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receptor for advanced glycation endproducts
Known as:
Advanced Glycosylation End Product Receptor
, Amphoterin Receptor
, Advanced Glycosylation End Product-Specific Receptor [Chemical/Ingredient]
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A single-pass transmembrane CELL SURFACE RECEPTOR that binds ADVANCED GLYCOSYLATION END PRODUCTS to mediate cellular responses to both acute and…
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National Institutes of Health
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Related topics
Related topics
12 relations
AGER gene
In Blood
agonists
antagonists & inhibitors
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Narrower (5)
Advanced Glycosylation End Product-Specific Receptor
Ager protein, rat
RAGE VC1 protein
esRAGE protein, human
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Broader (1)
receptor
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2015
Review
2015
Limitations of the use of the MP-RAGE to identify neural changes in the brain: recent cigarette smoking alters gray matter indices in the striatum
T. Franklin
,
R. Wetherill
,
K. Jagannathan
,
Nathan M. Hager
,
C. O'brien
,
A. Childress
Frontiers in Human Neuroscience
2015
Corpus ID: 54558233
The magnetization-prepared rapid gradient-echo (MP-RAGE) T1-weighted high resolution structural MRI is a mainstay tool used to…
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2012
2012
Elevated serum levels of AGEs, sRAGE, and pentosidine in Tunisian patients with severity of diabetic retinopathy.
M. Kerkeni
,
A. Saïdi
,
H. Bouzidi
,
S. Ben Yahya
,
M. Hammami
Microvascular Research
2012
Corpus ID: 31656085
2009
2009
Establishment of in vitro binding assay of high mobility group box-1 and S100A12 to receptor for advanced glycation endproducts: heparin's effect on binding.
Rui Liu
,
S. Mori
,
+6 authors
M. Nishibori
Acta Medica Okayama
2009
Corpus ID: 38080441
Interaction between the receptor for advanced glycation end products (RAGE) and its ligands has been implicated in the…
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Review
2008
Review
2008
Role of oxidative stress in the development of vascular injury and its therapeutic intervention by nifedipine.
S. Yamagishi
,
Kazuo Nakamura
,
T. Matsui
Current Medicinal Chemistry
2008
Corpus ID: 29851462
Dihydropyridine-based calcium antagonists (DHPs) are widely used drugs for the treatment of hypertension and angina pectoris. We…
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Highly Cited
2005
Highly Cited
2005
Importance of N-glycosylation positioning for cell-surface expression, targeting, affinity and quality control of the human AT1 receptor.
Pascal M Lanctôt
,
P. Leclerc
,
+4 authors
G. Guillemette
Biochemical Journal
2005
Corpus ID: 558980
GPCRs (G-protein-coupled receptors) are preferentially N-glycosylated on ECL2 (extracellular loop 2). We previously showed that N…
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Highly Cited
2003
Highly Cited
2003
Role of megalin in endocytosis of advanced glycation end products: implications for a novel protein binding to both megalin and advanced glycation end products.
A. Saito
,
R. Nagai
,
+8 authors
F. Gejyo
Journal of the American Society of Nephrology
2003
Corpus ID: 27178766
Advanced glycation end products (AGE) are filtered by glomeruli and reabsorbed and metabolized by proximal tubule cells (PTC). In…
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Review
2003
Review
2003
Pathophysiology of diabetic sexual dysfunction.
S. Morano
Journal of Endocrinological Investigation
2003
Corpus ID: 26706212
Sexual dysfunction is common in patients with diabetes mellitus. Vascular, neurological and hormonal alterations are involved in…
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2001
2001
Differential expression of RAGE in human pancreatic carcinoma cells.
M. Takada
,
Tamio Koizumi
,
H. Toyama
,
Yasuyuki Suzuki
,
Yoshikazu Kuroda
Hepato-Gastroenterology
2001
Corpus ID: 5324456
BACKGROUND/AIMS Amphoterin is a key protein in normal neurite outgrowth and that its receptor on the cell surface, RAGE, is an…
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Highly Cited
1999
Highly Cited
1999
Characterization of the advanced glycation end-product receptor complex in human vascular endothelial cells.
Alan W. Stitt
,
C. Hé
,
H. Vlassara
Biochemical and Biophysical Research…
1999
Corpus ID: 24905876
Advanced glycation end products (AGEs) have been implicated as causal factors in the vascular complications of diabetes and it is…
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Highly Cited
1989
Highly Cited
1989
Structural requirements for protein N-glycosylation. Influence of acceptor peptides on cotranslational glycosylation of yeast invertase and site-directed mutagenesis around a sequon sequence.
T. Roitsch
,
L. Lehle
European Journal of Biochemistry
1989
Corpus ID: 41472609
To understand better the structural requirements of the protein moiety important for N-glycosylation, we have examined the…
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