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September 1, 1991Journal of Biological ChemistryOpen Access

Characterization of cDNA clones encoding a human fibroblast caldesmon isoform and analysis of caldesmon expression in normal and transformed cells.

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Authors

RNRobert E. NovyUniversity of Iowa JLJenny LinEmory University JLJing‐Jer LinQingdao University of Science and Technology

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Implication

HUM 1-CaD cloning extends nonmuscle caldesmon tools; leaves open its regulatory role in vascular cells.

Key Points

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Cite This Study

Novy et al. (1991) studied this question.

synapsesocial.com/papers/6a702ce7b27f158178273ae0 https://doi.org/10.1016/s0021-9258(18)55390-4

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Also Consider

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

1The effects of caldesmon on smooth muscle heavy actomeromyosin ATPase activity and binding of heavy meromyosin to actin.1986 · 138 citations
2Caldesmon: A common actin‐linked regulatory protein in the smooth muscle and nonmuscle contractile system1988 · 78 citations
3Dissociation of the effect of caldesmon on the ATPase activity and on the binding of smooth heavy meromyosin to actin by partial digestion of caldesmon.1990 · 112 citations
4Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin1989 · 223 citations
5Annealing of Gelsolin-severed Actin Fragments by Tropomyosin in the Presence of Ca2+1989 · 109 citations