Role of Conformational Changes of Hexameric Bacterial Uridine Phosphorylases in Substrate Binding-Reference-Cited by-同舟云学术

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Role of Conformational Changes of Hexameric Bacterial Uridine Phosphorylases in Substrate Binding

Published:2021-09 Issue:5 Volume:66 Page:786-790
ISSN:1063-7745
Container-title:Crystallography Reports
language:en
Short-container-title:Crystallogr. Rep.

Author:

Polyakov K. M.,Mordkovich N. N.,Safonova T. N.,Antipov A. N.,Okorokova N. A.,Dorovatovskii P. V.,Veiko V. P.

Publisher

Pleiades Publishing Ltd

Subject

Condensed Matter Physics,General Materials Science,General Chemistry

Link

https://link.springer.com/content/pdf/10.1134/S1063774521050199.pdf

Reference18 articles.

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2. M. Cappiello, L. Mascia, C. Scolozzi, et al., Biochim. Biophys. Acta 1425, 273 (1998). https://doi.org/10.1016/s0304-4165(98)00071-3

3. M. G. Tozzi, M. Camici, L. Mascia, et al., FEBS J. 273, 1089 (2006). https://doi.org/10.1111/j.1742-4658.2006.05155.x

4. C. Luccioni, J. Beaumatin, V. Bardot, et al., Int. J. Cancer 58, 517 (1994). https://doi.org/10.1002/ijc.2910580411

5. S. Watanabe and T. Uchida, Biochem. Biophys. Res. Commun. 216, 265 (1995). https://doi.org/10.1006/bbrc.1995.2619

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. The Thermostability of Nucleoside Phosphorylases from Prokaryotes. I. The Role of the Primary Structure of the N-terminal fragment of the Protein in the Thermostability of Uridine Phosphorylases;Applied Biochemistry and Microbiology;2022-12

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