Results 41 to 50 of about 8,200,615 (297)
Zinc against advanced glycation end products [PDF]
SummaryAdvanced glycation end products (AGEs) are destructive compounds with pathogenic importance in age‐related chronic diseases. Zinc has antioxidant, anti‐inflammatory and anti‐apoptotic potential. This study aimed to summarize effects of zinc onAGEformation andAGE‐induced damaging agents.
Sorayya Kheirouri +2 more
openaire +2 more sources
Glycation is a non-enzymatic biochemical reaction between reducing sugars and amino acids, causing the crosslinking and rearrangement of glycated proteins, leading to irreversible formation of Advanced Glycation End products (AGEs).
Alpana Pande +4 more
doaj +1 more source
Advanced glycation end products
Advanced glycation end products (AGEs) are a heterogeneous group of compounds formed by non-enzymatic interactions between the carbonyl groups of reducing sugars and free amino groups of proteins, lipids, or nucleic acids.
Dat, Pham Thai
core
Introduction High mobility group box 1 is a versatile protein involved in gene transcription, extracellular signaling, and response to inflammation. Extracellularly, high mobility group box 1 binds to several receptors, notably the receptor for advanced ...
Austin Nguyen +4 more
doaj +1 more source
Background/Purpose: Periodontal disease and diabetes mellitus (DM) are both chronic inflammatory and highly prevalent diseases. A large amount of evidence suggested that the accumulation of oxidative stress plays a significant role in the deterioration ...
Chia-Ming Liu +5 more
doaj +1 more source
Advanced glycation end products and diabetic retinopathy [PDF]
Studies have established hyperglycemia as the most important factor in the progress of vascular complications. Formation of advanced glycation end products (AGEs) correlates with glycemic control. The AGE hypothesis proposes that hyperglycemia contributes to the pathogenesis of diabetic complications including retinopathy.
Yashodhara, Sharma +4 more
openaire +2 more sources
Advanced Glycation End-products and Atherosclerosis
The late rearrangements of the covalent nonenzymatic modification of proteins by glucose, called advanced glycation end-products (AGEs), have been shown to accumulate in diabetic and ageing tissues. AGEs elicit a wide range of cell-mediated responses leading to vascular dysfunction, matrix expansion and athero- and glomerulosclerosis.
openaire +2 more sources
Differential effects of glyoxalase 1 overexpression on diabetic atherosclerosis and renal dysfunction in streptozotocin-treated, apolipoprotein E-deficient mice [PDF]
The reactive dicarbonyls, glyoxal and methylglyoxal (MG), increase in diabetes and may participate in the development of diabetic complications. Glyoxal and MG are detoxified by the sequential activities of glyoxalase 1 (GLO1) and glyoxalase 2.
Rabbani, Naila +11 more
core +1 more source
The molecular consequences of specific lysine modifications in Alzheimer´s disease remain insufficiently resolved in the context of full‐length protein. Here we integrate protein semisynthesis, segmental isotope labelling, and high‐resolution NMR spectroscopy to achieve residue‐resolved interrogation of site‐specific acetylation and carboxymethylation.
Dominik P. Vogl +4 more
wiley +2 more sources
Advanced Glycation End Products and Inflammation in Type 1 Diabetes Development
Type 1 diabetes (T1D) is an autoimmune disease in which the β-cells of the pancreas are attacked by the host’s immune system, ultimately resulting in hyperglycemia. It is a complex multifactorial disease postulated to result from a combination
Rani O. Whiddett +14 more
core +1 more source

