Evidence map›Paper›PMID 21455759›Full record

ReviewJournal of muscle research and cell motility2011

The actin associated protein palladin in smooth muscle and in the development of diseases of the cardiovasculature and in cancer.

Li Jin

Open access · greenAbstract readReview
In one paragraph

Review in Journal of muscle research and cell motility, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

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  17. Actin-induced dimerization of palladin promotes actin-bundling.Protein science : a publication of the Protein Society · 2015
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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

1 author at 1 institution in 1 country.

Li JinDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA. LJ7Q@virginia.edu
University of Virginia · US

Funding

THE CONTRACTILE SYSTEM OF VASCULAR SMOOTH MUSCLEP01HL019242 · NHLBI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI OWENS, GARY K · 1985 to 2009
$16.9M
NHLBI NIH HHS P01 HL019242NHLBI NIH HHS P01 HL19242-33
6 · The paper itself

Abstract

Palladin is an actin associated protein serving as a cytoskeleton scaffold, and actin cross linker, localizing at stress fibers, focal adhesions, and other actin based structures. Recent studies showed that palladin plays a critical role in smooth muscle differentiation, migration, contraction, and more importantly contributes to embryonic development. This review will focus on the functions and possible mechanisms of palladin in smooth muscle and in pathological conditions such as cardiovascular diseases and cancers.

Indexed as

Cytoskeletal ProteinsPhosphoproteinsActinsAnimalsCardiovascular DiseasesCell DifferentiationCell Line, TumorColonic NeoplasmsFemaleHumansMiceMice, KnockoutMuscle ContractionMuscle, Smooth, VascularPancreatic NeoplasmsProtein IsoformsActinsCytoskeletal Proteinspalladin protein, mousePALLD protein, humanPhosphoproteinsProtein Isoforms

Identifiers

PMID21455759
PMCPMC3143271
OpenAlexW2000787778

What OpenQuestion holds

Textmetadata
LicenceTDM
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.