Article

Benchmark of force fields to characterize the intrinsically disordered R2-FUS-LC region

2022-12-21

Abstract excerpt

<h4>ABSTRACT</h4> Amyloid fibrils formations are involved in many neurodegenerative diseases such as Alzheimer’s disease, Parkinson disease, Amyotrophic Lateral Sclerosis (ALS) and others. The proteins associated with the formation of amyloid fibrils are Intrinsically Disordered Proteins (IDP) in the unbound state. Nevertheless, this type of proteins can self-aggregate and form cross-β amyloid fibrils structures...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 7d65599e-931c-572f-9a1a-0acd4425c5a5
DOI: 10.1101/2022.12.20.521322

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Benchmark of force fields to characterize the intrinsically disordered R2-FUS-LC regionDOI 10.1101/2022.12.20.521322Read

BenchIDPs: Evaluation of Conformational Preferences Molecular Mechanics and Solvent Interactions of IDPs across popular Force Fields and Water ModelsSemantic proximity Read

Condensing the Damage: The Roles of Intrinsically Disordered Proteins in Traumatic Brain InjurySemantic proximity Read

Drude2019IDPC polarizable force field reveals structure-function relationship of insulin.Semantic proximity Read

Structures of the Wild-Type and S59L Mutant CHCHD10 Proteins Important in Amyotrophic Lateral Sclerosis-Frontotemporal Dementia.Semantic proximity Read

Mutations in human prion-like domains: pathogenic but not always amyloidogenic.Semantic proximity Read

Dissecting how ALS-associated D290V mutation enhances pathogenic aggregation of hnRNPA2286-291 peptides: Dynamics and conformational ensembles.Semantic proximity Read

Mutational analysis of FUS gene and its structural and functional role in amyotrophic lateral sclerosis 6.Semantic proximity Read

Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation.Semantic proximity Read

Molecular dynamics and protein frustration analysis of human fused in Sarcoma protein variants in Amyotrophic Lateral Sclerosis type 6: An In Silico approach.Semantic proximity Read

Breaking β-sheets in FUS prion-like domain preserves phase separation and function but prevents aggregation and toxicitySemantic proximity Read

Benchmarking Molecular Dynamics Force Fields for All-Atom Simulations of Biological CondensatesSemantic proximity Read

ALS mutations in the TIA-1 prion-like domain trigger highly condensed pathogenic structures.Semantic proximity Read