Wright, MH orcid.org/0000-0003-2731-4707 (2018) Chemical proteomics of host-microbe interactions. Proteomics, 18 (18). ARTN1700333. ISSN 1615-9853
Abstract
The dynamic proteome plays numerous roles in the interactions of microbes - whether they are invading pathogens or symbiotic organisms - and their hosts. Host and microbe sense, respond and manipulate each other's biology via a multitude of mechanisms, resulting in alterations in protein expression or post-translational modification that influence protein localisation, activity or binding partners. The intrinsic, temporal and spatial complexity of multi-species systems makes identifying the molecular players challenging. Chemical proteomic approaches apply small molecule chemical tools to interrogate protein function, interactions or modifications. Here I highlight recent advances in the application of these methods at the host-microbe interface.
Metadata
| Item Type: | Article |
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| Authors/Creators: |
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| Copyright, Publisher and Additional Information: | © 2018 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim. This is the peer reviewed version of the following article: Wright, MH (2018) Chemical proteomics of host-microbe interactions. Proteomics, 18 (18). ARTN1700333, which has been published in final form at https://doi.org/10.1002/pmic.201700333. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving. |
| Keywords: | activity-based protein profiling, chemical probe, chemical proteomics, metabolic tagging, photoaffinity labelling |
| Dates: |
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| Institution: | The University of Leeds |
| Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) > Organic Chemistry (Leeds) |
| Depositing User: | Symplectic Publications |
| Date Deposited: | 21 May 2018 15:00 |
| Last Modified: | 09 May 2019 00:43 |
| Status: | Published |
| Publisher: | Wiley |
| Identification Number: | 10.1002/pmic.201700333 |
| Related URLs: | |
| Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:131079 |

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