Sara Snogerup Linse

This study investigates how DNAJB6b binds to Aβ42 fibrils and inhibits amyloid elongation, providing a quantitative mechanism for its role in suppressing amyloid formation.

This study shows that sequence imperfections in synthetic Aβ42 peptides cause differences in aggregation behavior compared to recombinant Aβ42.

The paper identifies potent CB2R antagonists from a peptide library that inhibit gut homing in a mouse model of Crohn's disease.

This study shows that structural defects in amyloid-β fibrils are key sites for secondary nucleation, suggesting new strategies for drug design to inhibit amyloid disorders.

This paper investigates how aducanumab binds to Aβ1-42 fibrils, showing it preserves the fibril core structure while altering N-terminal dynamics and reducing secondary nucleation.

The paper develops an in vitro tau aggregation assay combined with machine learning to identify polymorph-specific tau inhibitors, validated in a Drosophila model.

This study identifies secondary nucleation of α-Synuclein as the key mechanism driving mitochondrial dysfunction and Lewy body formation in Parkinson's Disease.

This study uses PICUP to identify transient α-synuclein contacts in different conformational states, revealing state-specific interactions in solution, membrane-bound, and fibril forms.

This paper shows that Alzheimer's amyloid-beta peptide forms biomolecular condensates on lipid bilayers, accelerating amyloid aggregation and revealing a new early step in the disease mechanism.

This study investigates how lipid membranes influence the equilibrium between free and membrane-bound α-synuclein and its amyloid formation, revealing conditions that promote or inhibit aggregation.

This study generates Aβ42 oligomers in human iPSC-derived neurons to model Alzheimer's disease and assess inhibitor effects.

This study shows α-synuclein oligomers form via secondary nucleation on fibril surfaces, not from monomers, and this process is enhanced by agitation under physiological conditions.

This study reveals that lipids promote α-synuclein aggregation by enabling elongation, using a kinetic model to describe the co-aggregation process in vitro.

The paper investigates A{beta}42 fibril self-replication using statistical mechanics and modeling, finding replication occurs on isolated small catalytic sites on the fibril surface.

This study investigates how different lipid membrane models affect Aβ42 aggregation kinetics in vitro, showing inhibition by ER and Golgi membranes.

This study identifies small molecules that inhibit alpha-synuclein aggregate proliferation using structure-based and kinetic assays.

The paper investigates self-replication in protein aggregates, finding it common in both functional and pathological contexts, with disease-related aggregates replicating faster than biological ones.

This study shows that Staphylococcus aureus PSM peptides catalyze alpha-synuclein aggregation, potentially linking the microbiome to Parkinson's disease pathology.

This study investigates the dynamics of Aβ42 oligomers during amyloid fibril formation, revealing that most oligomers dissociate into monomers rather than forming fibrils.

This study uses kinetic analysis and binding measurements to compare four anti-Aβ antibodies, showing aducanumab uniquely reduces Aβ oligomer flux.

This study develops a kinetic theory to identify thermodynamic and kinetic signatures of effective protein aggregation inhibitors.

This study identifies galectin-3 as a novel endogenous TREM2 ligand that regulates microglial activation and Aβ fibrillation in Alzheimer’s disease.