Evidence map›Paper›PMID 38300345›Full record

ArticleApplied microbiology and biotechnology2024

Functional and structural analysis of a cyclization domain in a cyclic β-1,2-glucan synthase.

Nobukiyo Tanaka, Ryotaro Saito, Kaito Kobayashi, Hiroyuki Nakai, Shogo Kamo, Kouji Kuramochi, Hayao Taguchi, Masahiro Nakajima, Tomoko Masaike

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

Article in Applied microbiology and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. New glycoside hydrolase families of β-1,2-glucanases.Protein science : a publication of the Protein Society · 2025
    Article
  3. Enzymes that catalyze cyclization of β-1,2-glucans.Applied microbiology and biotechnology · 2025
    Review
  4. 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

9 authors at 3 institutions in 1 country.

Nobukiyo TanakaDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan. n_tanaka@rs.tus.ac.jp.ORCID http://orcid.org/0000-0002-1845-5738
Ryotaro SaitoDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan.
Kaito KobayashiArtificial Intelligence Research Center, National Institute of Advanced Industrial Science and Technology (AIST), 2-4-7 Aomi, Koto-Ku, Tokyo, 135-0064, Japan.
Hiroyuki NakaiFaculty of Agriculture, Niigata University, Niigata, 950-2181, Japan.
Shogo KamoDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan.
Kouji KuramochiDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan.
Hayao TaguchiDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan.
Masahiro NakajimaDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan. m-nakajima@rs.tus.ac.jp.ORCID http://orcid.org/0000-0002-3182-0859
Tomoko MasaikeDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan. tmasaike@rs.tus.ac.jp.ORCID http://orcid.org/0000-0003-3290-1893
Tokyo University of Science · JPNational Institute of Advanced Industrial Science and Technology · JPNiigata University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclic β-1,2-glucan synthase (CGS) is a key enzyme in production of cyclic β-1,2-glucans (CβGs) which are involved in bacterial infection or symbiosis to host organisms. Nevertheless, a mechanism of cyclization, the final step in the CGS reaction, has not been fully understood. Here we performed functional and structural analyses of the cyclization domain of CGS alone from Thermoanaerobacter italicus (TiCGS

Indexed as

beta-GlucansGlucansGlycoside HydrolasesCatalysisCyclizationbeta-1,2-glucanbeta-GlucansGlucansGlycoside HydrolasesCyclic β-1,2-glucanGlycoside hydrolase familyTransglycosylationβ-1,2-Glucan

Identifiers

PMID38300345
PMCPMC10834661
OpenAlexW4391448277

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.