Evidence map›Paper›PMID 32690945›Full record

ArticleNature chemical biology2020

Development of a chemical probe against NUDT15.

Si Min Zhang, Matthieu Desroses, Anna Hagenkort, Nicholas C K Valerie, Daniel Rehling, Megan Carter, Olov Wallner, Tobias Koolmeister, Adam Throup, Ann-Sofie Jemth and 27 more

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

8 citing papers in PubMed, 25 citations in OpenAlex.

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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

37 authors at 8 institutions in 5 countries.

Si Min Zhang *Science for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0001-7763-603X
Matthieu Desroses *Science for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0003-4152-3855
Anna Hagenkort *Science for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Nicholas C K ValerieScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Daniel RehlingDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-8627-3469
Megan CarterDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Olov WallnerScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Tobias KoolmeisterScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Adam ThroupScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Ann-Sofie JemthScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Ingrid AlmlöfScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Olga LosevaScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Thomas LundbäckChemical Biology Consortium Sweden, Science for Life Laboratory, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-8145-7808
Hanna AxelssonChemical Biology Consortium Sweden, Science for Life Laboratory, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0003-2365-1749
Shruti RegmiChemical Biology Consortium Sweden, Science for Life Laboratory, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Antonio SarnoDepartment of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, Trondheim, Norway.
Andreas KrämerInstitute of Pharmaceutical Chemistry, Goethe-University Frankfurt, Frankfurt, Germany.
Linda PudelkoScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Lars BräutigamScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Azita RastiScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Mona GöttmannScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Elisée WiitaScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Juliane KutznerDepartment of Infectious Diseases, University Hospital Heidelberg, Heidelberg, Germany.
Torsten SchallerDepartment of Infectious Diseases, University Hospital Heidelberg, Heidelberg, Germany.ORCID http://orcid.org/0000-0001-9597-4112
Christina KalderénScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Armando Cázares-KörnerScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Brent D G PageScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Rosa KrimpenfortDivision of Translational Medicine and Chemical Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Saeed EshtadDivision of Translational Medicine and Chemical Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0001-6763-4700
Mikael AltunScience for Life Laboratory, Division of Clinical Physiology, Department of Laboratory Medicine, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-6937-6124
Sean G RuddScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-4368-3855
Stefan KnappInstitute of Pharmaceutical Chemistry, Goethe-University Frankfurt, Frankfurt, Germany.ORCID http://orcid.org/0000-0001-5995-6494
Martin ScobieScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Evert J HomanScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Ulrika Warpman BerglundScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-6372-1396
Pål StenmarkDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID http://orcid.org/0000-0003-4777-3417
Thomas HelledayScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden. thomas.helleday@scilifelab.se.
Science for Life Laboratory · SEStockholm University · SEGoethe University Frankfurt · DEHeidelberg University · DEKarolinska Institutet · SEKarolinska University Hospital · SENorwegian University of Science and Technology · NOUniversity of British Columbia · CA

Funding

CIHREuropean Research Council 695376Wellcome Trust 106169Wellcome Trust 106169/ZZ14/Z
6 · The paper itself

Abstract

The NUDIX hydrolase NUDT15 was originally implicated in sanitizing oxidized nucleotides, but was later shown to hydrolyze the active thiopurine metabolites, 6-thio-(d)GTP, thereby dictating the clinical response of this standard-of-care treatment for leukemia and inflammatory diseases. Nonetheless, its physiological roles remain elusive. Here, we sought to develop small-molecule NUDT15 inhibitors to elucidate its biological functions and potentially to improve NUDT15-dependent chemotherapeutics. Lead compound TH1760 demonstrated low-nanomolar biochemical potency through direct and specific binding into the NUDT15 catalytic pocket and engaged cellular NUDT15 in the low-micromolar range. We also employed thiopurine potentiation as a proxy functional readout and demonstrated that TH1760 sensitized cells to 6-thioguanine through enhanced accumulation of 6-thio-(d)GTP in nucleic acids. A biochemically validated, inactive structural analog, TH7285, confirmed that increased thiopurine toxicity takes place via direct NUDT15 inhibition. In conclusion, TH1760 represents the first chemical probe for interrogating NUDT15 biology and potential therapeutic avenues.

Indexed as

Binding SitesCell LineDrug DesignDrug DevelopmentEscherichia coliHumansInorganic PyrophosphataseModels, MolecularNudix HydrolasesProtein BindingProtein ConformationPyrophosphatasesStructure-Activity RelationshipInorganic PyrophosphataseNudix HydrolasesNUDT15 protein, humanPyrophosphatases

Identifiers

PMID32690945
PMCPMC7610571
OpenAlexW3042507802

What OpenQuestion holds

Textmetadata
LicenceTDM
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.