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Truttmann MC, Ploegh HL. . Bio Protoc. 2017;7(14)doi: 10.21769/BioProtoc.2416.
Truttmann, M. C., & Ploegh, H. L. (2017). . Bio-protocol, 7(14), . https://doi.org/10.21769/BioProtoc.2416
Truttmann, Matthias C, and Ploegh, Hidde L. "." Bio-protocol vol. 7,14 (2017). doi: https://doi.org/10.21769/BioProtoc.2416
Truttmann MC, Ploegh HL. . Bio Protoc. 2017 Jul 20;7(14). doi: 10.21769/BioProtoc.2416. PMID: 29170749; PMCID: PMC5697756.
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Bio Protoc. 2017 Jul 20;7(14). doi: 10.21769/BioProtoc.2416.

[No title available]

Bio-protocol

Matthias C Truttmann, Hidde L Ploegh

Affiliations

  1. Boston Children's Hospital and Harvard Medical School, Boston, MA, USA.

PMID: 29170749 PMCID: PMC5697756 DOI: 10.21769/BioProtoc.2416

Abstract

Post-translational protein modifications (PTMs) orchestrate the activity of individual proteins and ensure their proper function. While modifications such as phosphorylation or glycosylation are well understood, more unusual modifications, including nitrosylation or AMPylation remain comparatively poorly characterized. Research on protein AMPylation-which refers to the covalent addition of an AMP moiety to the side chains of serine, threonine or tyrosine-has undergone a renaissance (Yarbrough

Keywords: AMPylation; Adenylylation; GTPase; Grp78/BiP; HSP70; Proteostasis

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