Evidence map›Paper›PMID 19209827›Full record

ReviewAdvances in experimental medicine and biology2008

Caldesmon and the regulation of cytoskeletal functions.

C L Albert Wang

Open access · greenAbstract readReview
In one paragraph

Review in Advances in experimental medicine and biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
8.6field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Caldesmon: Biochemical and Clinical Implications in Cancer.Frontiers in cell and developmental biology · 2021
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. p53 in cell invasion, podosomes, and invadopodia.Cell adhesion & migration · 2014
    Review
  14. Article
  15. Article
  16. Review
  17. Subcellular distribution and relative expression of fibrocyte markers in the CD/1 mouse cochlea assessed by semiquantitative immunogold electron microscopy.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2011
    Article
  18. Article
  19. Article
  20. Histochemical localization of caldesmon in the CNS and ganglia of the mouse.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2011
    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 at 1 institution in 1 country.

C L Albert WangBoston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA. wang@bbri.org
Boston Biomedical Research Institute · US

Funding

X-ray Crystallographic Investigation of Smooth Muscle RegulationP01AR041637 · NIAMS · BOSTON BIOMEDICAL RESEARCH INSTITUTE · PI TAO, TERENCE · 1992 to 2007
$15.1M
NIAMS NIH HHS P01 AR041637NIAMS NIH HHS P01-AR41637
6 · The paper itself

Abstract

Caldesmon (CaD) is an extraordinary actin-binding protein, because in addition to actin, it also bindsmyosin, calmodulin and tropomyosin. As a component of the smoothmuscle and nonmuscle contractile apparatus CaD inhibits the actomyosin ATPase activity and its inhibitory action is modulated by both Ca2+ and phosphorylation. The multiplicity of binding partners and diverse biochemical properties suggest CaD is a potent and versatile regulatory protein both in contractility and cell motility. However, after decades ofinvestigation in numerous laboratories, hard evidence is still lacking to unequivocally identify its in vivo functions, although indirect evidence is mounting to support an important role in connection with the actin cytoskeleton. This chapter reviews the highlights of the past findings and summarizes the current views on this protein, with emphasis of its interaction with tropomyosin.

Indexed as

ActomyosinAnimalsAortaBiochemistryCalmodulinCalmodulin-Binding ProteinsCell MovementCytoskeletonHumansModels, BiologicalMyocytes, Smooth MusclePhosphorylationProtein Structure, TertiaryTropomyosinUrinary BladderActomyosinCalmodulinCalmodulin-Binding ProteinsTropomyosin

Identifiers

PMID19209827
PMCPMC2975104
OpenAlexW2128710639

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.