Holger F. Hebestreit

TL;DR: It is shown that the interaction between human pVHL and a specific domain of the HIF-1α subunit is regulated through hydroxylation of a proline residue by an enzyme the authors have termed Hif-α prolyl-hydroxylase (HIF-PH).

TL;DR: Analysis of the human platelet proteome contributes to a more thorough and holistic understanding of platelet biology, helping to build the basis for future identification of new drug targets and therapeutic strategies.

TL;DR: A new approach for the identification of novel signaling molecules in activated platelets is provided, providing new insights into the mechanisms of platelet activation and building the basis for the development of therapeutic agents for thrombotic diseases.

TL;DR: A unique inventory of the platelet proteome is provided, contributing to the understanding of platelet function and building the basis for the identification of new drug targets.

TL;DR: This biochemical approach to charting diseases that involve alterations in glycan processing provides a rapid indicator of the nature, severity, and cell type specificity of the suboptimal glycosylation steps; allows links to genetic mutations; indicates the expression levels of proteins; and gives insight into the pathways affected in the disease process.