Speaker: Elizabeth Neumann, University of California, Davis

Topic: Spatial Multiomics towards Understanding Neurological diseases

Date: Monday, March 9, 2026

Time: 6:15 pm Dinner, 7:15 pm Presentation

Location: University of Maryland College Park, Chemistry (Directions)

Dinner: Please RSVP to Sheng Feng (SFeng@som.umaryland.edu) by Friday, March 6 if you will be attending the dinner.

Abstract: Organ systems are composed of unique cell types that actively coordinate to enable higher order functions. Even slight deviances in the molecular or cellular states of these systems can result in debilitating disorders whose severity, treatment course, and overall treatment outcome vary widely from patient to patient. This level of complexity likely contributes to promising therapeutics failing within clinical trials and, thus, require further exploration. Thus, the Neumann lab focuses on developing and applying multimodal imaging and profiling techniques to study complex human diseases, such as renal cell carcinoma, Alzheimer’s Disease, and spina bifida. Beyond disease, we also develop methods for spatially assessing exogenous agents, including pharmaceuticals, toxins, and plastics, within organ and whole animal models.

Lightning Talk
Stellar MS: Redefining targeted proteomics with a quadrupole, collision cell and linear ion trap architecture
Romain Huguet, Ph.D.
Nominal Mass Product Management team, Thermo Fisher Scientific

Targeted mass spectrometry is traditionally applied at the final stage of the biomarker discovery pipeline for the quantification of limited numbers of candidate analytes. While targeted MS delivers superior quantitative accuracy, precision, and specificity, its broader application in upstream discovery and verification studies has been constrained by limited multiplexing capacity and throughput. The new Stellar MS platform integrates a quadrupole mass filter, collision cell, and radial ejection linear ion trap architecture that expands the practical range of targeted proteomics. Hardware and instrument control advancements, combined with a real-time Adaptive Retention Time (RT) algorithm that compensates for chromatographic shifts, enable substantially narrower acquisition windows. This approach supports the targeting of 5,000–8,000 peptides per hour, enabling robust high-plex quantitative workflows.
For low-plex applications, this platform further enhances specificity and sensitivity through an MS³ acquisition strategy, reducing interference and increasing quantitative confidence for small, high-value peptide panels.
By unifying high-multiplex throughput and low-plex analytical rigor within a single system, this platform extends the utility of targeted MS across discovery, verification/ validation, and translational proteomics applications

Speaker: Lance A. Liotta, George Mason University

Topic: Mapping tumor tissue communication networks for designer therapies

Date: Monday, February 9, 2026

Time: 6:15 pm Dinner, 7:15 pm Presentation

Location: Shimadzu Scientific Instrument, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)

Dinner: Please RSVP to Sheng Feng (SFeng@som.umaryland.edu) by Friday, February 6 if you will be attending the dinner.

Abstract: We envision a future in which spatial molecular portraits of the tumor tissue microenvironment can transcend static lists of analytes to become integrated maps of active cellular signaling networks. Spatial proteomic profiling of the cancer tissue microenvironment can be conducted on bothd the cellular and interstitial compartments as a means of eavesdropping on the ongoing tumor-host communications. Active in-use kinase pathways can be reconstructed by evaluating linked intracellular phosphorylated kinase substrates. Communication between the tissue tumor cells and the downstream sentinel lymph node can be studied by molecular analysis of extracellular vesicles shed into the interstitial space between cells. This combined analytical approach has succeeded in generating predictors of complete pathologic response for personalized therapy. Moreover, understanding the network spatial topology can pinpoint therapeutic targets that may be oncogenic drivers. A second revolution currently underway is the development of synthetic molecular therapies. Based on recent advances in AI, and DNA/protein folding coding, it is now possible to rapidly synthesize a therapeutic molecule that matches the 3-D face of the therapeutic target. A successful version of this approach uses DNA origami as a backbone to present protein ligands matching the hot-spots of the therapeutic target. The artificial molecule can achieve high sensitivity and specificity because its specific 3-D shape is sculptured in silico and then mass produced. Thus, we can image a future in which tissue spatial analytics reveals candidate individual molecular targets specific to a tumor biospecimen. If no drug exists for the target, we can design a matching antagonist or agonist molecule tailored to that tumor’s functional driver.

Lightning Talk
Characterizing the Effects of Protein Glycosylation Perturbation on Phosphorylation Signaling
Effram Wei
Johns Hopkins University

Protein glycosylation and phosphorylation constitute two pervasive regulatory layers in mammalian cells, yet the effects that protein glycosylation play in phosphorylation signaling remain poorly understood. Here we show that controlled perturbation of N-linked glycan biosynthesis through glycoengineering fundamentally rewires phosphorylation signaling networks in human cells. Using comprehensive proteomics approaches, we simultaneously profiled the global proteome, glycoproteome, and phosphoproteome in engineered HEK293 cells designed to eliminate core fucosylation while enhancing sialylation and reducing GlcNAc branching complexity. Glycoengineering emerged as the dominant source of molecular variation across all datasets, with over 9,800 intact glycopeptides identified of which 3,400 are significantly altered, establishing a remodeled baseline cellular state. Upon serum stimulation, engineered cells not only exhibited markedly decreased phosphorylation responses compared to wild-type cells, but comprehensively re-wired to prefer signaling away from canonical EGFR/mTOR growth pathways. These findings establish a systematic framework for targeting glycosylation-phosphorylation regulation and nominate glycan-dependent signaling nodes as potential therapeutic vulnerabilities in glycosylation-remodeled disease states.