Evolution of the Research Literature and the Scientific Community of Alzheimer’s Disease from 1983-2017: A 35-Year Survey.
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Evolution of the Research Literature and the Scientific Community of Alzheimer’s Disease from 1983-2017: A 35-Year Survey.
This study surveys the development of Alzheimer’s disease (AD) in the research literature, the scientific community, and journals containing the letters AD over a period of 35 years. research papers about AD 1983-2017 published in journals indexed in the Web of Science analyzed in seven five-year period.
Total paper AD increased from 1,095 in 1983-1987 to 50 532 by 2013 to 2017 and in the same time period, the number of participating countries went from 27 to 152. The US is the most productive country in the whole, followed by some European countries, Canada, Australia, and Japan. Asian countries have emerged and by 2013-2017, China surpassed all but the US in productivity. Countries in Latin America and Africa have also contributed to the study of AD.
In addition, several non-governmental organizations a new one (for example, ADNI, ADI) has emerged and now plays a key role in the fight against AD. Likewise, publishing scientific AD Universe is expanding in many aspects: the increase in the number of journals that contain the AD paper (227 journals in 1983-1987 to 3257 in 2013-2017); the appearance of several journals AD-focused, for example, Alzheimer’s & Dementia, the Journal of Alzheimer’s; and the development of special issues dedicated to AD. Our paper complements a range of papers that still exist in the theoretical and clinical aspects of AD and provide an overview of the research landscape of the country and contributes journal papers related to AD.
We sought to examine the association of race / ethnicity with a willingness to engage in a study involving a typical procedure of Alzheimer’s disease (AD) clinical trials and determine whether the observed differences can be explained by attitudes.We research studied 2749 adults aged ≥50 years who were enrolled in recruitment registry.
Compared to community-based non-Hispanic (NH) white (n = 2393, 87%), Hispanic (n = 191, 7%), NH Asia (n = 129, 5%) and NH blacks (n = 36 , 1%) was 44%, 46%, and 64% less willing, respectively, contacted for the study who had the typical requirements of AD prevention trials, namely: cognitive testing, brain imaging, blood draws, and studied medicine. Mediation by the attitude of research explored, but it does not explain the observed findings indicate that ethnoracial differences.Our minorities less willing to engage in the study were typical of AD prevention trials. Future work should focus on understanding the factors that drive these differences.
Evolution of the Research Literature and the Scientific Community of Alzheimer’s Disease from 1983-2017: A 35-Year Survey.
Photobiomodulation for Alzheimer’s Disease: Translating Basic Research in Clinical Applications.
One of the challenges in translating new therapeutic approaches for bedside patient lies in bridging the gap between laboratory scientists conducting basic research and medical practitioners who are not exposed to highly specialized journals.
This review covers the literature on photobiomodulation therapy as a new approach to prevent and treat Alzheimer’s disease, which aims to bridge the gap that by gathering together the requirements and technical specifications into a single brief advice to the treatment protocol. Given the predicted doubling the number of people affected by dementia and Alzheimer’s disease in the next 30 years, treatment options have shown promising results in studies of cell cultures and animal models, and has been proven safe in humans, should not be left in the dark.
Description: Human thalamus tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human thalamus tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the thalamus tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The thalamus tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human pons tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human pons tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the pons tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The pons tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human amygdala tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human amygdala tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the amygdala tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The amygdala tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human hippocamps tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human hippocamps tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the hippocamps tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The hippocamps tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Genomic DNA - Multiple Sclerosis Disease: Brain: Thalamus, from a single donor
Description: Human frontal lobe tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human frontal lobe tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the frontal lobe tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The frontal lobe tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Membrane Protein - Alzheimer's Disease:Brain: Hippocampus
Description: Human parietal lobe tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human parietal lobe tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the parietal lobe tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The parietal lobe tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human temporal lobe tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human temporal lobe tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the temporal lobe tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The temporal lobe tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human occipital lobe tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human occipital lobe tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the occipital lobe tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The occipital lobe tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Membrane Protein - Alzheimer's Disease:Brain: Temporal Lobe
Description: Human corpus Callosum tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human corpus Callosum tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the corpus Callosum tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The corpus Callosum tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human precentral gyrus tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human precentral gyrus tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the precentral gyrus tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The precentral gyrus tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human brain amygdala tissue membrane protein lysate was prepared by isolating the membrane protein from whole tissue homogenates using a proprietary technique. The human amygdala tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The membrane protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the isolated brain amygdala tissue membrane protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated brain amygdala tissue membrane protein is then Western analyzed by either GAPDH or β-actin antibody to confirm there is no signal or very weak signal.
Description: Human postcentral gyrus tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human postcentral gyrus tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the postcentral gyrus tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The postcentral gyrus tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human brain hippocamps tissue membrane protein lysate was prepared by isolating the membrane protein from whole tissue homogenates using a proprietary technique. The human hippocamps tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The membrane protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the isolated brain hippocamps tissue membrane protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated brain hippocamps tissue membrane protein is then Western analyzed by either GAPDH or β-actin antibody to confirm there is no signal or very weak signal.
Description: Human brain hippocamps tissue cytoplasmic protein lysate was prepared by isolating the cytoplasmic protein from whole tissue homogenates using a proprietary technique. The human hippocamps tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The cytoplasmic protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, glycerol, and a cocktail of protease inhibitors. For quality control purposes, the isolated brain hippocamps tissue cytoplasmic protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated brain hippocamps tissue cytoplasmic protein is then Western analyzed by GAPDH antibody, and the expression level is consistent with each lot.
Description: Human brain temporal lobe tissue membrane protein lysate was prepared by isolating the membrane protein from whole tissue homogenates using a proprietary technique. The human temporal lobe tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The membrane protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the isolated brain temporal lobe tissue membrane protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated brain temporal lobe tissue membrane protein is then Western analyzed by either GAPDH or β-actin antibody to confirm there is no signal or very weak signal.
Description: Accumulation of the amyloid-β peptide (Aβ) in the cerebral cortex is a critical event in the pathogenesis of Alzheimer’s disease. The β-amyloid protein precursor (APP) is cleaved by three enzymes (TACE, BACE/BACE2 and γ-secretase) at three distinct sites (α, β and γ respectively). The γ-secretase complex is a membrane-bound aspartyl protease that can cleave certain proteins at peptide bonds buried within the hydrophobic environment of the lipid bilayer and is composed of the proteins APH1, nicastrin, PEN2 and presenilin1. Its cleavage of APP results in either the non-toxic p3 (from the α and γ cleavage site) or the toxic Aβ (from the β and γ cleavage site). APH1 was initially identified as a component of the Notch pathway and exists in at least three distinct isoforms with APH1a as the principal isoform present in the γ-secretase complex. Mice deficient in this isoform, but not the other two, were lethal at E10.5, with impaired vascular and neural development observed. Besides acting as a critical component of the γ-secretase complex, nicastrin is also thought to be involved in cell proliferation and signaling, especially in regards to activation of Notch receptors as loss of nicastrin expression results in mouse embryonic lethality. Presenilin1 was initially identified a marker of susceptibility to early-onset Alzheimer’s disease.;;For images please see PDF data sheet
Description: Accumulation of the amyloid-β peptide (Aβ) in the cerebral cortex is a critical event in the pathogenesis of Alzheimer’s disease. The βamyloid protein precursor (APP) is cleaved by one of two βsecretases (BACE and BACE2), producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for βsecretase to generate the 4 kDa amyloid-β peptide (Aβ), which is deposited in the Alzheimer’s disease patients’ brains. BACE was identified by several groups independently and designated β-site APP cleaving enzyme (BACE) . BACE is a transmembrane aspartic protease and co-localizes with APP. BACE2 also cleaves APP at β-site and at a different site within Aβ. BACE2 locates on chromosome 21q22.3, the so-called ‘Down critical region’, suggesting that BACE2 and Aβ may also contribute to the pathogenesis of Down syndrome.;;For images please see PDF data sheet
Description: Human brain thalamus tissue membrane protein lysate was prepared by isolating the membrane protein from whole tissue homogenates using a proprietary technique. The human thalamus tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The membrane protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the isolated brain thalamus tissue membrane protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated brain thalamus tissue membrane protein is then Western analyzed by either GAPDH or β-actin antibody to confirm there is no signal or very weak signal.
This review covers the mechanistic action photobiomodulation therapies against Alzheimer’s disease at the cellular level. Safe and effective dose has been found in animal models, and the first human case studies have given reasons for doing large scale clinical trials. A brief discussion on the minimum effective dose tolerated and the maximum conclude this review, and provide the basis for a successful translation from bench to bedside.
