G. S. Kaminski Schierle

The paper investigates how fusogenic liposomes interact with Gram-negative and Gram-positive bacterial envelopes using microscopy, revealing differences in fusion and delivery mechanisms.

This study investigates how mutant FUS protein accumulation affects cytoskeletal, organelle, and cellular homeostasis, linking it to cellular aging and potential senescence mechanisms.

ERnet quantifies ER topology dynamics using video-rate super-resolution imaging and semantic segmentation, enabling analysis of ER morphology changes in response to genetic or metabolic perturbations.

This paper shows that Aβ42 aggregation in live cells increases intracellular temperature, which can be mitigated by aggregation inhibitors and is independent of mitochondrial damage.

This study tracks SARS-CoV-2 structural proteins' spatiotemporal dynamics during infection, revealing nucleocapsid's early association with ER membranes and lysosome involvement in viral egress.

This study shows that water mobility, influenced by ions like NaCl and CsI, affects the aggregation rate of α-synuclein, a protein linked to Parkinson's disease.

This paper presents a rapid protocol for purifying monomeric recombinant Aβ from E. coli and fluorescent Aβ-mCherry from mammalian cells, avoiding aggregation and freeze-drying steps.

The paper compares four protocols for isolating recombinant α-synuclein from E. coli, finding that acid precipitation and periplasmic lysis yield the highest purity and monomer content.

This paper develops a method to measure chromatin compaction in live and fixed cells using SiR-DNA fluorescence lifetime, revealing compaction in differentiating cells and decompaction during stem cell transitions.

The paper shows that short hydrogen bonds in L-glutamine enhance non-aromatic fluorescence through reduced non-radiative transitions, offering insights for bioactive material design.

This study investigates how calcium-induced conformational changes in monomeric alpha-synuclein affect N-terminus exposure and aggregation propensity, identifying sequence-specific conformational differences as key factors.

This study uses fast TG-FLIM to analyze α-synuclein and polyglutamine aggregation in aging C. elegans, revealing differences in their aggregation kinetics and amyloid-like features.

This study shows that age-dependent protein aggregation in C. elegans forms amyloid-like structures and accelerates tissue functional decline, suggesting a role for protein aggregation in aging.