Evidence map›Paper›PMID 32978636›Full record

ArticleEuropean biophysics journal : EBJ2020

The lid domain is important, but not essential, for catalysis of Escherichia coli pyruvate kinase.

Elena Sugrue, David Coombes, David Wood, Tong Zhu, Katherine A Donovan, Renwick C J Dobson

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in European biophysics journal : EBJ, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 49% 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

4 citing papers in PubMed, 6 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

6 authors at 3 institutions in 3 countries.

Elena SugrueBiomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.ORCID http://orcid.org/0000-0001-5014-9522
David CoombesBiomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.ORCID http://orcid.org/0000-0001-6384-2617
David WoodBiomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.ORCID http://orcid.org/0000-0002-8275-3510
Tong ZhuBiomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.
Katherine A DonovanBiomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.ORCID http://orcid.org/0000-0002-8539-5106
Renwick C J DobsonBiomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand. renwick.dobson@canterbury.ac.nz.ORCID http://orcid.org/0000-0002-5506-4939
University of Canterbury · NZBiotechnology Institute · USHarvard University · US

Funding

Army Research Office W911NF-11-1-0481Marsden Fund UOC1013
6 · The paper itself

Abstract

Pyruvate kinase catalyses the final step of the glycolytic pathway in central energy metabolism. The monomeric structure comprises three domains: a catalytic TIM-barrel, a regulatory domain involved in allosteric activation, and a lid domain that encloses the substrates. The lid domain is thought to close over the TIM-barrel domain forming contacts with the substrates to promote catalysis and may be involved in stabilising the activated state when the allosteric activator is bound. However, it remains unknown whether the lid domain is essential for pyruvate kinase catalytic or regulatory function. To address this, we removed the lid domain of Escherichia coli pyruvate kinase type 1 (PK

Indexed as

BiocatalysisEscherichia coliKineticsModels, MolecularProtein DomainsProtein EngineeringPyruvate KinasePyruvate KinaseAnalytical ultracentrifugationEnzyme evolutionEnzyme kineticsGlycolysisProtein engineeringPyruvate kinase

Identifiers

PMID32978636
OpenAlexW3089291481

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.