Chaperone and Immunoglobulin-Binding Activities of Skp Protein from Yersinia pseudotuberculosis
Author:
Publisher
Pleiades Publishing Ltd
Subject
Biochemistry,General Medicine
Link
http://link.springer.com/content/pdf/10.1134/S0006297920010071.pdf
Reference41 articles.
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2. Holck, A., and Kleppe, K. (1988) Cloning and sequencing of the gene for the DNA-binding 17K protein of Escherichia coli, Gene, 67, 117–124, doi: https://doi.org/10.1016/0378-1119(88)90014-5.
3. Koski, P., Rhen, M., Kantele, J., and Vaara, M. (1989) Isolation, cloning, and primary structure of a cationic 16- kDa outer membrane protein of Salmonella typhimurium, J. Biol. Chem., 264, 18973–18980.
4. Koski, P., Hirvas, L., and Vaara, M. (1990) Complete sequence of the ompH gene encoding the 16-kDa cationic outer membrane protein of Salmonella typhimurium, Gene, 88, 117–120, doi: https://doi.org/10.1016/0378-1119(90)90068-3.
5. De Cock, Y., Schafer, U., Potgeter, M., Demel, R., Muller, M., and Tommassen, J. (1999) Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein, Eur. J. Biochem., 259, 96–103, doi: https://doi.org/10.1046/j.14321327.1999.00010.x.
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