Phosphatidylserine liposomes can be tethered by caldesmon to actin filaments.

Rotary shadowing electron microscopy revealed that attachment of caldesmon to phosphatidylserine (PS) liposomes was mainly through its C-terminal end. To determine the PS-binding sites of caldesmon, we have made use of synthetic peptides covering the two C-terminal calmodulin binding sites and a rec...

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Bibliografske podrobnosti
Main Authors: Makuch, R, Zasada, A, Mabuchi, K, Krauze, K, Wang, C L, Dabrowska, R
Format: Artigo
Jezik:Inglês
Izdano: 1997
Teme:
Research Article
Online dostop:https://ncbi.nlm.nih.gov/pmc/articles/PMC1181059/
https://ncbi.nlm.nih.gov/pubmed/9284327
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