Evidence map›Paper›PMID 24273516›Full record

ArticleFrontiers in physiology2013

Skeletal muscle heat shock protein 70: diverse functions and therapeutic potential for wasting disorders.

Sarah M Senf

Open access · goldAbstract read
In one paragraph

Article in Frontiers in physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

55 citing papers in PubMed, 109 citations in OpenAlex.

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  8. ETASPharmaceuticals (Basel, Switzerland) · 2025
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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.

Sarah M SenfDepartment of Physical Therapy, University of Florida Gainesville, FL, USA.
University of Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The stress-inducible 70-kDa heat shock protein (HSP70) is a highly conserved protein with diverse intracellular and extracellular functions. In skeletal muscle, HSP70 is rapidly induced in response to both non-damaging and damaging stress stimuli including exercise and acute muscle injuries. This upregulation of HSP70 contributes to the maintenance of muscle fiber integrity and facilitates muscle regeneration and recovery. Conversely, HSP70 expression is decreased during muscle inactivity and aging, and evidence supports the loss of HSP70 as a key mechanism which may drive muscle atrophy, contractile dysfunction and reduced regenerative capacity associated with these conditions. To date, the therapeutic benefit of HSP70 upregulation in skeletal muscle has been established in rodent models of muscle injury, muscle atrophy, modified muscle use, aging, and muscular dystrophy, which highlights HSP70 as a key therapeutic target for the treatment of various conditions which negatively affect skeletal muscle mass and function. This article will review these important findings and provide perspective on the unanswered questions related to HSP70 and skeletal muscle plasticity which require further investigation.

Indexed as

damagedystrophyheat shock proteinsinflammatory responsemuscle atrophymuscle dysfunctionregenerationsarcopenia

Identifiers

PMID24273516
PMCPMC3822288
OpenAlexW1986623178

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.