@article{BennettFuerstGautel1999,
  author    = {Bennett, Pauline and F{\"u}rst, Dieter Oswald and Gautel, Mathias},
  title     = {The C-protein (myosin binding protein C) family : regulators of contraction and sarcomere function?},
  year      = {1999},
  language  = {en}
}
@article{ChakharovaWehnertUhletal.2000,
  author    = {Chakharova, Christina and Wehnert, Manfred and Uhl, K. and Sekthivel, S. and Vorsberg, Hans-Peter and F{\"u}rst, Dieter Oswald},
  title     = {Genomic structure and fine mapping of the two human filamin gene paralogues FLNB and FLNC and comparative analysis of the filamin gene family},
  year      = {2000},
  language  = {en}
}
@article{Fuerst1999,
  author    = {F{\"u}rst, Dieter Oswald},
  title     = {Titin, ein molekularer Gigant regiert im quergestreiften Muskel},
  year      = {1999},
  language  = {de}
}
@article{FuerstGautel1995,
  author    = {F{\"u}rst, Dieter Oswald and Gautel, Mathias},
  title     = {The anatomy of a molecular giant : how the sarcomere cytoskeleton is assembled from immunoglobulin superfamily molecules ; invited review},
  year      = {1995},
  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{GautelFuerstCoccoetal.1998,
  author    = {Gautel, Mathias and F{\"u}rst, Dieter Oswald and Cocco, Alessandra and Schiaffino, Stefano},
  title     = {Isoform transitions of the myosin-binding protein C family in developing human and mouse muscles : lack of isoform transcomplementation in cardiac muscle},
  year      = {1998},
  language  = {en}
}
@article{GautelGouldingBullardetal.1996,
  author    = {Gautel, Mathias and Goulding, David and Bullard, Bellinda and Weber, Klaus and F{\"u}rst, Dieter Oswald},
  title     = {The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers},
  year      = {1996},
  language  = {en}
}
@article{GehmlichGeierOsterzieletal.2004,
  author    = {Gehmlich, Katja and Geier, C. and Osterziel, Karl Joseph and F{\"u}rst, Dieter Oswald},
  title     = {Mutant muscle LIM protein is associated with hypertrophic cardiomyopathy and exhibits altered binding properties in the system MLP - N-RAP - alpha-actinin},
  issn      = {0171-9335},
  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{GiebingObermannFuerstetal.1997,
  author    = {Giebing, Thomas and Obermann, Wolfgang and F{\"u}rst, Dieter Oswald and D'Haese, Jochen},
  title     = {C-terminally deleted fragments of 40-kDa earthworm actin modulator still shows gelsolin activities},
  year      = {1997},
  language  = {en}
}