The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems

F Sterpone, S Melchionna, P Tuffery… - Chemical Society …, 2014 - pubs.rsc.org
The OPEP coarse-grained protein model has been applied to a wide range of applications
since its first release 15 years ago. The model, which combines energetic and structural …

Protein aggregation: in silico algorithms and applications

R Prabakaran, P Rawat, AM Thangakani, S Kumar… - Biophysical …, 2021 - Springer
Protein aggregation is a topic of immense interest to the scientific community due to its role
in several neurodegenerative diseases/disorders and industrial importance. Several in silico …

GROMACS in the cloud: A global supercomputer to speed up alchemical drug design

C Kutzner, C Kniep, A Cherian… - Journal of Chemical …, 2022 - ACS Publications
We assess costs and efficiency of state-of-the-art high-performance cloud computing and
compare the results to traditional on-premises compute clusters. Our use case is atomistic …

How do the size, charge and shape of nanoparticles affect amyloid β aggregation on brain lipid bilayer?

Y Kim, JH Park, H Lee, JM Nam - Scientific reports, 2016 - nature.com
Here, we studied the effect of the size, shape and surface charge of Au nanoparticles
(AuNPs) on amyloid beta (Aβ) aggregation on a total brain lipid-based supported lipid …

Advances in the simulation of protein aggregation at the atomistic scale

M Carballo-Pacheco, B Strodel - The journal of physical chemistry …, 2016 - ACS Publications
Protein aggregation into highly structured amyloid fibrils is associated with various diseases
including Alzheimer's disease, Parkinson's disease, and type II diabetes. Amyloids can also …

Formation and propagation of tau oligomeric seeds

JE Gerson, R Kayed - Frontiers in neurology, 2013 - frontiersin.org
Tau misfolding and aggregation leads to the formation of neurofibrillary tangles (NFTs),
which have long been considered one of the main pathological hallmarks for numerous …

Understanding amyloid fibril nucleation and Aβ oligomer/drug interactions from computer simulations

P Nguyen, P Derreumaux - Accounts of chemical research, 2014 - ACS Publications
Evolution has fine-tuned proteins to accomplish a variety of tasks. Yet, with aging, some
proteins assemble into harmful amyloid aggregates associated with neurodegenerative …

Amyloid self‐assembly of hIAPP8‐20 via the accumulation of helical oligomers, α‐helix to β‐sheet transition, and formation of β‐barrel intermediates

Y Sun, A Kakinen, Y **ng, P Faridi, A Nandakumar… - Small, 2019 - Wiley Online Library
The self‐assembly of human islet amyloid polypeptide (hIAPP) into β‐sheet‐rich nanofibrils
is associated with the pathogeny of type 2 diabetes. Soluble hIAPP is intrinsically disordered …

On the applicability of force fields to study the aggregation of amyloidogenic peptides using molecular dynamics simulations

M Carballo-Pacheco, AE Ismail… - Journal of Chemical …, 2018 - ACS Publications
Molecular dynamics simulations play an essential role in understanding biomolecular
processes such as protein aggregation at temporal and spatial resolutions which are not …

Phosphorylation drives a dynamic switch in serine/arginine-rich proteins

SQ **ang, V Gapsys, HY Kim, S Bessonov, HH Hsiao… - Structure, 2013 - cell.com
Summary Serine/arginine-rich (SR) proteins are important players in RNA metabolism and
are extensively phosphorylated at serine residues in RS repeats. Here, we show that …