Influence of nonenzymatic posttranslational modifications on constitution, oligomerization and receptor binding of S100A12.

Influence of nonenzymatic posttranslational modifications on constitution, oligomerization and receptor binding of S100A12.

This study examined the effect of methylglyoxal (MGO)-derived nonenzymatic posttranslational modifications (nePTMs) on the binding affinity of S100A12 to its natural receptor for advanced glycation end-products (RAGE). Binding of MGO-modified S100A12 to RAGE decreased significantly with increasing M...

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Bibliographic Details
Main Authors: Kerstin Augner, Jutta Eichler, Wolfgang Utz, Monika Pischetsrieder
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0113418&type=printable
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