Zobrazeno 1 - 10
of 57
pro vyhledávání: '"Protein sialylation"'
Autor:
Kai Dang, Han-Jie Yu, Shen-Hui Xu, Tian-Ran Ma, Hui-Ping Wang, Yang Li, Zheng Li, Yun-Fang Gao
Publikováno v:
Frontiers in Physiology, Vol 11 (2020)
As the most common post-translational protein modification, glycosylation is intimately linked to muscle atrophy. This study aimed to investigate the performance of protein glycosylation in the soleus muscle (SOL) in Daurian ground squirrels (Spermop
Externí odkaz:
https://doaj.org/article/443e72a6322e4ae1864bc38fa6aa66b4
Autor:
Xiaohong Wang, Hanjie Yu, Kun Zhang, Wei Guo, Zhuo Chen, Li Ding, Fuying Yang, Xiangqin Chen, Guang Zhu, Xinle Fu, Wang Xilong, Xiurong Wang, Yimin Cheng, Zheng Li
Publikováno v:
International Journal of Biological Macromolecules. 184:339-348
Salivary glycoproteins are known as an important barrier to inhibit influenza infection by presenting sialic acid (Sia) ligands that can bind with viral hemagglutination. Here, to further understand why pregnant women are more vulnerable to avian inf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b4c2dceb76abbaa086fc854077cc433
https://doi.org/10.1016/j.ijbiomac.2021.06.006
https://doi.org/10.1016/j.ijbiomac.2021.06.006
The impact of sialylation linkage‐type on the pharmacokinetics of recombinant butyrylcholinesterases
Autor:
Younji Seo, Sandra Chough, Shuang Yang, Joseph P. Balthasar, Cheng-Yu Chung, Michael J. Betenbaugh, John F. Cipollo, Qiong Wang
Publikováno v:
Biotechnology and Bioengineering. 117:157-166
Chinese hamster ovary (CHO) cells typically produce glycoproteins with N-glycans terminating in α-2,3 sialylation. Human cells produce glycoproteins that include α-2,3 and α-2,6 sialic acids. To examine the impact of altering protein sialylation o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abc810aa11b488c94bdb69dea390d38e
https://doi.org/10.1002/bit.27174
https://doi.org/10.1002/bit.27174
Publikováno v:
Applied Microbiology and Biotechnology. 103:4753-4765
Sialylation affects circulating half-life, charge distribution, and other biochemical properties of therapeutic glycoproteins. Loss of protein sialylation during glycoprotein-producing bioprocesses could lead to a low final protein sialylation level
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e84259c3c7a061dc302f49a1e184c1ed
https://doi.org/10.1007/s00253-019-09850-8
https://doi.org/10.1007/s00253-019-09850-8
Publikováno v:
Applied Microbiology and Biotechnology. 101:7837-7851
Increasing recombinant protein production while ensuring a high and consistent protein quality remains a challenge in mammalian cell culture process development. In this work, we combined a nutrient substitution approach with a metabolic engineering
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::030df4a6e7e478ceff2728ab4abdbec7
https://doi.org/10.1007/s00253-017-8513-0
https://doi.org/10.1007/s00253-017-8513-0
Autor:
Seungpyo Hong, Zhen Zheng, Fengfei Ma, Min Ma, Lingjun Li, Gongyu Li, Ashita Nair, Ashley Phetsanthad, Qinying Yu, Kellen DeLaney
Protein sialylation has been closely linked to many diseases including Alzheimer’s disease (AD) and is broadly implicated in therapeutics in a terminal structure-sensitive manner. However, how sialylation structurally affects mature glycoproteins a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3adc8909a13aaa74917e7d6c2bbda96
https://doi.org/10.26434/chemrxiv.13379957
https://doi.org/10.26434/chemrxiv.13379957
Autor:
Lennard L. Bohlender, Juliana Parsons, Sebastian N. W. Hoernstein, Christine Rempfer, Natalia Ruiz-Molina, Timo Lorenz, Fernando Rodríguez Jahnke, Rudolf Figl, Benjamin Fode, Friedrich Altmann, Ralf Reski, Eva L. Decker
Publikováno v:
Frontiers in Plant Science
Frontiers in Plant Science, Vol 11 (2020)
Frontiers in Plant Science, Vol 11 (2020)
Recombinantly produced proteins are indispensable tools for medical applications. Since the majority of them are glycoproteins, theirN-glycosylation profiles are major determinants for their activity, structural properties and safety. For therapeutic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd919498f42d4f7d49591acc292cdb48
https://pubmed.ncbi.nlm.nih.gov/33391325
https://pubmed.ncbi.nlm.nih.gov/33391325
Publikováno v:
Journal of chromatography. A. 1627
Sialylation, an important form of glycosylation, is involved in many biological processes and plays an important role in the development of diseases. However, due to the low abundance among various glycosylation and lack of efficient enrichment metho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4228e8f3e36dd1f52b0cdc128b0e3af4
https://pubmed.ncbi.nlm.nih.gov/32823117
https://pubmed.ncbi.nlm.nih.gov/32823117
Publikováno v:
Process Biochemistry. 73:162-169
Sialic acid content generally affects many biochemical properties of therapeutic glycoproteins. More specific properties, such as charge distribution, circulating half-life and bioactivity, are directly impacted by sialic acid content. Undesirable lo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::31d2f1ab73f4d77734bd7186664f48de
https://doi.org/10.1016/j.procbio.2018.08.015
https://doi.org/10.1016/j.procbio.2018.08.015
Publikováno v:
Journal of the American Society for Mass Spectrometry
Mass spectrometric analysis of intact glycopeptides can reveal detailed information about glycosite, glycan structural features, and their heterogeneity. Sialyl glycopeptides can be positively, negatively, or neutrally charged depending on pH of thei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7069e229a3929981a548a3c94f89db8c
http://europepmc.org/articles/PMC6744383
http://europepmc.org/articles/PMC6744383