Methodology for the in vitro assembly of multimeric membrane proteins and the utility of the approach for generating heteromeric variants of homo-multimeric proteins is described.

Despite the known heme attachment motif (CXXCH) in all c-type cytochromes, attachment elements recognized by human and bacterial cytochrome c biogenesis pathways are distinct, providing clear targets for differential inhibitors.

Theoretical analysis and in vitro reconstitution of a biological reaction-diffusion system identify key functional motifs as well as underlying principles and enable rebuilding pattern formation in a modular fashion.

Development of an enrichment method to facilitate RNA-sequencing of the Lyme disease pathogen from inside of ticks during a bloodmeal provides new candidates for genes important for disease transmission.

An in vitro reconstitution assay reveals stoichiometric levels of the short form of Opa1 work together with the long form of Opa1 to mediate efficient and fast membrane pore opening.

A new in vitro approach allows measurement of the efficiency of the early steps of translation initiation on every messenger RNA in yeast simultaneously.

The endoplasmic reticulum (ER) folding sensor UGGT1 essentially cooperates with the peptide editor TAPBPR to provide quality control of MHC I molecules in the antigen presentation pathway.

In rotaviruses, the selective packaging of eleven distinct genomic RNA segments requires virus-encoded protein NSP2 to alter the RNA structures, facilitating their interactions with each other.

Reproductive fluids help the correct establishment of some epigenetic marks and gene expression in preimplantation pig embryos.

Starfish feed by everting their stomach out of their mouth over prey and, interestingly, this unusual feeding mechanism is inhibited by substances similar to hormones that regulate feeding in humans.