Evidence map›Paper›PMID 29322631›Full record

ReviewWiley interdisciplinary reviews. RNA2018

Cold-inducible RNA binding protein in cancer and inflammation.

Daniel A Lujan, Joey L Ochoa, Rebecca S Hartley

Open access · greenAbstract readReview
In one paragraph

Review in Wiley interdisciplinary reviews. RNA, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

85 citing papers in PubMed, 134 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Microbiome-Derived Metabolites Shape CD4bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
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  11. Review
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  16. Review
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  18. Review
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25 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Daniel A LujanDepartment of Cell Biology and Physiology, University of New Mexico School of Medicine and University of New Mexico Comprehensive Cancer Center, Albuquerque, New Mexico.
Joey L OchoaDepartment of Cell Biology and Physiology, University of New Mexico School of Medicine and University of New Mexico Comprehensive Cancer Center, Albuquerque, New Mexico.
Rebecca S HartleyDepartment of Cell Biology and Physiology, University of New Mexico School of Medicine and University of New Mexico Comprehensive Cancer Center, Albuquerque, New Mexico.
University of New Mexico · USUNM Comprehensive Cancer Center

Funding

UNM Initiative to Maximize Student Diversity (IMSD)R25GM060201 · NIGMS · UNIVERSITY OF NEW MEXICO · PI WERNER-WASHBURNE, MARGRET C. · 2000 to 2017
$9.9M
Cold-inducible RNA binding protein links inflammation and breast cancerF31CA213933 · NCI · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI LUJAN, DANIEL ALBINO · 2017 to 2019
$98k
NCI NIH HHS F31 CA213933NIGMS NIH HHS R25 GM060201
6 · The paper itself

Abstract

RNA binding proteins (RBPs) play key roles in RNA dynamics, including subcellular localization, translational efficiency and metabolism. Cold-inducible RNA binding protein (CIRP) is a stress-induced protein that was initially described as a DNA damage-induced transcript (A18 hnRNP), as well as a cold-shock domain containing cold-stress response protein (CIRBP) that alters the translational efficiency of its target messenger RNAs (mRNAs). This review summarizes recent work on the roles of CIRP in the context of inflammation and cancer. The function of CIRP in cancer appeared to be solely driven though its functions as an RBP that targeted cancer-associated mRNAs, but it is increasingly clear that CIRP also modulates inflammation. Several recent studies highlight roles for CIRP in immune responses, ranging from sepsis to wound healing and tumor-promoting inflammation. While modulating inflammation is an established role for RBPs that target cytokine mRNAs, CIRP appears to modulate inflammation by several different mechanisms. CIRP has been found in serum, where it binds the TLR4-MD2 complex, acting as a Damage-associated molecular pattern (DAMP). CIRP activates the NF-κB pathway, increasing phosphorylation of Iκκ and IκBα, and stabilizes mRNAs encoding pro-inflammatory cytokines. While CIRP promotes higher levels of pro-inflammatory cytokines in certain cancers, it also decreases inflammation to accelerate wound healing. This dichotomy suggests that the influence of CIRP on inflammation is context dependent and highlights the importance of detailing the mechanisms by which CIRP modulates inflammation. WIREs RNA 2018, 9:e1462. doi: 10.1002/wrna.1462 This article is categorized under: RNA in Disease and Development > RNA in Disease RNA Interactions with Proteins and Other Molecules > Protein-RNA Interactions: Functional Implications.

Indexed as

AnimalsHumansInflammationNeoplasmsRNA-Binding ProteinsCIRBP protein, humanRNA-Binding ProteinsA18 hnRNPcancerCIRPinflammationRNA binding proteinstress

Identifiers

PMID29322631
PMCPMC5886743
OpenAlexW2782602358

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.