Evidence map›Paper›PMID 23907854›Full record

ReviewWiley interdisciplinary reviews. RNA

RNA protein interactions governing expression of the most abundant protein in human body, type I collagen.

Branko Stefanovic

Abstract readReview
In one paragraph

Review in Wiley interdisciplinary reviews. RNA. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

33 citing papers in PubMed, 65 citations in OpenAlex.

  1. Trial
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  6. Biomolecular NMR assignments · 2025
    Article
  7. Article
  8. Application of collagen in bone regeneration.Journal of orthopaedic translation · 2025
    Review
  9. Article
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  11. Multi-organ single-cell RNA sequencing in mice reveals early hyperglycemia responses that converge on fibroblast dysregulation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
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  18. 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

1 author at 1 institution in 1 country.

Branko StefanovicDepartment of Biomedical Sciences, College of Medicine, Florida State University, Tallahassee, FL, USA. branko.stefanovic@med.fsu.edu
Florida State University · US

Funding

Regulation of Type I Collagen in Hepatic FibrosisR01DK059466 · NIDDK · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI STEFANOVIC, BRANKO · 2002 to 2012
$2.4M
NIDDK NIH HHS 2R01DK059466-07A2NIDDK NIH HHS R01 DK059466
6 · The paper itself

Abstract

Type I collagen is the most abundant protein in human body. The protein turns over slowly and its replacement synthesis is low. However, in wound healing or in pathological fibrosis the cells can increase production of type I collagen several hundred fold. This increase is predominantly due to posttranscriptional regulation, including increased half-life of collagen messenger RNAs (mRNAs) and their increased translatability. Type I collagen is composed of two α1 and one α2 polypeptides that fold into a triple helix. This stoichiometry is strictly regulated to prevent detrimental synthesis of α1 homotrimers. Collagen polypeptides are co-translationally modified and the rate of modifications is in dynamic equilibrium with the rate of folding, suggesting coordinated translation of collagen α1(I) and α2(I) polypeptides. Collagen α1(I) mRNA has in the 3' untranslated region (UTR) a C-rich sequence that binds protein αCP, this binding stabilizes the mRNA in collagen producing cells. In the 5' UTR both collagen mRNAs have a conserved stem-loop (5' SL) structure. The 5' SL is critical for high collagen expression, knock in mice with disruption of the 5' SL are resistant to liver fibrosis. the 5' SL binds protein LARP6 with strict sequence specificity and high affinity. LARP6 recruits RNA helicase A to facilitate translation initiation and associates collagen mRNAs with vimentin and nonmuscle myosin filaments. Binding to vimentin stabilizes collagen mRNAs, while nonmuscle myosin regulates coordinated translation of α1(I) and α2(I) mRNAs. When nonmuscle myosin filaments are disrupted the cells secrete only α1 homotrimers. Thus, the mechanism governing high collagen expression involves two RNA binding proteins and development of cytoskeletal filaments.

Indexed as

Gene Expression RegulationRNA StabilityAnimalsAutoantigensCollagen Type IHeterogeneous-Nuclear RibonucleoproteinsHumansMiceRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerSS-B AntigenAutoantigensCollagen Type IHeterogeneous-Nuclear RibonucleoproteinsRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerSS-B Antigen

Identifiers

PMID23907854
PMCPMC3748166
OpenAlexW2109381471

What OpenQuestion holds

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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.