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131.
An unusual case of necrotic infection of the tongue and unilateral necrotic maxillar sinusitis, in a cow is reported. The prominent clinical findings were: a marked salivation, unilateral mucopurulent nasal discharge, diffuse necrotic lesions on the ventral side of the tongue and fetid breath. Clinico-pathological and pathological findings and abnormalities in the haemogram were probably caused by the toxins produced by the causative organism--Fusobacterium necrophorum like microorganism. 相似文献
132.
R Haklai MG Weisz G Elad A Paz D Marciano Y Egozi G Ben-Baruch Y Kloog 《Canadian Metallurgical Quarterly》1998,37(5):1306-1314
Membrane anchorage of Ras oncoproteins, required for transforming activity, depends on their carboxy-terminal farnesylcysteine. We previously showed that S-trans,trans-farnesylthiosalicylic acid (FTS), a synthetic farnesylcysteine mimetic, inhibits growth of ErbB2- and Ras-transformed cells, but not of v-Raf-transformed cells, suggesting that FTS interferes specifically with Ras functions. Here we demonstrate that FTS dislodges Ras from membranes of H-Ras-transformed (EJ) cells, facilitating its degradation and decreasing total cellular Ras. The dislodged Ras that was transiently present in the cytosol was degraded relatively rapidly, causing a decrease of up to 80% in total cellular Ras. The half-life of Ras was 10 +/- 4 h in FTS-treated EJ cells and 27 +/- 4 h in controls. The dislodgment of membrane Ras and decrease in total cellular Ras were dose-dependent: 50% of the effects occurred at 10-15 microM, comparable to concentrations (7-10 microM) required for 50% growth inhibition in EJ cells. Higher concentrations of FTS (25-50 microM) were required to dislodge Ras from Rat-1 cell membranes expressing normal Ras, suggesting some selectivity of FTS toward oncogenic Ras. Membrane localization of the prenylated G beta gamma of heterotrimeric G proteins was not affected by FTS in EJ cells. An FTS-related compound, N-acetyl-S-farnesyl-L-cysteine, which does not inhibit EJ cell growth, did not affect Ras. FTS did not inhibit growth of Rat-1 cells transformed by N-myristylated H-Ras and did not reduce the total amount of this Ras isoform. The results suggest that FTS affects docking of Ras in the cell membrane in a rather specific manner, rendering the protein susceptible to proteolytic degradation. 相似文献
133.
134.
Energy Storage: Oriented Multiwalled Organic–Co(OH)2 Nanotubes for Energy Storage (Adv. Funct. Mater. 3/2018)
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