2005
DOI: 10.1016/j.bbrc.2005.09.089
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N-Glycosylation of secretion enhancer peptide as influencing factor for the secretion of target proteins from Saccharomyces cerevisiae

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Cited by 6 publications
(5 citation statements)
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“…N ‐glycosylation of the propeptide derived from hIL‐1β, which occurs at a specific “Asn” site, has been found to play an important role in the secretion of heterologous proteins (K. S. Han et al, 2005 ; M. Han et al, 2014 ). N ‐glycosylation plays a significant role in the secretion of hG‐CSF (K. S. Han et al, 2005 ), presumably because of the enhanced folding of rhG‐CSF in the ER (Doyon et al, 2002 ; Sagt et al, 2000 ), and is subsequently involved in the transition of rhG‐CSF from the ER to the Golgi apparatus (Ari et al, 2001 ).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…N ‐glycosylation of the propeptide derived from hIL‐1β, which occurs at a specific “Asn” site, has been found to play an important role in the secretion of heterologous proteins (K. S. Han et al, 2005 ; M. Han et al, 2014 ). N ‐glycosylation plays a significant role in the secretion of hG‐CSF (K. S. Han et al, 2005 ), presumably because of the enhanced folding of rhG‐CSF in the ER (Doyon et al, 2002 ; Sagt et al, 2000 ), and is subsequently involved in the transition of rhG‐CSF from the ER to the Golgi apparatus (Ari et al, 2001 ).…”
Section: Resultsmentioning
confidence: 99%
“…Finally, the % increased efficiency of rhG-CSF secretion was estimated as the ratio of the concentration of mature rhG-CSF from the best pro-peptide sample in each stage to the concentration of mature rhG-CSF from the original pro-peptide. of hG-CSF (K. S. Han et al, 2005), presumably because of the enhanced folding of rhG-CSF in the ER (Doyon et al, 2002;Sagt et al, 2000), and is subsequently involved in the transition of rhG-CSF from the ER to the Golgi apparatus (Ari et al, 2001).…”
Section: Design Of Secretion Enhancing Peptide Cassette For Heterolog...mentioning
confidence: 99%
“…Many IL1 family members lack classical signal sequences necessary for secretion via the ER-Golgi complex pathway. These cytokines are released by autophagy, necrotic cells, or poorly defined nonclassical secretion pathways (34). No changes in the expression of the autophagy markers LC3-I, LC3-II, and p62 were observed after treatment with bleomycin (data not shown).…”
Section: Discussionmentioning
confidence: 98%
“…To enhance the quality and quantity of yeast-based VLPs, various factors, such as the type of plasmid and promoter and, especially the secretability and processing on exit out of the yeast cells, need to be carefully taken into account (Bae et al, 1998;Lee et al, 1999;Han et al, 2005). The baculovirus-insect cell and mammalian-cell systems have an advantage of eliciting more complete post-translational modification including glycosylation and expressing multiple component VLPs (Rodriguez-Limas et al, 2011).…”
Section: Expression Platforms For Vlpsmentioning
confidence: 99%