Proinsulin lacking the A7-B7 disulfide bond, Ins2Akita, tends to aggregate due to the exposed hydrophobic surface-Reference-Cited by-同舟云学术

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Proinsulin lacking the A7-B7 disulfide bond, Ins2Akita, tends to aggregate due to the exposed hydrophobic surface

Published:2005-01-01 Issue:11 Volume:386 Page:
ISSN:1431-6730
Container-title:Biological Chemistry
language:
Short-container-title:

Author:

Yoshinaga Takeo,Nakatome Keisuke,Nozaki Jun-ichi,Naitoh Motoko,Hoseki Jun,Kubota Hiroshi,Nagata Kazuhiro,Koizumi Akio

Publisher

Walter de Gruyter GmbH

Subject

Clinical Biochemistry,Molecular Biology,Biochemistry

Link

https://www.degruyter.com/document/doi/10.1515/BC.2005.124/pdf

Reference29 articles.

1. Integration of endoplasmic reticulum signaling in health and disease

2. Heat-shock proteins as molecular chaperones

3. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

4. Production of human insulin in anE. coli system with Met-Lys-human proinsulin as the expressed precursor

5. Acidic Residues on the N-Terminus of Proinsulin C-Peptide Are Important for the Folding of Insulin Precursor

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