Evidence map›Paper›PMID 19228069›Full record

ArticleACS chemical biology2009

When starting over makes more sense.

Scott C Blanchard

Abstract read
In one paragraph

Article in ACS chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Scott C BlanchardDepartment of Physiology and Biophysics, Weill Cornell Medical College of Cornell University, New York, New York 10021, USA. scb2005@med.cornell.edu

Funding

Imaging Protein Synthesis on the Ribosome using Single-Molecule FRETR01GM079238 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BLANCHARD, SCOTT C · 2006 to 2023
$7.0M
NIGMS NIH HHS R01 GM079238
6 · The paper itself

Abstract

Proofreading mechanisms intrinsic to DNA and RNA polymers that contribute substantially to overall fidelity are lacking in the ribosome. New evidence, however, suggests that quality control in translation can occur after substrate incorporation by an abortive mechanism entailing premature release factor-catalyzed termination. These data shed new light on the importance and ubiquity of retrospective quality control mechanisms in ensuring the overall fidelity of nature's processive enzymes and demonstrate that competitive elongation reactions on the ribosome are kinetically sensitive to compositional features of the translating particle.

Indexed as

Peptide Chain Termination, TranslationalRibosomesAminoacylationBase Pair MismatchBiocatalysisModels, BiologicalModels, MolecularPeptide Termination FactorsRNA, TransferSubstrate SpecificityPeptide Termination FactorsRNA, Transfer

Identifiers

PMID19228069
PMCPMC3433159

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.