D
David Singer
Researcher at Leipzig University
Publications - 33
Citations - 1023
David Singer is an academic researcher from Leipzig University. The author has contributed to research in topics: Epitope & Glycation. The author has an hindex of 17, co-authored 33 publications receiving 923 citations.
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Journal ArticleDOI
Advanced Glycation End Product Recognition by the Receptor for AGEs
Jing Xue,Vivek Rai,David Singer,Stefan Chabierski,Jingjing Xie,Sergey Reverdatto,David S. Burz,Ann Marie Schmidt,Ralf Hoffmann,Alexander Shekhtman +9 more
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.
Journal ArticleDOI
The Receptor for Advanced Glycation End Products (RAGE) Specifically Recognizes Methylglyoxal-Derived AGEs
Jing Xue,Rashmi Ray,David Singer,David Böhme,David S. Burz,Vivek Rai,Ralf Hoffmann,Alexander Shekhtman +7 more
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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Epitope mapping of mAbs AT8 and Tau5 directed against hyperphosphorylated regions of the human tau protein
TL;DR: It is reported that anti-PHF-tau mAb AT8 recognizes an epitope doubly phosphorylated at serine 202 and threonine 205, which was not influenced by a third phosphate group atSerine 199, but mAb At8 was cross-reactive to two doubly phosphate motifs containing either serines 199 and 202 or serines 205 and 208 of the human tau sequence.
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Organotypic brain slice cultures of adult transgenic P301S mice--a model for tauopathy studies.
TL;DR: Evidence is provided that adult organotypic brain slice cultures from 7- to 10-month-old mice independently of the transgenic modification undergo slow programmed cell death, caused by a dysfunction of the neuronal repair systems.
Journal ArticleDOI
Ion mobility separation of isomeric phosphopeptides from a protein with variant modification of adjacent residues
TL;DR: It is demonstrated that FAIMS (coupled to electrospray/mass spectrometry (ESI/MS) can broadly baseline-resolve variant phosphopeptides from a biologically modified human protein, including those involving phosphorylation of different residues and adjacent sites that challenge existing tandem mass spectromaetry methods most.