Robert H. Mach

In vivo imaging of reactive oxygen species after myocardial ischemia-reperfusion injury: a large animal multimodal imaging and transcriptomic study

This study uses multimodal imaging and transcriptomics to show increased reactive oxygen species activity in myocardial tissue and systemic organs after myocardial infarction, with associated gene expression changes.

Genetic Code Expansion and Enzymatic Modifications as Accessible Methods for Studying Site-Specific Post-Translational Modifications of Alpha-Synuclein and Tau

The paper provides methods for site-specific post-translational modification of alpha-synuclein and tau using genetic code expansion and enzymatic approaches, enabling studies of their structural dynamics and aggregation.

Complementary Structural and Chemical Biology Methods Reveal the Basis for Selective Radioligand Binding to α-Synuclein in MSA Tissue

The paper uses structural and chemical biology methods to show EX-6 binds selectively to α-synuclein fibrils in MSA tissue, with a 10-fold preference over PD tissue.

A Small-molecule Antagonist Radiotracer for Positron Emission Tomography Imaging of the Mu Opioid Receptor.

This paper designs and characterizes non-agonist ligands for the mu opioid receptor, identifies a radiotracer [11C]1A for PET imaging, and demonstrates its brain uptake and receptor specificity in rhesus macaques.

ROStrace detects oxidative stress in vivo and predicts progression of Alzheimer's disease pathology in APP/PS1 mice.

This paper demonstrates that [18F]ROStrace PET imaging detects oxidative stress in APP/PS1 mice and correlates with amyloid burden, predicting Alzheimer's disease progression.

The Sigma-2 Receptor/TMEM97, PGRMC1, and LDL Receptor complex are responsible for the cellular uptake of Aβ42 and its protein aggregates

This study identifies the Sigma-2 receptor/TMEM97, PGRMC1, and LDLR complex as a pathway for Aβ42 uptake in neurons, both with and without apoE, suggesting it as a potential therapeutic target for Alzheimer's disease.

Poly(ADP-ribose) induces α-synuclein aggregation in neuronal-like cells andinteracts with phosphorylated α-synuclein in post mortem PD samples

This study shows that PAR promotes α-synuclein aggregation and interacts with phosphorylated α-synuclein in Parkinson's disease samples.