Evidence map›Paper›PMID 38505507›Full record

ArticleCatalysis science & technology2024

Using BpyAla to generate copper artificial metalloenzymes: a catalytic and structural study.

E Klemencic, R C Brewster, H S Ali, J M Richardson, A G Jarvis

Open access · hybridAbstract read
In one paragraph

Article in Catalysis science & technology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

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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

5 authors at 2 institutions in 2 countries.

E KlemencicEaStCHEM School of Chemistry, University of Edinburgh Joseph Black Building David Brewster Road The King's Buildings Edinburgh EH9 3FJ UK amanda.jarvis@ed.ac.uk.ORCID https://orcid.org/0000-0002-0778-1589
R C BrewsterEaStCHEM School of Chemistry, University of Edinburgh Joseph Black Building David Brewster Road The King's Buildings Edinburgh EH9 3FJ UK amanda.jarvis@ed.ac.uk.ORCID https://orcid.org/0000-0002-3932-9570
H S AliEaStCHEM School of Chemistry, University of Edinburgh Joseph Black Building David Brewster Road The King's Buildings Edinburgh EH9 3FJ UK amanda.jarvis@ed.ac.uk.ORCID https://orcid.org/0000-0001-5770-5376
J M RichardsonSchool of Biological Sciences, University of Edinburgh Swann Building Edinburgh EH9 3BF UK.ORCID https://orcid.org/0000-0002-1547-3009
A G JarvisEaStCHEM School of Chemistry, University of Edinburgh Joseph Black Building David Brewster Road The King's Buildings Edinburgh EH9 3FJ UK amanda.jarvis@ed.ac.uk.ORCID https://orcid.org/0000-0002-6414-0497
University of Edinburgh · GBMansfield University · US

Funding

Medical Research Council MR/S017402/1
6 · The paper itself

Abstract

Artificial metalloenzymes (ArMs) have emerged as a promising avenue in the field of biocatalysis, offering new reactivity. However, their design remains challenging due to the limited understanding of their protein dynamics and how the introduced cofactors alter the protein scaffold structure. Here we present the structures and catalytic activity of novel copper ArMs capable of (

Identifiers

PMID38505507
PMCPMC10946309
OpenAlexW4391332029

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.