Evidence map›Paper›PMID 30683805›Full record

ArticleBioscience reports2019

Characterization of recombinant fructose-1,6-bisphosphatase gene mutations: evidence of inhibition/activation of FBPase protein by gene mutation.

Gemma Topaz, Victor Epiter-Smith, Cristina Robalo, Megan Emad, Vanessa Ford, Jadine Daley, Jennifer Byron, Kimberly A Stieglitz

Abstract read
In one paragraph

Article in Bioscience reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Fructose 1,6-Bioscience reports · 2019
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Gemma TopazBoston University, Biology Department, Boston, MA, U.S.A.
Victor Epiter-SmithRoxbury Community College, STEM Biotechnolgy Division, Roxbury, MA, U.S.A.
Cristina RobaloRoxbury Community College, STEM Biotechnolgy Division, Roxbury, MA, U.S.A.
Megan EmadRoxbury Community College, STEM Biotechnolgy Division, Roxbury, MA, U.S.A.
Vanessa FordRoxbury Community College, STEM Biotechnolgy Division, Roxbury, MA, U.S.A.
Jadine DaleyRoxbury Community College, STEM Biotechnolgy Division, Roxbury, MA, U.S.A.
Jennifer ByronRoxbury Community College, STEM Biotechnolgy Division, Roxbury, MA, U.S.A.
Kimberly A StieglitzRoxbury Community College, STEM Biotechnolgy Division, Roxbury, MA, U.S.A. kastieglitz@rcc.mass.edu.ORCID 0000-0001-6086-3682

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Specific residues of the highly regulated fructose-1,6-bisphosphatase (FBPase) enzyme serve as important contributors to the catalytic activity of the enzyme. Previous clinical studies exploring the genetic basis of hypoglycemia revealed two significant mutations in the coding region of the FBPase gene in patients with hypoglycemia, linking the AMP-binding site to the active site of the enzyme. In the present study, a full kinetic analysis of similar mutants was performed. Kinetic results of mutants Y164A and M177A revealed an approximate two to three-fold decrease in inhibitory constants (

Indexed as

MutationAdenosine MonophosphateAnimalsBinding SitesCatalytic DomainEnzyme ActivationFructose-BisphosphataseHumansMutagenesis, Site-DirectedRecombinant ProteinsSequence AlignmentSwineAdenosine MonophosphateFructose-BisphosphataseRecombinant Proteinsallosteric regulationenzymatic activityhyperglycemiahypoglycemiamutagenesis

Identifiers

PMID30683805
PMCPMC6386767

What OpenQuestion holds

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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.