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Kelleher, K.

Publications and source records attributed to Kelleher, K..

2 recordsLinked to original sources

SCOPE: Revealing Hidden Mechanisms in Phenotypic Screens Through Target and Pathway Enrichment

Phenotypic screening enables discovery of small molecules without requiring predefined targets, but mechanistic interpretation remains challenging due to polypharmacology and pathway complexity. We developed SCOPE (Screening Compound Ontology for Pathway Enrichment), a KNIME-based computational framework that resolves the molecular drivers of phenotypic activity by linking compound-level screening data to annotated targets and pathways. SCOPE integrates multi-source target annotations and performs statistical enrichment to identify shared mechanisms of action. Applied to a high-throughput screen for modulators of ER-stress induced secretion of endoplasmic reticulum (ER) resident proteins, a process known as exodosis, SCOPE identified calcium signaling as the most enriched KEGG pathway without prior biological context. Target enrichment revealed G protein-coupled receptors (GPCRs) involved in inositol 1,4,5-trisphosphate receptors (IP3Rs)-mediated signaling, with widespread antagonism among hit compounds implicating this pathway in the regulation of exodosis. Notably, SCOPE uncovered a novel role for the histamine receptor HRH1, which was validated by RNAi knockdown and pharmacological inhibition, implicating HRH1 as a potential therapeutic target in ER stress-related disorders. These results highlight SCOPEs potential to deconvolute phenotypic screens and uncover actionable mechanisms in complex cellular systems.

bioinformatics↗

Discovery of conformation-sensitive anti-amyloid protofibril monoclonal antibodies using an engineered chaperone-like amyloid-binding protein

The hypothesis that amyloid beta peptides (A{beta}) are central to the pathogenesis of sporadic Alzheimers disease (AD) is still hotly debated. Although several monoclonal antibodies (mAbs) against A{beta} have failed in therapeutic clinical trials, two conformation-selective, anti-A{beta} mAbs continue to show promise. A significant challenge has been to discover mAbs that preferentially target A{beta} protofibrils over natively-folded monomeric peptides or amyloid plaques. We have engineered a novel chaperone-like amyloid-binding protein (CLABP), Nucleobindin 1 (NUCB1), which enables the stabilization of protofibrils, allowing them to be used as immunogens in mice to facilitate the generation of mAbs that recognize A{beta} protofibrils. An immunization campaign and subsequent screening funnel identified a panel of mAbs with high-affinity to A{beta}. Two mAbs in particular, 1A8 and 7C8, displayed significant conformation sensitivity and preferentially bound A{beta} protofibrils over monomers. Furthermore, 1A8 delayed A{beta} aggregation, but did not prevent eventual fibril formation, while 7C8 significantly and dose-dependently reduced fibril formation by inhibiting both primary and secondary nucleation. Both mAbs protected against protofibril-induced cytotoxicity in vitro, and showed distinctive staining patterns by immunohistochemistry in PS1/APP mice and in post-mortem AD brain tissue. In summary, we describe a novel method to stabilize soluble A{beta} protofibrils for use in immunization campaigns. We hypothesize that the stabilized protofibrils retain the neoepitopes of the A{beta} protofibril and the aggregates found in mouse models of disease and post-mortem AD brain tissue.

molecular biology↗