Co-Investigator JHU NIMH Surrogate Markers Core
Professor of Pharmacology and Molecular Sciences, Johns Hopkins University
Dr Cotter received his doctoral degree from Johns Hopkins University School of Medicine in Physical Chemistry. Dr Cotter’s laboratory has been a leader in the development of time-of-flight (TOF) mass spectrometry, including a tandem TOF with a curved-field reflectron for rapid peptide amino acid sequencing using high energy collisions.
The laboratory has also developed ion trap mass spectrometers, a combined ion trap/time-of-flight mass spectrometer, a miniaturized TOF for rapid identification of microorganisms based upon their proteomes, and is currently designing a low power ion trap mass spectrometer for Mars below-surface exploration. In collaboration with the Heng Zhu laboratory we have constructed protein microarrays for direct analysis by MALDI mass spectrometry imaging.
An effective procedure for N-terminal sulfonation4 enables de novo sequencing of proteins that is being used to elucidate ubiquitylation sites in proteins and ubiquitylating enzymes. As part of the Technical Center for Networks and Pathways (TCNP) of Lysine modifications, the laboratory has developed an approach for determining acetylation sites that has been used to investigate regulatory mechanisms in histone acetyl transferases (HATs)6,7 and a method for quantitating acetylation on specific histone sites using hyper-deuteroacetylation of unoccupied lysines that has been used to explore the role of sirtuins hst3 and Hst4p in yeast8 and to distinguish isoforms of hyperacetylated H3 and H4 tail regions in human HeLa cells. In a novel approach to biomarker discovery, supported by the NHLBI Center for Proteomics of Ischemia and Hypoxia, the laboratory is utilizing the albuminome, the proteins bound to albumin following albumin removal, to investigate potential clinically-useful indicators of heart disease.