Page last updated: 2024-08-21

sodium hydroxide and amyloid beta-peptides

sodium hydroxide has been researched along with amyloid beta-peptides in 1 studies

Research

Studies (1)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Condron, MM; Fezoui, Y; Fink, AL; Harper, JD; Hartley, DM; Khurana, R; Lansbury, PT; Selkoe, DJ; Teplow, DB; Walsh, DM	1

Other Studies

1 other study(ies) available for sodium hydroxide and amyloid beta-peptides

Article	Year
An improved method of preparing the amyloid beta-protein for fibrillogenesis and neurotoxicity experiments. Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 2000, Volume: 7, Issue:3 Topics: Amino Acid Sequence; Amyloid beta-Peptides; Animals; Cells, Cultured; Chromatography, High Pressure Liquid; Circular Dichroism; Coculture Techniques; Coloring Agents; Congo Red; Dimerization; Filtration; Freeze Drying; Humans; Hydrogen-Ion Concentration; Isoelectric Point; Microscopy, Atomic Force; Molecular Sequence Data; Molecular Weight; Neuroglia; Neurons; Peptide Fragments; Protein Conformation; Protein Structure, Secondary; Rats; Sodium Hydroxide; Solubility; Solvents; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship; Time Factors	2000

Article

Year

An improved method of preparing the amyloid beta-protein for fibrillogenesis and neurotoxicity experiments.

Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 2000, Volume: 7, Issue:3

Topics: Amino Acid Sequence; Amyloid beta-Peptides; Animals; Cells, Cultured; Chromatography, High Pressure Liquid; Circular Dichroism; Coculture Techniques; Coloring Agents; Congo Red; Dimerization; Filtration; Freeze Drying; Humans; Hydrogen-Ion Concentration; Isoelectric Point; Microscopy, Atomic Force; Molecular Sequence Data; Molecular Weight; Neuroglia; Neurons; Peptide Fragments; Protein Conformation; Protein Structure, Secondary; Rats; Sodium Hydroxide; Solubility; Solvents; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship; Time Factors

2000