Evidence map›Paper›PMID 36327799›Full record

ReviewDNA repair2022

A moving target for drug discovery: Structure activity relationship and many genome (de)stabilizing functions of the RAD52 protein.

Divya S Bhat, M Ashley Spies, Maria Spies

Abstract readReview
In one paragraph

Review in DNA repair, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Dynamic Assemblies in Genome Maintenance.Advances in experimental medicine and biology · 2026
    Review
  5. RAD52's active form is not a ring.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. 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

3 authors.

Divya S BhatDepartment of Biochemistry, University of Iowa Carver College of Medicine, 51 Newton Road, Iowa City, IA 52242, USA.
M Ashley SpiesDepartment of Biochemistry, University of Iowa Carver College of Medicine, 51 Newton Road, Iowa City, IA 52242, USA; Division of Medicinal and Natural Products Chemistry, Department of Pharmaceutical Sciences and Experimental Therapeutics, The University of Iowa, Iowa City, Iowa 52242, USA.
Maria SpiesDepartment of Biochemistry, University of Iowa Carver College of Medicine, 51 Newton Road, Iowa City, IA 52242, USA. Electronic address: maria-spies@uiowa.edu.

Funding

Assembly and Dynamics of Molecular Machines in Genome MaintenanceR35GM131704 · NIGMS · UNIVERSITY OF IOWA · PI Maria Spies · 2019 to 2026
$3.9M
PREDOCTORAL TRAINING PROGRAM IN BIOTECHNOLOGYT32GM008365 · NIGMS · UNIVERSITY OF IOWA · PI KERNS, ROBERT JOHN · 1990 to 2021
$3.8M
The Role of Human RAD52 Protein in Genome StabilityR01CA232425 · NCI · UNIVERSITY OF IOWA · PI Maria Spies · 2019 to 2026
$3.1M
Dialing down caspase-7 through allosteric control: An integrated approachR01GM138471 · NIGMS · UNIVERSITY OF IOWA · PI SPIES, MICHAEL ASHLEY · 2020 to 2023
$1.2M
NCI NIH HHS R01 CA232425NIGMS NIH HHS R01 GM138471NIGMS NIH HHS R35 GM131704NIGMS NIH HHS T32 GM008365
6 · The paper itself

Abstract

BRCA-ness phenotype, a signature of many breast and ovarian cancers, manifests as deficiency in homologous recombination, and as defects in protection and repair of damaged DNA replication forks. A dependence of such cancers on DNA repair factors less important for survival of BRCA-proficient cells, offers opportunities for development of novel chemotherapeutic interventions. The first drugs targeting BRCA-deficient cancers, poly-ADP-ribose polymerase (PARP) inhibitors have been approved for the treatment of advanced, chemotherapy resistant cancers in patients with BRCA1/2 germline mutations. Nine additional proteins that can be targeted to selectively kill BRCA-deficient cancer cells have been identified. Among them, a DNA repair protein RAD52 is an especially attractive target due to general tolerance of the RAD52 loss of function, and protective role of an inactivating mutation. Yet, the effective pharmacological inhibitors of RAD52 have not been forthcoming. In this review, we discuss advances in the state of our knowledge of the RAD52 structure, activities and cellular functions, with a specific focus on the features that make RAD52 an attractive, but difficult drug target.

Indexed as

BRCA2 ProteinOvarian NeoplasmsBRCA1 ProteinDNA RepairDrug DiscoveryFemaleHumansRad52 DNA Repair and Recombination ProteinStructure-Activity RelationshipBRCA1 ProteinBRCA2 ProteinRad52 DNA Repair and Recombination ProteinRAD52 protein, humanBRCA1BRCA2DNA double strand break repairHomologous recombinationPharmacological inhibition of protein-DNA interactionsRAD52Synthetic lethality in cancer

Identifiers

PMID36327799
PMCPMC9888176

What OpenQuestion holds

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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.