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alpha mannosidase/сарком
Линкът е запазен в клипборда
6 резултата
Both acidic-type and neutral-type asparaginyl-oligosaccharides of host-cell glycoproteins are altered in Rous-sarcoma-virus-transformed chick-embryo fibroblasts.
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Вход / Регистрация
In comparisons of [3H]mannose-labelled glycopeptides from chick-embryo fibroblasts infected and transformed with non-defective Prague C Rous-sarcoma virus and from untransformed fibroblasts infected with a transformation-defective derivative of Prague C Rous-sarcoma virus, we have detected
Glycosidases in normal and regenerating chicken liver, hepatoma Mc-29, Rous sarcoma, in turkey poult liver and hemocytoblastomes, provoked by the leukosis virus strain Mc-31.
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Four glycosidases (beta-galactosidase, alpha-mannosidase, alpha-fucosidase and beta-N-acetylglucosaminidase) were studied in chicken normal and regenerating liver, in turkey poult liver and in virus induced avian tumors--chicken hepatoma (strain Mc-29), Rous sarcoma (strain Schmidt-Ruppin) and
Appropriate glycosylation of the fms gene product is a prerequisite for its transforming potency.
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Processing inhibitors of N-linked glycans were used to determine whether correct glycosylation of the oncogene product gp140v-fms, encoded by the McDonough strain of feline sarcoma virus (SM-FeSV), is required to maintain the oncogenic properties of v-fms. SM-FeSV-transformed cells treated with the
hMan2c1 transgene promotes tumor progress in mice.
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In order to study the biological significance of alpha-mannosidase Man2c1, hMan2c1 transgenic mice were developed. In 113 F0 mice, eight were found to be genomic PCR positive for hMan2c1; 9/20 (45%) F1 mice, 16/21 (76.2%) F2 mice, and 12/14 (85.7%) F3 mice were genomic PCR positive for hMan2c1.
Regulation of glycosylation. The influence of protein structure on N-linked oligosaccharide processing.
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The Sindbis virus glycoproteins, E1 and E2, comprise a useful model system for evaluating the effects of local protein structure on the processing of N-linked oligosaccharides by Golgi enzymes. The conversion of oligomannose to N-acetyllactosamine (complex) oligosaccharides is hindered to different
Transformation by the v-fms oncogene product: role of glycosylational processing and cell surface expression.
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The effect of glycosylational-processing inhibitors on the synthesis, cell surface expression, endocytosis, and transforming function of the v-fms oncogene protein (gp140fms) was examined in McDonough feline sarcoma virus-transformed Fischer rat embryo (SM-FRE) cells. Swainsonine (SW), a mannosidase
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