Molecular mechanism of secreted amyloid-β precursor protein in binding and modulating GABABR1a-Reference-Cited by-同舟云学术

Molecular mechanism of secreted amyloid-β precursor protein in binding and modulating GABABR1a

Published:2021 Issue:17 Volume:12 Page:6107-6116
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Feng Mei¹²³⁴⁵,Song Yi¹²³⁴⁵,Chen Serena H.⁶⁷⁸⁹^ORCID,Zhang Yuanzhao¹⁰¹¹¹²⁹,Zhou Ruhong¹²³⁴⁵^ORCID

Affiliation:

1. Institute of Quantitative Biology

2. Shanghai Institute for Advanced Study

3. College of Life Sciences

4. Department of Physics

5. Zhejiang University

6. Computational Sciences and Engineering Division

7. Oak Ridge National Laboratory

8. Oak Ridge

9. USA

10. Center for Applied Mathematics

11. Cornell University

12. Ithaca

Abstract

A recent phenomenal study discovered that the extension domain of secreted amyloid-β precursor protein (sAPP) can bind to the intrinsically disordered sushi 1 domain of the γ-aminobutyric acid type B receptor subunit 1a (GABA_BR1a) and modulate its synaptic transmission.

Funder

National Natural Science Foundation of China

China Postdoctoral Science Foundation

W. M. Keck Foundation

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2021/SC/D0SC06946A

Reference51 articles.

1. Secreted amyloid-β precursor protein functions as a GABA B R1a ligand to modulate synaptic transmission