Ulrich H. E. Hansmann

The paper uses molecular dynamics simulations to study how D-Retro-Inverso peptides modulate TTR fibril stability and identifies DRI-K6V as a potential disruptor of TTR fibrils.

The paper uses molecular dynamics simulations to investigate if SARS-CoV-2 peptides can initiate TTR tetramer dissociation, leading to amyloidosis.

The paper designs and evaluates D-amino acid-based peptides to inhibit SAA3 fibril formation in a mouse model of cardiac amyloidosis.

This study uses molecular dynamics simulations to show that SARS-COV-2 protein fragments alter α-synuclein dimer conformations, favoring rod-like fibrils over twister-like structures.

The paper investigates how a SARS-CoV-2 Spike protein fragment interacts with Aβ1-42 monomers and fibrils using molecular dynamics simulations.

This study identifies that Podoplanin-expressing mesenchymal stromal cells release exosomes that trigger SAA3 overproduction in macrophages, leading to cardiac amyloidosis after myocardial infarction.

This study shows that lipid II in bacterial membranes stabilizes pores formed by nisin, enhancing its antimicrobial effect by altering membrane properties.

This study investigates the conformational interconversion between native and fibril forms of SAA1-76 using Replica-Exchange-with-Tunneling, finding low energy barriers and identifying a critical salt bridge for fibril formation.

This study compares the stability of regular amylin fibrils with DRI-amylin fibrils, finding differences in hydrogen bonding and fibril stability when interacting with regular amylin.