Glycobiology Significant Achievement AwardThe Glycobiology Significant Achievement Award is given annually by Oxford University Press (publisher of Glycobiology) to honor new or mid-career scientists who have made key discoveries in their careers with the potential to have a substantial impact on the glycoscience community. 2026 Award Recipient
Oxford is delighted to present the 2026 Glycobiology Significant Achievement Award to Dr. Stacy Malaker. Stacy is a first-generation college student who grew up in metropolitan Detroit. She completed her undergraduate studies, earning degrees in biochemistry and anthropology-zoology at the University of Michigan, while also working two jobs—one at a bulk grocery store (where she won “Stocker of the Year”) and the other in a peptide synthesis core facility where she used mass spectrometry for quality control. She went on to earn a Ph.D. in chemistry at the University of Virginia in the laboratory of Dr. Donald Hunt. Dr. Malaker completed her postdoctoral training in the laboratory of Dr. Carolyn Bertozzi (Stanford University) and then went on to establish her own laboratory at Yale University in 2021. Her laboratory focuses on developing novel mass spectrometry approaches and chemical glycobiology tools to dissect mucin-domain glycoproteins and understand the broader implications of the glycocode. During her postdoc, Dr. Malaker performed seminal work identifying and characterizing enzymes that recognize and cleave proteins at sites where they are O-glycosylated. This discovery advanced the field by enabling the identification of proteins that are modified with these O-glycans and the mapping of specific sites of glycosylation. Prior to this discovery, it was difficult or impossible to identify many O-linked glycoproteins, making assessments of the biological roles of O-glycosylation challenging at best. Within her own laboratory, Dr. Malaker identified and characterized additional mucinases with unique abilities to detect and cleave O-glycoproteins, expanding the mapping of O-glycosites. hese tools enabled complete O-glycoproteomic mapping of the T-cell immunoglobulin and mucin-domain-containing (TIM) family of proteins (a class of checkpoint inhibitors), allowing a better understanding of how O-glycans influence the structure and function of these key immunological proteins. In addition to these enzymatic tools, she has developed several enrichment and separation techniques to enhance glycopeptide detection and has also optimized various search algorithms used in glycoproteomic analysis.
Her most recent work has focused on developing combined MALDI-MS and LC-MS approaches to map mucins, highly O-glycosylated proteins that are associated with the development and progression of many different types of cancer. Mapping mucins has heretofore been nearly impossible given their heavily glycosylated, repetitive regions rich in threonine and serine. However, Dr. Malaker’s work has resulted in the near-complete mapping of MUC2, the major mucin that lines and protects our intestinal system. This coupled MS approach revealed a striking stratification of different glycoforms in different regions of two colorectal mucinous adenocarcinomas. These approaches have advanced the field of mucin biology well beyond what was previously thought possible.
In addition to revolutionizing approaches to detect and map O-glycoproteins, Dr. Malaker’s laboratory is actively investigating the biological impact of O-glycosylation, with recent work in mucosal biology, immunology and inflammatory disease. Her work has been published in Cell, PNAS, Molecular Cell, Nature Communications, Nature Methods and Analytical Chemistry. Thus, her research has served to democratize the field as well as open new areas of investigation into the biological roles of O-glycoproteins. |
