@article{MatthesSchoenfeldZottnicketal.2015,
  author    = {Matthes, Philipp R. and Sch{\"o}nfeld, Fabian and Zottnick, Sven H. and M{\"u}ller-Buschbaum, Klaus},
  title     = {Post-synthetic shaping of porosity and crystal structure of Ln-Bipy-MOFs by thermal treatment},
  series = {Molecules},
  volume    = {20},
  journal   = {Molecules},
  doi       = {10.3390/molecules200712125},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-148404},
  pages     = {12125-12153},
  year      = {2015},
  abstract  = {The reaction of anhydrous lanthanide chlorides together with 4,4'-bipyridine yields the MOFs \(^{2}\)\(_{∞}\)[Ln\(_{2}\)Cl\(_{6}\)(bipy)\(_{3}\)]*2bipy, with Ln = Pr-Yb, bipy = 4,4'-bipyridine, and \(^{3}\)\(_{∞}\)[La\(_{2}\)Cl\(_{6}\)(bipy)\(_{5}\)]*4bipy. Post-synthetic thermal treatment in combination with different vacuum conditions was successfully used to shape the porosity of the MOFs. In addition to the MOFs microporosity, a tuneable mesoporosity can be implemented depending on the treatment conditions as a surface morphological modification. Furthermore, thermal treatment without vacuum results in several identifiable crystalline high-temperature phases. Instead of collapse of the frameworks upon heating, further aggregation under release of bipy is observed. \(^{3}\)\(_{∞}\)[LaCl\(_{3}\)(bipy)] and \(^{2}\)\(_{∞}\)[Ln\(_{3}\)Cl\(_{9}\)(bipy)\(_{3}\)], with Ln = La, Pr, Sm, and \(^{1}\)\(_{∞}\)[Ho\(_{2}\)Cl\(_{6}\)(bipy)\(_{2}\)] were identified and characterized, which can also exhibit luminescence. Besides being released upon heating, the linker 4,4'-bipyridine can undergo activation of C-C bonding in ortho-position leading to the in-situ formation of 4,4':2',2 '':4 '',4'''-quaterpyridine (qtpy). qtpy can thereby function as linker itself, as shown for the formation of the network \(^{2}\)\(_{∞}\)[Gd\(_{2}\)Cl\(_{6}\)(qtpy)\(_{2}\)(bipy)\(_{2}\)]*bipy. Altogether, the manuscript elaborates the influence of thermal treatment beyond the usual activation procedures reported for MOFs.},
  language  = {en}
}
@article{vanDintherZhangWeidaueretal.2013,
  author    = {van Dinther, Maarten and Zhang, Juan and Weidauer, Stella E. and Boschert, Verena and Muth, Eva-Maria and Knappik, Achim and de Gorter, David J. J. and van Kasteren, Puck B. and Frisch, Christian and M{\"u}ller, Thomas D. and ten Dijke, Peter},
  title     = {Anti-Sclerostin Antibody Inhibits Internalization of Sclerostin and Sclerostin-Mediated Antagonism of Wnt/LRP6 Signaling},
  series = {PLoS ONE},
  volume    = {8},
  journal   = {PLoS ONE},
  number    = {4},
  doi       = {10.1371/journal.pone.0062295},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-130981},
  pages     = {e62295},
  year      = {2013},
  abstract  = {Sclerosteosis is a rare high bone mass disease that is caused by inactivating mutations in the SOST gene. Its gene product, Sclerostin, is a key negative regulator of bone formation and might therefore serve as a target for the anabolic treatment of osteoporosis. The exact molecular mechanism by which Sclerostin exerts its antagonistic effects on Wnt signaling in bone forming osteoblasts remains unclear. Here we show that Wnt3a-induced transcriptional responses and induction of alkaline phosphatase activity, an early marker of osteoblast differentiation, require the Wnt co-receptors LRP5 and LRP6. Unlike Dickkopf1 (DKK1), Sclerostin does not inhibit Wnt-3a-induced phosphorylation of LRP5 at serine 1503 or LRP6 at serine 1490. Affinity labeling of cell surface proteins with \([^{125} I]\) Sclerostin identified LRP6 as the main specific Sclerostin receptor in multiple mesenchymal cell lines. When cells were challenged with Sclerostin fused to recombinant green fluorescent protein (GFP) this was internalized, likely via a Clathrin-dependent process, and subsequently degraded in a temperature and proteasome-dependent manner. Ectopic expression of LRP6 greatly enhanced binding and cellular uptake of Sclerostin-GFP, which was reduced by the addition of an excess of non-GFP-fused Sclerostin. Finally, an anti-Sclerostin antibody inhibited the internalization of Sclerostin-GFP and binding of Sclerostin to LRP6. Moreover, this antibody attenuated the antagonistic activity of Sclerostin on canonical Wnt-induced responses.},
  language  = {en}
}