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150 results for “amyloid beta”

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zenodo36/100

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

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

opencc-by-4.0Dec 2022View details →
zenodo36/100

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

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

opencc-by-4.0Dec 2022View details →
ClinicalTrials.gov36/100

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.

restrictedIPD-UNDECIDEDFeb 2026View details →
ClinicalTrials.gov36/100

SIESTA: Sleep Intervention to Enhance Cognitive Status and Reduce Beta Amyloid

ClinicalTrials.gov study NCT03954210. IPD Sharing: NO. Countries: 1. Publications: 31.

closedIPD-NOFeb 2026View details →
ClinicalTrials.gov36/100

Hypertension, Intracranial Pulsatility and Brain Amyloid-beta Accumulation in Older Adults (HIPAC Trial)

ClinicalTrials.gov study NCT03354143. IPD Sharing: YES. Countries: 1. Publications: 1.

controlledIPD-YESFeb 2026View details →
ClinicalTrials.gov36/100

Escitalopram Effects on CSF Amyloid Beta

ClinicalTrials.gov study NCT02161458. IPD Sharing: NO. Countries: 1. Publications: 1.

closedIPD-NOFeb 2026View details →
dryad36/100

Inhibition of amyloid beta oligomer accumulation by NU-9: A unifying mechanism for the treatment of neurodegenerative diseases data set

Open the record for dataset details and reuse information.

publicFeb 2025View details →
zenodo32/100

MD data for the article "Structure comparison of beta amyloid peptide Aβ 1-42 isoforms. Molecular dynamics modeling" by Anna P. Tolstova, Alexander A. Makarov, Alexei A. Adzhubei.

<p>There are CMD and REMD trajectories for&nbsp; A&beta; isoforms discussed in the paper together with&nbsp;final coordinate files for these trajectories.&nbsp;The resulting dataset of modeled structures includes wild type A&beta;42, isoD7, pS8, D7H and H6R-A&beta;42, and wild type A&beta;16, isoD7, pS8, D7H and H6R-A&beta;16.</p>

openOct 2023View details →
zenodo32/100

Amyloid-beta 16-22 peptide monomer simulation with the CHARMM-Drude force field and OpenMM (Run 2)

<p>Amyloid-beta 16-22 peptide (monomer) simulations with the CHARMM-Drude force field and OpenMM. This is the second independent simulation runs out of 3.</p> <p>Part 1-2 are 200 ns long, 3-8 are 100 ns each. Total trajectory length is 1 microseconds. Frame saving frequency is 10 ps.</p> <p>The system contains ~ 150 mM NaCl.</p>

opencc-by-4.0Feb 2022View details →
zenodo32/100

Amyloid-beta 16-22 peptide monomer simulation with the CHARMM-Drude force field and OpenMM (Run 3)

<p>Amyloid-beta 16-22 peptide (monomer) simulations with the CHARMM-Drude force field and OpenMM. This is the last independent simulation runs out of 3.</p> <p>Part 1-2 are 200 ns long, 3-8 are 100 ns each. Total trajectory length is 1 microseconds. Frame saving frequency is 10 ps.</p> <p>The system contains ~ 150 mM NaCl.</p>

opencc-by-4.0Mar 2022View details →
zenodo32/100

Amyloid-beta 16-22 peptide monomer simulation (without salt) with the CHARMM-Drude force field and OpenMM (Run 1)

<p>Amyloid-beta 16-22 peptide (monomer) simulations with the CHARMM-Drude force field and OpenMM. Initial structures are obtained from CHARMM-GUI. This is the first independent simulation runs out of three. The system does not contain any ions.</p> <p>Total trajectory length is 1 microseconds. Frame saving frequency is 10 ps.</p> <p>All the simulation parameters and force field files are uploaded into this repository. Simulations are done with OpenMM v. 7.5.1.</p> <p>&nbsp;</p>

opencc-by-4.0Mar 2022View details →
zenodo32/100

Amyloid-beta 16-22 peptide dimer simulation (150 mM NaCl) with the CHARMM-Drude force field and OpenMM (Run 2)

<p>MD simulations of the Amyloid-beta 16-22 dimer at 150 mM NaCl concentration with CHARMM-Drude force field and OpenMM. Initial structure is obtained from CHARMM-GUI. In the initial configuration, two amyloid-beta 16-22 monomers are not interacting. This repository contains the second out of three independent runs.</p> <p>All the simulation parameters and force field files are uploaded into this repository. Simulations are done with OpenMM v. 7.5.1.</p> <p>The trajectory is divided into 7 parts: part_1-2 are each 200 ns long; part_3-6 are each 100 ns long, and part_7 is 640 ns long. Frames are saved in every 10 ps.</p>

opencc-by-4.0Mar 2022View details →
zenodo32/100

Amyloid-beta 16-22 peptide monomer simulation (without salt) with the CHARMM-Drude force field and OpenMM (Run 2)

<p>Amyloid-beta 16-22 peptide (monomer) simulations with the CHARMM-Drude force field and OpenMM. Initial structures are obtained from CHARMM-GUI. This is the second independent simulation run out of three. The system does not contain any ions.</p> <p>Total trajectory length is 1 microseconds. Frame saving frequency is 10 ps.</p> <p>All the simulation parameters and force field files are uploaded into this repository. Simulations are done with OpenMM v. 7.5.1.</p> <p>&nbsp;</p>

opencc-by-4.0Mar 2022View details →
zenodo32/100

Amyloid-beta 16-22 peptide dimer simulation (150 mM NaCl) with the CHARMM-Drude force field and OpenMM (Run 1)

<p>MD simulations of the Amyloid-beta 16-22 dimer at 150 mM NaCl concentration with CHARMM-Drude force field and OpenMM. Initial structure is obtained from CHARMM-GUI. In the initial configuration, two amyloid-beta 16-22 monomers are not interacting. This repository contains the first out of three independent runs.</p> <p>All the simulation parameters and force field files are uploaded into this repository. Simulations are done with OpenMM v. 7.5.1.</p> <p>The trajectory is divided into 7 parts: part_1-2 are each 200 ns long; part_3-6 are each 100 ns long, and part_7 is 640 ns long. Frames are saved in every 10 ps.</p>

opencc-by-4.0Mar 2022View details →
zenodo32/100

Amyloid-beta 16-22 peptide dimer simulation (150 mM NaCl) with the CHARMM-Drude force field and OpenMM (Run 3)

<p>MD simulations of the Amyloid-beta 16-22 dimer at 150 mM NaCl concentration with CHARMM-Drude force field and OpenMM. Initial structure is obtained from CHARMM-GUI. In the initial configuration, two amyloid-beta 16-22 monomers are not interacting. This repository contains the third out of three independent runs.</p> <p>All the simulation parameters and force field files are uploaded into this repository. Simulations are done with OpenMM v. 7.5.1.</p> <p>The trajectory is divided into 7 parts: part_1-2 are each 200 ns long; part_3-6 are each 100 ns long, and part_7 is 640 ns long. Frames are saved in every 10 ps.</p>

opencc-by-4.0Mar 2022View details →
zenodo32/100

Amyloid-beta 16-22 peptide dimer simulation (150mM NaCl) with the CHARMM36m force field and Gromacs (Run 2)

<p>Amyloid-beta 16-22 peptide dimer simulation with the CHARMM36m force field. This directory contains the&nbsp;second&nbsp;of the three independent trajectories and the simulation length is 1 microseconds. The system contains two amyloid-beta 16-22 monomers, 30 Na+, 30 Cl-, and 10564 TIP3P water.</p>

opencc-by-4.0May 2022View details →
zenodo32/100

Amyloid-beta 16-22 peptide dimer simulation (150mM NaCl) with the CHARMM36m force field and Gromacs (Run 1)

<p>Amyloid-beta 16-22 peptide dimer simulation with the CHARMM36m force field. This directory contains first of the three independent trajectories and the simulation length is 1 microseconds. The system contains two amyloid-beta 16-22 monomers, 30 Na+, 30 Cl-, and 10564 TIP3P water.</p>

opencc-by-4.0May 2022View details →
zenodo32/100

Ligand Field Molecular Dynamics Simulation of Pt(II)-Phenanthroline Binding to N-Terminal Fragment of Amyloid-beta Peptide

<p>DL_POLY Classic input and output files for 10 MD simulations: 5 of free peptide, 5 with Pt(phen)</p>

opencc-by-4.0Nov 2017View details →
zenodo32/100

Metal Binding to Amyloid Beta 1-42: A Ligand Field Molecular Dynamics Study

<p>DL_POLY Classic inputs and trajectories (PDB format) for 3 x free, Cu and Pt simulations</p>

opencc-by-4.0Jun 2018View details →
zenodo32/100

Molecular Dynamics Simulation of Aluminium Binding to Amyloid-beta and its Effect on Peptide Structure

<p>MD frames and highest populated clusters, in PDB format</p>

opencc-by-4.0Mar 2019View details →

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