Influence of a Single Point Mutation in the Constant Domain of the Bence-Jones Protein BIF on Its Aggregation Properties
Author:
Publisher
Pleiades Publishing Ltd
Subject
Biochemistry,General Medicine
Link
http://link.springer.com/article/10.1134/S0006297918020037/fulltext.html
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4. Mukherjee, S., Pondaven, S. P., and Jaroniec, C. P. (2011) Conformational flexibility of a human immunoglobulin light chain variable domain by relaxation dispersion nuclear magnetic resonance spectroscopy: implications for protein misfolding and amyloid assembly, Biochemistry, 50, 5845–5857.
5. Wilkins-Stevens, P., Raffen, R., Hanson, D. K., Deng, Y. L., Berrios-Hammond, M., Westholm, F. A., Murphy, C., Eulitz, M., Wetzel, R., Solomon, A., Schiffer, M., and Stevens, F. J. (1995) Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light-chain amyloid proteins, Protein Sci., 4, 421–432.
Cited by 2 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. Does protein aggregation drive postmitotic tissue degeneration?;Science Translational Medicine;2021-01-20
2. Effect of Single Amino Acid Substitutions by Asn and Gln on Aggregation Properties of Bence-Jones Protein BIF;International Journal of Molecular Sciences;2019-10-20
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