Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.2169/internalmedicine.55.6870 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Cytoplasmic expression of trans-active response DNA-binding protein-43 in aged mice display hippocampal sclerosis-like degeneration and neuronal loss with reduced lifespan.
J Neuropathol Exp Neurol
January 2025
Department of Biological Sciences, Delaware State University, Dover, DE, United States.
Trans-active response DNA-binding protein-43 (TDP-43) is the major pathological protein in motor neuron disease and TDP-43 pathology has been described in the brains of up to 50% of patients with Alzheimer disease (AD). Hippocampal sclerosis of aging (HS-A), an age-related neuropathology characterized by severe neuronal loss and gliosis in CA1 and/or subiculum, is found in ∼80% of cases that are positive for phosphorylated TDP-43. HS-A is seen as a co-pathology in cases with AD, limbic-predominant age-related TDP-43 encephalopathy neuropathologic changes (LATE-NC), and frontotemporal degeneration.
View Article and Find Full Text PDFA rare case of recurrent calcifying epithelial odontogenic tumor in an adolescent patient: Case report and review of literature.
Oral Oncol
January 2025
Department of Oral and Maxillofacial Surgery, Hospital of Stomatology, Jilin University, Changchun 130012, China. Electronic address:
Calcifying epithelial odontogenic tumor (CEOT) is a rare benign odontogenic epithelial tumor characterized by the presence of amyloid material within the tumor that can undergo calcification. CEOT affects individuals across a broad age range, typically between 20 and 60 years, with an average onset age of 40 years. However, it is extremely rare in children and adolescents.
View Article and Find Full Text PDFRole of Copper and Zinc Ions in the Hydrolytic Degradation of Neurodegeneration-Related Peptides.
Molecules
January 2025
Dipartimento di Chimica, Università di Pavia, Via Taramelli 12, 27100 Pavia, Italy.
Spontaneous cleavage reactions normally occur in vivo on amino acid peptide backbones, leading to fragmentation products that can have different physiological roles and toxicity, particularly when the substrate of the hydrolytic processes are neuronal peptides and proteins highly related to neurodegeneration. We report a hydrolytic study performed with the HPLC-MS technique at different temperatures (4 °C and 37 °C) on peptide fragments of different neuronal proteins (amyloid-β, tau, and α-synuclein) in physiological conditions in the presence of Cu and Zn ions, two metal ions found at millimolar concentrations in amyloid plaques. The coordination of these metal ions with these peptides significantly protects their backbones toward hydrolytic degradation, preserving the entire sequences over two weeks in solution, while the free peptides in the same buffer are fully fragmented after the same or even shorter incubation period.
View Article and Find Full Text PDFDiverse Interactions of Sterols with Amyloid Precursor Protein Transmembrane Domain Can Shift Distribution Between Alternative Amyloid-β Production Cascades in Manner Dependent on Local Lipid Environment.
Int J Mol Sci
January 2025
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, 117997 Moscow, Russia.
Alzheimer's disease (AD) pathogenesis is correlated with the membrane content of various lipid species, including cholesterol, whose interactions with amyloid precursor protein (APP) have been extensively explored. Amyloid-β peptides triggering AD are products of APP cleavage by secretases, which differ depending on the APP and secretase location relative to ordered or disordered membrane microdomains. We used high-resolution NMR to probe the interactions of the cholesterol analog with APP transmembrane domain in two membrane-mimicking systems resembling ordered or perturbed lipid environments (bicelles/micelles).
View Article and Find Full Text PDFCo-Localized in Amyloid Plaques Cathepsin B as a Source of Peptide Analogs Potential Drug Candidates for Alzheimer's Disease.
Biomolecules
December 2024
Section of Cell Biology and Biophysics, Department of Biology, School of Sciences, National and Kapodistrian University of Athens, Panepistimiopolis, 157 01 Athens, Greece.
Alzheimer's disease (AD) is a complex neurodegenerative disorder characterized by extracellular amyloid plaques, predominantly consisting of amyloid- (A) peptides. The oligomeric form of A is acknowledged as the most neurotoxic, propelling the pathological progression of AD. Interestingly, besides A, other proteins are co-localized within amyloid plaques.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!