Evidence map›Paper›PMID 40294343›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2025

Organocatalytic Switches of DNA Glycosylase OGG1 Catalyze a Highly Efficient AP-Lyase Function.

Mario Kehler, Kaixin Zhou, Aurino M Kemas, Alicia Del Prado, Emma Scaletti Hutchinson, Elinor Hesslefors Nairn, Marek Varga, Yvonne Plattner, Yi Zhong, Oryn Purewal-Sidhu and 19 more

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2025. 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
–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

8 citing papers in PubMed.

  1. Review
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  8. Review
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

29 authors.

Mario KehlerScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Kaixin ZhouScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Aurino M KemasDepartment of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden.
Alicia Del PradoCentro de Biología Molecular 'Severo Ochoa' (CSIC-UAM), Nicolás Cabrera 1, Cantoblanco, Madrid, Spain.
Emma Scaletti HutchinsonDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Elinor Hesslefors NairnScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Marek VargaScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Yvonne PlattnerDepartment of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden.
Yi ZhongDepartment of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden.
Oryn Purewal-SidhuScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
James HaslamScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Elisée WiitaScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Heather GildieScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Karolina SingerovaScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Zuzanna SzarugaScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Ingrid AlmlöfScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Femke M HormannScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Kang-Cheng LiuCenter for Molecular Medicine, Karolinska Institutet and Karolinska Hospital, Stockholm, Sweden.
Olov WallnerScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Florian OrtisScience 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.
Opher GileadiCenter for Molecular Medicine, Karolinska Institutet and Karolinska Hospital, Stockholm, Sweden.
Sean G RuddScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Pål StenmarkDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Miguel de VegaCentro de Biología Molecular 'Severo Ochoa' (CSIC-UAM), Nicolás Cabrera 1, Cantoblanco, Madrid, Spain.
Thomas HelledayScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Nicholas D D'Arcy-EvansScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Volker M LauschkeDepartment of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden.
Maurice MichelScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.ORCID https://orcid.org/0000-0003-3261-2493

Funding

Åke Wiberg Stiftelse M23-0043Barncancerfonden PR2021-0030Cancerfonden CAN2021/1490Innovative Medicines Initiative 875510Novo Nordisk Fonden NNF23OC0084420Vetenskapsrådet 2022-03681
6 · The paper itself

Abstract

8-oxoGuanine DNA glycosylase 1 (OGG1) is the first known target of organocatalytic switches (ORCAs), which rewrite the biochemical function of the enzyme through redirection of its preferred substrate from 8-oxoG to AP sites. Previously, different ORCA chemotypes were shown to enhance the operational pH window for OGG1, possibly through direct involvement in proton transfer events during DNA strand cleavage. Accordingly, compound pK

Indexed as

DNA-(Apurinic or Apyrimidinic Site) LyaseDNA GlycosylasesPyridinesPyrimidinesCatalysisCatalytic DomainDNAGuanineHumansHydrogen-Ion ConcentrationDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA GlycosylasesGuanineoxoguanine glycosylase 1, humanPyridinesPyrimidinesBase excision repairDNA glycosylaseDNA repairOGG1Organocatalytic switches

Identifiers

PMID40294343
PMCPMC12160960

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.