Multiscale time-resolved fluorescence study of a glycogen phosphorylase inhibitor combined with quantum chemistry calculations-Reference-Cited by-同舟云学术

Multiscale time-resolved fluorescence study of a glycogen phosphorylase inhibitor combined with quantum chemistry calculations

Published:2019 Issue:14 Volume:21 Page:7685-7696
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Maffeis Valentin¹²³⁴⁵^ORCID,Mavreas Konstantinos⁶⁷⁸⁹^ORCID,Monti Filippo¹⁰¹¹¹²¹³^ORCID,Mamais Michael¹²³⁴⁵^ORCID,Gustavsson Thomas¹²³⁴⁵^ORCID,Chrysina Evangelia D.¹⁴¹⁵¹⁶⁸⁹,Markovitsi Dimitra¹²³⁴⁵^ORCID,Gimisis Thanasis⁶⁷⁸⁹^ORCID,Venturini Alessandro¹⁰¹¹¹²¹³

Affiliation:

1. LIDYL

2. CEA

3. CNRS

4. Université Paris-Saclay

5. Gif-sur-Yvette

6. Department of Chemistry

7. National and Kapodistrian University of Athens

8. Athens

9. Greece

10. Istituto ISOF

11. Consiglio Nazionale delle Ricerche

12. Bologna

13. Italy

14. Institute of Biology

15. Medicinal Chemistry & Biotechnology

16. National Hellenic Research Foundation

Abstract

A study of the first fluorescent potent inhibitor of glycogen phosphorylase showcases how emission is controlled by two independent rotations of two aromatic moieties.

Funder

European Social Fund

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2019/CP/C8CP07538G

Reference48 articles.

1. The Prototype of Glycogen Phosphorylase

2. Synthesis of N-Glucopyranosidic Derivatives as Potential Inhibitors that Bind at the Catalytic Site of Glycogen Phosphorylase

3. Role of glycogen phosphorylase in liver glycogen metabolism

4. A New Potent Inhibitor of Glycogen Phosphorylase Reveals the Basicity of the Catalytic Site

5. Binding of oxalyl derivatives of β-d-glucopyranosylamine to muscle glycogen phosphorylase b

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