Evidence map›Paper›PMID 21177848›Full record

ArticleThe Journal of biological chemistry2011

Structure-functional analyses of CRHSP-24 plasticity and dynamics in oxidative stress response.

Hai Hou, Fengsong Wang, Wenchi Zhang, Dongmei Wang, Xuemei Li, Mark Bartlam, Xuebiao Yao, Zihe Rao

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

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  13. MicroRNAs as Potential Biomarkers in Atherosclerosis.International journal of molecular sciences · 2019
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. The role of cold shock domain proteins in inflammatory diseases.Journal of molecular medicine (Berlin, Germany) · 2014
    Review
  19. 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

8 authors at 4 institutions in 1 country.

Hai HouNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Fengsong Wang
Wenchi Zhang
Dongmei Wang
Xuemei Li
Mark Bartlam
Xuebiao Yao
Zihe Rao
Chinese Academy of Sciences · CNHefei National Center for Physical Sciences at Nanoscale · CNInstitute of Biophysics · CNNankai University · CN

Funding

Atlanta Clinical and Translational Science Institute (ACTSI) RenewalUL1TR000454 · NCATS · EMORY UNIVERSITY · PI STEPHENS, DAVID S · 2012 to 2016
$25.8M
NCATS NIH HHS UL1 TR000454
6 · The paper itself

Abstract

The cold shock domain (CSD) is an evolutionarily conserved nucleic acid binding domain that exhibits binding activity to RNA, ssDNA, and dsDNA. Mammalian CRHSP-24 contains CSD, but its structure-functional relationship has remained elusive. Here we report the crystal structure of human CRHSP-24 and characterization of the molecular trafficking of CRHSP-24 between stress granules and processing bodies in response to oxidative stress. The structure of CRHSP-24 determined by single-wavelength anomalous dispersion exhibits an α-helix and a compact β-barrel formed by five curved anti-parallel β strands. Ligand binding activity of the CSD is orchestrated by residues Ser(41) to Leu(43). Interestingly, a phosphomimetic S41D mutant abolishes the ssDNA binding in vitro and causes CRHSP-24 liberated from stress granules in vivo without apparent alternation of its localization to the processing bodies. This new class of phosphorylation-regulated interaction between the CSD and nucleic acids is unique in stress granule plasticity. Importantly, the association of CRHSP-24 with stress granules is blocked by PP4/PP2A inhibitor calyculin A as PP2A catalyzes the dephosphorylation of Ser(41) of CRHSP-24. Therefore, we speculate that CRHSP-24 participates in oxidative stress response via a dynamic and temporal association between stress granules and processing bodies.

Indexed as

Amino Acid SubstitutionDNA-Binding ProteinsEnzyme InhibitorsHeLa CellsHumansMarine ToxinsMutation, MissenseOxazolesOxidative StressPhosphoprotein PhosphatasesPhosphoproteinsProtein Phosphatase 2Protein Structure, SecondaryStructure-Activity RelationshipTranscription Factorscalyculin ACARHSP1 protein, humanDNA-Binding ProteinsEnzyme InhibitorsMarine ToxinsOxazolesPhosphoprotein PhosphatasesPhosphoproteinsProtein Phosphatase 2protein phosphatase 4Transcription Factors

Identifiers

PMID21177848
PMCPMC3058955
OpenAlexW2002861864

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.