Summary
Erhard Hohenester is a structural biologist investigating the assembly, structure, and function of extracellular matrix. He is known for his work on laminins – huge proteins that are a key component of all basement membranes. His current research focuses on the enzymes in glycosaminoglycan biosynthesis. Erhard trained as a chemist in his native Austria and received his PhD in Biophysics from the University of Basel (Switzerland) in 1995. He joined Imperial College London in 1998 with a Wellcome Trust Senior Research Fellowship, which he held for 15 years. He currently is Director of Research in the Department of Life Sciences.
Selected Publications
Journal Articles
Niu M, McGrath M, Sammon D, et al., 2023, Structure of the transmembrane protein 2 (TMEM2) ectodomain and its apparent lack of hyaluronidase activity, Wellcome Open Research, Vol:8, ISSN:2398-502X, Pages:1-19
Sammon D, Hohenester E, Leitinger B, 2020, Two-step release of kinase autoinhibition in discoidin domain receptor 1, Proceedings of the National Academy of Sciences of the United States of America, Vol:117, ISSN:0027-8424, Pages:22051-22060
Briggs DC, Hohenester E, 2018, Structural Basis for the Initiation of Glycosaminoglycan Biosynthesis by Human Xylosyltransferase 1., Structure, Vol:26, ISSN:0969-2126, Pages:801-809.e3
Pulido D, Hussain S, Hohenester E, 2017, Crystal structure of the heterotrimeric integrin-binding region of laminin-111, Structure, Vol:25, ISSN:1878-4186, Pages:530-535
Briggs DC, Yoshida-Moriguchi T, Zheng T, et al., 2016, Structural basis of laminin binding to the LARGE glycans on dystroglycan, Nature Chemical Biology, Vol:12, ISSN:1552-4469, Pages:810-814