Evidence map›Paper›PMID 32883811›Full record

ArticleThe Journal of biological chemistry2020

A ribonucleotide reductase from

Markel Martínez-Carranza, Venkateswara Rao Jonna, Daniel Lundin, Margareta Sahlin, Lars-Anders Carlson, Newal Jemal, Martin Högbom, Britt-Marie Sjöberg, Pål Stenmark, Anders Hofer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-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

11 citing papers in PubMed, 21 citations in OpenAlex.

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  10. Radicals in Biology: Your Life Is in Their Hands.Journal of the American Chemical Society · 2021
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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

10 authors at 2 institutions in 1 country.

Markel Martínez-CarranzaDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Venkateswara Rao JonnaDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Daniel LundinDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Margareta SahlinDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Lars-Anders CarlsonDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden; Wallenberg Centre for Molecular Medicine, Umeå University, Umeå, Sweden.
Newal JemalDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Martin HögbomDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Britt-Marie SjöbergDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Pål StenmarkDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden; Department of Experimental Medical Science, Lund University, Lund, Sweden. Electronic address: pal.stenmark@med.lu.se.
Anders HoferDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden. Electronic address: anders.hofer@umu.se.
Stockholm University · SEUmeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribonucleotide reductase (RNR) is a central enzyme for the synthesis of DNA building blocks. Most aerobic organisms, including nearly all eukaryotes, have class I RNRs consisting of R1 and R2 subunits. The catalytic R1 subunit contains an overall activity site that can allosterically turn the enzyme on or off by the binding of ATP or dATP, respectively. The mechanism behind the ability to turn the enzyme off via the R1 subunit involves the formation of different types of R1 oligomers in most studied species and R1-R2 octamers in

Indexed as

Bacterial ProteinsCatalytic DomainClostridium botulinumCrystallography, X-RayDeoxyadenine NucleotidesDimerizationEscherichia coliPhylogenyProtein Structure, QuaternaryRecombinant ProteinsRibonucleotide Reductases2'-deoxyadenosine triphosphateBacterial ProteinsDeoxyadenine NucleotidesRecombinant ProteinsRibonucleotide Reductasesallosteric regulationa-siteClostridium botulinumevolutioninhibition mechanismoligomerizationoverall activity regulationphylogeneticsribonucleotide reductasestructure–function

Identifiers

PMID32883811
PMCPMC7667963
OpenAlexW3082258754

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.