AMPylation is a new post-translational modiFICation

Melanie L. Yarbrough; Kim Orth

doi:10.1038/nchembio0609-378

AMPylation is a new post-translational modiFICation

Melanie L. Yarbrough, Kim Orth

Research output: Contribution to journal › Short survey › peer-review

28 Scopus citations

Abstract

A class of proteins containing domains that are evolutionarily conserved among prokaryotes and eukaryotes was recently found to mediate post-translational AMP additiona new protein modification called AMPylation. Similarities to the post-translational modification phosphorylation suggest that AMPylation may be an important regulatory mechanism.

Original language	English
Pages (from-to)	378-379
Number of pages	2
Journal	Nature Chemical Biology
Volume	5
Issue number	6
DOIs	https://doi.org/10.1038/nchembio0609-378
State	Published - Jun 2009

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abstract = "A class of proteins containing domains that are evolutionarily conserved among prokaryotes and eukaryotes was recently found to mediate post-translational AMP additiona new protein modification called AMPylation. Similarities to the post-translational modification phosphorylation suggest that AMPylation may be an important regulatory mechanism.",

author = "Yarbrough, {Melanie L.} and Kim Orth",

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M3 - Short survey

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AMPylation is a new post-translational modiFICation

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