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Regulation of the unfolded protein response via S-nitrosylation of sensors of endoplasmic reticulum stress

Academic Article
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Overview

authors

  • Nakato, R.
  • Ohkubo, Y.
  • Konishi, A.
  • Shibata, M.
  • Kaneko, Y.
  • Iwawaki, T.
  • Nakamura, T.
  • Lipton, Stuart
  • Uehara, T.

publication date

  • October 2015

journal

  • Scientific Reports  Journal

subject areas

  • Amino Acid Substitution
  • Animals
  • Cell Death
  • Cell Line
  • Cell Line, Tumor
  • Cysteine
  • Endoplasmic Reticulum
  • Endoplasmic Reticulum Stress
  • Endoribonucleases
  • Eukaryotic Initiation Factor-2
  • Fibroblasts
  • Mice
  • Models, Biological
  • Mutagenesis, Site-Directed
  • Neurons
  • Nitric Oxide
  • Parkinson Disease
  • Phosphorylation
  • Protein Processing, Post-Translational
  • Protein Serine-Threonine Kinases
  • Serine
  • Signal Transduction
  • Unfolded Protein Response
  • eIF-2 Kinase
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Identity

PubMed Central ID

  • PMC4597200

International Standard Serial Number (ISSN)

  • 2045-2322

Digital Object Identifier (DOI)

  • 10.1038/srep14812

PubMed ID

  • 26446798
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Additional Document Info

volume

  • 5

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