Evidence map›Paper›PMID 33154157›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Structure of human endo-α-1,2-mannosidase (MANEA), an antiviral host-glycosylation target.

Łukasz F Sobala, Pearl Z Fernandes, Zalihe Hakki, Andrew J Thompson, Jonathon D Howe, Michelle Hill, Nicole Zitzmann, Scott Davies, Zania Stamataki, Terry D Butters and 3 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
1.2field-weighted citation impact, top 22% 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

16 citing papers in PubMed, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.

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  15. Conformational flexibility in the zinc solute-binding protein ZnuA.Acta crystallographica. Section F, Structural biology communications · 2022
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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

13 authors at 4 institutions in 2 countries.

Łukasz F SobalaDepartment of Chemistry, University of York, York YO10 5DD, United Kingdom.ORCID 0000-0002-3807-6452
Pearl Z FernandesSchool of Chemistry, University of Melbourne, Parkville, VIC 3010, Australia.ORCID 0000-0003-3902-8273
Zalihe HakkiSchool of Chemistry, University of Melbourne, Parkville, VIC 3010, Australia.ORCID 0000-0001-9415-7890
Andrew J ThompsonDepartment of Chemistry, University of York, York YO10 5DD, United Kingdom.
Jonathon D HoweOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.ORCID 0000-0002-0496-0573
Michelle HillOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
Nicole ZitzmannOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.ORCID 0000-0003-1969-4949
Scott DaviesInstitute for Immunology and Immunotherapy, University of Birmingham, Birmingham B15 2TT, United Kingdom.ORCID 0000-0001-6899-1339
Zania StamatakiInstitute for Immunology and Immunotherapy, University of Birmingham, Birmingham B15 2TT, United Kingdom.ORCID 0000-0003-3823-4497
Terry D ButtersOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.ORCID 0000-0002-5335-3761
Dominic S AlonziOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.ORCID 0000-0002-1330-9109
Spencer J WilliamsSchool of Chemistry, University of Melbourne, Parkville, VIC 3010, Australia; sjwill@unimelb.edu.au gideon.davies@york.ac.uk.ORCID 0000-0001-6341-4364
Gideon J DaviesDepartment of Chemistry, University of York, York YO10 5DD, United Kingdom; sjwill@unimelb.edu.au gideon.davies@york.ac.uk.ORCID 0000-0002-7343-776X
University of Oxford · GBThe University of Melbourne · AUUniversity of York · GBUniversity of Birmingham · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mammalian protein N-linked glycosylation is critical for glycoprotein folding, quality control, trafficking, recognition, and function. N-linked glycans are synthesized from Glc

Indexed as

AnimalsAntiviral AgentsBovine Virus Diarrhea-Mucosal DiseaseCattleCell LineDengue VirusDogsGlucosidasesGlycosylationHumansMadin Darby Canine Kidney CellsMannosidasesPolysaccharidesSecretory PathwayAntiviral AgentsGlucosidasesMannosidasesPolysaccharidesantiviralenzymeglycosylationsecretory pathwaystructural biology

Identifiers

PMID33154157
PMCPMC7703563
OpenAlexW3094331125

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.