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The fate of glycoproteins in the endoplasmic reticulum whether they are directed toward folding or targeted to degradation depends on a tug of war between UGGT1 and EDEM family proteins.

The cyclic neuropeptide somatostatin binds to human Aβ1-42 through an interface that critically relies on a specific tryptophan, thereby blocking the propensity of Aβ to aggregate, a critical step in the pathobiology of Alzheimer's disease.

The important oncogene KRasG13C can be targeted by covalently binding nucleotide-analogues, resulting in a locked protein that can no longer induce oncogenic signaling.

DYRK1A, a kinase associated with intellectual developmental disorders and organ growth regulation, functions in cell growth by promoting mTORC1 activity.

A novel toxicophore, a 1H-1,2,3-triazole, has been identified in a wide-number of therapeutically-relevant compounds, including two anti-cancer chemotherapeutics, which inhibits mitochondria function and is mechanistically linked to adverse cardiac-cell events.

A virtual balancing task with parallel experiments on human and non-human primates revealed a spectrum of behaviors (classified by a computational model into position, velocity, or mixed control strategy) that can serve as basis for analyzing neural population dynamics.

The exon junction complex regulates the cell polarity determinant Discs large 1, which acts independently from its role in cell polarity to protect Dishevelled protein from lysosomal degradation in Wingless/Wnt signaling.

Computational pipeline SPICE systematically screens and predicts novel protein-protein binding complexes including the previously unrecognized global association and functional cooperation between IKZF1 and AP1.

Substrate recognition by a receptor protein tyrosine phosphatase is mediated by binding to its pseudophosphatase domain via a short helix that is >100 amino acids distant from the target phosphosite, uncovering principles of phosphatase substrate recognition and potential scaffolding functions.

Targeting the CRL5 ubiquitin ligase complex in combination with CDK9 or MCL1 inhibition could combat innate and acquired resistance of cancer cells to MCL1-targeting therapeutics.