Evidence map›Paper›PMID 41042980›Full record

ArticleBiochemistry2025

Exploring Helical Fraying Linked to Dynamics and Catalysis in Adenylate Kinase.

Jonna Mattsson, Chanrith Phoeurk, Léon Schierholz, Ameeq Ul Mushtaq, Jhon Alexander Rodriguez Buitrago, Per Rogne, A Elisabeth Sauer-Eriksson, Magnus Wolf-Watz

Abstract read
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In one paragraph

Article in Biochemistry, 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.

Jonna MattssonDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.
Chanrith PhoeurkDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.
Léon SchierholzDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.
Ameeq Ul MushtaqDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.
Jhon Alexander Rodriguez BuitragoDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.
Per RogneDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.ORCID 0000-0002-3687-9200
A Elisabeth Sauer-ErikssonDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.ORCID 0000-0003-0124-0199
Magnus Wolf-WatzDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.ORCID 0000-0002-9098-7974

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Conformational dynamics is a fundamental aspect of enzymatic catalysis that, for example, can be linked to ligand binding and release, assembly of the active site, and the catalytic mechanism. The essential and metabolic enzyme adenylate kinase (AK) undergoes large-scale conformational changes in response to binding of its substrates ATP and AMP. As such, it has been intensely studied in search of linkages between dynamics and catalysis. For a complex conformational change to occur in a protein, whether it is of an induced fit or conformational selection nature, changes at several hinges are often required. Here, based on a comparative structure-function analysis of AK enzymes from

Indexed as

Adenylate KinaseArchaeal ProteinsAdenosine TriphosphateBiocatalysisCatalysisCatalytic DomainEscherichia coliHumansModels, MolecularProtein ConformationProtein Conformation, alpha-HelicalAdenosine TriphosphateAdenylate KinaseArchaeal Proteins

Identifiers

PMID41042980
PMCPMC12548092

What OpenQuestion holds

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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.