User profiles for Birgit Strodel

Birgit Strodel

Professor, Computational Biochemistry, Research Centre Jülich & University Düsseldorf …
Verified email at strodel.info
Cited by 5463

Amyloid oligomers: A joint experimental/computational perspective on Alzheimer's disease, Parkinson's disease, type II diabetes, and amyotrophic lateral sclerosis

…, S Timr, J Chen, B Hnath, B Strodel… - Chemical …, 2021 - ACS Publications
Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Amyloid β protein and Alzheimer's disease: When computer simulations complement experimental studies

…, S Pasquali, DJ Rosenman, B Strodel… - Chemical …, 2015 - ACS Publications
Alzheimer’s disease (AD) challenges our society with an annual estimated cost of $1.08
trillion in the United States alone by 2050. 1 AD is a progressive irreversible neurological …

Thermodynamics and kinetics of aggregation for the GNNQQNY peptide

B Strodel, CS Whittleston, DJ Wales - Journal of the American …, 2007 - ACS Publications
The energy landscape of the monomer and dimer are explored for the amyloidogenic
heptapeptide GNNQQNY from the N-terminal prion-determining domain of the yeast protein Sup35…

Amyloid-type protein aggregation and prion-like properties of amyloids

D Willbold, B Strodel, GF Schröder, W Hoyer… - Chemical …, 2021 - ACS Publications
This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

Effects of in vivo conditions on amyloid aggregation

…, R Winter, S Ebbinghaus, B Strodel - Chemical Society …, 2019 - pubs.rsc.org
One of the grand challenges of biophysical chemistry is to understand the principles that
govern protein misfolding and aggregation, which is a highly complex process that is sensitive …

Comparison of force fields for Alzheimer's A: A case study for intrinsically disordered proteins

M Carballo‐Pacheco, B Strodel - Protein science, 2017 - Wiley Online Library
Intrinsically disordered proteins are essential for biological processes such as cell signalling,
but are also associated to devastating diseases including Alzheimer's disease, Parkinson's …

Pathways of amyloid-β aggregation depend on oligomer shape

B Barz, Q Liao, B Strodel - Journal of the American Chemical …, 2018 - ACS Publications
One of the main research topics related to Alzheimer’s disease is the aggregation of the
amyloid-β peptide, which was shown to follow different pathways for the two major alloforms of …

Amyloid aggregation simulations: challenges, advances and perspectives

B Strodel - Current opinion in structural biology, 2021 - Elsevier
In amyloid aggregation diseases soluble proteins coalesce into a wide array of undesirable
structures, ranging through oligomers and prefibrillar assemblies to highly ordered amyloid …

Multiple substrate binding mode-guided engineering of a thermophilic PET hydrolase

…, GJ Palm, M Lammers, J Damborsky, B Strodel… - ACS …, 2022 - ACS Publications
Thermophilic polyester hydrolases (PES-H) have recently enabled biocatalytic recycling of
the mass-produced synthetic polyester polyethylene terephthalate (PET), which has found …

Transmembrane Structures for Alzheimer's Aβ1−42 Oligomers

B Strodel, JWL Lee, CS Whittleston… - Journal of the American …, 2010 - ACS Publications
We model oligomers of the Alzheimer’s amyloid β-peptide Aβ 1−42 in an implicit membrane
to obtain insight into the mechanism of amyloid toxicity. It has been suggested that Aβ …