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Martin W. Hetzer

Martin W. Hetzer


NOMIS Project(s)

Martin W. Hetzer is a NOMIS board member and the president and CEO of the Institute of Science and Technology Austria (ISTA). He led the Determining Biological Age in Humans project.

Hetzer received his PhD in biochemistry and genetics from the University of Vienna (Austria), and completed postdoctoral work at the European Molecular Biology Laboratory (EMBL; Heidelberg, Germany). He joined the faculty at the Salk Institute for Biological Studies (La Jolla, US) in 2004 and became a full professor in 2011. He has received numerous awards, including a Pew Scholar Award, an Early Life Scientist Award from the American Society of Cell Biology, a Senior Scholar Award for Aging from the Ellison Medical Foundation, a Senior Scholar Award from the American Cancer Society, a Royal Society Research Merit Award and the Glenn Award for Research in Biological Mechanisms of Aging. Hetzer was the Jesse and Caryl Philips Professor of Molecular and Cell Biology and the director of the Waitt Advanced Biophotonics Center at the Salk Institute until 2023, when he was appointed president and CEO of ISTA.

His research focuses on fundamental aspects of organismal aging with special emphasis on the heart and central nervous system. His laboratory has also made important contributions to the field of cancer research and cell differentiation.

Martin W. Hetzer | Awards Film

Martin W. Hetzer | Insights Film

Martin W. Hetzer's News

NOMIS board member Martin Hetzer has been appointed president of the Institute of Science and Technology Austria, a NOMIS partner institution, effective January 2023. Hetzer is currently a senior vice […]

Salk scientists tackle COVID-19 pandemic with innovative research projects on immunity, vaccine development, viral imaging and more LA JOLLA—As the COVID-19 pandemic continues across the globe, the Salk Institute joins […]

Martin W. Hetzer's Insights

Abstract: During apoptosis, caspases degrade 8 out of ~30 nucleoporins to irreversibly demolish the nuclear pore complex. However, for poorly understood reasons, caspases are also activated during cell differentiation. Here, we show that sublethal activation of caspases during myogenesis results in the transient proteolysis of four peripheral Nups and one transmembrane
Abstract: The LINC complex tethers the cell nucleus to the cytoskeleton to regulate mechanical forces during cell migration, differentiation, and various diseases. The function of LINC complexes relies on the interaction between highly conserved SUN and KASH proteins that form higher-order assemblies capable of load bearing. These structural details have emerged