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October 1, 1999Microscopy Research and Technique

Structure, assembly, and dynamics of actin filaments in situ and in vitro

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Key result

Actin isoforms exhibit versatile functions despite extremely high sequence identity, driven by their intrinsic ability to rapidly assemble and disassemble filamentous structures.

Design

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Authors

CSCora‐Ann SchoenenbergerUniversity of BaselMSMichel O. SteinmetzUniversity of BaselDSDaniel StofflerRoche (Switzerland)

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Implication

Actin isoform versatility warrants cytoskeletal studies in cardiomyocytes; leaves open isoform-specific targeting in cardiac disease.

Key Points

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

Cite This Study

Schoenenberger et al. (1999) reported a review. Actin isoforms exhibit versatile functions despite extremely high sequence identity, driven by their intrinsic ability to rapidly assemble and disassemble filamentous structures.

synapsesocial.com/papers/6a97d549cb7f2a2edc74cabahttps://doi.org/10.1002/(sici)1097-0029(19991001)47:1<38::aid-jemt4>3.0.co;2-5
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Also Consider

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

  1. 1Isolation and characterization of covalently cross-linked actin dimer.1981 · 51 citations
  2. 2A Correlative Analysis of Actin Filament Assembly, Structure, and Dynamics1997 · 122 citations
  3. 3Probing actin polymerization by intermolecular cross-linking.1988 · 118 citations
  4. 4Flexibility of Actin Filaments Derived from Thermal Fluctuations1995 · 651 citations
  5. 5Dominant negative effect of cytoplasmic actin isoproteins on cardiomyocyte cytoarchitecture and function.1995 · 92 citations