Awardees' Articles

HFSP Long-Term Fellow Daniel Koster and HFSP Program Grant holder Uri Alon and colleagues

Tuesday 18th December 2012

Bacteria are usually studied in well-mixed environments such as in shaken tubes or chemostats. However, bacteria often live on surfaces and migrate in space while they grow. The growth laws of such planar bacterial populations have been less studied. Here we employ a novel method for quantifying growth and gene expression in space and time and find that motile bacteria expand outward and continuously leave a portion of the population behind. The advancing bacteria grow and keep their density constant...


HFSP Long-Term Fellow Noam Stern-Ginossar and colleagues

Monday 17th December 2012

A closer look at the human cytomegalovirus genome uncovers many novel viral open reading frames.


HFSP Cross-Disciplinary Fellow Sabine Hauert and colleagues

Thursday 13th December 2012

Small interfering RNAs (siRNAs) are used to decrease the production of specific proteins in cells and promise new types of therapies to treat tumors. The challenge is to design drug-delivery tools capable of specifically transporting siRNAs to cancer cells. This paper systematically explores a variety of nanocomplex designs and identifies key criteria that allow them to enter cells and release siRNA cargo.


Review by HFSP Program Grant holders Henk Haagsman and Annelise Barron and colleagues

Monday 10th December 2012

Our paper highlights recent advances in the field of microfabricated encapsulating devices, emphasizing the development of emulsifying encapsulations, device design and current assays that are performed using encapsulating droplets on microfluidic chips.


HFSP Program Grant holders Ignacio Tinoco and Harry Noller and colleagues

Friday 7th December 2012

The synthesis of a protein requires that the ribosome unwinds structures at the 5'-end of the messenger RNA to prevent inhibition of the translation initiation. Ribosomal protein S1 reversibly binds single-stranded RNA in steps of two or three nucleotides to uncover the site for ribosome binding and subsequent translation.


HFSP Young Investigator Grant holders Adam Engler and Guiseppe Battaglia and colleagues

Monday 3rd December 2012

Just like the bones that support your body, your cells have their own scaffolding to hold them up. This scaffolding, known as the extracellular matrix or ECM, not just props up cells but also provides attachment sites, or “sticky spots”, to which cells can bind, just as bones hold muscles in place.


HFSP Career Development Award holder Gregory Vert and colleagues

Thursday 29th November 2012

Our research has revealed distinct signaling pathways in the model plant Arabidopsis that control iron-deficiency responses and further highlights the complexity of the networks driving plant responses to low iron nutrition. Understanding how plants deal with iron deficiency is critical to human nutrition because vegetarian diets based on iron deprived crops may enforce anemia.


HFSP Career Development Award holder Ilona Grunwald-Kadow and colleagues

Thursday 22nd November 2012

The formation of neuronal networks relies on the proper development and targeting of the neurons within. The actin cytoskeleton plays an important role during the process of axon guidance. The non-catalytic subunit of the Drosophila NatB complex, Psidin, is essential to maintain the actin cytoskeleton in a dynamic and responsive state. At the same time Psidin, together with the catalytic part of the NatB complex, is required for the survival of neurons.


HFSP Cross-Disciplinary Fellow Fernando Montealegre-Z and colleagues

Friday 16th November 2012

A newly identified hearing organ in a South American bush cricket, which possesses one of the smallest ears known, shows insect hearing is so sophisticated that it rivals our own. The study, published in Science, is the first to identify a hearing mechanism in an insect that is evolutionarily convergent to those of mammals.


HFSP Program Grant holders Derek Woolfson, Heiner Linker, Nancy Forde, Paul Curmi and colleagues

Tuesday 13th November 2012

There are many examples of peptides that self-assemble to form long, fibrous structures. Forming closed assemblies is more difficult. This HFSP-funded study shows that two α-helical peptides can be joined by a series of peptide linkers of different lengths to form a range of new peptide assemblies. The structure formed depends on the length of the linker employed, with short linkers favoring fibers and the longer linkers leading to closed nanostructures.