Allosteric Regulation of Glycogen Phosphorylase by Order/Disorder Transition of the 250′ and 280s Loops-Reference-Cited by-同舟云学术

Allosteric Regulation of Glycogen Phosphorylase by Order/Disorder Transition of the 250′ and 280s Loops

Published:2023-03-29 Issue:8 Volume:62 Page:1360-1368
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kish Monika¹,Subramanian Sivaraman²^ORCID,Smith Victoria³,Lethbridge Natasha³,Cole Lindsay⁴,Vollmer Frank²,Bond Nicholas. J.⁵^ORCID,Phillips Jonathan J.¹⁶^ORCID

Affiliation:

1. Living Systems Institute, Department of Biosciences, University of Exeter, Stocker Road, Exeter, EX4 4QD, U.K.

2. Living Systems Institute, Department of Physics, University of Exeter, Stocker Road, Exeter, EX4 6QD, U.K.

3. CPI, Darlington, DL1 1GL, U.K.

4. Applied Photophysics Ltd, Leatherhead, KT227BA, U.K.

5. Analytical Sciences, Biopharmaceutical Development, BioPharmaceuticals R&D, AstraZeneca, Milstein Building, Granta Park, Cambridge, CB21 6GH, U.K.

6. Alan Turing Institute, British Library, London, NW1 2DB, U.K.

Funder

Medical Research Council

Innovate UK

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.2c00671

Reference52 articles.

1. Allosteric proteins and cellular control systems

2. On the nature of allosteric transitions: A plausible model

3. Protein Allostery and Conformational Dynamics

4. Allostery in Its Many Disguises: From Theory to Applications

5. The allosteric transition of glycogen phosphorylase

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