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Multi-site FRET measurements of moPrP oligomerization at low pH indicate that major conformational changes take place as monomers reversibly transform into large oligomers, which subsequently disassemble reversibly into small oligomers.

Ceapins specifically inhibit the unfolded protein sensor ATF6α by directly tethering the cytosolic domain of ATF6α to ABCD3 in cells and in vitro.

Modern microorganisms growing in fossils provide major challenges for researchers trying to detect ancient molecules in the same fossils.

The modularity and unequivocal input/response of Notch signaling are harnessed to measure cell-surface shedding of diverse transmembrane receptors to identify new proteolytic switches and detect modulation of proteolysis by therapeutics.

By increasing intracellular cysteine levels, NRF2 engages a tumor suppressive metabolic pathway mediated by cysteine dioxygenase 1.

Subterranean fossil bone hosts a living microbiome different from the surrounding sediment without evidence of original protein preservation.

Integrated experimental-computational approaches were implemented to reveal the dynamic conformational landscape of a biologically relevant protein methyltransferase SETD8 for functional annotation.

Unique methodology was used to generate a large HDX-MS dataset to inform ligand-mediated activation of RORγ, an approach that can be extended to other nuclear receptors with unresolved ligand-dependent activities.

Mass spectrometry analysis of purified pre-ribosomal RNAs shows that stable ribosomal RNA domains independently recruit assembly factors, and the cryo-EM structure of the 5' ETS ribonucleoprotein reveals regulatory conformational switches.

Absolute quantification of CTCF and cohesin reveals quantitative constraints on 3D genome organization and illuminates the molecular architecture of the cohesin complex.