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An NMR-based structural study of sperm proteins reveals a novel protein packaging/dispersion system embedded in a coevolutionary arms race.

Transcriptional activation of the orphan nuclear receptor Nurr1 by ligands targeting its heterodimer partner retinoid X receptor alpha (RXRα) occurs through a nonclassical pharmacological mechanism involving ligand-binding domain protein-protein interaction inhibition.

A comprehensive allosteric model describes how inhibitors can activate rather than inhibit a target kinase by selectively driving formation of kinase dimers with one inhibited and one activated subunit.

A cargo recognition α-helix was identified in Nup358, which is required for activation of a dynein-dependent transport pathway that is essential for brain development.

The BPTF PHD finger is inhibited from binding the methylated H3 tails in the context of the nucleosome due to their robust interaction with the nucleosomal DNA, which can be modulated by additional histone PTMs.

Product release from human lysozyme is mediated by an intermediate state with transient weak interactions between the product and enzyme.

Structural and functional analyses reveal the general mechanism of activation of the thrombopoietin receptor and unravel the critical role of W515.

NMR spectroscopy has been used to explain a central unresolved issue of nuclear transport, namely how it can be both fast and specific.

The development of an integrative computational-experimental approach for identifying small molecules that can disrupt RNA:protein interactions in vitro and in cells led to the identification of several inhibitors of YBX1 in the micromolar range, including a previously approved drug.

Urinary metabolic signatures relate to adherence to the Mediterranean diet and ultra-processed food intake in childhood and reflect associations of these diet quality indicators with metabolic health.