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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