Results 81 to 90 of about 23,171 (195)

Portability of a Small-Molecule Binding Site between Disordered Proteins

Biomolecules, 2022
Intrinsically disordered proteins (IDPs) are important in both normal and disease states. Small molecules can be targeted to disordered regions, but we currently have only a limited understanding of the nature of small-molecule binding sites in IDPs ...
Rajesh Jaiprashad, Sachith Roch De Silva, Lisette M. Fred Lucena, Ella Meyer, Steven J. Metallo   +4 more
doaj   +1 more source

The roles of intrinsically disordered proteins in neurodegeneration.

Biochimica et Biophysica Acta - General Subjects
Neurodegenerative diseases such as Amyotrophic Lateral Sclerosis, Alzheimer's disease, Parkinson's disease, and Huntington's disease share a common pathological hallmark: the accumulation of misfolded proteins, particularly involving intrinsically ...
K. Utami, Satoru Morimoto, Yasue Mitsukura, Hideyuki Okano   +3 more
semanticscholar   +1 more source

α‐Synuclein Forms Distinct Micelle‐Like Assemblies at Low Ionic Strengths

Advanced Science, EarlyView.
At high ionic strength, α‐synuclein forms diverse assemblies, including oligomers, fibrils, and condensates. Here, we show that at low ionic strength, α‐synuclein adopts a distinct, low‐abundance assembly state. These assemblies maintain a constant size above a critical concentration and do not coalesce, suggesting a micelle‐like organization ...
Sophie Hertel, Soumik Ray, Federica Saraceno, Giacomo Nisini, Georgia Nasi, Thomas Oliver Mason, Antonin Kunka, Effrosyni Agrimaki, Dannie Juul Olesen, Francesco Simone Ruggeri, Alexander K. Buell   +10 more
wiley   +1 more source

Creating and Exploiting the Intrinsically Disordered Protein Knowledge Graph (IDP-KG).

, 2022
There are many data sources containing overlapping information about Intrinsically Disordered Proteins (IDP). IDPcentral aims to be a registry to aid the discovery of data about proteins known to be intrinsically disordered by aggregating the content from these sources. Traditional ETL approaches for populating IDPcentral require the API and data model
Gray, Alasdair, Papadopoulos, Petros, Asif, Imran, Micetic, Ivan, Hatos, Andras   +4 more
openaire   +2 more sources

SPEADI: Accelerated Analysis of IDP-Ion Interactions from MD-Trajectories

Biology, 2023
The disordered nature of Intrinsically Disordered Proteins (IDPs) makes their structural ensembles particularly susceptible to changes in chemical environmental conditions, often leading to an alteration of their normal functions.
Emile de Bruyn, Anton Emil Dorn, Olav Zimmermann, Giulia Rossetti   +3 more
doaj   +1 more source

Probing the Energy Landscape of α‐Synuclein Amyloid Fibril Formation by Systematic K‐to‐Q Mutagenesis

Advanced Science, EarlyView.
We use lysine‐to‐glutamine mutations to study the effect of electrostatics on the kinetics and thermodynamics of alpha‐synuclein amyloid fibril formation. We find that mutational effects map on their structural context within fibrils and identify residues that modulate the energy landscape of alpha‐synuclein self‐assembly. Our work outlines a scalable,
Antonin Kunka, Azad Farzadfard, Jacob Aunstrup Larsen, Rasmus Krogh Norrild, Federica Saraceno, Celia Fricke, Hossein Mohammad‐Beigi, Ahmed Sadek, Jonas Folke, Susana Aznar, Alexander K. Buell   +10 more
wiley   +1 more source

Intrinsically Disordered Proteins (IDPs): Experimental and Computational Approaches in Drug Discovery [PDF]

Drug Designing & Intellectual Properties International Journal, 2018
Intrinsically disordered proteins (IDPs) are proteins that usually do not adopt well-defined native structures when isolated in solution under physiological conditions. Numerous IDPs have close relationships with human diseases such as Parkinson disease, Alzheimer disease, diabetes, and so on.
openaire   +1 more source

Accurate Generation of Conformational Ensembles for Intrinsically Disordered Proteins with IDPFold

Advancement of science
Intrinsically disordered proteins (IDPs) play pivotal roles in various biological functions whose dynamic structures are closely associated with many human diseases, including cancer, diabetes, and Alzheimer disease.
Jun-Jie Zhu, Zheng-Xin Li, Zhuoqi Zheng, Bo Zhang, Bozitao Zhong, Jie Bai, Xiao-Kun Hong, Taifeng Wang, Ting Wei, Jian-Yi Yang, Hai-Feng Chen   +10 more
semanticscholar   +1 more source

Atomistic Molecular Dynamics Simulations of Intrinsically Disordered Proteins

Current Opinion in Structural Biology
Recent years have seen remarkable gains in the accuracy of atomistic molecular dynamics (MD) simulations of intrinsically disordered proteins (IDPs) and expansion in the types of calculated properties that can be directly compared with experimental ...
Fidha Nazreen Kunnath Muhammedkutty, Matthew MacAinsh, Huan-Xiang Zhou   +2 more
semanticscholar   +1 more source

Prediction of Prion Proteins in E. coli Based on Bimodal Sequence Characteristics

Proteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT Prions are infectious proteins that bear misfolded conformations capable of converting folded states into misfolded aggregates under physiologically relevant conditions. In mammals, prions cause deadly maladies including Creutzfeldt‐Jakob and chronic wasting disease. To date, several prion proteins have been identified in eukaryotes, primarily
Katherine Shreeve, Jinoh Jang, Mridula Srivathsan, Siyu Li, Taylor D. Scott, Silvia Cavagnero   +5 more
wiley   +1 more source