Two novel rat liver membrane proteins that bind advanced glycosylation endproducts: relationship to macrophage receptor for glucose-modified proteins - Wikidata - awgldk - TriplyDB

Two novel rat liver membrane proteins that bind advanced glycosylation endproducts: relationship to macrophage receptor for glucose-modified proteins

Two novel rat liver membrane proteins that bind advanced glycosylation endproducts: relationship to macrophage receptor for glucose-modified proteins

http://www.wikidata.org/entity/Q28645665

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Advanced glycation end products are eliminated by scavenger-receptor-mediated endocytosis in hepatic sinusoidal Kupffer and endothelial cells beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis Role of advanced glycation end products in cellular signaling Advanced glycation end products cause epithelial-myofibroblast transdifferentiation via the receptor for advanced glycation end products (RAGE)Identification of galectin-3 as a high-affinity binding protein for advanced glycation end products (AGE): a new member of the AGE-receptor complex Advanced glycation end products induce a prothrombotic phenotype in mice via interaction with platelet CD36.Receptors for advanced glycosylation endproducts in human brain: role in brain homeostasis Controlling the receptor for advanced glycation end-products to conquer diabetic vascular complications Co-expression of BirA with biotin bait achieves in vivo biotinylation of overexpressed stable N-glycosylated sRAGE in transgenic silkworms.The AGE-receptor in the pathogenesis of diabetic complications.Survey of the distribution of a newly characterized receptor for advanced glycation end products in tissues.Diabetic vascular dysfunction: links to glucose-induced reductive stress and VEGF.Regulation of RAGE for attenuating progression of diabetic vascular complications.Carbonyl stress and diabetic complications.Receptor-specific induction of insulin-like growth factor I in human monocytes by advanced glycosylation end product-modified proteins.Role of glycation in aging.Advanced glycation end products (AGEs) on the surface of diabetic erythrocytes bind to the vessel wall via a specific receptor inducing oxidant stress in the vasculature: a link between surface-associated AGEs and diabetic complications.Receptor for advanced glycation end products (AGEs) has a central role in vessel wall interactions and gene activation in response to circulating AGE proteins Advanced glycation end products (AGEs) co-localize with AGE receptors in the retinal vasculature of diabetic and of AGE-infused rats.Immunohistochemical and ultrastructural detection of advanced glycation end products in atherosclerotic lesions of human aorta with a novel specific monoclonal antibody.Localization of the ezrin binding epitope for glycated proteins.Elevated AGE-modified ApoB in sera of euglycemic, normolipidemic patients with atherosclerosis: relationship to tissue AGEs Receptor-specific increase in extracellular matrix production in mouse mesangial cells by advanced glycosylation end products is mediated via platelet-derived growth factor Molecular identity and cellular distribution of advanced glycation endproduct receptors: relationship of p60 to OST-48 and p90 to 80K-H membrane proteins.Exogenous advanced glycosylation end products induce complex vascular dysfunction in normal animals: a model for diabetic and aging complications.Advanced glycation end product receptor-1 transgenic mice are resistant to inflammation, oxidative stress, and post-injury intimal hyperplasia.What is the role of the receptor for advanced glycation end products-ligand axis in liver injury?Advanced glycation endproducts interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice. A potential mechanism for the accelerated vasculopathy of dia Advanced glycosylation endproduct-specific receptors on human and rat T-lymphocytes mediate synthesis of interferon gamma: role in tissue remodeling.Mechanisms of distal axonal degeneration in peripheral neuropathies.Diabetes mellitus in patients with cirrhosis: clinical implications and management.Receptor-mediated endothelial cell dysfunction in diabetic vasculopathy. Soluble receptor for advanced glycation end products blocks hyperpermeability in diabetic rats.The receptor for advanced glycation end products (RAGE) is a central mediator of the interaction of AGE-beta2microglobulin with human mononuclear phagocytes via an oxidant-sensitive pathway. Implications for the pathogenesis of dialysis-related amyl Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products.The use of optical sensors to understand cellular interactions with renal cells.Advanced glycation end-products and atherosclerosis.Atherogenesis and advanced glycation: promotion, progression, and prevention.Expression of receptors for advanced glycation end products in peripheral occlusive vascular disease.The amino-terminal domains of the ezrin, radixin, and moesin (ERM) proteins bind advanced glycation end products, an interaction that may play a role in the development of diabetic complications.Advanced glycation endproducts (AGEs) induce oxidant stress in the gingiva: a potential mechanism underlying accelerated periodontal disease associated with diabetes.

P2860

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P2860

Two novel rat liver membrane proteins that bind advanced glycosylation endproducts: relationship to macrophage receptor for glucose-modified proteins

http://www.wikidata.org/entity/Q28645665

description

1991 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

1991 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

artículu científicu espublizáu en 1991

@ast

im September 1991 veröffentlichter wissenschaftlicher Artikel

@de

scientific journal article

@en

vedecký článok (publikovaný 1991/09/01)

@sk

vědecký článek publikovaný v roce 1991

@cs

wetenschappelijk artikel (gepubliceerd op 1991/09/01)

@nl

наукова стаття, опублікована у вересні 1991

@uk

مقالة علمية (نشرت في سبتمبر 1991)

@ar

name

Two novel rat liver membrane p ...... for glucose-modified proteins

@ast

Two novel rat liver membrane p ...... for glucose-modified proteins

@en

Two novel rat liver membrane p ...... for glucose-modified proteins

@nl

type

label

Two novel rat liver membrane p ...... for glucose-modified proteins

@ast

Two novel rat liver membrane p ...... for glucose-modified proteins

@en

Two novel rat liver membrane p ...... for glucose-modified proteins

@nl

prefLabel

Two novel rat liver membrane p ...... for glucose-modified proteins

@ast

Two novel rat liver membrane p ...... for glucose-modified proteins

@en

Two novel rat liver membrane p ...... for glucose-modified proteins

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Journal of Experimental Medicine

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Two novel rat liver membrane p ...... for glucose-modified proteins

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A. Cerami

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H. Vlassara

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M. Suthanthiran

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P. Sehajpal

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S. Brunelle

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Y. Horii

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Z. Makita

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Z. Yang

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P2860

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Phase separation of integral membrane proteins in Triton X-114 solution

Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril

Purification and characterization of a bovine acetyl low density lipoprotein receptor.

Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of platelet-derived growth factor: role in vascular disease of diabetes and aging.

Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking.

Nonenzymatic browning in vivo: possible process for aging of long-lived proteins.

Aging of proteins: isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose

Accumulation of diabetic rat peripheral nerve myelin by macrophages increases with the presence of advanced glycosylation endproducts

Endothelial receptor-mediated binding of glucose-modified albumin is associated with increased monolayer permeability and modulation of cell surface coagulant properties.

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515–524

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scholarly article

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10.1084/JEM.174.3.515

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3

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174

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1991-09-01T00:00:00Z

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21503712

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1651976

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2118929

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