Protein interactions: who is partying with whom and who is ruining the party?

New method for investigating protein interaction networks - also of interest for pharmaceutical research

18-Oct-2024 - Inside cells, it's like in a packed dance club: hundreds are partying. Some keep to themselves, others make their way through the crowd, chatting to everyone they meet. Some just say a quick hello, others stay with their best friends. In this club, there are all kinds of different interactions ...

Harnessing the organisation of the cell surface

07-Dec-2021 - Scientists at ETH Zurich have developed a new method to determine how proteins are organised on the surface of cells. Insights gained with the technology could lead to the development of novel drugs to fight cancer. Biological cells have multiple functions, and they need to communicate with each ...

Researchers film fundamental life process

Study provides more detailed insights into the formation of ribosomes

29-Oct-2021 - All proteins in a cell are assembled by complicated molecular machines. The precursors of these ribosomes are produced in the cell nucleus and then enter the cell through the so-called nuclear pores. Researchers at the University of Bonn and ETH Zurich have now filmed this fundamental process in ...

Mechanism discovered how the coronavirus hijacks the cell

A starting point for vaccine and drug development

15-Sep-2020 - Researchers at ETH Zurich and the University of Bern have discovered a mechanism by which the corona virus manipulates human cells to ensure its own replication. This knowledge will help to develop drugs and vaccines against the corona virus. Like a pirate hijacking a ship, a virus takes control ...

Healthy organelles, healthy cells

02-Oct-2019 - It has recently become clear just how important membraneless organelles are for cells. Now biochemists at ETH Zurich have discovered a novel mechanism that regulates the formation of these organelles. This has laid the foundation for more targeted research into diseases such as Alzheimer’s or ...

New tool for structural biology

New method of crystallising large membrane proteins

08-Mar-2018 - ETH researchers have developed a new method of crystallising large membrane proteins in order to determine their structure. This will be of benefit to biological research and the pharmaceutical industry. Membrane-embedded proteins are an essential part of cells and any form of life. They not only ...

Sticking sugar to protein

Researchers clarified the 3D structure of an important enzyme that links sugar to proteins – a breakthrough

09-Feb-2018 - Whenever cells receive signals, interact with other cells or identify viruses and bacteria, the process involves not only proteins but also sugar chains attached to their surface. The subject of relatively little attention until now, these structures differ widely in composition and branching, ...

Measuring molecular interactions

Previously unknown interactions between proteins and small metabolic molecules discovered

02-Feb-2018 - ETH researchers have used a new approach to discover previously unknown interactions between proteins and small metabolic molecules in bacterial cells. The technique can also be used to test the effect of medications. Science now has a new “omics” – an interactomics, which deals with the ...

More inflexible than imagined

29-Aug-2017 - Oligosaccharides – chains of sugar building blocks – are essential for biological cells. Scientists had thought that these molecules were freely mobile, but an international research team has now shown that such sugar molecules can form rigid structures, previously found only in DNA and ...

Vigilin, the lock keeper

Researchers have discovered a molecule in liver cells that controls the release of fat

29-Sep-2016 - ETH researchers have discovered a molecule in liver cells that controls the release of fat into the bloodstream. This “lock keeper” is present in large quantities in overweight people and leads indirectly to vascular narrowing. Anyone attending Munich’s famous Oktoberfest will know it can leave ...