Protein Interaction Kinetics Delimit the Performance of Phosphorylation-Driven Protein Switches-Reference-Cited by-同舟云学术

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Protein Interaction Kinetics Delimit the Performance of Phosphorylation-Driven Protein Switches

Published:2024-06-03 Issue:6 Volume:13 Page:1781-1797
ISSN:2161-5063
Container-title:ACS Synthetic Biology
language:en
Short-container-title:ACS Synth. Biol.

Author:

Winter Daniel L.¹²^ORCID,Wairara Adelgisa R.¹,Bennett Jack L.³,Donald William A.³^ORCID,Glover Dominic J.¹^ORCID

Affiliation:

1. School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW 2052, Australia

2. Synthetic Biology Future Science Platform, Commonwealth Scientific and Industrial Research Organisation (CSIRO), Canberra, ACT 2601, Australia

3. School of Chemistry, University of New South Wales, Sydney, NSW 2052, Australia

Funder

Air Force Office of Scientific Research

Australian Research Council

Commonwealth Scientific and Industrial Research Organisation

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acssynbio.4c00101

Reference43 articles.

1. High-throughput phosphoproteomics reveals in vivo insulin signaling dynamics

2. Multisite protein phosphorylation - from molecular mechanisms to kinetic models

3. Design of Tunable Protein Interfaces Controlled by Post-Translational Modifications

4. De novo design of a reversible phosphorylation-dependent switch for membrane targeting

5. De novo design of tyrosine and serine kinase-driven protein switches

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