Evidence map›Paper›PMID 38213970›Full record

ArticleRSC advances2024

Improving the thermostability and modulating the inulin profile of inulosucrase through rational glycine-to-proline substitution.

Thanapon Charoenwongpaiboon, Nawapat Sommanat, Karan Wangpaiboon, Manatsanan Puangpathanachai, Piamsook Pongsawasdi, Rath Pichyangkura

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
2.8field-weighted citation impact, top 11% 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

0 citing papers in PubMed, 9 citations in OpenAlex.

No citing paper in PubMed yet.

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 2 institutions in 1 country.

Thanapon CharoenwongpaiboonDepartment of Chemistry, Faculty of Science, Silpakorn University Nakhon Pathom 73000 Thailand charoenwongpaib_t@su.ac.th.ORCID https://orcid.org/0000-0001-9322-0261
Nawapat SommanatDepartment of Chemistry, Faculty of Science, Silpakorn University Nakhon Pathom 73000 Thailand charoenwongpaib_t@su.ac.th.
Karan WangpaiboonDepartment of Biochemistry, Faculty of Science, Chulalongkorn University Bangkok 10330 Thailand.
Manatsanan PuangpathanachaiDepartment of Biochemistry, Faculty of Science, Chulalongkorn University Bangkok 10330 Thailand.
Piamsook PongsawasdiDepartment of Biochemistry, Faculty of Science, Chulalongkorn University Bangkok 10330 Thailand.
Rath PichyangkuraDepartment of Biochemistry, Faculty of Science, Chulalongkorn University Bangkok 10330 Thailand.
Chulalongkorn University · THSilpakorn University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The flexibility of protein structure plays a crucial role in enzyme stability and catalysis. Among the amino acids, glycine is particularly important in conferring flexibility to proteins. In this study, the effects of flexible glycine residues in

Identifiers

PMID38213970
PMCPMC10782431
OpenAlexW4390794945

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.