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RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease
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scholarly article
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title
RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease
(English)
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main subject
Alzheimer's disease
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inferred from title
neurotoxicity
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inferred from title
toxic encephalopathy
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author
Peter P Nawroth
series ordinal
12
object named as
P Nawroth
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author name string
S D Yan
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1
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X Chen
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2
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J Fu
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3
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M Chen
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4
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H Zhu
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5
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A Roher
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6
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T Slattery
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7
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L Zhao
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8
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M Nagashima
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9
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J Morser
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10
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A Migheli
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11
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D Stern
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13
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A M Schmidt
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14
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language of work or name
English
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publication date
22 August 1996
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published in
Nature
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volume
382
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page(s)
685-91
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issue
6593
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cites work
Tau protein and the neurofibrillary pathology of Alzheimer's disease
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The Alzheimer's disease sphinx: a riddle with plaques and tangles
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Amyloid beta-protein as a substrate interacts with extracellular matrix to promote neurite outgrowth
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Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides
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The amyloid beta-protein of Alzheimer's disease is chemotactic for mononuclear phagocytes
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A model for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease
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Hydrogen peroxide mediates amyloid beta protein toxicity
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β-Amyloid stimulates glial cells in vitro to produce growth factors that accumulate in senile plaques in Alzheimer's disease
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?1-Antichymotrypsin Binding to Alzheimer A? Peptides Is Sequence Specific and Induces Fibril Disaggregation In Vitro
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The cerebrospinal-fluid soluble form of Alzheimer's amyloid beta is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex
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Amyloid beta-protein activates tachykinin receptors and inositol trisphosphate accumulation by synergy with glutamate
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Avid binding of beta A amyloid peptide to its own precursor
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Transthyretin sequesters amyloid beta protein and prevents amyloid formation
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Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: implications for Alzheimer's disease.
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The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of rage and amphoterin in the developing nervous system
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Glycated tau protein in Alzheimer disease: a mechanism for induction of oxidant stress
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Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide.
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Direct evidence of oxidative injury produced by the Alzheimer's beta-amyloid peptide (1-40) in cultured hippocampal neurons
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Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium
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beta-Amyloid-mediated vasoactivity and vascular endothelial damage.
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Direct expression cloning of vascular cell adhesion molecule 1, a cytokine-induced endothelial protein that binds to lymphocytes
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Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products
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Microglia and cytokines in neurological disease, with special reference to AIDS and Alzheimer's disease
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Clinical trial of indomethacin in Alzheimer's disease.
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Effect of fatty acid profiles on the susceptibility of cultured rabbit tracheal epithelial cells to hyperoxic injury.
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Identifiers
DOI
10.1038/382685A0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
124759
Dimensions Publication ID
1012543542
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OpenCitations bibliographic resource ID
124759
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
124759
PubMed ID
8751438
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
124759
ResearchGate publication ID
232755942
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Springer Nature article ID
10.1038/382685a0
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