A communication pathway linking memory processing and feeding behavior exists between the gut hormone ghrelin, the hippocampus and the hypothalamic neuropeptide orexin.

A combination of state-of-the-art biochemical, biophysical, and computational methods revealed that water molecules play a central role in signal propagation through G protein-coupled receptors.

A pooled genetic screening method measures the effect of knocking down every gene on a transcriptional stress response to proteotoxic stress (the heat shock response) using only nucleic acid sequencing, without cell enrichment or single-cell isolation.

Eukaryotic translation elongation factor 1A1 controls the process of heat shock response, from transcriptional activation of the HSP70 gene, to HSP70 mRNA stabilization, nuclear export, and translation.

Helitron transposable elements, by providing high density transcription factor binding sites upstream of host genes, have diversified the heat shock response within and among Caenorhabditis species.

The chaperones Hsp70 and Sis1 collaborate to repress the heat shock response and are both transcriptional targets of the heat shock response, yet only Hsp70 acts as a negative feedback regulator of the heat shock response.

Summation of metabotropic GABAergic responses remain linear even if most superficial layer interneurons specialized to recruit GABA_B receptors are simultaneously active.

The prolactin receptor, Janus kinase 2, and PI(4,5)P₂ form a co-structure with the membrane resulting in orientations with different accessibility fixing the disordered juxtamembrane domain of the receptor in an extended structure.

Hsp70 restricts DNA binding activity of Hsf1 to control the width and amplitude of the heat-shock regulon.