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January 1, 1997Cell Structure and FunctionOpen Access

Assembly of Titin, Myomesin and M-protein into the Sarcomeric M band in Differentiating Human Skeletal Muscle Cells in vitro.

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Authors

PVPeter F. M. van der VenUniversity of Bonn DFDieter O. FürstHeart Failure & Transplant

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Implication

No immediate clinical implications; leaves open the in vivo role of titin-M band anchoring in muscle disorders.

Key Points

Key points are not available for this paper at this time.

Cite This Study

Ven et al. (1997) studied this question.

synapsesocial.com/papers/6a766da83da069e66cbd3016 https://doi.org/10.1247/csf.22.163

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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1The 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.1996 · 216 citations
2Titin aggregates associated with intermediate filaments align along stress fiber-like structures during human skeletal muscle cell differentiation1993 · 63 citations
3Differential distribution of subsets of myofibrillar proteins in cardiac nonstriated and striated myofibrils.1990 · 212 citations
4The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line.1988 · 626 citations
5Myogenesis in the mouse embryo: differential onset of expression of myogenic proteins and the involvement of titin in myofibril assembly.1989 · 300 citations