Evidence map›Paper›PMID 31239351›Full record

ArticleThe Journal of biological chemistry2019

X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate.

Percival Yang-Ting Chen, Alicia A DeColli, Caren L Freel Meyers, Catherine L Drennan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 39 citations in OpenAlex.

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  20. TheFrontiers in plant science · 2021
    Article
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 3 institutions in 1 country.

Percival Yang-Ting ChenDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139.
Alicia A DeColliDepartment of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Caren L Freel MeyersDepartment of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205. Electronic address: cmeyers@jhmi.edu.
Catherine L DrennanDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139; Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139. Electronic address: cdrennan@mit.edu.
Johns Hopkins University · USHoward Hughes Medical Institute · USMassachusetts Institute of Technology · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
PHARMACOLOGY TRAINING GRANTT32GM008763 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FREEL MEYERS, CAREN L. · 2000 to 2019
$6.1M
Metalloenzyme structure, function and assemblyR35GM126982 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI CATHERINE L DRENNAN · 2018 to 2026
$3.4M
Targeting Non-mammalian Isoprenoid BiosynthesisR01GM084998 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FREEL MEYERS, CAREN L. · 2010 to 2019
$3.0M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
NCRR NIH HHS S10 RR029205NIGMS NIH HHS P30 GM124165NIGMS NIH HHS R01 GM084998NIGMS NIH HHS R35 GM126982NIGMS NIH HHS T32 GM008763
6 · The paper itself

Abstract

1-Deoxy-d-xylulose 5-phosphate synthase (DXPS) uses thiamine diphosphate (ThDP) to convert pyruvate and d-glyceraldehyde 3-phosphate (d-GAP) into 1-deoxy-d-xylulose 5-phosphate (DXP), an essential bacterial metabolite. DXP is not utilized by humans; hence, DXPS has been an attractive antibacterial target. Here, we investigate DXPS from

Indexed as

Bacterial ProteinsCrystallography, X-RayDeinococcusGlyceraldehyde 3-PhosphatePentosephosphatesProtein DomainsTransferases1-deoxylulose 5-phosphateBacterial Proteinsdeoxyxylulose-5-phosphate synthaseGlyceraldehyde 3-PhosphatePentosephosphatesTransferases1-deoxy-D-xylulose 5-phosphate synthase (DXPS)bacterial metabolismconformational changeconformational dynamicscrystallographydecarboxylaseDXP synthasemethylerythritol phosphate (MEP) pathwaypyruvatethiamine diphosphate (ThDP)

Identifiers

PMID31239351
PMCPMC6699841
OpenAlexW2953941295

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.