Evidence map›Paper›PMID 23288433›Full record

ArticleJournal of molecular evolution2013

Fixation and accumulation of thermotolerant catalytic competence of a pair of ligase ribozymes through complex formation and cross ligation.

Nana Isomoto, Yuri Maeda, Takahiro Tanaka, Hiroyuki Furuta, Yoshiya Ikawa

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Article in Journal of molecular evolution, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

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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

1 citing paper in PubMed.

  1. 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.

Nana IsomotoDepartment of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Moto-oka 744, Fukuoka 819-0395, Japan.
Yuri Maeda
Takahiro Tanaka
Hiroyuki Furuta
Yoshiya Ikawa

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the early stages of the hypothetical RNA world, some primitive RNA catalysts (ribozymes) may have emerged through self-assembly of short RNA oligomers. Although they may be unstable against temperature fluctuations and other environmental changes, ligase ribozymes (ribozymes with RNA strand-joining activity) may resolve structural instability of self-assembling RNAs by converting them to the corresponding unimolecular formats. To investigate this possibility, we constructed a model system using a cross-ligation system composed of a pair of self-assembling ligase ribozymes. Their abilities to act as catalysts, substrates, and a cross-ligation system were analyzed with or without thermal pretreatment before the reactions. A pair of self-assembling ligase ribozymes, each of which can form multiple conformations, demonstrated that thermotolerance was acquired and accumulated through complex-formation that stabilized the active forms of the bimolecular ribozymes and also cross-ligation that produced the unimolecular ribozymes.

Indexed as

Amino Acid SequenceCatalysisMolecular Sequence DataNucleic Acid ConformationOligonucleotidesPolymorphism, GeneticPromoter Regions, GeneticRNA, CatalyticRNA Ligase (ATP)OligonucleotidesRNA, CatalyticRNA Ligase (ATP)

Identifiers

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.