Structural Basis for Ligand Recognition and Activation of RAGE - Test2 - elhamkhani - TriplyDB

Structural Basis for Ligand Recognition and Activation of RAGE

Structural Basis for Ligand Recognition and Activation of RAGE

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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 Structural characterization of S100A15 reveals a novel zinc coordination site among S100 proteins and altered surface chemistry with functional implications for receptor binding Does Infection-Induced Immune Activation Contribute to Dementia?Parallel manifestations of neuropathologies in the enteric and central nervous systems RAGE: a new frontier in chronic airways disease Advanced Glycation End Product Recognition by the Receptor for AGEs Experimental phasing using zinc anomalous scattering 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 NMR structure note: the structure of human calcium-bound S100A11 The Receptor for Advanced Glycation End Products (RAGE) Specifically Recognizes Methylglyoxal-Derived AGEs HMGB1 conveys immunosuppressive characteristics on regulatory and conventional T cells A multimodal RAGE-specific inhibitor reduces amyloid β-mediated brain disorder in a mouse model of Alzheimer disease Blocking the Interactions between Calcium-Bound S100A12 Protein and the V Domain of RAGE Using Tranilast The multiple faces of RAGE--opportunities for therapeutic intervention in aging and chronic disease The receptor for advanced glycation end-products supports lung tissue biomechanics.Tranilast Blocks the Interaction between the Protein S100A11 and Receptor for Advanced Glycation End Products (RAGE) V Domain and Inhibits Cell Proliferation Characterization of αX I-Domain Binding to Receptors for Advanced Glycation End Products (RAGE)Ischemia-reperfusion injury of the retina is linked to necroptosis via the ERK1/2-RIP3 pathway.Peptide aptamers: development and applications.Disulfide bonds within the C2 domain of RAGE play key roles in its dimerization and biogenesis.Relating form and function of EF-hand calcium binding proteins.Combinatorial library of improved peptide aptamers, CLIPs to inhibit RAGE signal transduction in mammalian cells.Oligomerization interface of RAGE receptor revealed by MS-monitored hydrogen deuterium exchange Blockade of the formation of insoluble ubiquitinated protein aggregates by EGCG3"Me in the alloxan-induced diabetic kidney.Modeling the interaction between quinolinate and the receptor for advanced glycation end products (RAGE): relevance for early neuropathological processes Influence of nonenzymatic posttranslational modifications on constitution, oligomerization and receptor binding of S100A12 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.Isolevuglandin-type lipid aldehydes induce the inflammatory response of macrophages by modifying phosphatidylethanolamines and activating the receptor for advanced glycation endproducts.A specific RAGE-binding peptide biopanning from phage display random peptide library that ameliorates symptoms in amyloid β peptide-mediated neuronal disorder.Role of advanced glycation end products in cardiovascular disease.Structures of CD6 and Its Ligand CD166 Give Insight into Their Interaction.Small Molecule Inhibition of Ligand-Stimulated RAGE-DIAPH1 Signal Transduction Mouse RAGE Variant 4 Is a Dominant Membrane Receptor that Does Not Shed to Generate Soluble RAGE.Virtual screening of RAGE inhibitors using molecular docking Neurovascular dysfunction and faulty amyloid β-peptide clearance in Alzheimer disease.Lysophosphatidic acid targets vascular and oncogenic pathways via RAGE signaling.

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Structural Basis for Ligand Recognition and Activation of RAGE

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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年學術文章

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Structural Basis for Ligand Recognition and Activation of RAGE

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Structural Basis for Ligand Recognition and Activation of RAGE

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Structural Basis for Ligand Recognition and Activation of RAGE

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Structural Basis for Ligand Recognition and Activation of RAGE

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Structural Basis for Ligand Recognition and Activation of RAGE

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Structural basis for ligand recognition and activation of RAGE

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Brian M Dattilo

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Joachim Diez

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Michael Koch

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Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors

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

Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations

Structural and functional characterization of the monomeric U-box domain from E4B

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

Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100 target specificity and activation of the kinase

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

Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor

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