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Gebhard Schertler on Muck Rack

Gebhard Schertler

Eidgenössische Technische Hochschule Zürich
As seen in: Nature, Science Magazine, Cell Press
Co Founder leadXpro and InterAx, Prof. for Structural Biology ETH, Head of Biology and Chemistry Devision PSI
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Articles

Factors modulating the assembly of human β 2 -adrenergic receptor–β-arrestin complexes

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By Florian Wilhelm, Kristyna Pluhackova, John Janetzko, Matthieu Masureel, Erin Marsh, Jesse Hudspeth, Gebhard Schertler, Brian K. Kobilka, Daniel Muller, Daniel Müller, Wenzel Gaßner
| Nature Verified
Abstract β-arrestins, pivotal regulators of G protein-coupled receptor (GPCR) signaling, assemble with hundreds of GPCRs. How this assembly rises to functionally distinct complexes in which β-arrestin engages the GPCR tail, core or both, remains a central question.
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Illuminating the molecular basis of human daylight vision

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By Grace A. Pan, Seok-Jin Kim, K.P. Lamers, Sarah Schmidt, Jakub Dostál, Saumik Sen, Andrej Hovan, Deborah Walter, Martin Appleby, Asato Kojima, Hideaki E. Kato, John Beale, Miroslav Kloz, Gebhard Schertler, Polina Isaikina
| Science Magazine Verified
Editor’s summary Structured Abstract Abstract Supplementary Materials References and Notes Information & Authors Metrics & Citations Check Access References Figures Tables Media Share Editor’s summary Human daytime vision relies on a trio of visual receptors called opsins, which are found in the cone cells in and around the central region of the retina.
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Advances of 3D microcrystals electron diffraction for transmembrane protein structure determination

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By Giorgia Fiorini, Gebhard Schertler, Valerie Panneels
| Cell Press Verified
Significance Determining the 3D structures of proteins is essential for understanding how they function. However, proteins structural biology is challenging, and the currently available methods used for structural studies have many limitations. Recent advances in a relatively new method, microcrystal electron diffraction (MicroED), have the potential to broaden the range of accessible targets for structural study.
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