Evidence map›Paper›PMID 29124141›Full record

ArticleBiochemistry and biophysics reports2015

A novel binding of GTP stabilizes the structure and modulates the activities of human phosphoglucose isomerase/autocrine motility factor.

Hua-Yang Lin, Jyung-Hurng Liu, Ka-Lik Cheng, Jia-Yun Lin, Ni-Rung Liu, Menghsiao Meng

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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 42% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

6 authors at 1 institution in 1 country.

Hua-Yang LinGraduate Institute of Biotechnology, National Chung Hsing University (NCHU), 250 Kuo-Kuang Road, Taichung, Taiwan 40227.
Jyung-Hurng LiuGraduate Institute of Genomics and Bioinformatics, NCHU, Taichung, Taiwan 40227.
Ka-Lik ChengGraduate Institute of Biotechnology, National Chung Hsing University (NCHU), 250 Kuo-Kuang Road, Taichung, Taiwan 40227.
Jia-Yun LinGraduate Institute of Biotechnology, National Chung Hsing University (NCHU), 250 Kuo-Kuang Road, Taichung, Taiwan 40227.
Ni-Rung LiuGraduate Institute of Biotechnology, National Chung Hsing University (NCHU), 250 Kuo-Kuang Road, Taichung, Taiwan 40227.
Menghsiao MengGraduate Institute of Biotechnology, National Chung Hsing University (NCHU), 250 Kuo-Kuang Road, Taichung, Taiwan 40227.
National Chung Hsing University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphoglucose isomerase (PGI) catalyzes the interconversion between glucose 6-phosphate and fructose 6-phosphate in the glycolysis pathway. In mammals, the enzyme is also identical to the extracellular proteins neuroleukin, tumor-secreted autocrine motility factor (AMF) and differentiation and maturation mediator for myeloid leukemia. Hereditary deficiency of the enzyme causes non-spherocytic hemolytic anemia in human. In the present study, a novel interaction between GTP and human PGI was corroborated by UV-induced crosslinking, affinity purification and kinetic study. GTP not only inhibits the isomerization activity but also compromises the AMF function of the enzyme. Kinetic studies, including the Yonetani-Theorell method, suggest that GTP is a competitive inhibitor with a

Indexed as

Autocrine motility factorGlucose-6-phosphate isomeraseGTPInhibition kineticsPhosphoglucose isomerase

Identifiers

PMID29124141
PMCPMC5668625
OpenAlexW2017308641

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.