In vivo aspects of protein folding and quality control

D Balchin, M Hayer-Hartl, FU Hartl - Science, 2016 - science.org
BACKGROUND Proteins are synthesized on ribosomes as linear chains of amino acids and
must fold into unique three-dimensional structures to fulfill their biological functions. Protein …

[HTML][HTML] Pure shift NMR

K Zangger - Progress in nuclear magnetic resonance spectroscopy, 2015 - Elsevier
Although scalar-coupling provides important structural information, the resulting signal
splittings significantly reduce the resolution of NMR spectra. Limited resolution is a particular …

Investigating protein–ligand interactions by solution nuclear magnetic resonance spectroscopy

W Becker, KC Bhattiprolu, N Gubensäk… - …, 2018 - Wiley Online Library
Protein–ligand interactions are of fundamental importance in almost all processes in living
organisms. The ligands comprise small molecules, drugs or biological macromolecules and …

Looking beyond the core: the role of flanking regions in the aggregation of amyloidogenic peptides and proteins

SM Ulamec, DJ Brockwell, SE Radford - Frontiers in Neuroscience, 2020 - frontiersin.org
Amyloid proteins are involved in many neurodegenerative disorders such as Alzheimer's
disease [Tau, Amyloid β (Aβ)], Parkinson's disease [alpha-synuclein (αSyn)], and …

The ubiquitin-proteasome system: potential therapeutic targets for Alzheimer's disease and spinal cord injury

B Gong, M Radulovic… - Frontiers in molecular …, 2016 - frontiersin.org
The ubiquitin-proteasome system (UPS) is a crucial protein degradation system in
eukaryotes. Herein, we will review advances in the understanding of the role of several …

Cellular regulation of amyloid formation in aging and disease

E Stroo, M Koopman, EAA Nollen… - Frontiers in …, 2017 - frontiersin.org
As the population is aging, the incidence of age-related neurodegenerative diseases, such
as Alzheimer and Parkinson disease, is growing. The pathology of neurodegenerative …

Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core

HK Lin, JC Boatz, IE Krabbendam, R Kodali… - Nature …, 2017 - nature.com
Polyglutamine expansion in the huntingtin protein is the primary genetic cause of
Huntington's disease (HD). Fragments coinciding with mutant huntingtin exon1 aggregate in …

The disordered protein SERF promotes α-Synuclein aggregation through liquid–liquid phase separation

HN Liu, T Wang, JJ Hu, L Chen, X Shi, YM Li… - Journal of Biological …, 2024 - ASBMB
The aggregation of α-Synuclein (α-Syn) into amyloid fibrils is the hallmark of Parkinson's
disease. Under stress or other pathological conditions, the accumulation of α-Syn oligomers …

[HTML][HTML] 10q26–The enigma in age-related macular degeneration

DA Merle, M Sen, A Armento, CM Stanton… - Progress in Retinal and …, 2023 - Elsevier
Despite comprehensive research efforts over the last decades, the pathomechanisms of age-
related macular degeneration (AMD) remain far from being understood. Large-scale …

[HTML][HTML] Genetic screens in Caenorhabditis elegans models for neurodegenerative diseases

O Sin, H Michels, EAA Nollen - … et Biophysica Acta (BBA)-Molecular Basis …, 2014 - Elsevier
Caenorhabditis elegans comprises unique features that make it an attractive model
organism in diverse fields of biology. Genetic screens are powerful to identify genes and C …