Evidence map›Paper›PMID 40421147›Full record

ArticleBiophysics and physicobiology2025

Structure-activity relationship of PET-degrading cutinase regulated by weak Ca

Fumiya Kondo, Narutoshi Kamiya, Gert-Jan Bekker, Satoshi Nagao, Nobutaka Numoto, Hiroshi Sekiguchi, Nobutoshi Ito, Masayuki Oda

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysics and physicobiology, 2025. 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
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.

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.

Fumiya KondoGraduate School of Life and Environmental Sciences, Kyoto Prefectural University, Kyoto 606-8522, Japan.
Narutoshi KamiyaGraduate School of Information Science, University of Hyogo, Kobe, Hyogo 650-0047, Japan.
Gert-Jan BekkerInstitute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.
Satoshi NagaoCenter for Synchrotron Radiation Research, Japan Synchrotron Radiation Research Institute, Hyogo 679-5198, Japan.
Nobutaka NumotoMedical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo, Tokyo 113-8510, Japan.
Hiroshi SekiguchiCenter for Synchrotron Radiation Research, Japan Synchrotron Radiation Research Institute, Hyogo 679-5198, Japan.
Nobutoshi ItoMedical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo, Tokyo 113-8510, Japan.
Masayuki OdaGraduate School of Life and Environmental Sciences, Kyoto Prefectural University, Kyoto 606-8522, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzyme function is often regulated by weak metal-ion binding, which results from conformational changes while maintaining conformational fluctuations. We analyzed the structure and function of cutinase-like enzyme, Cut190, using biophysical methods such as X-ray crystallography and molecular dynamics (MD) simulations, showing that its structure and function are finely regulated by weak Ca

Indexed as

catalytic activityconformational changeenzymemulticanonical molecular dynamics simulationsweak metal-ion binding

Identifiers

PMID40421147
PMCPMC12105869

What OpenQuestion holds

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Registered trials

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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.