S. S. Taylor

This study identifies the αC-β4 loop as a key regulator of allosteric cooperativity between nucleotide and substrate in PKA-C through simulations and mutagenesis experiments.

This study identifies molecular determinants of PKA RIα phase separation and shows how it regulates cAMP compartmentation and PKA-C spatial restriction.

This study uses simulations and HDX-MS to analyze how two LRRK2 inhibitors affect the protein's conformational dynamics and kinase activity.

This study compares habitat suitability models for Golden-winged Warblers using structured survey data and community science data, finding similar performance and identifying road density as a key landscape variable.

The paper applies molecular-dynamics simulations to macromolecular crystallography to refine protein structures and improve interpretation of electron density.

The paper identifies two helices that regulate the conformation and function of the kinase domain in LRRK2 through dynamic crosstalk.

This study identifies a PKA inhibitor motif in Smoothened that blocks PKA activity, enabling GLI activation in the Hedgehog pathway, revealing a mechanism similar to the Wnt cascade.

SCA14 driver mutations in PKCγ impair autoinhibition, with defect correlating inversely with age of disease onset.

This study shows that TP53 loss in fallopian tube epithelial cells drives chromosomal instability through cell cycle deregulation, without requiring additional mutations.

This paper classifies ovarian cancer cell lines into five subtypes using transcriptional profiles, aligning with known pathological subtypes and providing a method for future classification.

This study investigates how Parkinson's Disease mutations affect LRRK2 activation and subcellular localization through conformational changes and domain interactions.

This study compares two Bub1 kinase inhibitors, finding that BAY-320 inhibits Bub1 in vivo but with high concentrations and potential off-target effects, while 2OH-BNPP1 is ineffective.

The paper investigates how cAMP binding regulates PKA through asymmetric allosteric coupling, identifying a new cAMP-responsive switch that acts as a signaling hub.