A5051869254- Alzheimer's disease research and treatments
- Neuroinflammation and Neurodegeneration Mechanisms
- Computational Drug Discovery Methods
- Supramolecular Self-Assembly in Materials
- American Constitutional Law and Politics
- Prion Diseases and Protein Misfolding
- Phosphodiesterase function and regulation
- Cholinesterase and Neurodegenerative Diseases
- Epigenetics and DNA Methylation
- Point processes and geometric inequalities
- Biblical Studies and Interpretation
- Inflammasome and immune disorders
- Chinese history and philosophy
- Proteins in Food Systems
- Inflammation biomarkers and pathways
- Phytoestrogen effects and research
- Neurological Disease Mechanisms and Treatments
- Immune Response and Inflammation
- Advanced Glycation End Products research
- Religion, Society, and Development
- Religion, Gender, and Enlightenment
- Sphingolipid Metabolism and Signaling
- Medicinal Plants and Neuroprotection
- Reformation and Early Modern Christianity
- S100 Proteins and Annexins
University of Missouri–St. Louis
2014-2023
Purdue University West Lafayette
1999-2022
Transylvania University
2009
Mayo Clinic
2005
Jacksonville College
2004
Mayo Clinic in Florida
2001-2004
WinnMed
2004
Johns Hopkins University
2002-2004
Johns Hopkins Medicine
2002
Wilmington University
2001
Abstract The primary molecules for mediating the innate immune response are Toll‐like family of receptors (TLRs). Recent work has established that amyloid‐beta (Aβ) fibrils, components senile plaques in Alzheimer’s disease (AD), can interact with TLR2/4 accessory protein CD14. Using antibody neutralization assays and tumor necrosis factor alpha release human monocytic THP‐1 cell line, we determined both TLR2 TLR4 mediated an inflammatory to aggregated Aβ(1–42). This was contrast exclusive...
Amyloid plaques in brain tissue are a hallmark of Alzheimer's disease. Primary components these 40- and 42-residue peptides, denoted Aβ(1−40) Aβ(1−42), that derived by proteolysis cellular amyloid precursor protein. Synthetic Aβ(1−42) form fibrils vitro share many features with the plaques. Soluble intermediates Aβ fibrillogenesis, termed protofibrils, have been identified previously, here we describe formation isolation protofibrils size exclusion chromatography. In some experiments, was...
The brains of Alzheimer's disease (AD) patients contain large numbers amyloid plaques that are rich in fibrils composed 40- and 42-residue amyloid-beta (Abeta) peptides. Several lines evidence indicate fibrillar Abeta especially soluble aggregates important the etiology AD. Recent reports also stress polymorphic a single polypeptide can fold into multiple conformations. Here we demonstrate Abeta-(1-40) form with predominant beta-structures differ stability morphology. One class involved...
Senile plaques composed of amyloid-β protein (Aβ) are an unshakable feature the Alzheimer's disease (AD) brain. Although there is significant debate on role in AD progression, little disagreement their stimulating a robust inflammatory response within context disease. Significant markers such as activated microglia and cytokines observed almost exclusively surrounding plaques. However, recent evidence suggests that plaque exterior may contain measurable level soluble Aβ aggregates. The...
Prior work suggests that amyloid precursor protein (APP) can function as a proinflammatory receptor on immune cells, such monocytes and microglia. Therefore, we hypothesized APP serves this in microglia during Alzheimer9s disease. Although fibrillar β (Aβ)-stimulated cytokine secretion from both wild-type knock-out (mAPP<sup>−/−</sup>) microglial cultures, oligomeric Aβ was unable to stimulate increased mAPP<sup>−/−</sup> cells. This consistent with an ability of bind APP. Similarly,...
Some of the pathological hallmarks Alzheimer's disease brain are senile plaques composed insoluble amyloid-β protein (Aβ) fibrils. However, much recent emphasis in research has been on soluble Aβ aggregates response to a growing body evidence that shows these species may be more neurotoxic than Within this subset aggregated protofibrils and oligomers. Although each widely investigated separately, few studies have directly compared contrasted their physical properties. In work, we examined...
Microvesicles (MVs) and exosomes comprise a class of cell-secreted particles termed extracellular vesicles (EVs). These cargo-holding mediate cell-to-cell communication have recently been implicated in neurodegenerative diseases such as Alzheimer's disease (AD). The two types EVs are distinguished by the mechanism cell release their size, with smaller larger MVs ranging from 30 to 100 nm 1 μm diameter, respectively. MV numbers increased AD appear interact amyloid-β peptide (Aβ), primary...