Contributions to senescence: non-enzymatic glycosylation of proteins.

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A homologous production system for Trichoderma reesei secreted proteins in a cellulase-free background N-acetylcysteine and taurine prevent hyperglycemia-induced insulin resistance in vivo: possible role of oxidative stress.

P2860

Q35745643-81992C6D-CBFC-4DEB-A01B-C6EEBC7147C9 Q44473636-B7E7C845-E947-4012-96E1-D3D728022D47

P2860

Contributions to senescence: non-enzymatic glycosylation of proteins.

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http://www.wikidata.org/entity/Q41452034

description

1996 nî lūn-bûn

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1996年の論文

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1996年論文

@yue

1996年論文

@zh-hant

1996年論文

@zh-hk

1996年論文

@zh-mo

1996年論文

@zh-tw

1996年论文

@wuu

1996年论文

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1996年论文

@zh-cn

name

Contributions to senescence: non-enzymatic glycosylation of proteins.

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type

Item

label

Contributions to senescence: non-enzymatic glycosylation of proteins.

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prefLabel

Contributions to senescence: non-enzymatic glycosylation of proteins.

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P1476

Contributions to senescence: non-enzymatic glycosylation of proteins.

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P2093

Sullivan R

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P2860

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

Advanced glycosylation products quench nitric oxide and mediate defective endothelium-dependent vasodilatation in experimental diabetes.

Phagocytosis of aged human neutrophils by macrophages is mediated by a novel "charge-sensitive" recognition mechanism

Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus

Maillard reaction-mediated molecular damage to extracellular matrix and other tissue proteins in diabetes, aging, and uremia.

New insights on non-enzymatic glycosylation may lead to therapeutic approaches for the prevention of diabetic complications.

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

High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules.

Glycosylation products as toxic mediators of diabetic complications.

Hepatocyte fine structure during maturation and senescence.

P304

797-806

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P31

scholarly article

P356

10.1076/APAB.104.7.797.13107

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P433

http://www.w3.org/2001/XMLSchema#string

P478

104

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1996-12-01T00:00:00Z

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P698

9127674

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P921

glycosylation

Contributions to senescence: non-enzymatic glycosylation of proteins.

about

P2860

P2860

Contributions to senescence: non-enzymatic glycosylation of proteins.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P921