Allosterically Linked Binding Sites in Serotonin Transporter Revealed by Single Molecule Force Spectroscopy-Reference-Cited by-同舟云学术

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Allosterically Linked Binding Sites in Serotonin Transporter Revealed by Single Molecule Force Spectroscopy

Published:2020-06-03 Issue: Volume:7 Page:
ISSN:2296-889X
Container-title:Frontiers in Molecular Biosciences
language:
Short-container-title:Front. Mol. Biosci.

Author:

Zhu Rong,Sandtner Walter,Ahiable Joan E. A.,Newman Amy Hauck,Freissmuth Michael,Sitte Harald H.,Hinterdorfer Peter

Funder

Austrian Science Fund

National Institute on Drug Abuse

Publisher

Frontiers Media SA

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Molecular Biology,Biochemistry

Reference29 articles.

1. Interrogating the molecular basis for substrate recognition in serotonin and dopamine transporters with high-affinity substrate-based bivalent ligands.;Andersen;ACS Chem. Neurosci.,2016

2. Coupled global and local changes direct substrate translocation by neurotransmitter-sodium symporter ortholog LeuT.;Cheng;Biophys. J.,2013

3. Monoamine transporters: structure, intrinsic dynamics and allosteric regulation.;Cheng;Nat. Struct. Mol. Biol.,2019

4. X-ray structures and mechanism of the human serotonin transporter.;Coleman;Nature,2016

5. Structural basis for recognition of diverse antidepressants by the human serotonin transporter.;Coleman;Nat. Struct. Mol. Biol.,2018

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