Marissa Martinez Email and Phone Number

• Determined the binding sites of various bio- and small molecule interactors on large multi-subunit complexes by covalent labeling mass spectrometry (CLMS) and crosslinking MS (XLMS).• Developed enrichment strategies for the purification of endogenous multi-subunit chromatin remodeling complexes in relevant cancer cell lines.• Generated targeted quantitative MS assays for the subunits and paralogs of large chromatin remodeling complexes, enabling characterization of their composition and stoichiometry.• Assessed potential vulnerabilities following subunit degradation via quantitative (TMT) proteomics, including analysis of off-targets and their pathways, as well as maintenance of complex integrity.• Characterized covalent modification of compounds on protein target, including stoichiometry and sites of modification by intact and tandem MS. • Developed targeted quantitative assays to determine target engagement for in vitro and in vivo analysis.

• Employed liquid chromatography mass spectrometry-based (LC-MS/MS) proteomics approaches to identify and quantify protein interactors and post-translational modifications of enzymes involved in intracellular glycosylation.• Utilized HPLC for separating large macromolecular protein complexes for downstream identification of proteins and sites of glycosylation by HCD and ETD LC-MS/MS.• Used LPLC to obtain glycosylated protein complexes from immuno-affinity enrichment columns.• Collaborated with other investigators to map sites of glycosylation on proteins involved in transcription as well as cytokine signaling.• Worked with collaborators to develop ETD MS-based strategies to map sites of intracellular glycosylation for PRM-based quantitation.• Performed radiolabeled assays detecting enzymatic activity of intracellular glycosyltransferases and hexosaminidases. • Investigated intracellular signaling pathways that regulate both glycosylation and phosphorylation in vitro and in vivo by protein biochemical and molecular biology approaches.

• Collaborated with clinicians to recruit over 300 subjects suspected of venous thromboembolism (VTE); recorded and maintained their demographics and health history in compliance with HIPPA and the University of Pennyslvania’s internal review board; obtained plasma from each subject for studies on the role of fibrinogen in VTE. From this cohort I completed the following studies resulting in two first author publications:• Identified differentially regulated sites of nitration on fibrinogen by LC-MS/MS.• Studied the viscoelastic properties that dictate embolization in ex vivo and in vitro fibrin clots by rheometry.• Evaluated nitrated fibrinogen as a biomarker of VTE by ELISA.• Identified nitrated proteins in platelets by LC-MS/MS.• Investigated platelet and nitrated fibrinogen interactions during ex vivo thrombus formation.