S. C. Blacklow

This study determines the structure of PP2A/B55 inhibited by IER5-N50 and shows its role in suppressing pTau dephosphorylation and KRT1 expression.

This study tracks Notch and Delta interactions in real-time, showing 1:1 stoichiometry at synapses and NICD nuclear entry after 45 minutes, inhibited by signaling blockers.

This study maps B cell co-receptor signaling dynamics using proximity labeling and mass spectrometry, identifying new mediators of B cell activation and metabolic reprogramming.

This study determines the cryo-EM structure of ADAM10-Tspan15 complex, revealing how Tspan15 relieves autoinhibition and positions the active site for membrane-proximal substrate cleavage.

The paper reports the cryo-EM structure of ADGRF1, revealing structural features that explain its preference for Gq signaling over Gs.

The paper profiles tethered agonist (TA) signaling in all 33 human aGPCRs using a platform across assays, revealing heterogeneous responses and aligning with AlphaFold2 predictions.

This study develops DeltaMAX, an affinity-matured DLL4 ligand that broadly activates or inhibits Notch signaling in human and murine systems.

This paper develops a SHP2 PROTAC that degrades SHP2 in leukemic cells, inhibits MAPK signaling, and suppresses cancer growth.

The paper identifies IER5 as a Notch-induced DNA-damage response gene required for squamous cell differentiation and shows its interaction with PP2A subunit PPP2R2A.

This study shows that CD81 controls CD19 trafficking to the cell surface through a dynamic interaction, with implications for B cell function and tetraspanin biology.

This study identifies the molecular mechanism by which NRARP inhibits Notch signaling by binding to the NTC complex and disrupting its function.

This study develops a covalent inhibitor of gut bacterial bile salt hydrolases, showing it reduces BSH activity and deconjugated bile acids in mice.

The paper uses time-resolved phosphoproteomics to analyze SHP2's role in EGFR signaling, identifying distinct phosphotyrosine response patterns upon SHP099 treatment.

This paper introduces a flow extension tethered particle motion assay to study single-molecule proteolysis, enabling accurate assessment of protease activity by excluding multiply-tethered beads.