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Chemical Proteomics of Host-Microbe Interactions
被引:16
|作者:
Wright, Megan H.
[1
]
机构:
[1] Univ Leeds, Sch Chem, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, W Yorkshire, England
来源:
关键词:
activity-based protein profiling;
chemical probe;
chemical proteomics;
metabolic tagging;
photoaffinity labeling;
NEWLY SYNTHESIZED PROTEINS;
PROFILING REVEALS;
PROTEASOME ACTIVITY;
ANTIVIRAL ACTIVITY;
ADP-RIBOSYLATION;
FATTY-ACYLATION;
CROSS-LINKING;
IDENTIFICATION;
AMPYLATION;
DISCOVERY;
D O I:
10.1002/pmic.201700333
中图分类号:
Q5 [生物化学];
学科分类号:
071010 ;
081704 ;
摘要:
The dynamic proteome plays numerous roles in the interactions of microbeswhether they are invading pathogens or symbiotic organismsand 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 posttranslational modification that influence protein localization, activity, or binding partners. The intrinsic, temporal, and spatial complexity of multispecies systems makes identifying the molecular players challenging. Chemical proteomic approaches apply small molecule chemical tools to interrogate protein function, interactions or modifications. This review highlights recent advances in the application of these methods at the host-microbe interface.
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页数:10
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