ArticleThe Biochemical journal1992
Caldesmon-phospholipid interaction. Effect of protein kinase C phosphorylation and sequence similarity with other phospholipid-binding proteins.
Article in The Biochemical journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed, 18 citations in OpenAlex.
- Intrinsically disordered caldesmon binds calmodulin via the "buttons on a string" mechanism.PeerJ · 2015Article
- Phosphatidylserine liposomes can be tethered by caldesmon to actin filaments.Biophysical journal · 1997Article
- Phosphorylation of aorta caldesmon by endogenous proteolytic fragments of protein kinase C.Journal of muscle research and cell motility · 1994Article
- Interaction of caldesmon with phospholipids.The Biochemical journal · 1993Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently published data [Vorotnikov & Gusev (1990) FEBS Lett. 277, 134-136] indicate that smooth muscle caldesmon interacts with a mixture of soybean phospholipids (azolectin). Continuing this investigation, we found that duck gizzard caldesmon interacts more tightly with acidic (phosphatidylserine) than with neutral (phosphatidylcholine) phospholipids. A high concentration of Ca2+ (50 microM) decreased the interaction of caldesmon with phosphatidylserine. Among chymotryptic peptides of caldesmon, only those having molecular masses of 45, 40, 23, 22 and 20 kDa were able to specifically interact with phospholipids. These peptides, derived from the C-terminal part of caldesmon, contained the sites phosphorylated by Ca2+/phospholipid-dependent protein kinase, and phosphorylation catalysed by this enzyme decreased the affinity of these peptides for phospholipids. In the presence of Ca2+, calmodulin competed with phospholipids for the interaction with the caldesmon peptides. The C-terminal part of caldesmon contains three peptides with a primary structure similar to that of the calmodulin- and phospholipid-binding site of neuromodulin. These sites may be involved in the interaction of caldesmon with calmodulin and phospholipids.
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Registered trials
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