Adrienne W. Paton

Induction of the ISR by AB5 subtilase cytotoxin drives IFN-I expression in pDCs via STING activation

The paper shows SubAB induces IFN-I in pDCs via STING activation and UPR, highlighting a novel mechanism of immune regulation.

Simple and practical sialoglycan encoding system reveals vast diversity in nature and identifies a universal sialoglycan-recognizing probe derived from AB5 toxin B subunits

The paper introduces a 9-digit code system for sialyltrisaccharides, revealing vast sialoglycan diversity and identifying a universal probe from AB5 toxin B subunits.

Stress-induced protein disaggregation in the Endoplasmic Reticulum catalysed by BiP

The paper shows that ER stress activates a protein disaggregation system catalyzed by BiP, resolving aggregates in the ER using a novel live-cell monitoring method.

Rapid evolution of bacterial AB5 toxin B subunits independent of A subunits: sialic acid binding preferences correlate with host range and toxicity

The paper shows bacterial AB5 toxin B subunits evolve rapidly and independently of A subunits, with sialic acid binding preferences linked to host range and toxicity.

Factor VIII exhibits chaperone-dependent and glucose-regulated reversible amyloid formation in the endoplasmic reticulum

This study identifies factors causing FVIII aggregation in the ER and shows that chaperones and glucose metabolism regulate its solubility and secretion.

SMRT sequencing reveals differential patterns of methylation in two O111:H- Shiga toxigenic Escherichia coli isolates from a historic hemolytic uremic syndrome outbreak in Australia

This study uses SMRT sequencing to compare the methylome of two STEC isolates, identifying differential methylation patterns linked to regulatory differences.

Intermolecular Disulfide-Bond Formation In Human FICD Modulates The Activity Of The Hyperactive E234G Mutant

This paper shows that FICD's adenylyltransferase activity induces ER stress and that its disulfide-bond formation modulates its activity in the context of a hyperactive mutant.