2005
DOI: 10.1016/j.molbiopara.2005.04.008
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High-level expression of the Toxoplasma gondii STT3 gene is required for suppression of the yeast STT3 gene mutation

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Cited by 13 publications
(14 citation statements)
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“…The pooled chloroform phases (1.5 ml) were then washed eight times with ultrapure water. The methylated derivative-containing chloroform phase was finally dried under a stream of nitrogen, and the extracted products were further purified on a Sep-Pak C 18 . The Sep-Pack C 18 was sequentially conditioned with methanol (5 ml) and water (2 ϫ 5 ml).…”
Section: Methodsmentioning
confidence: 99%
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“…The pooled chloroform phases (1.5 ml) were then washed eight times with ultrapure water. The methylated derivative-containing chloroform phase was finally dried under a stream of nitrogen, and the extracted products were further purified on a Sep-Pak C 18 . The Sep-Pack C 18 was sequentially conditioned with methanol (5 ml) and water (2 ϫ 5 ml).…”
Section: Methodsmentioning
confidence: 99%
“…Reduced and carboxamidomethylated Toxoplasma products were first digested with trypsin, and glycans were released from the resulting peptide/glycopeptide mixture by digestion with PNGase F. This enzyme is capable of releasing all known N-linked oligosaccharides except those with fucose attached to the 3-position of the Asn-linked GlcNAc residue. Such PNGase F-resistant oligosaccharides have been found to be sensitive to PNGase A. PNGase F-released glycans were separated from peptides and were analyzed by MALDI-TOF-MS after permethylation and purification on a Sep-Pak C 18 (Fig. 1).…”
Section: Maldi-tof-ms Of N-glycans Released From Detergent Extracts-mentioning
confidence: 99%
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“…Although the molecular basis for the complementation of stt3 mutation by the expression of the T. gondii STT3 protein was not analyzed in detail (Shams-Eldin et al, 2005), Castro et al (2006) showed that the T. cruzi STT3 protein most likely replaced the yeast Stt3p in the complex. Our analysis revealed that such integration into the complex was not observed for the LmSTT3 proteins when expressed in yeast.…”
Section: Lmstt3d Acts Independently Of Endogenous Otase Subunits In Ymentioning
confidence: 99%