Evidence map›Paper›PMID 29124191›Full record

ArticleBiochemistry and biophysics reports2015

Characterization of acetohydroxyacid synthase from the hyperthermophilic bacterium

Mohammad S Eram, Benozir Sarafuddin, Frank Gong, Kesen Ma

Open access · goldAbstract read
In one paragraph

Article in Biochemistry and biophysics reports, 2015. 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
0.5field-weighted citation impact, top 35% 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, 7 citations in OpenAlex.

  1. Engineering New-to-Nature Biological Pathways for β,γ-Alkanediol Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Comparative genomics ofFrontiers in microbiology · 2024
    Article
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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

4 authors at 1 institution in 1 country.

Mohammad S EramDepartment of Biology, University of Waterloo, Waterloo, Ontario, Canada.
Benozir SarafuddinDepartment of Biology, University of Waterloo, Waterloo, Ontario, Canada.
Frank GongDepartment of Biology, University of Waterloo, Waterloo, Ontario, Canada.
Kesen MaDepartment of Biology, University of Waterloo, Waterloo, Ontario, Canada.
University of Waterloo · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetohydroxyacid synthase (AHAS) is the key enzyme in branched chain amino acid biosynthesis pathway. The enzyme activity and properties of a highly thermostable AHAS from the hyperthermophilic bacterium

Indexed as

Acetohydroxyacid synthaseAHAS, acetohydroxyacid synthaseBCAA, branched chain amino acidBranched-chain amino acidsCCE, crude cell extractCFE, cell-free extractHTCCE, heat-treated crude cell extractHyperthermophilesIB, inclusion bodyilv, isoleucine, leucine, valineIMAC, immobilized metal affinity chromatographyThermotogalesTmAHAS, Thermotoga maritima acetohydroxyacid synthaseTPP, thiamine pyrophosphate

Identifiers

PMID29124191
PMCPMC5668897
OpenAlexW1166864816

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.