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Methods for Identifying and Examining HTLV-1 HBZ Post-translational Modifications.
Al-Saleem, Jacob; Kvaratskhelia, Mamuka; Green, Patrick L.
Affiliation
  • Al-Saleem J; Center for Retrovirus Research, The Ohio State University, Columbus, OH, 43210, USA.
  • Kvaratskhelia M; Department of Veterinary Biosciences, The Ohio State University, Columbus, OH, 43210, USA.
  • Green PL; Center for Retrovirus Research, The Ohio State University, Columbus, OH, 43210, USA.
Methods Mol Biol ; 1582: 111-126, 2017.
Article in En | MEDLINE | ID: mdl-28357666
ABSTRACT
Post-translational modifications (PTMs) are chemical alterations to individual amino acids that alter a protein's conformation, stability, and/or function. Several pathogenic viruses have been shown to encode proteins with PTMs, including human T-cell leukemia virus type 1 (HTLV-1) Tax and Rex regulatory proteins. HTLV-1 basic leucine zipper protein (HBZ) was hypothesized to feature PTMs due to its functional activities and interactions with cellular transcription factors and acetyltransferases. Here, we describe the approach used to identify, via mass spectrometry, the PTMs of HBZ. In addition, we describe methods to determine the functional relevance of the identified PTMs.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Mass Spectrometry / Human T-lymphotropic virus 1 / Protein Processing, Post-Translational / Retroviridae Proteins / Basic-Leucine Zipper Transcription Factors Type of study: Prognostic_studies Limits: Humans Language: En Journal: Methods Mol Biol Journal subject: BIOLOGIA MOLECULAR Year: 2017 Document type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Mass Spectrometry / Human T-lymphotropic virus 1 / Protein Processing, Post-Translational / Retroviridae Proteins / Basic-Leucine Zipper Transcription Factors Type of study: Prognostic_studies Limits: Humans Language: En Journal: Methods Mol Biol Journal subject: BIOLOGIA MOLECULAR Year: 2017 Document type: Article Affiliation country: United States