Evidence map›Paper›PMID 36279447›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

In vitro evolution of ribonucleases from expanded genetic alphabets.

Craig A Jerome, Shuichi Hoshika, Kevin M Bradley, Steven A Benner, Elisa Biondi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.3field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

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  12. Functional Selection of Tau Oligomerization-Inhibiting Aptamers.Angewandte Chemie (International ed. in English) · 2024
    Article
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  20. Construction and Application of DNAzyme-based Nanodevices.Chemical research in Chinese universities · 2023
    Review
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 2 institutions in 1 country.

Craig A JeromeFoundation for Applied Molecular Evolution, Alachua, FL 32615.
Shuichi HoshikaFoundation for Applied Molecular Evolution, Alachua, FL 32615.ORCID 0000-0001-9128-1183
Kevin M BradleyFirebird Biomolecular Sciences, LLC, Alachua, FL 32615.
Steven A BennerFoundation for Applied Molecular Evolution, Alachua, FL 32615.ORCID 0000-0002-3318-9917
Elisa BiondiFoundation for Applied Molecular Evolution, Alachua, FL 32615.ORCID 0000-0002-3660-2607
Firebird Biomolecular Sciences (United States) · USFoundation for Applied Molecular Evolution · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability of nucleic acids to catalyze reactions (as well as store and transmit information) is important for both basic and applied science, the first in the context of molecular evolution and the origin of life and the second for biomedical applications. However, the catalytic power of standard nucleic acids (NAs) assembled from just four nucleotide building blocks is limited when compared with that of proteins. Here, we assess the evolutionary potential of libraries of nucleic acids with six nucleotide building blocks as reservoirs for catalysis. We compare the outcomes of in vitro selection experiments toward RNA-cleavage activity of two nucleic acid libraries: one built from the standard four independently replicable nucleotides and the other from six, with the two added nucleotides coming from an artificially expanded genetic information system (AEGIS). Results from comparative experiments suggest that DNA libraries with increased chemical diversity, higher information density, and larger searchable sequence spaces are one order of magnitude richer reservoirs of molecules that catalyze the cleavage of a phosphodiester bond in RNA than DNA libraries built from a standard four-nucleotide alphabet. Evolved AEGISzymes with nitro-carrying nucleobase Z appear to exploit a general acid-base catalytic mechanism to cleave that bond, analogous to the mechanism of the ribonuclease A family of protein enzymes and heavily modified DNAzymes. The AEGISzyme described here represents a new type of catalysts evolved from libraries built from expanded genetic alphabets.

Indexed as

DNA, CatalyticNucleotidesProteinsRibonuclease, PancreaticRibonucleasesRNADNA, CatalyticNucleotidesProteinsRibonuclease, PancreaticRibonucleasesRNAexpanded genetic alphabetsinformation densityin vitro evolutionRNA-cleaving DNAzymes

Identifiers

PMID36279447
PMCPMC9636917
OpenAlexW4307188379

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.