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Jing Xue

Researcher at University at Albany, SUNY

Publications -  7
Citations -  486

Jing Xue is an academic researcher from University at Albany, SUNY. The author has contributed to research in topics: RAGE (receptor) & Glycation. The author has an hindex of 7, co-authored 7 publications receiving 407 citations. Previous affiliations of Jing Xue include State University of New York System.

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Advanced Glycation End Product Recognition by the Receptor for AGEs

TL;DR: The solution structure of a CEL-containing peptide-RAGE V domain complex reveals that the carboxyethyl moiety fits inside a positively charged cavity of the V domain.
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The Receptor for Advanced Glycation End Products (RAGE) Specifically Recognizes Methylglyoxal-Derived AGEs

TL;DR: It is shown that binding of methylglyoxal-modified albumin to RAGE results in signal transduction and the high affinity and specificity of hydroimidozolones binding to the V domain of RAGE suggest that they are the primary AGE structures that give rise to AGEs–RAGE pathologies.
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Probing protein quinary interactions by in-cell nuclear magnetic resonance spectroscopy.

TL;DR: Cross-correlated relaxation-induced polarization transfer-based in-cell nuclear magnetic resonance allows the characterization of protein quinary interactions with atomic resolution inside live prokaryotic and eukaryotic cells.
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Change in the Molecular Dimension of a RAGE-Ligand Complex Triggers RAGE Signaling.

TL;DR: The weak oligomerization exhibited by many transmembrane receptors has a profound effect on signal transduction, and ligand-induced association of RAGE homo-dimers on the cell surface increases the molecular dimension of the receptor, recruiting Diaphanous 1 (DIAPH1) and activating signaling pathways.
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Combinatorial library of improved peptide aptamers, CLIPs to inhibit RAGE signal transduction in mammalian cells.

TL;DR: Cellular functional assays revealed that in addition to directly interfering with known binding sites, peptide aptamer binding distal to ligand sites also inhibits RAGE ligand-induced signal transduction, which underscores the potential of using CLIPs to select allosteric inhibitors of biological targets.