A5047357453- Genetics, Aging, and Longevity in Model Organisms
- Redox biology and oxidative stress
- Alzheimer's disease research and treatments
- Machine Learning in Bioinformatics
- Circadian rhythm and melatonin
- Prion Diseases and Protein Misfolding
- Receptor Mechanisms and Signaling
- Endoplasmic Reticulum Stress and Disease
- Heat shock proteins research
- Advanced Proteomics Techniques and Applications
- Spaceflight effects on biology
- Protein Hydrolysis and Bioactive Peptides
- Neuroscience and Neuropharmacology Research
- Neuroinflammation and Neurodegeneration Mechanisms
- Adipose Tissue and Metabolism
University of Groningen
2020-2021
KU Leuven
2018
Article7 October 2021Open Access Source DataTransparent process The cellular modifier MOAG-4/SERF drives amyloid formation through charge complementation Anita Pras orcid.org/0000-0003-2752-152X European Research Institute for the Biology of Ageing, University Groningen, Medical Centre Netherlands These authors contributed equally to this work. Search more papers by author Bert Houben orcid.org/0000-0002-6750-011X VIB-KU Leuven Center Brain and Disease Research, Leuven, Belgium Switch...
Introduction: Neuropeptides are neuro-endocrine signaling molecules capable of as neurotransmitters, neuromodulators or neurohormones. Studying how neuropeptide is integrated in endocrine pathways and neuropeptides regulate endogenous processes crucial to understanding multicellular organisms respond environmental internal cues.Areas covered: This review will cover proteomics peptidomics approaches used researching peptide systems breakthroughs that were achieved this field. Both...
Abstract While aggregation-prone proteins are known to accelerate ageing and cause age-related diseases, the cellular mechanisms that drive their cytotoxicity remain unresolved. The orthologous MOAG-4, SERF1A SERF2 have recently been identified as modifiers of such cytotoxicity. Using a peptide array screening approach on human amyloidogenic proteins, we found interacted with specific patterns negatively charged hydrophobic, aromatic amino acids. absence patterns, or neutralization positive...