Evidence map›Paper›PMID 29414784›Full record

ArticleThe Journal of biological chemistry2018

Coenzyme M biosynthesis in bacteria involves phosphate elimination by a functionally distinct member of the aspartase/fumarase superfamily.

Sarah E Partovi, Florence Mus, Andrew E Gutknecht, Hunter A Martinez, Brian P Tripet, Bernd Markus Lange, Jennifer L DuBois, John W Peters

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

6 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The pathway for coenzyme M biosynthesis in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. 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

8 authors at 2 institutions in 1 country.

Sarah E PartoviFrom the Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717 and.
Florence Musthe Institute of Biological Chemistry and.
Andrew E GutknechtFrom the Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717 and.
Hunter A MartinezFrom the Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717 and.
Brian P TripetFrom the Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717 and.
Bernd Markus Langethe Institute of Biological Chemistry and.
Jennifer L DuBoisFrom the Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717 and.
John W Petersthe Institute of Biological Chemistry and jw.peters@wsu.edu.
Montana State University · USWashington State University · US

Funding

Research Core (Developmental Research Project Program)P20GM103474 · NIGMS · MONTANA STATE UNIVERSITY - BOZEMAN · PI Jeffrey Good · 2012 to 2026
$60.0M
Acquisition of a 600 MHz NMR cryoprobe and 600 MHz spectrometer console upgradeS10RR026659 · NCRR · MONTANA STATE UNIVERSITY - BOZEMAN · PI COPIE, VALERIE · 2011 to 2011
$600k
NCRR NIH HHS S10 RR026659NIGMS NIH HHS P20 GM103474
6 · The paper itself

Abstract

For nearly 30 years, coenzyme M (CoM) was assumed to be present solely in methanogenic archaea. In the late 1990s, CoM was reported to play a role in bacterial propene metabolism, but no biosynthetic pathway for CoM has yet been identified in bacteria. Here, using bioinformatics and proteomic approaches in the metabolically versatile bacterium

Indexed as

Aspartate Ammonia-LyaseBacteriaComputational BiologyCrystallography, X-RayFumarate HydrataseFumaratesMesnaPhosphatesPhosphoenolpyruvatePhosphoric AcidsPhosphoric Monoester HydrolasesProteomicsPyridoxal PhosphateXanthobacterAspartate Ammonia-LyaseFumarate HydrataseFumaratesMesnaPhosphatesPhosphoenolpyruvatephosphoric acidPhosphoric AcidsPhosphoric Monoester HydrolasesPyridoxal Phosphatebacteriabacterial metabolismbiosynthesiscoenzyme Menzyme purificationMSNMR

Identifiers

PMID29414784
PMCPMC5892593
OpenAlexW2787795052

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.