Evidence map›Paper›PMID 18457655›Full record

ArticleBiochemical and biophysical research communications2008

The actin binding protein, fesselin, is a member of the synaptopodin family.

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

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

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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 at 2 institutions in 2 countries.

Mechthild M SchroeterDepartment of Biochemistry & Molecular Biology, Brody School of Medicine at East Carolina University, 600 Moye Blvd, Greenville, NC 27834, USA. schroeterm@ecu.edu
Brent Beall
Hans W Heid
Joseph M Chalovich
East Carolina University · USGerman Cancer Research Center · DE

Funding

Acting Based Regulation of Smooth Muscle ContractionR01AR035216 · NIAMS · EAST CAROLINA UNIVERSITY · PI CHALOVICH, JOSEPH M · 1986 to 2007
$1.5M
NIAMS NIH HHS AR035216NIAMS NIH HHS R01 AR035216
6 · The paper itself

Abstract

Fesselin is a natively unfolded protein that is abundant in avian smooth muscle. Like many natively unfolded proteins, fesselin has multiple binding partners including actin, myosin, calmodulin and alpha-actinin. Fesselin accelerates actin polymerization and bundles actin. These and other observations suggest that fesselin is a component of the cytoskeleton. We have now cloned fesselin and have determined the cDNA derived amino acid sequence. We verified parts of the sequence by Edman analysis and by mass spectroscopy. Our results confirmed fesselin is homologous to human synaptopodin 2 and belongs to the synaptopodin family of proteins.

Indexed as

TurkeysAmino Acid SequenceAnimalsAvian ProteinsHumansMembrane ProteinsMicrofilament ProteinsMolecular Sequence DataPeptidesSequence AlignmentSequence Analysis, ProteinSequence Homology, Amino AcidAvian ProteinsfesselinMembrane ProteinsMicrofilament ProteinsPeptidesSYNPO2 protein, human

Identifiers

PMID18457655
PMCPMC2453309
OpenAlexW1979746436

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.