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Dennis R. Voelker

Researcher at University of Colorado Denver

Publications -  199
Citations -  21426

Dennis R. Voelker is an academic researcher from University of Colorado Denver. The author has contributed to research in topics: Surfactant protein A & Endoplasmic reticulum. The author has an hindex of 64, co-authored 191 publications receiving 19685 citations. Previous affiliations of Dennis R. Voelker include Anschutz Medical Campus & National Jewish Health.

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Membrane lipids: where they are and how they behave.

TL;DR: How do cells apply anabolic and catabolic enzymes, translocases and transporters, plus the intrinsic physical phase behaviour of lipids and their interactions with membrane proteins, to create the unique compositions and multiple functions of their individual membranes?
Journal Article

Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages.

TL;DR: The data suggest that macrophages specifically recognize phosphatidylserine that is exposed on the surface of lymphocytes during the development of apoptosis, and suggest that apoptotic lymphocytes lose membrane phospholipid asymmetry and expose phosphorus on the outer leaflet of the plasma membrane.
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By Binding SIRPα or Calreticulin/CD91, Lung Collectins Act as Dual Function Surveillance Molecules to Suppress or Enhance Inflammation

TL;DR: Evidence is provided that SP-A and SP-D act in a dual manner, to enhance or suppress inflammatory mediator production depending on binding orientation, and interaction of these heads with PAMPs on foreign organisms or damaged cells and presentation of the collagenous tails in an aggregated state to calreticulin/CD91, stimulates phagocytosis and proinflammatory responses.
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Making heads or tails of phospholipids in mitochondria

TL;DR: The discovery of proteins that regulate mitochondrial membrane lipid composition and of a multiprotein complex tethering ER to mitochondrial membranes has unveiled novel mechanisms of mitochondrial membrane biogenesis.
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Identification of a Non-mitochondrial Phosphatidylserine Decarboxylase Activity (PSD2) in the Yeast Saccharomyces cerevisiae

TL;DR: The present studies demonstrate the presence of a second enzyme activity (denoted PSD2) which, depending on the method of evaluation, accounts for 4-12% of the total cellular phosphatidylserine decarboxylase activity found in wild type.