C
Christian Henning
Researcher at Martin Luther University of Halle-Wittenberg
Publications - 19
Citations - 604
Christian Henning is an academic researcher from Martin Luther University of Halle-Wittenberg. The author has contributed to research in topics: Glycation & Maillard reaction. The author has an hindex of 10, co-authored 17 publications receiving 444 citations. Previous affiliations of Christian Henning include Kyushu University.
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Journal ArticleDOI
Pathways of the Maillard reaction under physiological conditions
TL;DR: The present review critically discusses the relevant α-dicarbonyl compounds as central intermediates of AGE formation in vivo with a special focus on fragmentation pathways leading to formation of amide-AGEs.
Journal ArticleDOI
Medium Cut-Off (MCO) Membranes Reduce Inflammation in Chronic Dialysis Patients-A Randomized Controlled Clinical Trial.
Daniel Zickler,Ralf Schindler,Kevin Willy,Peter Martus,Michael Pawlak,Markus Storr,Michael Hulko,Torsten Boehler,Marcus A. Glomb,Kristin Liehr,Christian Henning,Markus F. Templin,Bogusz Trojanowicz,Christof Ulrich,Kristin Werner,Roman Fiedler,Matthias Girndt +16 more
TL;DR: MCO-Ci Dialyzers modulate inflammation in chronic HD patients to a greater extent compared to High-flux dialyzers and Transcription of pro-inflammatory cytokines in peripheral leukocytes is markedly reduced and removal of soluble mediators is enhanced with MCO dialysis.
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Extending the spectrum of α-dicarbonyl compounds in vivo.
TL;DR: A highly sensitive LC-MS/MS multimethod for human blood plasma based on derivatization with o-phenylenediamine under acidic conditions is introduced and for the first time that a complete spectrum of α-dicarbonyl compounds relevant in vivo has been established.
Journal ArticleDOI
Comprehensive Analysis of Maillard Protein Modifications in Human Lenses: Effect of Age and Cataract
Mareen Smuda,Christian Henning,Cibin T. Raghavan,Kaid Johar,Abhay R. Vasavada,Ram H. Nagaraj,Marcus A. Glomb +6 more
TL;DR: A highly sensitive liquid chromatography-tandem mass spectrometry multimethod was developed that allowed us to quantitate 21 protein modifications in normal and cataractous lenses, respectively, and AGEs from the Amadori product and methylglyoxal were dominant.
Journal ArticleDOI
Molecular Basis of Maillard Amide-Advanced Glycation End Product (AGE) Formation in Vivo
TL;DR: The results strongly suggest a major participation of non-enzymatic Maillard mechanisms on amide-AGE formation pathways in vivo, which, in the case of N6-acetyl lysine, parallels enzymatic processes.