Homodimerization is essential for the receptor for advanced glycation end products (RAGE)-mediated signal transduction. - Wikidata - awgldk - TriplyDB

Homodimerization is essential for the receptor for advanced glycation end products (RAGE)-mediated signal transduction.

Homodimerization is essential for the receptor for advanced glycation end products (RAGE)-mediated signal transduction.

http://www.wikidata.org/entity/Q39700115

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Structural insights into calcium-bound S100P and the V domain of the RAGE complex Structural insights into the oligomerization mode of the human receptor for advanced glycation end-products RAGE: a new frontier in chronic airways disease Advanced Glycation End Product Recognition by the Receptor for AGEs Signal Transduction in Receptor for Advanced Glycation End Products (RAGE): SOLUTION STRUCTURE OF C-TERMINAL RAGE (ctRAGE) AND ITS BINDING TO mDia1 Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction RAGE is a nucleic acid receptor that promotes inflammatory responses to DNA The Receptor for Advanced Glycation End Products (RAGE) Specifically Recognizes Methylglyoxal-Derived AGEs The receptor for advanced glycation end-products supports lung tissue biomechanics.Plasma levels of high-mobility group box 1 and soluble receptor for advanced glycation end products in primary antiphospholipid antibody syndrome patients.Ischemia-reperfusion injury of the retina is linked to necroptosis via the ERK1/2-RIP3 pathway.Disulfide bonds within the C2 domain of RAGE play key roles in its dimerization and biogenesis.Oligomerization interface of RAGE receptor revealed by MS-monitored hydrogen deuterium exchange Alternative splicing of the RAGE cytoplasmic domain regulates cell signaling and function.RAGE regulates immune cell infiltration and angiogenesis in choroidal neovascularization.Electroacupuncture-like stimulation at the Baihui (GV20) and Dazhui (GV14) acupoints protects rats against subacute-phase cerebral ischemia-reperfusion injuries by reducing S100B-mediated neurotoxicity Structural insights into the binding of the human receptor for advanced glycation end products (RAGE) by S100B, as revealed by an S100B-RAGE-derived peptide complex.Adaptive evolution of the MHC class III-encoded receptor RAGE in primates and murine rodents.RAGE and tobacco smoke: insights into modeling chronic obstructive pulmonary disease.Senescence-dependent impact of anti-RAGE antibody on endotoxemic liver failure AGEs, RAGE, and diabetic retinopathy.Cell signaling and receptors in toxicity of advanced glycation end products (AGEs): α-dicarbonyls, radicals, oxidative stress and antioxidants.Unlocking the biology of RAGE in diabetic microvascular complications The emerging role of the receptor for advanced glycation end products on innate immunity.ADAM-family metalloproteinases in lung inflammation: potential therapeutic targets.Circulating soluble receptor for advanced glycation end products (sRAGE) as a biomarker of emphysema and the RAGE axis in the lung.Targeting the Receptor for Advanced Glycation Endproducts (RAGE): A Medicinal Chemistry Perspective.Tetrameric Acetyl-CoA Acetyltransferase 1 Is Important for Tumor Growth.Maillard reaction in food allergy: Pros and cons.Solution structure of the soluble receptor for advanced glycation end products (sRAGE).Low-molecular weight fractions of Japanese soy sauce act as a RAGE antagonist via inhibition of RAGE trafficking to lipid rafts.RAGE-Mediated Suppression of Interleukin-10 Results in Enhanced Mortality in a Murine Model of Acinetobacter baumannii Sepsis.Change in the Molecular Dimension of a RAGE-Ligand Complex Triggers RAGE Signaling.Increased expression of receptor for advanced glycation end-products worsens focal brain ischemia in diabetic rats.Identifying key juxtamembrane interactions in cell membranes using AraC-based transcriptional reporter assay (AraTM).DNAX-activating protein 10 (DAP10) membrane adaptor associates with receptor for advanced glycation end products (RAGE) and modulates the RAGE-triggered signaling pathway in human keratinocytes Injury of cortical neurons is caused by the advanced glycation end products-mediated pathway.The gut as a sensory organ.Danger-Associated Molecular Patterns Derived From the Extracellular Matrix Provide Temporal Control of Innate Immunity.Advanced glycation end products (AGEs) are cross-sectionally associated with insulin secretion in healthy subjects.

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Homodimerization is essential for the receptor for advanced glycation end products (RAGE)-mediated signal transduction.

http://www.wikidata.org/entity/Q39700115

description

2010 nî lūn-bûn

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2010年の論文

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年学术文章

@zh-sg

2010年學術文章

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2010年學術文章

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2010年學術文章

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name

Homodimerization is essential ...... -mediated signal transduction.

@en

Homodimerization is essential for the receptor for advanced glycation end products

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type

label

Homodimerization is essential ...... -mediated signal transduction.

@en

Homodimerization is essential for the receptor for advanced glycation end products

@nl

prefLabel

Homodimerization is essential ...... -mediated signal transduction.

@en

Homodimerization is essential for the receptor for advanced glycation end products

@nl

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JBC.M110.133827

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Journal of Biological Chemistry

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Homodimerization is essential ...... )-mediated signal transduction

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P2093

Angelina Madden

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Christopher T Elliott

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Hongliang Zong

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Mark H Mooney

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Micheal Ward

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P2860

Receptor for advanced glycation end products (RAGE)-mediated neurite outgrowth and activation of NF-kappaB require the cytoplasmic domain of the receptor but different downstream signaling pathways

RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides

Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins

RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease

Structural and functional insights into RAGE activation by multimeric S100B

Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42

S100B and S100A6 differentially modulate cell survival by interacting with distinct RAGE (receptor for advanced glycation end products) immunoglobulin domains

Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Isolation and characterization of the wild-type enzyme

Characterization of the advanced glycation end-product receptor complex in human vascular endothelial cells

S100A8 and S100A9 activate MAP kinase and NF-kappaB signaling pathways and trigger translocation of RAGE in human prostate cancer cells

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23137-23146

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2906307

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