Evidence map›Paper›PMID 7756522›Full record

ArticleBiophysical journal1995

Physics of actin networks. I. Rheology of semi-dilute F-actin.

K S Zaner

Abstract read
In one paragraph

Article in Biophysical journal, 1995. 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
–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

3 citing papers in PubMed.

  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

1 author.

K S ZanerSection of Hematology-Oncology, Boston City Hospital, Boston University School of Medicine, Massachusetts 02119, USA.

Funding

NIGMS NIH HHS GM 37590
6 · The paper itself

Abstract

The mechanical properties of cytoplasm are considered to be of underlying importance in the mechanism of cell movement and are to a large extent determined by an actin-containing cytoskeleton. Several laboratories have begun to accumulate data on the mechanical or rheologic properties of protein systems derived from the actin cytoskeleton. The focus of this manuscript is to attempt to reproduce the experimentally determined mechanical properties of non-cross-linked F-actin from theoretical considerations. It was found that a mechanical spectrum for 1 mg/ml F-actin could be calculated, which approximated experimental data, from a relaxation spectrum consisting of a long range rotational diffusion motion and short range bending motion, assuming an exponential distribution of filament lengths with a weight average length of 4 mu. The calculated spectrum underestimated the dynamic moduli at high frequencies, suggesting that a more complex actin structure is present that enhances the high frequency component.

Indexed as

ActinsAnimalsBiomechanical PhenomenaBiophysical PhenomenaBiophysicsCell MovementCytoskeletonIn Vitro TechniquesMuscle, SkeletalRabbitsRheologySolutionsActinsSolutions

Identifiers

PMID7756522
PMCPMC1281825

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.