Andreas C. Woerner

ORCID: 0009-0002-4322-2052
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About
Contact & Profiles
Research Areas
  • Photoreceptor and optogenetics research
  • Neuroscience and Neuropharmacology Research
  • Endoplasmic Reticulum Stress and Disease
  • Genetic Neurodegenerative Diseases
  • Alzheimer's disease research and treatments
  • Advanced NMR Techniques and Applications
  • Ubiquitin and proteasome pathways
  • Nicotinic Acetylcholine Receptors Study
  • Neural dynamics and brain function
  • Protein Structure and Dynamics
  • RNA Research and Splicing
  • Molecular Communication and Nanonetworks
  • Neurological diseases and metabolism
  • Prion Diseases and Protein Misfolding

Max Planck Institute of Biochemistry
2011-2019

Goethe University Frankfurt
2006-2011

Amyloid-like protein aggregation is associated with neurodegeneration and other pathologies. The nature of the toxic aggregate species their mechanism action remain elusive. Here, we analyzed compartment specificity toxicity using artificial β-sheet proteins, as well fragments mutant huntingtin TAR DNA binding protein-43 (TDP-43). Aggregation in cytoplasm interfered nucleocytoplasmic RNA transport. In contrast, same proteins did not inhibit transport when forming inclusions nucleus at or...

10.1126/science.aad2033 article EN Science 2015-12-04

The proteorhodopsin (PR) family found in bacteria near the ocean's surface consists of hundreds PR variants color-tuned to their environment. contains a highly conserved single histidine at position 75, which is not most other retinal proteins. Using 13C and 15N MAS NMR, we were able prove for green that His75 forms pH-dependent H-bond with primary proton acceptor Asp97, explains its unusually high pKa. functional role has been studied using site-directed mutagenesis time-resolved optical...

10.1021/ja111116a article EN Journal of the American Chemical Society 2011-03-02

The first steps of the photocycle D97N mutant proteorhodopsin (PR) have been investigated by means ultrafast transient absorption spectroscopy. A comparison with primary dynamics native PR and D85N bacteriorhodopsin is given. Upon photoexcitation covalently bound all-trans retinal excited state decays biexponentially time constants 1.4 20 ps via a conical intersection, resulting in 13-cis isomerized retinal. Neither two-deactivation channels significantly preferred. slowed down at pH 9...

10.1562/2006-05-31-ra-909 article EN Photochemistry and Photobiology 2006-01-01
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