Evidence map›Paper›PMID 33918749›Full record

ArticleInternational journal of molecular sciences2021

Room-Temperature Structure of Xylitol-Bound Glucose Isomerase by Serial Crystallography: Xylitol Binding in the M1 Site Induces Release of Metal Bound in the M2 Site.

Ki Hyun Nam

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

11 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The metal cofactor: stationary or mobile?Applied microbiology and biotechnology · 2024
    Review
  5. Article
  6. Article
  7. Molecular Dynamics-From Macromolecule to Small Molecules.International journal of molecular sciences · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. 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

1 author at 1 institution in 1 country.

Ki Hyun NamDepartment of Life Science, Pohang University of Science and Technology, Pohang 37673, Korea.ORCID 0000-0003-3268-354X
Pohang University of Science and Technology · KR

Funding

National Research Foundation of Korea 2017M3A9F6029736National Research Foundation of Korea 2017R1D1A1B03033087
6 · The paper itself

Abstract

Glucose isomerase (GI) is an important enzyme that is widely used in industrial applications, such as in the production of high-fructose corn syrup or bioethanol. Studying inhibitor effects on GI is important to deciphering GI-specific molecular functions, as well as potential industrial applications. Analysis of the existing xylitol-bound GI structure revealed low metal occupancy at the M2 site; however, it remains unknown why this phenomenon occurs. This study reports the room-temperature structures of native and xylitol-bound GI from

Indexed as

Models, MolecularProtein ConformationAldose-Ketose IsomerasesBinding SitesCrystallography, X-RayMetalsProtein BindingStructure-Activity RelationshipTemperatureXylitolAldose-Ketose IsomerasesMetalsXylitolxylose isomeraseglucose isomeraseinhibitormetal bindingmetal coordinationroom-temperature structureserial crystallographyxylitolxylose isomerase

Identifiers

PMID33918749
PMCPMC8070043
OpenAlexW3153182665

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.