Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction - Wikidata - wikimedia - TriplyDB

Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction

Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction

http://www.wikidata.org/entity/Q27678167

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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 is a nucleic acid receptor that promotes inflammatory responses to DNA The specificity of DNA recognition by the RAGE receptor The receptor for advanced glycation end products (RAGE) affects T cell differentiation in OVA induced asthma.Modeling the interaction between quinolinate and the receptor for advanced glycation end products (RAGE): relevance for early neuropathological processes Adaptive evolution of the MHC class III-encoded receptor RAGE in primates and murine rodents.THE GLYCOCALYX AND TRAUMA: A REVIEW.The pattern recognition reagents RAGE VC1 and peptide p5 share common binding sites and exhibit specific reactivity with AA amyloid in mice Heparan sulfate: a ubiquitous glycosaminoglycan with multiple roles in immunity Small molecule antagonists of cell-surface heparan sulfate and heparin-protein interactions.Unlocking the biology of RAGE in diabetic microvascular complications Investigation of phosphoproteome in RAGE signaling.Sugar-coated proteins: the importance of degree of polymerisation of oligo-galacturonic acid on protein binding and aggregation.Targeting the Receptor for Advanced Glycation Endproducts (RAGE): A Medicinal Chemistry Perspective.Heparan Sulfate Regulates the Structure and Function of Osteoprotegerin in Osteoclastogenesis.Danger signals in regulating the immune response to solid organ transplantation.Expression and subcellular localization of RAGE in melanoma cells.Change in the Molecular Dimension of a RAGE-Ligand Complex Triggers RAGE Signaling.The receptor for advanced glycation end-products (RAGE) is only present in mammals, and belongs to a family of cell adhesion molecules (CAMs).Glycosaminoglycan-Mediated Downstream Signaling of CXCL8 Binding to Endothelial Cells.Danger-Associated Molecular Patterns Derived From the Extracellular Matrix Provide Temporal Control of Innate Immunity.Tannerella forsythia-produced methylglyoxal causes accumulation of advanced glycation endproducts to trigger cytokine secretion in human monocytes.

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Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction

http://www.wikidata.org/entity/Q27678167

description

2013 nî lūn-bûn

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2013 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2013 թվականի հուլիսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction

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Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction

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Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction

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Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction

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Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction

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Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction

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Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction

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Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction

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Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction

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ACS Chemical Biology

P1476

Stable RAGE-heparan sulfate complexes are essential for signal transduction

@en

P2093

Danyin Song

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

Jeffrey D Esko

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Jeffrey H Young

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

Juno M Krahn

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Walter J Chazin

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P2860

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

Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization

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

Matuzumab Binding to EGFR Prevents the Conformational Rearrangement Required for Dimerization

Antibody-based targeting of FGFR3 in bladder carcinoma and t(4;14)-positive multiple myeloma in mice

The 1.5 A Crystal Structure of Human Receptor for Advanced Glycation Endproducts (RAGE) Ectodomains Reveals Unique Features Determining Ligand Binding

Structural Basis for Ligand Recognition and Activation of RAGE

Advanced Glycation End Product Recognition by the Receptor for AGEs

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1611-1620

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scholarly article

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10.1021/CB4001553

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7

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8

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Kevin D Corbett

Lars C Pedersen

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2013-05-28T00:00:00Z

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23679870

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3806902

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