Literature DB >> 28109444

Monitoring Protein Synthesis in Caenorhabditis elegans Using SILAC.

M Miyagi1.   

Abstract

The static levels of proteins are the net results of their production and clearance regulated by the activities of proteins involved in their synthesis, degradation, and transportation. Therefore, the information on the rates of protein synthesis and clearance is needed to understand the underlying dynamic nature of a proteome. In this chapter, the experimental technique, we use in our laboratory for monitoring the synthesis of individual proteins in Caenorhabditis elegans (C. elegans) is described. The technique utilizes a preisotopically labeled amino acid (13C6-Lys) as a precursor for protein synthesis and monitors the kinetics of the precursor incorporation into the newly synthesized proteins. C. elegans is a powerful animal model in various fields of biomedical science such as aging, developmental biology, and neurobiology. The experimental technique would, therefore, be useful for research laboratories using C. elegans as an animal model.
© 2017 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  Caenorhabditis elegans; Isotope labeling; LC–MS/MS; Mass spectrometry; Protein synthesis; Proteomics; SILAC

Mesh:

Year:  2016        PMID: 28109444     DOI: 10.1016/bs.mie.2016.09.015

Source DB:  PubMed          Journal:  Methods Enzymol        ISSN: 0076-6879            Impact factor:   1.600


  1 in total

1.  A mass spectrometry-based assay using metabolic labeling to rapidly monitor chromatin accessibility of modified histone proteins.

Authors:  Simone Sidoli; Mariana Lopes; Peder J Lund; Naomi Goldman; Maria Fasolino; Mariel Coradin; Katarzyna Kulej; Natarajan V Bhanu; Golnaz Vahedi; Benjamin A Garcia
Journal:  Sci Rep       Date:  2019-09-20       Impact factor: 4.379

  1 in total

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