Evidence map›Paper›PMID 9017208›Full record

ArticleBiophysical journal1997

The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations.

E A Czuryło, T Hellweg, W Eimer, R Dabrowska

Abstract read
In one paragraph

Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

4 authors.

E A CzuryłoDepartment of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
T Hellweg
W Eimer
R Dabrowska

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The size and the shape of caldesmon as well as its 50-kDa central and 19-kDa C-terminal fragments were investigated by photon correlation spectroscopy. The hydrodynamic radii, which have been calculated from the experimentally obtained translational diffusion coefficients, are 9.8 nm, 6.0 nm, and 2.9 nm, respectively. Moreover, the experimental values for the translational diffusion coefficients are compared with results obtained from hydrodynamic model calculations. Detailed models for the structure of caldesmon in solution are derived. The contour length is about 64 nm for all of the models used for caldesmon.

Indexed as

AnimalsCalmodulin-Binding ProteinsChemical PhenomenaChemistry, PhysicalChickensDiffusionModels, MolecularMuscle, SmoothParticle SizePeptide FragmentsProtein ConformationScattering, RadiationSpectrum AnalysisCalmodulin-Binding ProteinsPeptide Fragments

Identifiers

PMID9017208
PMCPMC1185606

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.