Evidence map›Paper›PMID 38505292›Full record

ArticleAngewandte Chemie (Weinheim an der Bergstrasse, Germany)2022

Scaling Catalytic Contributions of Small Self-Cleaving Ribozymes.

Michaela Egger, Raphael Bereiter, Stefan Mair, Ronald Micura

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (Weinheim an der Bergstrasse, Germany), 2022. 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, top 91% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

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

4 authors at 1 institution in 1 country.

Michaela EggerInstitute of Organic Chemistry and Center for Molecular Biosciences University of Innsbruck Innrain 80-82 6020 Innsbruck Austria.
Raphael BereiterInstitute of Organic Chemistry and Center for Molecular Biosciences University of Innsbruck Innrain 80-82 6020 Innsbruck Austria.
Stefan MairInstitute of Organic Chemistry and Center for Molecular Biosciences University of Innsbruck Innrain 80-82 6020 Innsbruck Austria.
Ronald MicuraInstitute of Organic Chemistry and Center for Molecular Biosciences University of Innsbruck Innrain 80-82 6020 Innsbruck Austria.ORCID 0000-0003-2661-6105
Universität Innsbruck · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleolytic ribozymes utilize general acid-base catalysis to perform phosphodiester cleavage. In most ribozyme classes, a conserved active site guanosine is positioned to act as general base, thereby activating the 2'-OH group to attack the scissile phosphate (γ-catalysis). Here, we present an atomic mutagenesis study for the pistol ribozyme class. Strikingly, "general base knockout" by replacement of the guanine N1 atom by carbon results in only 2.7-fold decreased rate. Therefore, the common view that γ-catalysis critically depends on the N1 moiety becomes challenged. For pistol ribozymes we found that γ-catalysis is subordinate in overall catalysis, made up by two other catalytic factors (α and δ). Our approach allows scaling of the different catalytic contributions (α, β, γ, δ) with unprecedented precision and paves the way for a thorough mechanistic understanding of nucleolytic ribozymes with active site guanines.

Indexed as

DeazapurinesOligoribonucleotidesRNA CatalysisRNA ModificationsRNA Solid Phase Synthesis

Identifiers

PMID38505292
PMCPMC10946891
OpenAlexW4293809339

What OpenQuestion holds

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LicenceCC BY
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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.