Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–7 of 7 results
Advanced filters: Author: Christian Brix Folsted Andersen Clear advanced filters

  • Vitamin B12 (cobalamin) is an essential coenzyme in mammals, and is taken up from the diet. The proteins required for its uptake are the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor, which is in turn formed from the proteins cubilin and amnionless. Here, the crystal structure is presented of the complex between IF–cobalamin and the IF–cobalamin-binding region (CUB) of cubilin. The structure illustrates how numerous CUB domains function together as modular ligand-binding regions.

    • Christian Brix Folsted Andersen
    • Mette Madsen
    • Gregers R. Andersen
    Research
    Nature
    Volume: 464, P: 445-448

  • This study reports the crystal structure of porcine haptoglobin in complex with haemoglobin at 2.9 Å resolution; this provides a structural basis of haptoglobin-mediated recognition of haemoglobin, and insight into the protective role of haptoglobin at the atomic level.

    • Christian Brix Folsted Andersen
    • Morten Torvund-Jensen
    • Søren Kragh Moestrup
    Research
    Nature
    Volume: 489, P: 456-459

  • CD163, a macrophage receptor, is essential for clearing hemoglobin during hemolysis to prevent oxidative damage. Here, the authors reveal the cryo-electron microscopy structure of CD163 bound to haptoglobin-hemoglobin, uncovering calcium-dependent interactions critical for its function and oligomerization.

    • Anders Etzerodt
    • Jakob Hauge Mikkelsen
    • Christian Brix Folsted Andersen
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-13

  • Cubilin and the transmembrane protein amnionless (AMN) form the endocytic receptor cubam that is essential for intestinal vitamin B12 uptake. Here the authors present the 2.3 Å crystal structure of AMN in complex with the amino-terminal region of cubilin and discuss cubam architecture and disease causing mutations.

    • Casper Larsen
    • Anders Etzerodt
    • Christian Brix Folsted Andersen
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-11

  • Vitamin B12 functions as an essential coenzyme in humans. The absorption of this molecule and its subsequent distribution in the body is mediated by a complex set of carrier proteins, receptors and transporters. This Review describes basic and clinical features of this multistep pathway with emphasis on the gastrointestinal transport of vitamin B12and its importance in clinical medicine.

    • Marianne J. Nielsen
    • Mie R. Rasmussen
    • Søren K. Moestrup
    Reviews
    Nature Reviews Gastroenterology & Hepatology
    Volume: 9, P: 345-354