Evidence map›Paper›PMID 9892639›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Site-directed hydroxyl radical probing of 30S ribosomal subunits by using Fe(II) tethered to an interruption in the 16S rRNA chain.

R R Samaha, S Joseph, B O'Brien, T W O'Brien, H F Noller

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 40% 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

5 citing papers in PubMed, 12 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

R R SamahaCenter for Molecular Biology of RNA, Sinsheimer Laboratories, University of California, Santa Cruz, CA 95064, USA.
S Joseph
B O'Brien
T W O'Brien
H F Noller
University of California, Santa Cruz · US

Funding

RIBOSOME STRUCTURE AND FUNCTIONR01GM017129 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI NOLLER, HARRY F · 1985 to 2015
$6.9M
RIBOSOME STRUCTURE AND FUNCTIONR37GM017129 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI NOLLER, HARRY F · 1990 to 1999
–
NIGMS NIH HHS GM-17129NIGMS NIH HHS R01 GM017129NIGMS NIH HHS R37 GM017129
6 · The paper itself

Abstract

Two in vitro transcripts, one corresponding to the 5' and central domains (residues 1-920) of 16S rRNA and the other corresponding to its 3' domain (residues 922-1542), assemble efficiently in trans with 30S ribosomal proteins to form a compact ribonucleoprotein particle that cosediments with natural 30S subunits. Isolated particles are similar in appearance to natural 30S subunits with electron microscopy and contain a full complement of the small subunit ribosomal proteins. The particles have a reduced ability to bind tRNA (attributable to the location of the discontinuity in a conserved region of the rRNA) near features that have been implicated in tRNA binding. Association of these two halves of 16S rRNA in trans must be stabilized by either previously unidentified RNA-RNA contacts or interactions mediated by ribosomal proteins because there are no known direct interactions between them. The trans construct was used to probe the three-dimensional RNA neighborhood around position 922 of 16S rRNA by generating hydroxyl radicals from Fe(II) tethered to the 5' end of the 3' transcript. Hydroxyl radical-induced cuts in the 16S rRNA chain were localized by primer extension to nucleotides 923-929 and 1192-1198, providing evidence for the mutual proximity of the 920 and 1192 regions.

Indexed as

Centrifugation, Density GradientEdetic AcidElectrophoresis, Gel, Two-DimensionalHydroxyl RadicalIron Chelating AgentsMicroscopy, ElectronNucleic Acid ConformationOrganometallic CompoundsRibonucleoproteinsRibosomal ProteinsRNA, Ribosomal, 16SRNA, TransferTranscription, Genetic1-(4-bromoacetamidobenzyl)EDTAEdetic AcidHydroxyl RadicalIron Chelating AgentsOrganometallic CompoundsRibonucleoproteinsRibosomal Proteinsribosomal protein S30RNA, Ribosomal, 16SRNA, Transfer

Identifiers

PMID9892639
PMCPMC15142
OpenAlexW2004918277

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.