Zobrazeno 1 - 8
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pro vyhledávání: '"Tzu-Chiang Han"'
Publikováno v:
Polymers, Vol 10, Iss 5, p 468 (2018)
Conventional column chromatography processes to purify recombinant proteins are associated with high production costs and slow volumetric throughput at both laboratory and large scale. Non-chromatographic purifications based on selective aggregating
Externí odkaz:
https://doaj.org/article/e4c7821c0f4e4e798f40228600e4d905
Autor:
Tzu-Chiang Han, 韓子強
97
More than twenty different human proteins can fold abnormally into amyloid fibril deposits which may lead to lethal diseases. Despite extensive investigations on amyloid fibril formation, the detail of molecular mechanism remained rather elus
More than twenty different human proteins can fold abnormally into amyloid fibril deposits which may lead to lethal diseases. Despite extensive investigations on amyloid fibril formation, the detail of molecular mechanism remained rather elus
Externí odkaz:
http://ndltd.ncl.edu.tw/handle/68724243602006881681
Autor:
Veera Padmanbhan, Bijan Zakeri, Sudheer Sami, Stefan Minning, Michael DiFore, Jessica Mondia, Nathaniel Fair, Doug Berry, Chris Lyman, Laura McFadden, Veronique Deparis, Janmeet Anant, Wade Nudson, Laura Bentley, Vesna Stergar, Xiaoya Hu, Chris Wiedel, Tzu Chiang Han, Eric Shierly, Stefan Paschen, Divya Vasudevan, Elham Biouet, Sara Dorman, Fan Gao, Catherien Buchere, Benjamin Jequier, Michelle Ferreri, Nicola Coles, Lesley Holt, Jannika Kremer, Isabelle Lequeux
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6a8c43c6e81643c443a67b61b01b068a
https://doi.org/10.46220/2022ds004
https://doi.org/10.46220/2022ds004
Autor:
Yordan Kostov, Michael Tolosa, Chandrasekhar Gurramkonda, Tzu-Chiang Han, Joseph E. Taris, David W. Wood, Merideth A. Cooper, Douglas D. Frey, Christina Dinkins, Niloufar Pezeshk, Leah Tolosa, Adil Zuber, Chariz Peñalber-Johnstone, Manohar Pilli, Nicholas Selock, Govind Rao, Kevin Tran
Publikováno v:
Biotechnology and Bioengineering. 115:92-102
The use of cell-free systems to produce recombinant proteins has grown rapidly over the past decade. In particular, cell-free protein synthesis (CFPS) systems based on mammalian cells provide alternative methods for the production of many proteins, i
Publikováno v:
Polymers, Vol 10, Iss 5, p 468 (2018)
Polymers
Polymers; Volume 10; Issue 5; Pages: 468
Polymers
Polymers; Volume 10; Issue 5; Pages: 468
Conventional column chromatography processes to purify recombinant proteins are associated with high production costs and slow volumetric throughput at both laboratory and large scale. Non-chromatographic purifications based on selective aggregating
Autor:
Yordan Kostov, Shayan Borhani, Sevda Deldari, Niloufar Pezeshk, Aniruddha Rao, David W. Wood, Douglas D. Frey, Krishna Vattem, Leah Tolosa, Manohar Pilli, Xudong Ge, Govind Rao, Michael Tolosa, Tzu-Chiang Han, Chandrasekhar Gurramkonda
Publikováno v:
Biotechnology and bioengineering. 115(5)
Cell-Free Protein Synthesis (CFPS) offers many advantages for the production of recombinant therapeutic proteins using the CHO cell-free system. However, many complex proteins are still difficult to express using this method. To investigate the curre
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1495
Fusions of elastin-like peptide (ELP) purification tags and self-cleaving inteins provide a powerful platform for purifying tagless recombinant proteins without the need for conventional packed-bed columns. A drawback to this method has been prematur
Publikováno v:
Methods in Molecular Biology ISBN: 9781493964499
Fusions of elastin-like peptide (ELP) purification tags and self-cleaving inteins provide a powerful platform for purifying tagless recombinant proteins without the need for conventional packed-bed columns. A drawback to this method has been prematur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::08e5318e44bbec01c1b6b03f177abc89
https://doi.org/10.1007/978-1-4939-6451-2_2
https://doi.org/10.1007/978-1-4939-6451-2_2