A New Chemical Handle for Protein AMPylation at the Host-Pathogen Interface
File(s)Broncel CBC 2011 submitted manuscript.pdf (251.31 KB)
Accepted version
Author(s)
Broncel, M
Serwa, RA
Tate, EW
Type
Journal Article
Abstract
agging protein AMPylation: A new chemical reporter for AMPylation, recently identified as a key post-translational modification during bacterial infection, is a robust tool for detecting and identifying AMPylated proteins in vitro.
Date Issued
2012-01-16
Date Acceptance
2011-11-24
Citation
Chembiochem, 2012, 13 (2), pp.183-185
ISSN
1439-7633
Publisher
Wiley-VCH Verlag
Start Page
183
End Page
185
Journal / Book Title
Chembiochem
Volume
13
Issue
2
Copyright Statement
This is the peer reviewed version of the following article: Broncel, M., Serwa, R. A. and Tate, E. W. (2012), A New Chemical Handle for Protein AMPylation at the Host–Pathogen Interface. ChemBioChem, 13: 183–185, which has been published in final form at https://dx.doi.org/10.1002/cbic.201100743. This article may be used for non-commercial purposes in accordance With Wiley Terms and Conditions for self-archiving.
Subjects
Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
Chemistry, Medicinal
Pharmacology & Pharmacy
BIOCHEMISTRY & MOLECULAR BIOLOGY
CHEMISTRY, MEDICINAL
AMPylation
bacterial effectors
chemical reporters
post-translational modifications
proteomics
LEGIONELLA-PNEUMOPHILA
RHO GTPASES
FIC DOMAIN
ADENYLYLATION
MODULATION
RAB1
Publication Status
Published