Export of a hyperexpressed mammalian globular cytochrome b5precursor inEscherichia coliis dramatically affected by the nature of the amino acid flanking the secretory signal sequence cleavage bond-Reference-Cited by-同舟云学术

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Export of a hyperexpressed mammalian globular cytochrome b5precursor inEscherichia coliis dramatically affected by the nature of the amino acid flanking the secretory signal sequence cleavage bond

Published:2010-05-05 Issue:7 Volume:19 Page:1344-1353
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Kaderbhai Naheed N.,Ahmed Khalil,Kaderbhai Mustak A.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.411/fullpdf

Reference54 articles.

1. Periplasmically-exported lupanine hydroxylase undergoes transition from soluble to functional inclusion bodies in Escherichia coli;Stampolidis;Arch Biochem Biophys,2009

2. Ser/Thr/Tyr protein phosphorylation in bacteria-for long time neglected, now well established;Deutscher;J Mol Microbiol Biotechnol,2005

3. N-linked glycosylation in bacteria: an unexpected application;Langdon;Future Microbiol,2009

4. Cloning, sequencing and heterologous expression of the gene for lupanine hydroxylase, a quinocytochrome c from a Pseudomonas sp;Hopper;Biochem J,2002

Cited by 1 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Optimisation of signal peptide for recombinant protein secretion in bacterial hosts;Applied Microbiology and Biotechnology;2013-03-26

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