The comparative analysis of the properties and structures of purine nucleoside phosphorylases from thermophilic bacterium Thermus thermophilus HB27-Reference-Cited by-同舟云学术

The comparative analysis of the properties and structures of purine nucleoside phosphorylases from thermophilic bacterium Thermus thermophilus HB27

Published:2020-11-23 Issue: Volume: Page:1-16
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Timofeev Vladimir I.¹,Fateev Ilya V.²,Kostromina Maria A.²,Abramchik Yuliya A.²,Konstantinova Irina D.²,Volkov Vladimir V.¹,Lykoshin Dmitry D.²,Mikheeva Olga O.²,Muravieva Tatiana I.²,Esipov Roman S.²,Kuranova Inna P.¹

Affiliation:

1. Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics” of Russian Academy of Sciences, Moscow, Russian Federation;

2. Shemyakin−Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2020.1848628

Reference37 articles.

1. Thermus thermophilus Nucleoside Phosphorylases Active in the Synthesis of Nucleoside Analogues

2. Structural Basis for Substrate Specificity of Escherichia coli Purine Nucleoside Phosphorylase

3. Purine nucleoside phosphorylases: properties, functions, and clinical aspects

4. Structures of human purine nucleoside phosphorylase complexed with inosine and ddI

5. Cancer gene therapy: connecting basic research with clinical inquiry.

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