Gerald W. Hart, PhD, The John Hopkins University

Gerald W. Hart, PhD
Gerald W. Hart, PhD

The Gerald Hart Laboratory discovered O-GIcNAc, a type of protein modification, present on proteins within the nucleus and cytoplasm of cells, in which a glucose-derived sugar is attached to serine or threonine side chains of proteins, exactly analogous to phosphorylation. In their recent studies, they discovered that O-GlcNAc plays an important role in diabetes and glucose toxicity, Alzhemier's disease and in the functions of oncogenes and tumor suppressors important to cancer. The Hart lab continues to focus on dynamic O-GicNAcylatino of nuclear and cytosolic proteins.

Products

References

  1. Comer FI, Vosseller K, Wells L, Accavitti MA, Hart GW. Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine. Anal Biochem. 2001 Jun 15;293(2):169-77.
  2. Zachara, Natasha E; Vosseller, Keith; Hart, Gerald W. Detection and analysis of proteins modified by O-linked N-acetylglucosamine. Curr Protoc Protein Sci. 2011 11;Chapter 12:Unit12.8.
  3. Ma J, Hart GW. O-GlcNAc profiling: from proteins to proteomes. Clin Proteomics. 2014 Mar 5;11(1):8. doi: 10.1186/1559-0275-11-8.
  4. Hart GW, Slawson C, Ramirez-Correa G, Lagerlof O. Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu Rev Biochem. 2011;80:825-58.
  5. Hardivillé S, Hart GW. Nutrient regulation of signaling, transcription, and cell physiology by O-GlcNAcylation. Cell Metab. 2014 Aug 5;20(2):208-13.
  6. Comer, F I; Vosseller, K; Wells, L; Accavitti, M A; Hart, G W. Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine.