Evidence map›Paper›PMID 34958446›Full record

ArticleAMB Express2021

Thermococcus sp. KS-1 PPIase as a fusion partner improving soluble production of aromatic amino acid decarboxylase.

Takashi Koyanagi, Ayumi Hara, Kanako Kobayashi, Yuji Habara, Akira Nakagawa, Hiromichi Minami, Takane Katayama, Norihiko Misawa

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

Article in AMB Express, 2021. 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
–field-weighted citation impact, top 87% 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, 0 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

8 authors at 2 institutions in 1 country.

Takashi KoyanagiDepartment of Food Science, Ishikawa Prefectural University, Nonoichi, Ishikawa, 921-8836, Japan. koyataka@ishikawa-pu.ac.jp.ORCID http://orcid.org/0000-0003-3688-0022
Ayumi HaraDepartment of Food Science, Ishikawa Prefectural University, Nonoichi, Ishikawa, 921-8836, Japan.
Kanako KobayashiDepartment of Food Science, Ishikawa Prefectural University, Nonoichi, Ishikawa, 921-8836, Japan.
Yuji HabaraDepartment of Food Science, Ishikawa Prefectural University, Nonoichi, Ishikawa, 921-8836, Japan.
Akira NakagawaResearch Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa, 921-8836, Japan.
Hiromichi MinamiResearch Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa, 921-8836, Japan.
Takane KatayamaGraduate School of Biostudies, Kyoto University, Sakyo-ku, 606-8501, Kyoto, Japan.
Norihiko MisawaResearch Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa, 921-8836, Japan.
Ishikawa Prefectural University · JPKyoto University · JP

Funding

Japan Society for the Promotion of Science Grant-in-Aid for Young Scientists (B) (No. 25870604)
6 · The paper itself

Abstract

Peptidyl-prolyl cis-trans isomerase (PPIase, EC 5.2.1.8) catalyzes the racemization reaction of proline residues on a polypeptide chain. This enzyme is also known to function as a molecular chaperon to stabilize protein conformation during the folding process. In this study, we noted FK506 binding protein (FKBP)-type PPIase from a hyperthemophilic archaeon Thermococcus sp. strain KS-1 (PPIase

Indexed as

Aromatic amino acid decarboxylaseEscherichia coliMolecular chaperonPeptidyl-prolyl cis-trans isomerase (PPIase)Thermococcus sp. strain KS-1

Identifiers

PMID34958446
PMCPMC8712285
OpenAlexW4200491547

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.