(Q27664995)

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

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scholarly article

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

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crystal structure

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1 reference

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Jeffrey C Boyington

3

object named as

Jeffrey C Boyington

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author name string

Hajeung Park

1

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Floyd G Adsit

2

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language of work or name

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publication date

24 December 2010

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Journal of Biological Chemistry

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285

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52

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40762-70

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Structural and functional insights into RAGE activation by multimeric S100B

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Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Protein structure comparison by alignment of distance matrices

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20 March 2017

The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of rage and amphoterin in the developing nervous system

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Structural basis for pattern recognition by the receptor for advanced glycation end products (RAGE).

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Crystallographic refinement of ligand complexes

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cDNA cloning of a novel secreted isoform of the human receptor for advanced glycation end products and characterization of cells co-expressing cell-surface scavenger receptors and Swedish mutant amyloid precursor protein.

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Zinc-dependent affinity chromatography of the S100b protein on phenyl-Sepharose. A rapid purification method.

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