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Sci. Signal., 1 January 2013
[DOI: 10.1126/scisignal.2003252]

Supplementary Materials for:

Nitric Oxide Regulates Mitochondrial Fatty Acid Metabolism Through Reversible Protein S-Nitrosylation

Paschalis-Thomas Doulias, Margarita Tenopoulou, Jennifer L. Greene, Karthik Raju, Harry Ischiropoulos*

*To whom correspondence should be addressed. E-mail: ischirop{at}mail.med.upenn.edu

This PDF file includes:

  • Fig. S1. Functional analysis of the S-nitrosocysteine proteome.
  • Fig. S2. Identification of the S-nitrosylation site in VLCAD.
  • Fig. S3. Trichrome staining of liver tissue.
  • Fig. S4. Effect of S-nitrosylation on the enzymatic activity of VLCAD in eNOS–/– mouse liver.
  • Fig. S5. S-nitrosylation of VLCAD increases its enzymatic activity.
  • Fig. S6. Structure and normal mode analysis of unmodified and S-nitrosylated VLCAD.
  • Table S1. Endogenously S-nitrosylated proteins in wild-type mouse brain.
  • Table S2. Endogenously S-nitrosylated proteins in wild-type mouse heart.
  • Table S3. Endogenously S-nitrosylated proteins in wild-type mouse kidney.
  • Table S4. Endogenously S-nitrosylated proteins in wild-type mouse liver.
  • Table S5. Endogenously S-nitrosylated proteins in wild-type mouse lung.
  • Table S6. Endogenously S-nitrosylated proteins in wild-type mouse thymus.

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Technical Details

Format: Adobe Acrobat PDF

Size: 1.52 MB


Citation: P.-T. Doulias, M. Tenopoulou, J. L. Greene, K. Raju, H. Ischiropoulos, Nitric Oxide Regulates Mitochondrial Fatty Acid Metabolism Through Reversible Protein S-Nitrosylation. Sci. Signal. 6, rs1 (2013).

© 2013 American Association for the Advancement of Science


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