Evidence map›Paper›PMID 38611720›Full record

ArticleMolecules (Basel, Switzerland)2024

Bacterial Chaperone Domain Insertions Convert Human FKBP12 into an Excellent Protein-Folding Catalyst-A Structural and Functional Analysis.

Gabriel Žoldák, Thomas A Knappe, Anne-Juliane Geitner, Christian Scholz, Holger Dobbek, Franz X Schmid, Roman P Jakob

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

Article in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 96% 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

1 citing paper in PubMed, 0 citations in OpenAlex.

  1. 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

7 authors at 5 institutions in 3 countries.

Gabriel ŽoldákCenter for Interdisciplinary Biosciences, Technology and Innovation Park, Pavol Jozef Šafárik University in Košice, 040 11 Kosice, Slovakia.ORCID 0000-0002-5271-8837
Thomas A KnappeLaboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth, 95447 Bayreuth, Germany.
Anne-Juliane GeitnerLaboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth, 95447 Bayreuth, Germany.
Christian ScholzRoche Diagnostics GmbH, Nonnenwald 2, 82377 Penzberg, Germany.
Holger DobbekInstitut für Biologie, Strukturbiologie/Biochemie, Humboldt-Universität zu Berlin, Unter den Linden 6, 10099 Berlin, Germany.
Franz X SchmidLaboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth, 95447 Bayreuth, Germany.
Roman P JakobDepartement Biozentrum, University of Basel, Spitalstrasse 41, 4056 Basel, Switzerland.ORCID 0000-0002-6451-8656
University of Bayreuth · DEHumboldt-Universität zu Berlin · DERoche Pharma AG (Germany) · DEUniversity of Basel · CHUniversity of Pavol Jozef Šafárik · SK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many folding enzymes use separate domains for the binding of substrate proteins and for the catalysis of slow folding reactions such as prolyl isomerization. FKBP12 is a small prolyl isomerase without a chaperone domain. Its folding activity is low, but it could be increased by inserting the chaperone domain from the homolog SlyD of

Indexed as

Escherichia coli ProteinsTacrolimus Binding Protein 1ACatalysisEscherichia coliHumansMolecular ChaperonesPeptidylprolyl IsomeraseEscherichia coli ProteinsMolecular ChaperonesPeptidylprolyl IsomeraseSlyD protein, E coliTacrolimus Binding Protein 1AchaperoneFKBPimmunophilinprolyl isomeraseprotein foldingSlpASlyD

Identifiers

PMID38611720
PMCPMC11013033
OpenAlexW4393158791

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.