Evidence map›Paper›PMID 30082290›Full record

ArticleAntimicrobial agents and chemotherapy2018

Crystal Structures of Penicillin-Binding Protein D2 from Listeria monocytogenes and Structural Basis for Antibiotic Specificity.

Jae-Hee Jeong, Hyung Jin Cha, Yeon-Gil Kim

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.2field-weighted citation impact, top 56% 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

5 citing papers in PubMed, 8 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

3 authors at 2 institutions in 1 country.

Jae-Hee Jeong *Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Republic of Korea.
Hyung Jin Cha *School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.
Yeon-Gil KimPohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Republic of Korea ygkim76@postech.ac.kr.
Pohang University of Science and Technology · KRInstitute for Basic Science · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-Lactam antibiotics that inhibit penicillin-binding proteins (PBPs) have been widely used in the treatment of bacterial infections. However, the molecular basis underlying the different inhibitory potencies of β-lactams against specific PBPs is not fully understood. Here, we present the crystal structures of penicillin-binding protein D2 (PBPD2) from

Indexed as

AmpicillinAnti-Bacterial AgentsBacterial Proteinsbeta-LactamsCefotaximeCefuroximeCrystallography, X-RayHumansListeria monocytogenesPenicillin-Binding ProteinsPenicillin GAmpicillinAnti-Bacterial AgentsBacterial Proteinsbeta-LactamsCefotaximeCefuroximePenicillin-Binding ProteinsPenicillin Gantibioticscrystal structuredd-carboxypeptidaseListeria monocytogenespenicillin-binding protein D2β-lactams

Identifiers

PMID30082290
PMCPMC6125574
OpenAlexW2811561733

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.