Ellinor was born and raised in Sweden, received a dual Master of Science in Molecular Biology and Chemistry from Umeå University, Sweden, and obtained my Ph.D. at Stockholm University, Stockholm, Sweden, under the supervision of Professor Mikael Oliveberg. She joined Professor José Onuchic at University of California, San Diego, CA, and the Center for Theoretical Biological Physics (CTBP), and Professor Patricia Jennings in May 2010 as a postdoctoral research associate. She moved with Professor Onuchic to Rice University, and CTBP, TX, in May 2015. Ellinor joined the Chemistry Department at University of Hawai‘i at Mānoa in August 2018.

6. Bruno da Silva F, Simien JM, Viegas RG, Haglund E*, Barbanti Pereira Leite V (2024) Exploring the Folding Landscape of Leptin: Insights into Threading Pathways, J. Struc. Biol., PMID: 38065428

5. Noel JK, Haglund E* (2023) Identifying the folding transition state ensemble for pierced-lasso topologies, J Chem. Phys. B, PMID: 38118146

4. Haglund E* (2023) The Biological Implications of Threaded Protein Topologies, Accepted at the Chem. Engineer. Proc. Techniq.

3. Simien JM, Orellana GE, Phan HTN, Hu Y, Kurth EA, Ruf C, Kricek F, Wand Q, Smrcka VA, Haglund E* (2023) A Small Contribution to a Large System: The Leptin Receptor Complex, J Phys. Chem. B. 127, 11, 2457–2465, PMID: 36912891

2. Simien JM, Haglund E* (2021) Topological Twist in Nature, Trends Biochem. Sci. 2021;46(6):461-71, PMID: 33419636

1. Danielsson J, Noel JK, Simien J.M., Duggan B, Oliveberg M, Onuchic JN, Jennings PJ, Haglund E* (2020) The pierced lasso topology leptin has a bolt on dynamic domain
composed by the disordered loops I and III., J. Mol. Biol. 17;432(9):3050-3063, PMID: 32081588

Ellinor’s research is focused on the folding and function of proteins, utilizing both computational and experimental techniques to understand the molecular details of how proteins fold into biologically active molecules. Through her postdoctoral study she discovered a new class of “knot-like” motifs called pierced lasso topologies (PLTs). Interestingly, these threaded topologies exist in all kingdoms of life, with 14 different biological functions, and populate about 18% of known protein structures containing a disulphide bond. Ellinor’s research focuses on three strategically selected model systems (i) the pleiotropic hormone leptin and the leptin receptor, (ii) the oxidoreductase superoxide dismutase, and (iii) chemokine ligands and their cognate receptors. The long-term goal is to understand the biological relevance of its PLT and their role in human health and disease. Ellinor is inspired by how nature works and utilize my multidisciplinary training to answer questions at the interface of chemistry, biology, and physics.