Evidence map›Paper›PMID 16314459›Full record

ArticleRNA (New York, N.Y.)2005

Accessibility of 18S rRNA in human 40S subunits and 80S ribosomes at physiological magnesium ion concentrations--implications for the study of ribosome dynamics.

Christina L Shenvi, Ken C Dong, Eric M Friedman, Jeffrey A Hanson, Jamie H D Cate

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in RNA (New York, N.Y.), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

36 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. A ribosomal kinetic checkpoint governs selective mRNA recruitment.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Preinitiation Complex Loading onto mRNAs with Long versus Short 5' TLs.International journal of molecular sciences · 2022
    Article
  7. Article
  8. Hepatitis C Virus Translation Regulation.International journal of molecular sciences · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. A researcher's guide to the galaxy of IRESs.Cellular and molecular life sciences : CMLS · 2017
    Review
  14. Dynamics of IRES-mediated translation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. When Too Much ATP Is Bad for Protein Synthesis.Journal of molecular biology · 2015
    Review
  19. Article
  20. 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

5 authors at 3 institutions in 2 countries.

Christina L ShenviDepartment of Chemistry, University of California, 202 Melvin Calvin Lab, Berkeley, CA 94720, USA.
Ken C Dong
Eric M Friedman
Jeffrey A Hanson
Jamie H D Cate
Calvin University · KRLawrence Berkeley National Laboratory · USUniversity of California, Berkeley · US

Funding

THE MOLECULAR BASIS OF CELL FUNCTIONT32GM007232 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BILDER, DAVID, UNAL, ELCIN · 1985 to 2022
$36.4M
Univ of Calif Berkeley Chemistry-Biology Interface ProgramT32GM066698 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CHANG, CHRISTOPHER J., FRANCIS, MATTHEW B · 2004 to 2023
$7.5M
The Role of the Ribosome in the Accuracy of TranslationR01GM065050 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CATE, JAMIE H · 2001 to 2022
$7.4M
NIGMS NIH HHS 1 T32 GM066698-01AINIGMS NIH HHS R01 GM065050NIGMS NIH HHS R01-GM65050NIGMS NIH HHS T32 GM007232NIGMS NIH HHS T32 GM066698NIGMS NIH HHS T32-GM07232-27
6 · The paper itself

Abstract

Protein biosynthesis requires numerous conformational rearrangements within the ribosome. The structural core of the ribosome is composed of RNA and is therefore dependent on counterions such as magnesium ions for function. Many steps of translation can be compromised or inhibited if the concentration of Mg(2+) is too low or too high. Conditions previously used to probe the conformation of the mammalian ribosome in vitro used high Mg(2+) concentrations that we find completely inhibit translation in vitro. We have therefore probed the conformation of the small ribosomal subunit in low concentrations of Mg(2+) that support translation in vitro and compared it with the conformation of the 40S subunit at high Mg(2+) concentrations. In low Mg(2+) concentrations, we find significantly more changes in chemical probe accessibility in the 40S subunit due to subunit association or binding of the hepatitis C internal ribosomal entry site (HCV IRES) than had been observed before. These results suggest that the ribosome is more dynamic in its functional state than previously appreciated.

Indexed as

HumansMagnesiumModels, GeneticModels, MolecularNucleic Acid ConformationProtein BiosynthesisRibosomesRNA, MessengerRNA, RibosomalRNA, Ribosomal, 18SMagnesiumRNA, MessengerRNA, RibosomalRNA, Ribosomal, 18S

Identifiers

PMID16314459
PMCPMC1370877
OpenAlexW2147674707

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.