TY  - JOUR
A1  - Himmel, Mirko
A1  - VanderVen, Peter F. M.
A1  - Stöcklein, Walter F. M.
A1  - Fürst, Dieter Oswald
T1  - The limits of promiscuity : isoform-specific dimerization of filamins
Y1  - 2003
ER  - 
TY  - JOUR
A1  - Speel, Ernst J. M.
A1  - VanDerVen, Peter F. M.
A1  - Albrechts, Jozefa C. M.
A1  - Hopman, Anton H. N.
A1  - Fürst, Dieter Oswald
T1  - Chromosomal assignment of the human myomesin gene
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Speel, Ernst J. M.
A1  - VanDerVen, Peter F. M.
A1  - Albrechts, Jozefa C. M.
A1  - Ramaekers, Frans C. S.
A1  - Fürst, Dieter Oswald
A1  - Hopman, Anton H. N.
T1  - Assignment of the human gene for the sarcomeric M-band protein myomesin (MYOM1) to 18p11.31-p11.32
Y1  - 1998
ER  - 
TY  - JOUR
A1  - VanDerVen, Peter F. M.
A1  - Speel, Ernst J. M.
A1  - Albrechts, Jozefa C. M.
A1  - Ramaekers, Frans C. S.
A1  - Hopman, Anton H. N.
A1  - Fürst, Dieter Oswald
T1  - Chromosomal assignment of the human gene for endosarcomeric cytoskeletal M-protein (MYOM2) to 8p23.3
Y1  - 1999
ER  - 
TY  - JOUR
A1  - VanDerVen, Peter F. M.
A1  - Speel, Ernst J. M.
A1  - Albrechts, Jozefa C. M.
A1  - Ramaekers, Frans C. S.
A1  - Hopman, Anton H. N.
A1  - Fürst, Dieter Oswald
T1  - Assignment of the human gene for endosarcomeric cytoskeletal M-protein (MYOM2) to 8p23.3
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Obermann, Wolfgang
A1  - Gautel, Mathias
A1  - Steiner, F.
A1  - VanDerVen, Peter F. M.
A1  - Weber, Klaus
A1  - Fürst, Dieter Oswald
T1  - 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
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Vorgerd, M.
A1  - vanderVen, Peter F. M.
A1  - Bruchertseifer, V.
A1  - Lowe, T.
A1  - Kley, R. A.
A1  - Schröder, Rolf
A1  - Lochmuller, H.
A1  - Himmel, Mirko
A1  - Koehler, K.
A1  - Fürst, Dieter Oswald
A1  - Huebner, A.
T1  - A mutation in the dimerization domain of filamin C causes a novel type of autosomal dominant myofibrillar myopathy
N2  - 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
Y1  - 2005
SN  - 0002-9297
ER  - 
TY  - JOUR
A1  - Schröder, Rolf
A1  - VanDerVen, Peter F. M.
A1  - Warlo, Irene
A1  - Schumann, H.
A1  - Fürst, Dieter Oswald
A1  - Blümke, Ingmar
A1  - Goebel, Hans H.
A1  - Schmidt, M. C.
A1  - Hatzfeld, Mechthild
T1  - A member of the armadillo multigene family, is a constituent of sarcomeric I-bands in human skeletal muscle
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Beatham, Jane L.
A1  - Romero, Rosario
A1  - Townsend, Stuart K.M.
A1  - Hacker, Terry
A1  - VanderVen, Peter F. M.
A1  - Blanco, Gonzalo
T1  - Filamin C interacts with the muscular dystrophy KY protein and is abnormally distributed in mouse KY deficient muscle fibres
N2  - 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
Y1  - 2004
SN  - 0964-6906
ER  - 
TY  - JOUR
A1  - Obermann, Wolfgang
A1  - VanDerVen, Peter F. M
A1  - Steiner, F.
A1  - Weber, Klaus
A1  - Fürst, Dieter Oswald
T1  - Mapping of a myosin binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M-band
Y1  - 1998
ER  -