Evidence map›Paper›PMID 18784650›Full record

ArticleNature2008

Concurrent nucleation of 16S folding and induced fit in 30S ribosome assembly.

Tadepalli Adilakshmi, Deepti L Bellur, Sarah A Woodson

Open access · greenAbstract read
In one paragraph

Article in Nature, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

137 citing papers in PubMed, 175 citations in OpenAlex.

  1. Methyltransferase RsmB chaperonesScience advances · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Mechanism of 30S subunit recognition and modification by the conserved bacterial ribosomal RNA methyltransferase RsmI.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Article
  8. Mechanistic insights intobioRxiv : the preprint server for biology · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Autonomous ribosome biogenesis in vitro.Nature communications · 2025
    Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

77 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 1 institution in 1 country.

Tadepalli AdilakshmiT.C. Jenkins Department of Biophysics, Johns Hopkins University, 3400 North Charles Street, Baltimore, Maryland 21218-2685, USA.
Deepti L Bellur
Sarah A Woodson
University of Chicago · US

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
TIME RESOLVED HYDROXYL RADICAL FOOTPRINTING OF RNAR01GM060819 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WOODSON, SARAH A. · 1999 to 2019
$6.1M
Center for Synchrotron BiosciencesP41EB001979 · NIBIB · YESHIVA UNIVERSITY · PI CHANCE, MARK R · 2003 to 2008
$5.6M
NIBIB NIH HHS P30 EB009998NIBIB NIH HHS P41-EB0001979NIBIB NIH HHS P41 EB001979NIGMS NIH HHS GM60819NIGMS NIH HHS R01 GM060819
6 · The paper itself

Abstract

Rapidly growing cells produce thousands of new ribosomes each minute, in a tightly regulated process that is essential to cell growth. How the Escherichia coli 16S ribosomal RNA and the 20 proteins that make up the 30S ribosomal subunit can assemble correctly in a few minutes remains a challenging problem, partly because of the lack of real-time data on the earliest stages of assembly. By providing snapshots of individual RNA and protein interactions as they emerge in real time, here we show that 30S assembly nucleates concurrently from different points along the rRNA. Time-resolved hydroxyl radical footprinting was used to map changes in the structure of the rRNA within 20 milliseconds after the addition of total 30S proteins. Helical junctions in each domain fold within 100 ms. In contrast, interactions surrounding the decoding site and between the 5', the central and the 3' domains require 2-200 seconds to form. Unexpectedly, nucleotides contacted by the same protein are protected at different rates, indicating that initial RNA-protein encounter complexes refold during assembly. Although early steps in assembly are linked to intrinsically stable rRNA structure, later steps correspond to regions of induced fit between the proteins and the rRNA.

Indexed as

Nucleic Acid ConformationEscherichia coliKineticsModels, MolecularProtein BindingProtein ConformationRibosomal ProteinsRibosomesRNA, Ribosomal, 16SSynchrotronsX-RaysRibosomal ProteinsRNA, Ribosomal, 16S

Identifiers

PMID18784650
PMCPMC2720798
OpenAlexW1986581714

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.