Evidence map›Paper›PMID 18588515›Full record

ArticleBioscience reports2008

In vitro characterization of native mammalian smooth-muscle protein synaptopodin 2.

Mechthild M Schroeter, Brent Beall, Hans W Heid, Joseph M Chalovich

Abstract read
In one paragraph

Article in Bioscience reports, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. 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.

Mechthild M SchroeterDepartment of Biochemistry and Molecular Biology, Brody School of Medicine at East Carolina University, Greenville, NC 27834, USA. schroeterm@ecu.edu
Brent Beall
Hans W Heid
Joseph M Chalovich

Funding

Acting Based Regulation of Smooth Muscle ContractionR01AR035216 · NIAMS · EAST CAROLINA UNIVERSITY · PI CHALOVICH, JOSEPH M · 1986 to 2007
$1.5M
NIAMS NIH HHS AR 035216NIAMS NIH HHS R01 AR035216
6 · The paper itself

Abstract

An analysis of the primary structure of the actin-binding protein fesselin revealed it to be the avian homologue of mammalian synaptopodin 2 [Schroeter, Beall, Heid, and Chalovich (2008) Biochem. Biophys. Res. Commun. 371, 582-586]. We isolated two synaptopodin 2 isoforms from rabbit stomach that corresponded to known types of human synaptopodin 2. The purification scheme used was that developed for avian fesselin. These synaptopodin 2 forms shared several key functions with fesselin. Both avian fesselin and mammalian synaptopodin 2 bound to Ca(2+)-calmodulin, alpha-actinin and smooth-muscle myosin. In addition, both proteins stimulated the polymerization of actin in a Ca(2+)-calmodulin-dependent manner. Synaptopodin 2 has never before been shown to polymerize actin in the absence of alpha-actinin, to polymerize actin in a Ca(2+)-calmodulin-dependent manner, or to bind to Ca(2+)-calmodulin or myosin. These properties are consistent with the proposed function of synaptopodin 2 in organizing the cytoskeleton.

Indexed as

ActininAnimalsCalmodulinCalmodulin-Binding ProteinsHumansMembrane ProteinsMicrofilament ProteinsMuscle ProteinsMuscle, SmoothMyosinsRabbitsActininCalmodulinCalmodulin-Binding ProteinsfesselinMembrane ProteinsMicrofilament ProteinsMuscle ProteinsMyosinsSYNPO2 protein, human

Identifiers

PMID18588515
PMCPMC3763723

What OpenQuestion holds

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Registered trials

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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.