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Figure 5 in Potential neuroprotective of trans-resveratrol a promising agent tempeh and soybean seed coats-derived against beta-amyloid neurotoxicity on primary culture of nerve cells induced by 2-methoxyethanol

Figure 5. Treatment group: 2- ME (10 x10).

Figure 9. Treatment Group with 2 in Potential neuroprotective of trans-resveratrol a promising agent tempeh and soybean seed coats-derived against beta-amyloid neurotoxicity on primary culture of nerve cells induced by 2-methoxyethanol

Figure 9. Treatment Group with 2-ME after induced by Beta-Amyloid (10 x10).

Figure 2 in Potential neuroprotective of trans-resveratrol a promising agent tempeh and soybean seed coats-derived against beta-amyloid neurotoxicity on primary culture of nerve cells induced by 2-methoxyethanol

Figure 2. Treatment group: 2- ME + Resveratrol Standard (10 x10).

Figure 1 in Potential neuroprotective of trans-resveratrol a promising agent tempeh and soybean seed coats-derived against beta-amyloid neurotoxicity on primary culture of nerve cells induced by 2-methoxyethanol

Figure 1. Control Group (10 x10).

Table 4 in Potential neuroprotective of trans-resveratrol a promising agent tempeh and soybean seed coats-derived against beta-amyloid neurotoxicity on primary culture of nerve cells induced by 2 - methoxyethanol

Table 4. Cytotoxic effect of various concentrations of Resveratrol and 2-Methoxyethanol Against Primary Neuron cell viability in MTT assay (570 nm).<table><tbody><tr><th>% Inhibition</th></tr></tbody><tbody><tr><th>Concentration of 2-Methoxyethanol</th><td>2-ME (10mM)</td><td>2-ME (10mM)</td><td>2-ME (10mM)</td></tr><tr><th>and Resveratrol</th><td>Resveratrol (Standard)</td><td>Resveratrol (Tempeh)</td><td>Resveratrol (Soybean Seed Coat)</td></tr><tr><th>IC50</th><td>(17.38 ± 0.99 µg/mL)</td><td>(31.14 ± 0.02 µg/mL)</td><td>(13.40 ± 0.30 µg/mL)</td></tr><tr><th>1.4 (µg/mL)</th><td>12.57</td><td>0</td><td>11.98</td></tr><tr><th>2.8 (µg/mL)</th><td>4.59</td><td>1.75</td><td>17.03</td></tr><tr><th>4.2 (µg/mL)</th><td>0</td><td>0</td><td>0</td></tr></tbody></table>

Table 3 in Potential neuroprotective of trans-resveratrol a promising agent tempeh and soybean seed coats-derived against beta-amyloid neurotoxicity on primary culture of nerve cells induced by 2 - methoxyethanol

Table 3. Cytotoxic effect of various concentrations of Resveratrol and 2-Methoxyethanol Against Primary Neuron cell viability in MTT assay (540 nm).<table><tbody><tr><th>% Inhibition</th></tr></tbody><tbody><tr><th>Concentration of 2-Methoxyethanol</th><td>2-ME (10mM)</td><td>2-ME (10mM)</td><td>2-ME (10mM)</td></tr><tr><th>and Resveratrol</th><td>Resveratrol (Standard)</td><td>Resveratrol (Tempeh)</td><td>Resveratrol (Soybean Seed Coat)</td></tr><tr><th>IC50</th><td>(17.64 ± 0.99 µg/mL)</td><td>(32.22 ± 1.18 µg/mL)</td><td>(17.43 ± 0.16 µg/mL)</td></tr><tr><th>1.4 (µg/mL)</th><td>11.8</td><td>0</td><td>7.95</td></tr><tr><th>2.8 (µg/mL)</th><td>5.27</td><td>0</td><td>14.41</td></tr><tr><th>4.2 (µg/mL)</th><td>0</td><td>0</td><td>0</td></tr></tbody></table>

opencc-by-4.0Sep 2024View details →

Proteome Data for Amyloid Atlas

Datafile for collected and calculated data for proteins in Amyloid Atlas

Table 2 in Potential neuroprotective of trans-resveratrol a promising agent tempeh and soybean seed coats-derived against beta-amyloid neurotoxicity on primary culture of nerve cells induced by 2 - methoxyethanol

Table 2. Effect of Various concentrations of Resveratrol and 2-Methoxyethanol against Primary Neuron cell viability (570 nm).<table><tbody><tr><th>% Cell Viability</th></tr></tbody><tbody><tr><th>Concentration of 2-Methoxyethanol</th><td>2-ME (10mM)</td><td>2-ME (10mM)</td><td>2-ME (10mM)</td></tr><tr><th>and Resveratrol</th><td>Resveratrol (Standard)</td><td>Resveratrol (Tempeh)</td><td>Resveratrol (Soybean Seed Coat)</td></tr><tr><th>1.4 (µg/mL)</th><td>87.43</td><td>100</td><td>88.02</td></tr><tr><th>2.8 (µg/mL)</th><td>95.41</td><td>98.25</td><td>82.97</td></tr><tr><th>4.2 (µg/mL)</th><td>100</td><td>100</td><td>100</td></tr></tbody></table>

Table 1 in Potential neuroprotective of trans-resveratrol a promising agent tempeh and soybean seed coats-derived against beta-amyloid neurotoxicity on primary culture of nerve cells induced by 2 - methoxyethanol

Table 1. Effect of Various concentrations of Resveratrol and 2-Methoxyethanol against Primary Neuron cell viability (540 nm).<table><tbody><tr><th>% Cell Viability</th></tr></tbody><tbody><tr><th>Concentration of 2-Methoxyethanol</th><td>2-ME (10mM)</td><td>2-ME (10mM)</td><td>2-ME (10mM)</td></tr><tr><th>and Resveratrol</th><td>Resveratrol (Standard)</td><td>Resveratrol (Tempeh)</td><td>Resveratrol (Soybean Seed Coat)</td></tr><tr><th>1.4 (µg/mL)</th><td>88.2</td><td>100</td><td>92.05</td></tr><tr><th>2.8 (µg/mL)</th><td>94.73</td><td>100</td><td>85.59</td></tr><tr><th>4.2 (µg/mL)</th><td>100</td><td>100</td><td>100</td></tr></tbody></table>

opencc-by-4.0Dec 2021View details →

Atomic Structure of Amyloid Crystals

3D ED/MicroED data collected on micro-crystals of a fragment of amyloid-beta peptide. The specimen was prepared using the Preassis method (Zhao et. al. Nature Communications 2021) on Quantifoil R2/1 (300 mesh) grid. 3D ED/MicroED data were collected on a 200kV JEOL JEM-2100 LaB6 TEM equipped with a Timepix hybrid pixel detector. A Gatan 914 cryo-transfer holder was used to keep the specimen at liquid nitrogen temperature during data collection. The rotation speed of goniometer, exposure time, electron dose rate and camera length were 0.23 degree/s, 0.5 s, 0.1 e-/Å2/s and 30cm, respectively. The software Instamatic was used for electron diffraction data collection. The rotation range of individual dataset was limited between 40 degree and 50 degree due to beam damage. The data was saved in TIFF, SMV, and DM3 (for REDp processing) format. Information of the individual data collection can be found in the cRED_log file. Input files for PETS processing and XDS processing (automatically generated) are also included.

opencc-by-4.0Oct 2018View details →

Molecular Dynamics Simulation on the Effect of Transition Metal Binding to the N-Terminal Fragment of Amyloid-β

Molecular dynamics trajectories in PDB format for 3x Cu-Aβ, 3x Zn-Aβ and 9x Fe-Aβ simulations.

opencc-by-4.0Feb 2023View details →

DATASET RELATED TO ARTICLE"SORL1 GENE MUTATION AND OCTAPEPTIDE REPEAT INSERTION IN PRNP GENE IN A CASE PRESENTING WITH RAPIDLY PROGRESSIVE DEMENTIA AND CEREBRAL AMYLOID ANGIOPATHY"

electropherogram of prnp octarepeat region ngs analysis of causal and risk genes associated to dementia prnp octarepeat region analysis by size discrimination of pcr amplicons

opencc-by-4.0Feb 2023View details →

FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregation

Amyloid deposition of the microtubule-associated protein tau is a unifying theme in a multitude of neurodegenerative diseases. Disease-associated missense mutations in tau are associated with frontotemporal dementia (FTD) and enhance tau aggregation propensity. However, the molecular mechanism of how mutations in tau promote tau assembly into amyloids remains obscure. There is a need to understand how tau folds into pathogenic conformations to cause disease. Here we describe the structural mechanism for how an FTD-tau S320F mutation drives spontaneous aggregation. We use recombinant protein and synthetic peptide systems, computational modeling, cross-linking mass spectrometry, and cell models to investigate the mechanism of spontaneous aggregation of the S320F FTD-tau mutant. We discover that the S320F mutation drives the stabilization of a local hydrophobic cluster which allosterically exposes the 306VQIVYK311 amyloid motif. We identify a suppressor mutation that reverses the S320F aggregation phenotype through the reduction of S320F-based hydrophobic clustering in vitro and in cells. Finally, we use structure-based computational design to engineer rapidly aggregating tau sequences by optimizing nonpolar clusters in proximity to the S320 site revealing a new principle governing the regulation of tau aggregation. We uncover a mechanism for regulating aggregation that balances transient nonpolar contacts within local protective structures or in longer-range interactions that sequester amyloid motifs. The introduction of a pathogenic mutation redistributes these transient interactions to drive spontaneous aggregation.  We anticipate that more profound knowledge of this process will permit control of tau aggregation into discrete structural polymorphs to aid the design of reagents that can detect disease-specific tau conformations.

dryad36/100

The amyloid precursor protein regulates synaptic transmission at medial perforant path synapses

The perforant path provides the primary cortical excitatory input to the hippocampus. Due to its important role in information processing and coding, entorhinal projections to the dentate gyrus have been studied in considerable detail. Nevertheless, synaptic transmission between individual connected pairs of entorhinal stellate cells and dentate granule cells remains to be characterized. Here, we have used mouse organotypic entorhino-hippocampal tissue cultures of either sex, in which the entorhino-dentate (EC-GC) projection is present and EC-GC pairs can be studied using whole-cell patch clamp recordings. By using cultures of wildtype mice, the properties of EC-GC synapses formed by afferents from the lateral and medial entorhinal cortex were compared and differences in short-term plasticity were identified. Since the perforant path is severely affected in Alzheimer´s disease, we used tissue cultures of amyloid-precursor protein (APP)-deficient mice to examine the role of APP at this synapse. APP deficiency altered excitatory neurotransmission at medial perforant path synapses, which was accompanied by transcriptomic and ultrastructural changes. Moreover, presynaptic but not postsynaptic APP deletion through the local injection of Cre-expressing adeno-associated viruses in conditional APPflox/flox tissue cultures increased the neurotransmission efficacy at perforant path synapses. In summary, these data suggest a physiological role for presynaptic APP at medial perforant path synapses that may be adversely affected under altered APP processing conditions.

opencc-zeroJun 2023View details →

Statin Effects on Beta-Amyloid and Cerebral Perfusion in Adults at Risk for Alzheimer's Disease

ClinicalTrials.gov study NCT00939822. IPD Sharing: Not stated. Countries: 1. Publications: 2.

An Extension of Study Fx-005 Evaluating Long-Term Safety And Clinical Outcomes Of Fx-1006A In Patients With Transthyretin Amyloid Polyneuropathy

ClinicalTrials.gov study NCT00791492. IPD Sharing: Not stated. Countries: 6. Publications: 5.

Measuring Brain Amyloid Plaque Load in Older Adults Using BAY 94-9172

ClinicalTrials.gov study NCT01222351. IPD Sharing: Not stated. Countries: 1. Publications: 3.

Phase II Study of Florbetaben (BAY94-9172) PET Imaging for Detection/Exclusion of Cerebral β-amyloid.

ClinicalTrials.gov study NCT00928304. IPD Sharing: Not stated. Countries: 1. Publications: 1.

closedIPD-NOFeb 2026View details →

Study of AG10 in Amyloid Cardiomyopathy

ClinicalTrials.gov study NCT03458130. IPD Sharing: NO. Countries: 1. Publications: 1.