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Glycosylation End Products, Advanced
Known as:
Advanced Glycation End Products
, Advanced Glycation End-Product
, Advanced Glycation Endproducts
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Products derived from the nonenzymatic reaction of GLUCOSE and PROTEINS in vivo that exhibit a yellow-brown pigmentation and an ability to…
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National Institutes of Health
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Related topics
Related topics
11 relations
Diabetes Mellitus
In Blood
Process of secretion
agonists
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glucosepane
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2015
Review
2015
Cardiovascular Consequences of Obesity and Type 2 Diabetes Damaging effects of hyperglycemia on cardiovascular function : spotlight on glucose metabolic pathways
R. Mapanga
,
M. Essop
2015
Corpus ID: 29981752
Mapanga RF, Essop MF. Damaging effects of hyperglycemia on cardiovascular function: spotlight on glucose metabolic pathways. Am J…
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Highly Cited
2004
Highly Cited
2004
Association between acute-phase reactants and advanced glycation end products in type 2 diabetes.
K. Tan
,
W. Chow
,
S. Tam
,
R. Bucala
,
J. Betteridge
Diabetes Care
2004
Corpus ID: 15139480
OBJECTIVE Type 2 diabetes is associated with chronic low-grade inflammation, but the underlying mechanism(s) is not well…
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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
1999
Highly Cited
1999
Diabetic retinopathy risk correlates with intracellular concentrations of the glycoxidation product Ne-(carboxymethyl) lysine independently of glycohaemoglobin concentrations
H. Hammes
,
M. Brownlee
,
J. Lin
,
E. Schleicher
,
R. Bretzel
Diabetologia
1999
Corpus ID: 27479242
Aims/hypothesis. We investigated whether either the amount of diabetes-induced intracellular oxidative stress or the…
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Highly Cited
1998
Highly Cited
1998
The advanced glycation end product Nepsilon-(carboxymethyl)lysine is increased in serum from children and adolescents with type 1 diabetes.
Tore Julsrud Berg
,
J. Clausen
,
P. A. Torjesen
,
K. Dahl-Jørgensen
,
H. Bangstad
,
Kristian F. Hanssen
Diabetes Care
1998
Corpus ID: 25890334
OBJECTIVE To investigate whether children and adolescents with type 1 diabetes have increased serum levels of the glycoxidation…
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Highly Cited
1997
Highly Cited
1997
Relative contributions of advanced glycation and nitric oxide synthase inhibition to aminoguanidine-mediated renoprotection in diabetic rats
T. Soulis
,
Mark E. Cooper
,
+4 authors
George Jerums
Diabetologia
1997
Corpus ID: 785987
Summary Advanced glycation end products (AGEs) have previously been shown to be increased in the diabetic kidney. Aminoguanidine…
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Highly Cited
1997
Highly Cited
1997
Methylglyoxal-modified arginine residues--a signal for receptor-mediated endocytosis and degradation of proteins by monocytic THP-1 cells.
M. Westwood
,
O. Argirov
,
E. A. Abordo
,
Paul J Thornalley
Biochimica et Biophysica Acta
1997
Corpus ID: 27409534
Highly Cited
1995
Highly Cited
1995
Receptor-mediated toxicity to pericytes of advanced glycosylation end products: a possible mechanism of pericyte loss in diabetic microangiopathy.
S. Yamagishi
,
C. C. Hsu
,
+5 authors
H. Yamamoto
Biochemical and Biophysical Research…
1995
Corpus ID: 29617293
The influence of advanced glycosylation end products (AGE) on bovine retinal pericytes was investigated. When pericytes were…
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Review
1988
Review
1988
Role of advanced glycosylation products in complications of diabetes.
A. Cerami
,
H. Vlassara
,
M. Brownlee
Diabetes Care
1988
Corpus ID: 20753391
Glucose and other reducing sugars can react with proteins and nucleic acids, without the aid of enzymes, to form stable covalent…
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Highly Cited
1988
Highly Cited
1988
Specific Macrophage Receptor Activity for Advanced Glycosylation End Products Inversely Correlates With Insulin Levels In Vivo
H. Vlassara
,
M. Brownlee
,
A. Cerami
Diabetes
1988
Corpus ID: 30125315
A high-affinity macrophage receptor has been shown to mediate the removal of proteins modified by advanced nonenzymatic…
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