Deletion of SERF2 in mice delays embryonic development and alters amyloid deposit structure in the brain | Life Science Alliance
The cellular modifier MOAG‐4/SERF drives amyloid formation through charge complementation | The EMBO Journal
Polyglutamine protein aggregates are dynamic | Nature Cell Biology
Frontiers | Regulation of Age-Related Protein Toxicity
Delivery of Native Proteins into C. elegans Using a Transduction Protocol Based on Lipid Vesicles | Scientific Reports
The cellular modifier MOAG‐4/SERF drives amyloid formation through charge complementation | The EMBO Journal
Cornelis CALKHOVEN | University of Groningen, Groningen | RUG | European Research Institute for the Biology of Ageing | Research profile
A Brain-Permeable Aminosterol Regulates Cell Membranes to Mitigate the Toxicity of Diverse Pore-Forming Agents | ACS Chemical Neuroscience
Tryptophan metabolism: entering the field of aging and age-related pathologies: Trends in Molecular Medicine
MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions - ScienceDirect
Speakers | ARDD 2022
Speakers | ARDD 2022
Julius Bier Kirkegaard — Theoretical Biophysics & Data Science
Ellen Nollen | VIB Conferences
Immune regulation through tryptophan metabolism | Experimental & Molecular Medicine
Frontiers | Parasexuality of Candida Species
Cognitive impairments correlate with increased central nervous system immune activation after allogeneic haematopoietic stem cell transplantation | Leukemia
Alliance for Healthy Aging
Deletion of SERF2 in mice delays embryonic development and alters amyloid deposit structure in the brain | Life Science Alliance
Probing the Origin of the Toxicity of Oligomeric Aggregates of α-Synuclein with Antibodies | ACS Chemical Biology
Identification of MOAG-4/SERF as a Regulator of Age-Related Proteotoxicity: Cell
Untargeted Metabolomic Characterization of Glioblastoma Intra-Tumor Heterogeneity Using OrbiSIMS | Analytical Chemistry
Crystal Structure and Mechanism of Tryptophan 2,3-Dioxygenase, a Heme Enzyme Involved in Tryptophan Catabolism and in Quinolinate Biosynthesis, | Biochemistry
Frontiers | Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers
MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions - ScienceDirect
