Evidence map›Paper›PMID 36494361›Full record

ArticleNature communications2022

Allosteric rescue of catalytically impaired ATP phosphoribosyltransferase variants links protein dynamics to active-site electrostatic preorganisation.

Gemma Fisher, Marina Corbella, Magnus S Alphey, John Nicholson, Benjamin J Read, Shina C L Kamerlin, Rafael G da Silva

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. 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
1.6field-weighted citation impact, top 17% 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, 19 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

7 authors at 2 institutions in 3 countries.

Gemma FisherSchool of Biology, Biomedical Sciences Research Complex, University of St Andrews, St Andrews, KY16 9ST, UK.
Marina CorbellaScience for Life Laboratory, Department of Chemistry - BMC, Uppsala University, S-751 23, Uppsala, Sweden.ORCID http://orcid.org/0000-0001-9209-868X
Magnus S AlpheySchool of Biology, Biomedical Sciences Research Complex, University of St Andrews, St Andrews, KY16 9ST, UK.
John NicholsonSchool of Biology, Biomedical Sciences Research Complex, University of St Andrews, St Andrews, KY16 9ST, UK.
Benjamin J ReadSchool of Biology, Biomedical Sciences Research Complex, University of St Andrews, St Andrews, KY16 9ST, UK.
Shina C L KamerlinScience for Life Laboratory, Department of Chemistry - BMC, Uppsala University, S-751 23, Uppsala, Sweden. lynn.kamerlin@kemi.uu.se.ORCID http://orcid.org/0000-0002-3190-1173
Rafael G da SilvaSchool of Biology, Biomedical Sciences Research Complex, University of St Andrews, St Andrews, KY16 9ST, UK. rgds@st-andrews.ac.uk.ORCID http://orcid.org/0000-0002-1308-8190
University of St Andrews · GBUppsala University · SE

Funding

Knut och Alice Wallenbergs Stiftelse (Knut and Alice Wallenberg Foundation) 2018.0140Knut och Alice Wallenbergs Stiftelse (Knut and Alice Wallenberg Foundation) 2019.0431RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/M010996/1Stiftelsen Olle Engkvist Byggmästare 190-0335
6 · The paper itself

Abstract

ATP phosphoribosyltransferase catalyses the first step of histidine biosynthesis and is controlled via a complex allosteric mechanism where the regulatory protein HisZ enhances catalysis by the catalytic protein HisG

Indexed as

ATP PhosphoribosyltransferaseAllosteric RegulationCatalytic DomainHistidineATP PhosphoribosyltransferaseHistidine

Identifiers

PMID36494361
PMCPMC9734150
OpenAlexW4311676694

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.