Identification and pathogenicity analysis of a novel highly virulent strain of spring viraemia of carp virus and production of its structural proteins by the mammalian expression system

Aquaculture ◽  
2021 ◽  
pp. 737487
Author(s):  
Wei-Chao Chen ◽  
Er-Long Wang ◽  
Fei Luo ◽  
Kai-Ge Song ◽  
Gao-Xue Wang
2013 ◽  
Vol 288 (46) ◽  
pp. 32873-32885 ◽  
Author(s):  
Terry H. Y. Lee ◽  
Ainslie Mitchell ◽  
Sydney Liu Lau ◽  
Hongyan An ◽  
Poornima Rajeaskariah ◽  
...  

Ion Channels ◽  
2006 ◽  
pp. 3-13
Author(s):  
Alexander Staruschenko ◽  
Rachell E. Booth ◽  
Oleh Pochynyuk ◽  
James D. Stockand ◽  
Qiusheng Tong

Ion Channels ◽  
2006 ◽  
pp. 1-114
Author(s):  
Alexander Staruschenko ◽  
Rachell E. Booth ◽  
Oleh Pochynyuk ◽  
James D. Stockand ◽  
Qiusheng Tong

1992 ◽  
pp. 68-70
Author(s):  
J McLean ◽  
M Hollis ◽  
M Needham ◽  
C Gooding ◽  
K Hudson ◽  
...  

1988 ◽  
Vol 6 (3) ◽  
pp. 287-290 ◽  
Author(s):  
John F. Weaver ◽  
Frank McCormick ◽  
M. Michele Manos

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Wei Li ◽  
Xiang Gao ◽  
Junle Ren ◽  
Ting An ◽  
Yan Liu

The cleaved amino-terminal fragment of human amyloid precursor protein (N-APP) binds death receptor 6 (DR6) and triggers a caspase-dependent self-destruction process, which was suggested to contribute to Alzheimer’s disease. To investigate the N-APP-DR6-induced degeneration pathway at the molecular level, obtaining abundant and purified N-APP is fundamental and critical. The recombinant N-APP has been produced in mammalian expression system. However, the cost and yield disadvantages of mammalian expression system make it less ideal for protein mass production. Here, we successfully expressed and purified recombinant N-terminal 18-285 amino acid residues of human amyloid precursor protein from the methylotrophic yeastPichia pastoriswith a high yield of 50 mg/L. Flow cytometry indicated the purified N-APP-induced obvious apoptosis of human neuroblastoma SHEP cells.


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