Evidence map›Paper›PMID 29150502›Full record

ArticleApplied and environmental microbiology2018

Hyperthermophilic Carbamate Kinase Stability and Anabolic

James E Hennessy, Melissa J Latter, Somayeh Fazelinejad, Amy Philbrook, Daniel M Bartkus, Hye-Kyung Kim, Hideki Onagi, John G Oakeshott, Colin Scott, Apostolos Alissandratos and 1 more

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

Article in Applied and environmental microbiology, 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
0.6field-weighted citation impact, top 33% 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, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Biotechnology of extremely thermophilic archaea.FEMS microbiology reviews · 2018
    Review
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

11 authors at 2 institutions in 1 country.

James E HennessyResearch School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.
Melissa J LatterResearch School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.
Somayeh FazelinejadResearch School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.
Amy PhilbrookResearch School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.
Daniel M BartkusResearch School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.
Hye-Kyung KimResearch School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.
Hideki OnagiResearch School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.
John G OakeshottCSIRO Land and Water, Black Mountain Laboratories, Canberra, Australian Capital Territory, Australia.
Colin ScottCSIRO Land and Water, Black Mountain Laboratories, Canberra, Australian Capital Territory, Australia.
Apostolos AlissandratosResearch School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia Apostolos.Alissandratos@anu.edu.au Chris.Easton@anu.edu.au.ORCID http://orcid.org/0000-0002-0177-3617
Christopher J EastonResearch School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia Apostolos.Alissandratos@anu.edu.au Chris.Easton@anu.edu.au.
Australian National University · AUCSIRO Land and Water · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbamate kinases catalyze the conversion of carbamate to carbamoyl phosphate, which is readily transformed into other compounds. Carbamate forms spontaneously from ammonia and carbon dioxide in aqueous solutions, so the kinases have potential for sequestrative utilization of the latter compounds. Here, we compare seven carbamate kinases from mesophilic, thermophilic, and hyperthermophilic sources. In addition to the known enzymes from

Indexed as

TemperatureAlkaliesAmmoniaAnabolic AgentsCarbamatesCarbamyl PhosphateCatalysisClostridium tetaniEnterococcus faecalisEnzyme StabilityHydrogen-Ion ConcentrationKineticsModels, MolecularPhosphotransferases (Carboxyl Group Acceptor)Protein ConformationPyrococcus furiosusAlkaliesAmmoniaAnabolic Agentscarbamate kinaseCarbamatesCarbamyl PhosphatePhosphotransferases (Carboxyl Group Acceptor)ammoniabioremediationcarbamate kinasecarbamoyl phosphatecarbon dioxidehyperthermophiles

Identifiers

PMID29150502
PMCPMC5772250
OpenAlexW2768514291

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.