Roland Riek

This paper introduces LDDM, a generative model for drug design that produces synthetically accessible compounds validated experimentally for five protein targets.

The paper uses cryo-EM to determine amyloid fibril structures of a truncated alpha-synuclein construct, revealing disease-like motifs without forming the Parkinson's Disease polymorph.

This study investigates factors influencing the formation of α-synuclein amyloid fibrils at atomic resolution using cryo-electron microscopy.

This study shows that alpha-synuclein fibrils cause mitochondrial-derived vesicle budding and structural changes in mitochondria, linking alpha-synuclein aggregation to mitochondrial toxicity.

This paper develops a method to quantitatively analyze the structural states of alpha-synuclein in vitro and in situ, revealing conformational changes in yeast and human neurons.

This study shows TNF-α disrupts the malate-aspartate shuttle in iPSC-derived enteric neural cells from PD patients, causing metabolic shifts and mitochondrial dysfunction, which can be reversed by targeting glutamate metabolism.

This study identifies structural and functional differences in alpha-synuclein fibrils from Parkinson's disease, Dementia with Lewy Bodies, and Multiple System Atrophy, linking these differences to disease-specific cellular responses and potential therapeutic targets.

The paper identifies oxidized MIF as a drug target that links HSV-1 infection and external stressors to tau pathology in Alzheimer's disease.

FragmentScope uses learned protein surface representations to guide fragment placement and small molecule design, achieving accurate placement and promising lead compounds.

This paper designs phosphorylation-induced protein switches that control transcription in cells, demonstrating their functionality in synthetic signaling.

This study systematically identifies structure-specific protein-protein interactions using LiP-MS, demonstrating its application to alpha-synuclein in Parkinson's disease.

This paper introduces a structural proteomic pipeline to study anti-amyloidogenic compounds' mechanisms in vitro and in situ, revealing off-target effects and structural interactions with α-Synuclein.

This paper demonstrates non-invasive whole brain imaging of tau deposits using vMSOT and PBB5 probe in P301L mice, showing specific binding and retention in tau-laden regions.

This study detects cerebral tauopathy in P301L mice using large-field multifocal illumination fluorescence microscopy and a fluorescent ligand, showing increased probe retention in affected mice.

This study shows that α-synuclein undergoes liquid-liquid phase separation, which transitions to solid amyloid fibrils, contributing to Parkinson's disease pathogenesis.

The paper reports two new polymorphic structures of alpha-synuclein fibrils solved by cryo-EM, showing distinct structural features and interactions compared to previous structures.

The paper reports the cryo-EM structure of alpha-synuclein fibrils, revealing key features relevant to disease mechanisms and therapeutic design.