Evidence map›Paper›PMID 39569159›Full record

ArticleACS catalysis2024

Keeping the Distance: Activity Control in Solid-Supported Sucrose Phosphorylase by a Rigid α-Helical Linker of Tunable Spacer Length.

Chao Zhong, Anisha Vyas, Jakob D H Liu, Chris Oostenbrink, Bernd Nidetzky

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS catalysis, 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
–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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

5 authors.

Chao ZhongInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Petersgasse 12, Graz 8010, Austria.
Anisha VyasInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Petersgasse 12, Graz 8010, Austria.
Jakob D H LiuInstitute of Molecular Modeling and Simulation, University of Natural Resources and Life Sciences (BOKU), Muthgasse 18, Vienna 1190, Austria.
Chris OostenbrinkInstitute of Molecular Modeling and Simulation, University of Natural Resources and Life Sciences (BOKU), Muthgasse 18, Vienna 1190, Austria.ORCID https://orcid.org/0000-0002-4232-2556
Bernd NidetzkyInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Petersgasse 12, Graz 8010, Austria.ORCID https://orcid.org/0000-0002-5030-2643

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzyme immobilization into carrier materials has broad importance in biotechnology, yet understanding the catalysis of enzymes bound to solid surfaces remains challenging. Here, we explore surface effects on the catalysis of sucrose phosphorylase through a fusion protein approach. We immobilize the enzyme via a structurally rigid α-helical linker [EA

Identifiers

PMID39569159
PMCPMC11574764

What OpenQuestion holds

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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.