@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{SpeelVanDerVenAlbrechtsetal.1998,
  author    = {Speel, Ernst J. M. and VanDerVen, Peter F. M. and Albrechts, Jozefa C. M. and Hopman, Anton H. N. and F{\"u}rst, Dieter Oswald},
  title     = {Chromosomal assignment of the human myomesin gene},
  year      = {1998},
  language  = {en}
}
@article{SpeelVanDerVenAlbrechtsetal.1998,
  author    = {Speel, Ernst J. M. and VanDerVen, Peter F. M. and Albrechts, Jozefa C. M. and Ramaekers, Frans C. S. and F{\"u}rst, Dieter Oswald and Hopman, Anton H. N.},
  title     = {Assignment of the human gene for the sarcomeric M-band protein myomesin (MYOM1) to 18p11.31-p11.32},
  year      = {1998},
  language  = {en}
}
@article{VanDerVenSpeelAlbrechtsetal.1999,
  author    = {VanDerVen, Peter F. M. and Speel, Ernst J. M. and Albrechts, Jozefa C. M. and Ramaekers, Frans C. S. and Hopman, Anton H. N. and F{\"u}rst, Dieter Oswald},
  title     = {Chromosomal assignment of the human gene for endosarcomeric cytoskeletal M-protein (MYOM2) to 8p23.3},
  year      = {1999},
  language  = {en}
}
@article{VanDerVenSpeelAlbrechtsetal.1999,
  author    = {VanDerVen, Peter F. M. and Speel, Ernst J. M. and Albrechts, Jozefa C. M. and Ramaekers, Frans C. S. and Hopman, Anton H. N. and F{\"u}rst, Dieter Oswald},
  title     = {Assignment of the human gene for endosarcomeric cytoskeletal M-protein (MYOM2) to 8p23.3},
  year      = {1999},
  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{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{SchroederVanDerVenWarloetal.2000,
  author    = {Schr{\"o}der, Rolf and VanDerVen, Peter F. M. and Warlo, Irene and Schumann, H. and F{\"u}rst, Dieter Oswald and Bl{\"u}mke, Ingmar and Goebel, Hans H. and Schmidt, M. C. and Hatzfeld, Mechthild},
  title     = {A member of the armadillo multigene family, is a constituent of sarcomeric I-bands in human skeletal muscle},
  year      = {2000},
  language  = {en}
}
@article{BeathamRomeroTownsendetal.2004,
  author    = {Beatham, Jane L. and Romero, Rosario and Townsend, Stuart K.M. and Hacker, Terry and VanderVen, Peter F. M. and Blanco, Gonzalo},
  title     = {Filamin C interacts with the muscular dystrophy KY protein and is abnormally distributed in mouse KY deficient muscle fibres},
  issn      = {0964-6906},
  year      = {2004},
  abstract  = {The KY protein has been implicated in a neuromuscular dystrophy in the mouse, but its role in muscle function remains unclear. Here, we show that KY interacts with several sarcomeric cytoskeletal proteins including, amongst others, filamin C and the slow isoform of the myosin-binding protein C. These interactions were confirmed in vitro and because of its central role in skeletal muscle disease, characterized in more detail for filamin C. A role for KY in regulating filamin C function in vivo is supported by the expression analysis of filamin C in the null ky mouse mutant, where distinct irregular subcellular localization of filamin C was found in subsets of muscle fibres, which appears to be a specific outcome of KY deficiency. Furthermore, KY shows protease activity in in vitro assays, and specific degradation of filamin C by KY is shown in transfected cells. Given the enzymatic nature of the KY protein, it is likely that some of the identified partners are catalytic substrates. These results suggest that KY is an intrinsic part of the protein networks underlying the molecular mechanism of several limb-girdle muscular dystrophies, particularly those where interactions between filamin C and disease causing proteins have been shown},
  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{BeathamMiddletonRomeroetal.2004,
  author    = {Beatham, Jane L. and Middleton, A. and Romero, Rosario and VanderVen, Peter F. M. and Blanco, Gonzalo},
  title     = {Functional characterisation of the Ky protein},
  issn      = {0960-8966},
  year      = {2004},
  language  = {en}
}
@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{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{SchroederFuerstKlasenetal.2000,
  author    = {Schr{\"o}der, Rolf and F{\"u}rst, Dieter Oswald and Klasen, Christian and Reiman, Jens and Herrmann, Harald and VanDerVen, Peter F. M.},
  title     = {The association of plectin with Z-discs is a prerequisite for the formation of the intermyofibrillar desmin cytoskeleton},
  year      = {2000},
  language  = {en}
}
@article{VanDerVenBartschGauteletal.2000,
  author    = {VanDerVen, Peter F. M. and Bartsch, J{\"o}rg and Gautel, Mathias and Jokusch, Harald and F{\"u}rst, Dieter Oswald},
  title     = {A functional knock-out of titin results in defective myofibril assembly},
  year      = {2000},
  language  = {en}
}
@article{VanderVenEhlerVakeeletal.2006,
  author    = {VanderVen, Peter F. M. and Ehler, Elisabeth and Vakeel, Padmanabhan and Eulitz, Stefan and Schenk, J{\"o}rg A. and Milting, Hendrik and Micheel, Burkhard and F{\"u}rst, Dieter Oswald},
  title     = {Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mena/ VASP},
  doi       = {10.1016/j.yexcr.2006.03.015},
  year      = {2006},
  abstract  = {Filamin c is the predominantly expressed filamin isoform in striated muscles. It is localized in myofibrillar Z- discs, where it binds FATZ and myotilin, and in myotendinous junctions and intercalated discs. Here, we identify Xin, the protein encoded by the human gene 'cardiomyopathy associated 1' (CMYA1) as filamin c binding partner at these specialized structures where the ends of myofibrils are attached to the sarcolemma. Xin directly binds the EVH1 domain proteins Mena and VASP. In the adult heart, Xin and Mena/VASP colocalize with filamin c in intercalated discs. In cultured cardiomyocytes, the proteins also localize in the nonstriated part of myofibrils, where sarcomeres are assembled and an extensive reorganization of the actin cytoskeleton occurs. Unusual intraexonic splicing events result in the existence of three Xin isoforms that associate differentially with its ligands. The identification of the complex filamin c-Xin-Mena/VASP provides a first glance on the role of Xin in the molecular mechanisms involved in developmental and adaptive remodeling of the actin cytoskeleton during cardiac morphogenesis and sarcomere assembly. (c) 2006 Elsevier Inc. All rights reserved},
  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}
}
@article{VanDerVenObermannWeberetal.1996,
  author    = {VanDerVen, Peter F. M and Obermann, Wolfgang and Weber, Klaus and F{\"u}rst, Dieter Oswald},
  title     = {Myomesin, M-protein and the structure of the sarcomeric M-band},
  year      = {1996},
  language  = {en}
}
@article{MayansVanDerVenWilmannsetal.1998,
  author    = {Mayans, Olga and VanDerVen, Peter F. M and Wilmanns, Matthias and Mues, Alexander and Young, Paul and F{\"u}rst, Dieter Oswald and Wilmanns, Matthias and Gautel, Mathias},
  title     = {The structural basis of the activation of the serine kinase domain of the giant muscle protein titin during myofibrillogenesis},
  year      = {1998},
  language  = {en}
}
@article{VanDerVenFuerst1998,
  author    = {VanDerVen, Peter F. M and F{\"u}rst, Dieter Oswald},
  title     = {Expression of sarcomeric proteins and assembly of myofibrils in the putative myofibroblast cell line BHK-21/C13},
  year      = {1998},
  language  = {en}
}
@article{VanDerVenFuerst1997,
  author    = {VanDerVen, Peter F. M and F{\"u}rst, Dieter Oswald},
  title     = {Assembly of titin, myomesin and M-protein into the sarcomeric M-band in differentiating human skeletal muscle cells in vitro},
  year      = {1997},
  language  = {en}
}
@article{MuesVanDerVenYoungetal.1998,
  author    = {Mues, Alexander and VanDerVen, Peter F. M and Young, Paul and F{\"u}rst, Dieter Oswald and Gautel, Mathias},
  title     = {Two immunoglobulin-like domains of the Z-disk portion of titin interact in a conformation-dependent way with telethonin},
  year      = {1998},
  language  = {en}
}
@article{VanDerVenObermannLemkeetal.2000,
  author    = {VanDerVen, Peter F. M and Obermann, Wolfgang and Lemke, Britt and Gautel, Mathias and Weber, Klaus and F{\"u}rst, Dieter Oswald},
  title     = {The characterization of muscle filamin isoforms suggests a possible role of ABP-L/gamma-filamin in sarcomeric Z- disc formation},
  year      = {2000},
  language  = {en}
}
@article{FuerstObermannVanDerVen1999,
  author    = {F{\"u}rst, Dieter Oswald and Obermann, Wolfgang and VanDerVen, Peter F. M},
  title     = {Structure and assembly of the sarcomeric M-band},
  year      = {1999},
  language  = {en}
}
@article{SchroederWarloHerrmannetal.1999,
  author    = {Schr{\"o}der, Rolf and Warlo, Irene and Herrmann, Harald and VanDerVen, Peter F. M and Klasen, Christian and Bl{\"u}mke, Ingmar and Mundegar, Rustam R. and F{\"u}rst, Dieter Oswald and G{\"o}bel, Hans H. and Magin, Thomas},
  title     = {Immunogold EM reveals a close association of plectin and the desmin cytoskeleton in human skeletal muscle},
  year      = {1999},
  language  = {en}
}