Evidence map›Paper›PMID 28695855›Full record

ArticleActa crystallographica. Section D, Structural biology2017

1.8 Å resolution crystal structure of the carbapenem intrinsic resistance protein CarF.

Evelyn M Tichy, Steven W Hardwick, Ben F Luisi, George P C Salmond

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 96% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

4 authors at 1 institution in 1 country.

Evelyn M TichyDepartment of Biochemistry, University of Cambridge, Building O, Downing Site, Cambridge CB2 1QW, England.
Steven W HardwickDepartment of Biochemistry, University of Cambridge, Building O, Downing Site, Cambridge CB2 1QW, England.
Ben F LuisiDepartment of Biochemistry, University of Cambridge, Building O, Downing Site, Cambridge CB2 1QW, England.
George P C SalmondDepartment of Biochemistry, University of Cambridge, Building O, Downing Site, Cambridge CB2 1QW, England.
University of Cambridge · GB

Funding

Wellcome Trust 076846Wellcome Trust 200873/Z/16/Z
6 · The paper itself

Abstract

The natural production of the β-lactam antibiotic carbapenem in bacteria involves a group of enzymes that form a synthetic pathway as well as proteins that protect the cell from self-intoxification by the products. Here, the crystal structure of CarF, one of the two proteins that confer resistance to synthesis of the antibiotic in the host organism, is reported. The CarF fold places it within a widely occurring structural family, indicating an ancient structural origin from which the resistance function has been derived.

Indexed as

Amino Acid SequenceBacterial Proteinsbeta-Lactam ResistanceCarbapenemsCrystallography, X-RayHumansModels, MolecularProtein ConformationSerratiaSerratia InfectionsBacterial ProteinsCarbapenemsantibiotic resistancecarbapenemCIR familyCLec domainintrinsic resistance

Identifiers

PMID28695855
PMCPMC7610886
OpenAlexW2708372934

What OpenQuestion holds

Textmetadata
LicenceTDM
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.