Identification of ADAR1 p150 and p110 Associated Edit Sites

Tony Sun, Brad R. Rosenberg, Hachung Chung, Charles M. Rice

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

2 Scopus citations


Adenosine deaminase acting on RNA 1 (ADAR1) catalyzes adenosine-to-inosine editing on double-stranded RNA molecules and is involved in regulating cellular responses to endogenous and exogenous RNA. ADAR1 is the primary A-to-I editor of RNA in humans, and the majority of edit sites are found in a class of short interspersed nuclear elements called Alu elements, many of which are located in introns and 3′ untranslated regions. Two ADAR1 protein isoforms, p110 (110 kDa) and p150 (150 kDa), are known to be coupled in expression, and decoupling the expression of these isoforms has revealed that the p150 isoform edits a broader range of targets compared to p110. Numerous methods for identification of ADAR1-associated edits have been developed, and we present here a specific method for identification of edit sites associated with individual ADAR1 isoforms.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Number of pages10
StatePublished - 2023

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029


  • A-to-I editing
  • ADAR1
  • RNA sequencing


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