FMP Publications

Our publications are recorded in a searchable database since 2010, updates will be added regularly.

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Visualizing Brain Inflammation with a Shingled-Leg Radio-Frequency Head Probe for F-19/H-1 MRI
Waiczies(*), H., Lepore(*), S., Drechsler(*), S., Qadri(*), F., Purfurst(*), B., Sydow, K., Dathe, M., Kühne(*), A., Lindel(*), T., Hoffmann(*), W., Pohlmann(*), A., Niendorf(*), T.; Waiczies(*), S.
Sci Rep-Uk, 3

Tags: Peptide-Lipid-Interaction/ Peptide Transport (Dathe)

Abstract: Magnetic resonance imaging (MRI) provides the opportunity of tracking cells in vivo. Major challenges in dissecting cells from the recipient tissue and signal sensitivity constraints albeit exist. In this study, we aimed to tackle these limitations in order to study inflammation in autoimmune encephalomyelitis. We constructed a very small dual-tunable radio frequency (RF) birdcage probe tailored for F-19 (fluorine) and H-1 (proton) MR mouse neuroimaging. The novel design eliminated the need for extra electrical components on the probe structure and afforded a uniform B-1(+)-field as well as good SNR. We employed fluorescently-tagged F-19 nanoparticles and could study the dynamics of inflammatory cells between CNS and lymphatic system during development of encephalomyelitis, even within regions of the brain that are otherwise not easily visualized by conventional probes. F-19/H-1 MR Neuroimaging will allow us to study the nature of immune cell infiltration during brain inflammation over an extensive period of time.

The Clip-Segment of the von Willebrand Domain 1 of the BMP Modulator Protein Crossveinless 2 Is Preformed
Fiebig(*), J. E., Weidauer(*), S. E., Qiu(*), L. Y., Bauer(*), M., Schmieder, P., Beerbaum, M., Zhang(*), J. L., Oschkinat, H., Sebald(*), W.; Mueller(*), T. D.
Molecules, 18:11658-11682

Tags: NMR-Supported Structural Biology (Oschkinat), Solution NMR (Schmieder)

Abstract: Bone Morphogenetic Proteins (BMPs) are secreted protein hormones that act as morphogens and exert essential roles during embryonic development of tissues and organs. Signaling by BMPs occurs via hetero-oligomerization of two types of serine/threonine kinase transmembrane receptors. Due to the small number of available receptors for a large number of BMP ligands ligand-receptor promiscuity presents an evident problem requiring additional regulatory mechanisms for ligand-specific signaling. Such additional regulation is achieved through a plethora of extracellular antagonists, among them members of the Chordin superfamily, that modulate BMP signaling activity by binding. The key-element in Chordin-related antagonists for interacting with BMPs is the von Willebrand type C (VWC) module, which is a small domain of about 50 to 60 residues occurring in many different proteins. Although a structure of the VWC domain of the Chordin-member Crossveinless 2 (CV2) bound to BMP-2 has been determined by X-ray crystallography, the molecular mechanism by which the VWC domain binds BMPs has remained unclear. Here we present the NMR structure of the Danio rerio CV2 VWC1 domain in its unbound state showing that the key features for high affinity binding to BMP-2 is a pre-oriented peptide loop.

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Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
Robert-Roessle-Str. 10
13125 Berlin, Germany
+4930 94793 - 100 
+4930 94793 - 109 (Fax)

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