@article{HimmelVanderVenStoeckleinetal.2003, author = {Himmel, Mirko and VanderVen, Peter F. M. and St{\"o}cklein, Walter F. M. and F{\"u}rst, Dieter Oswald}, title = {The limits of promiscuity : isoform-specific dimerization of filamins}, year = {2003}, language = {en} } @article{ObermannGautelSteineretal.1996, author = {Obermann, Wolfgang and Gautel, Mathias and Steiner, F. and VanDerVen, Peter F. M. and Weber, Klaus and F{\"u}rst, Dieter Oswald}, title = {The structure of the sarcomeric M band : localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy}, year = {1996}, language = {en} } @article{ObermannVanDerVenSteineretal.1998, author = {Obermann, Wolfgang and VanDerVen, Peter F. M and Steiner, F. and Weber, Klaus and F{\"u}rst, Dieter Oswald}, title = {Mapping of a myosin binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M-band}, year = {1998}, language = {en} } @article{VorgerdvanderVenBruchertseiferetal.2005, author = {Vorgerd, M. and vanderVen, Peter F. M. and Bruchertseifer, V. and Lowe, T. and Kley, R. A. and Schr{\"o}der, Rolf and Lochmuller, H. and Himmel, Mirko and Koehler, K. and F{\"u}rst, Dieter Oswald and Huebner, A.}, title = {A mutation in the dimerization domain of filamin C causes a novel type of autosomal dominant myofibrillar myopathy}, issn = {0002-9297}, year = {2005}, abstract = {Myofibrillar myopathy (MFM) is a human disease that is characterized by focal myofibrillar destruction and pathological cytoplasmic protein aggregations. In an extended German pedigree with a novel form of MFM characterized by clinical features of a limb-girdle myopathy and morphological features of MFM, we identified a cosegregating, heterozygous nonsense mutation (8130G -> A; W2710X) in the filamin c gene ( FLNC) on chromosome 7q32.1. The mutation is the first found in FLNC and is localized in the dimerization domain of filamin c. Functional studies showed that, in the truncated mutant protein, this domain has a disturbed secondary structure that leads to the inability to dimerize properly. As a consequence of this malfunction, the muscle fibers of our patients display massive cytoplasmic aggregates containing filamin c and several Z-disk-associated and sarcolemmal proteins}, language = {en} } @article{KleuserStoeckleinPieperFuerstetal.2004, author = {Kleuser, U. and St{\"o}cklein, Walter F. M. and Pieper-F{\"u}rst, U. and Scheller, Frieder W.}, title = {Partikelverst{\"a}rkte Oberfl{\"a}chenplasmonresonanz f{\"u}r die Quantifizierung von Matrix Metalloproteinase-2}, year = {2004}, language = {de} } @article{GehmlichGeierOsterzieletal.2004, author = {Gehmlich, Katja and Geier, C. and Osterziel, Karl Joseph and VanderVen, Peter F. M. and F{\"u}rst, Dieter Oswald}, title = {Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and alpha-actinin and their implication for hypertrophic cardiomyopathy}, issn = {0302-766X}, year = {2004}, abstract = {Previous work has shown that mutations in muscle LIM protein (MLP) can cause hypertrophic cardiomyopathy (HCM). In order to gain an insight into the molecular basis of the disease phenotype, we analysed the binding characteristics of wild-type MLP and of the (C58G) mutant MLP that causes hypertrophic cardiomyopathy. We show that MLP can form a ternary complex with two of its previously documented myofibrillar ligand proteins, N-RAP and alpha-actinin, which indicates the presence of distinct, non-overlapping binding sites. Our data also show that, in comparison to wild-type MLP, the capacity of the mutated MLP protein to bind both N-RAP and alpha-actinin is significantly decreased. In addition, this single point mutation prevents zinc coordination and proper folding of the second zinc-finger in the first LIM domain, which consequently renders the protein less stable and more susceptible to proteolysis. The molecular basis for HCM-causing mutations in the MLP gene might therefore be an alteration in the equilibrium of interactions of the ternary complex MLP-N-RAP-alpha-actinin. This assumption is supported by the previous observation that in the pathological situation accompanied by MLP down regulation, cardiomyocytes try to compensate for the decreased stability of MLP protein by increasing the expression of its ligand N-RAP, which might finally result in the development of myocyte disarray that is characteristic of this disease}, language = {en} } @article{PieperFuerstKleuserStoeckleinetal.2004, author = {Pieper-F{\"u}rst, U. and Kleuser, U. and St{\"o}cklein, Walter F. M. and Warsinke, Axel and Scheller, Frieder W.}, title = {Detection of subicomolar concentrations of human matrix metalloproteinase-2 by an optical biosensor}, year = {2004}, abstract = {We describe in this paper the development of a one-step sandwich assay for the highly sensitive and fast detection of human matrix metalloproteinase (MMP)-2 (EC 3.4.24.24), using surface plasmon resonance (SPR). For the assay, two ligands were selected: monoclonal anti-MMP-2 antibody Ab-2 and the tissue inhibitor of metalloproteinases (TIMP)-2. They were chosen on the basis of (1) their affinities to MMP-2, (2) the efficiency of immobilization to the sensor chip, (3) the efficiency of adsorption to colloidal gold, and (4) the stability of these protein-coated gold particles. The assay included mixing of MMP-2 with antibody Ab-2 adsorbed to colloidal gold with a diameter of about 20 rim and injection into the flowcell of the SPR instrument containing immobilized TIMP-2. By using colloidal gold particles an amplification factor of 114 and a detection limit of 0.5 pM for MMP-2 were obtained. The precision of the assay was high even at low analyte concentrations, the standard deviation being 8.3\% for five determinations of 1 pM MMP- 2. No significant binding was observed with the structurally related MMP-9. The assay is far more sensitive and faster than commonly used methods for MMP-2 detection. As TIMP-bound MMP-2 is not detected by this method, the assay can be applied for measuring free MMP-2, reflecting the imbalance of free and inhibitor-bound enzyme in various pathological situations. (C) 2004 Elsevier Inc. All rights reserved}, language = {en} } @article{PacholskyVakeelHimmeletal.2004, author = {Pacholsky, Dirk and Vakeel, Padmanabhan and Himmel, Mirko and Lowe, T. and Stradal, T. and Rottner, K. and F{\"u}rst, Dieter Oswald and vanderVen, Peter F. M.}, title = {Xin repeats define a novel actin-binding motif}, issn = {0021-9533}, year = {2004}, abstract = {Xin is a protein that is expressed during early developmental stages of cardiac and skeletal muscles. Immunolocalization studies indicated a peripheral localization in embryonic mouse heart, where Xin localizes with beta- catenin and N-cadherin. In adult tissues, Xin is found primarily in the intercalated discs of cardiomyocytes and the myotendinous junctions of skeletal muscle cells, both specialized attachment sites of the myofibrillar ends to the sarcolemma. A large part of the Xin protein consists of unique 16 amino acid repeats with unknown function. We have investigated the characteristics of the Xin repeats by transfection experiments and actin-binding assays and ascertained that, upon expression in cultured cells, these repeats bind to and stabilize the actin-based cytoskeleton. In vitro co- sedimentation assays with skeletal muscle actin indicated that they not only directly bind actin filaments, but also have the capability of arranging microfilaments into networks that sediment upon low-speed centrifugation. Very similar repeats were also found in Xin-repeat protein 2' (XIRP2), a novel protein that seems to be expressed mainly in striated muscles. Human XIRP2 contains 28 Xin repeats with properties identical to those of Xin. We conclude that the Xin repeats define a novel, repetitive actin-binding motif present in at least two different muscle proteins. These Xin- repeat proteins therefore constitute the first two members of a novel family of actin-binding proteins}, language = {en} } @article{MartinezChicharroTorrejonOskinovaetal.2018, author = {Martinez-Chicharro, M. and Torrejon, J. M. and Oskinova, Lida and Furst, F. and Postnov, K. and Rodes-Roca, J. J. and Hainich, Rainer and Bodaghee, A.}, title = {Evidence of Compton cooling during an X-ray flare supports a neutron star nature of the compact object in 4U1700-37}, series = {Monthly notices of the Royal Astronomical Society}, volume = {473}, journal = {Monthly notices of the Royal Astronomical Society}, number = {1}, publisher = {Oxford Univ. Press}, address = {Oxford}, issn = {0035-8711}, doi = {10.1093/mnrasl/slx165}, pages = {L74 -- L78}, year = {2018}, abstract = {Based on new Chandra X-ray telescope data, we present empirical evidence of plasma Compton cooling during a flare in the non-pulsating massive X-ray binary 4U1700-37. This behaviour might be explained by quasi-spherical accretion on to a slowly rotating magnetized neutron star (NS). In quiescence, the NS in 4U1700-37 is surrounded by a hot radiatively cooling shell. Its presence is supported by the detection of mHz quasi-periodic oscillations likely produced by its convection cells. The high plasma temperature and the relatively low X-ray luminosity observed during the quiescence, point to a small emitting area similar to 1 km, compatible with a hotspot on an NS surface. The sudden transition from a radiative to a significantly more efficient Compton cooling regime triggers an episode of enhanced accretion resulting in a flare. During the flare, the plasma temperature drops quickly. The predicted luminosity for such transitions, similar to 3 x 10(35) erg s(-1), is very close to the luminosity of 4U1700-37 during quiescence. The transition may be caused by the accretion of a clump in the stellar wind of the donor star. Thus, a magnetized NS nature of the compact object is strongly favoured.}, language = {en} } @article{VanDerLoopVanDerVenFuerstetal.1996, author = {VanDerLoop, Frank T. L. and VanDerVen, Peter F. M and F{\"u}rst, Dieter Oswald and Gautel, Mathias and VanEys, Guillaume and Ramaekers, Frans C. S.}, title = {Integration of titin into the sarcomeres of cultured differentiating human skeletal muscle cells}, year = {1996}, language = {en} }