Evidence map›Paper›PMID 26210153›Full record

ReviewCellular and molecular life sciences : CMLS2015

Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis.

Erin Thornell, Andrew Aquilina

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

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  17. Small heat shock proteins: Simplicity meets complexity.The Journal of biological chemistry · 2019
    Review
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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

2 authors at 2 institutions in 1 country.

Erin ThornellIllawarra Health and Medical Research Institute, University of Wollongong, Northfields Ave., Wollongong, NSW, 2522, Australia. emt910@uowmail.edu.au.ORCID http://orcid.org/0000-0002-1908-6735
Andrew AquilinaIllawarra Health and Medical Research Institute, University of Wollongong, Northfields Ave., Wollongong, NSW, 2522, Australia.
Illawarra Health and Medical Research Institute · AUUniversity of Wollongong · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

αA-Crystallin (αA) and αB-crystallin (αB) are small heat shock proteins responsible for the maintenance of transparency in the lens. In non-lenticular tissues, αB is involved in both maintenance of the cytoskeleton and suppression of neurodegeneration amongst other roles. Despite their importance in maintaining cellular health, modifications and mutations to αA and αB appear to play a role in disease states such as cataract and myopathies. The list of modifications that have been reported is extensive and include oxidation, disulphide bond formation, C- and N-terminal truncation, acetylation, carboxymethylation, carboxyethylation, carbamylation, deamidation, phosphorylation and methylation. Such modifications, notably phosphorylation, are alleged to cause changes to chaperone activity by inducing substructural changes and altering subunit exchange dynamics. Although the effect modification has on the activities of αA and αB is contentious, it has been proposed that these changes are responsible for the induction of hyperactivity and are thereby indirectly responsible for protein deposition characteristic of many diseases associated with αA and αB. This review compiles all reported sites of αA and αB modifications, and investigates the role phosphorylation, in particular, plays in cellular processes.

Indexed as

alpha-Crystallin A Chainalpha-Crystallin B ChainCataractHomeostasisHumansMutationPhosphorylationProtein Processing, Post-Translationalalpha-Crystallin A Chainalpha-Crystallin B ChainChaperonesProteostasisPTMsStructure

Identifiers

PMID26210153
PMCPMC11113999
OpenAlexW948039569

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.