Evidence map›Paper›PMID 8484721›Full record

ArticleThe Biochemical journal1993

Interaction of caldesmon with phospholipids.

E A Czuryło, J Zborowski, R Dabrowska

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 28% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

E A CzuryłoDepartment of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
J Zborowski
R Dabrowska
Instytut Biologii Doświadczalnej im. Marcelego Nenckiego · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interaction of caldesmon with liposomes composed of various phospholipids has been examined by tryptophan fluorescence spectroscopy. The results indicate that caldesmon makes its strongest complex with phosphatidylserine (PS) vesicles (Kass. = 1.45 x 10(5) M-1). Both electrostatic and hydrophobic interactions contribute to the stability of this complex. The site for strong binding of PS seems to be located in the N-terminal part of the 34 kDa C-terminal fragment of caldesmon. Binding of PS at this site results in displacement of calmodulin from its complex with caldesmon.

Indexed as

AnimalsBinding, CompetitiveBinding SitesCalmodulinCalmodulin-Binding ProteinsChemical PhenomenaChemistry, PhysicalChickensElectrochemistryGizzard, AvianLiposomesPeptide FragmentsPhosphatidylserinesPhospholipidsSodium ChlorideSpectrometry, FluorescenceCalmodulinCalmodulin-Binding ProteinsLiposomesPeptide FragmentsPhosphatidylserinesPhospholipidsSodium Chloride

Identifiers

PMID8484721
PMCPMC1132539
OpenAlexW2220186003

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.