984 ◽  
Vol 4 (8) ◽  
pp. 1647-1652 ◽  
Author(s):  
L S Ulsh ◽  
T Y Shih
Keyword(s):  
Bladder Carcinoma ◽  
Half Life ◽  
P21 Protein ◽  
Metabolic Turnover ◽  
Ras Genes ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Processed Products ◽  
Murine Sarcoma ◽  
P21 Proteins

The EJ bladder carcinoma oncogene is activated by a point mutation in the c-rasH proto-oncogene at the 12th amino acid codon. In an attempt to understand the mechanism of oncogenic activation, a comparative study was undertaken to examine the metabolic turnover and subcellular localization of the p21 protein encoded by the EJ oncogene, the viral oncogene, and its normal cellular homolog. Pulse-labeling experiments indicated that both c-ras p21 proteins were synthesized by a very similar pathway, as was observed for the viral p21 protein of Harvey murine sarcoma virus. The pro-p21 proteins were detected in free cytosol, and the processed products were associated with plasma membrane. The intracellular half-life of p21 proteins was determined by pulse-labeling and chasing in the presence of excess unlabeled methionine. Although both p21 proteins of EJ and the normal c-ras genes which are not phosphorylated have a half-life of 20 h, the viral p21 protein of Harvey murine sarcoma virus which includes a phosphorylated form is much more stable in cells, having a half-life of 42 h, apparently due to phosphorylation.

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