Awardees' Articles

HFSP Long-Term Fellow Christof Gebhardt and colleagues

Tuesday 18th June 2013

Signals from individual fluorescent proteins in a cell nucleus are generally overwhelmed by out-of-focus background in common microscopy. We developed a microscopy method that restricts fluorescence excitation to a small horizontal nuclear section and thus enables fast single molecule imaging in living mammalian cells.

 

HFSP Long-Term Fellow Tim Lämmermann and colleagues

Friday 7th June 2013

Which molecules direct neutrophil swarm formation at sites of tissue damage and infection? We employed intravital microscopy of skin and lymph nodes to analyze neutrophil swarming upon sterile tissue injury and infection in mice, provide an initial molecular map of the factors that contribute to the coordinated neutrophil movement and aggregation, and show that “swarm”-like intercellular communication exists between neutrophils in the living tissue.

 

HFSP Cross-Disciplinary Fellow Marija Zanic and colleagues

Friday 31st May 2013

Microtubules formed from purified tubulin in the test tube typically grow much more slowly than those in cells. In this study, we identified a minimal system, consisting only of tubulin and two regulatory proteins, sufficient to promote microtubule growth to cellular rates.

 

HFSP Career Development Award holder Patrick Müller and colleagues

Thursday 23rd May 2013

How do the molecules that regulate embryo development end up in the right place at the right time? We examined several current theories and suggest that diffusion-based mechanisms are the most commonly used during development.

 

HFSP Long-Term Fellow César Nombela-Arrieta and colleagues

Monday 13th May 2013

Hematopoietic stem cells reside in specific bone marrow niches, which are thought to be low in oxygen content. We employed advanced quantitative imaging techniques to comprehensively analyze the spatial distribution of stem and progenitor cells in the bone marrow, describe their interaction with distinct types of blood vessels, and determine that their characteristic hypoxic status is not dictated by localization in specific regions but is rather physiologically inherent to the hematopoietic stem...

 

HFSP Long-Term Fellow Bastien Boussau and colleagues

Tuesday 30th April 2013

Genomes are often analyzed in a historical, evolutionary framework. To establish this framework, we have developed a new method that reconstructs both gene trees and species trees with high accuracy.

 

HFSP Program Grant holders Maxime Dahan, Yohanns Bellaiche and Jacob Piehler and colleagues

Thursday 25th April 2013

Cellular functions like migration or division rely on the orchestration of different signaling networks both in time and in the intracellular space. While many tools have been developed over the years to observe these activities within the cell, only a few are able to create local and controlled biochemical activities inside cells. We have designed such a technique, based on magnetic nanoparticles, allowing the activation of signaling networks at the subcellular scale with an unprecedented spatiotemporal...

 

HFSP Long-Term Fellow Alphée Michelot and colleagues

Monday 15th April 2013

Cells often have partially redundant mechanisms to perform cellular functions, which can be an obstacle in deciphering molecular functions in a single mutant background. In this study, we were interested in determining how yeast cells control the elongation of actin filaments in endocytic actin networks and we successfully identified three partially overlapping mechanisms.

 

HFSP Long-Term Fellow Joseph Marsh and colleagues

Thursday 11th April 2013

The assembly of proteins into complexes underlies a wide variety of biological processes. By combining mass spectrometry experiments with large-scale analyses of protein structure, protein interaction and genome sequence data, we found that protein complexes have experienced evolutionary selection to assemble via well-defined, ordered pathways.

 

HFSP Long-Term Fellow Franz Hagn and colleagues

Thursday 4th April 2013

Structural studies of membrane proteins are still hampered by difficulties in finding appropriate membrane mimicking media that maintain protein structure and function. A novel membrane system, called phospholipid nanodiscs, consisting of a patch of lipids surrounded by two copies of a lipid-binding protein, recently became popular in the membrane protein field. In this system, membrane proteins can be investigated in a real detergent-free and native-like lipid environment. Smaller nanodiscs tailored...