Evidence map›Paper›PMID 42522928›Full record

ArticleActa crystallographica. Section D, Structural biology2026

Replacement soaking for human tankyrase 2 enables studies on substrate analogues and inhibitors.

Johan Pääkkönen, Sven T Sowa, Chiara Bosetti, Lari Lehtiö

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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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

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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

4 authors.

Johan PääkkönenFaculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland.ORCID 0000-0002-2772-3327
Sven T SowaFaculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland.ORCID 0000-0001-7411-5925
Chiara BosettiFaculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland.ORCID 0000-0003-3809-7533
Lari LehtiöFaculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland.ORCID 0000-0001-7250-832X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Crystallography has facilitated the development of inhibitors in modern drug discovery. Complex structures are traditionally obtained by co-crystallization or soaking methods, but they are not always successful; co-crystallization may lead to selective crystallization of the apoprotein, and compounds cannot necessarily be soaked into preformed crystals. Successful endeavours in this field include human tankyrases TNKS1 and TNKS2, which are promising drug targets controlling a wide range of signalling events. In the case of TNKS2, apo crystals have a closed conformation in the donor loop, delineating the NAD

Indexed as

Enzyme InhibitorsTankyrasesBinding SitesCrystallizationCrystallography, X-RayHumansModels, MolecularNADProtein ConformationSubstrate SpecificityEnzyme InhibitorsNADTankyrasesTNKS2 protein, humancomplex structuredrug designinhibitorsreplacement soakingtankyrase

Identifiers

PMID42522928
PMCPMC13431646

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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.