Evidence map›Paper›PMID 21862385›Full record

ReviewCurrent opinion in chemical biology2011

Inside the 40S ribosome assembly machinery.

Katrin Karbstein

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structural Heterogeneity in Pre-40S Ribosomes.Structure (London, England : 1993) · 2017
    Article
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  14. 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.

Katrin KarbsteinDepartment of Cancer Biology, The Scripps Research Institute, Jupiter, FL 33458, USA. kkarbst@scripps.edu
Scripps Research Institute · US

Funding

Quality Control in Ribosome Assembly - the Function of Regulatory ProteinsR01GM086451 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KARBSTEIN, KATRIN · 2009 to 2019
$4.8M
NIGMS NIH HHS 1R01GM086451NIGMS NIH HHS R01 GM086451
6 · The paper itself

Abstract

Ribosome assembly involves rRNA transcription, modification, folding and cleavage from precursor transcripts, and association of ribosomal proteins (Rps). In bacteria, this complex process requires only a handful of proteins in addition to those needed for rRNA transcription, modification and cleavage, while in eukaryotes a large machinery comprising ∼200 proteins in the yeast S. cerevisiae has been identified. Furthermore, while the bacterial assembly factors generally produce only cold-sensitive phenotypes upon deletion, most of the eukaryotic assembly factors are essential, comprising ∼20% of essential yeast proteins. This review explores recent rapid progress in the structural and functional dissection of the 40S assembly machinery.

Indexed as

Models, MolecularPeptide Chain Initiation, TranslationalProtein Interaction MappingRibosomal ProteinsRibosome Subunits, Small, EukaryoticRNA FoldingRNA PrecursorsRNA, RibosomalRNA, Small NucleolarSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription, GeneticRibosomal ProteinsRNA PrecursorsRNA, RibosomalRNA, Small NucleolarSaccharomyces cerevisiae Proteins

Identifiers

PMID21862385
PMCPMC3329787
OpenAlexW2013051407

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.