Evidence map›Paper›PMID 27671650›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Tyrosine phosphorylation stimulates activity of human RAD51 recombinase through altered nucleoprotein filament dynamics.

Shyamal Subramanyam, Mohammed Ismail, Ipshita Bhattacharya, Maria Spies

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
3.7field-weighted citation impact, top 7% 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

41 citing papers in PubMed, 1 synthesis or guideline pooled it, 68 citations in OpenAlex.

  1. The Role of c-Abl in Alzheimer's Disease: Guilty or not Guilty?Cellular and molecular neurobiology · 2025
    Pooled it
  2. Article
  3. Article
  4. Targeting the ANGPTL4/NRP1/ABL1/RAD51 axis reverses cisplatin resistance by impairing DNA damage repair in head and neck cancer.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. RAD51AP1 is a versatile RAD51 modulator.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. International journal of oncology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. RAD52 prevents accumulation ofbioRxiv : the preprint server for biology · 2024
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. A Facile Platform to EngineerACS central science · 2022
    Article
  20. Article
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 at 1 institution in 1 country.

Shyamal SubramanyamDepartment of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, IA 52242; Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801.
Mohammed IsmailDepartment of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, IA 52242.
Ipshita BhattacharyaDepartment of Electrical and Computer Engineering, University of Iowa, Iowa City, IA 52242.
Maria SpiesDepartment of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, IA 52242; maria-spies@uiowa.edu.ORCID 0000-0002-7375-8037
University of Iowa · US

Funding

Viral VectorP30CA086862 · NCI · UNIVERSITY OF IOWA · PI Douglas Robert Spitz · 2000 to 2026
$70.0M
Regulation of unwinding and remodeling activities in FeS-DNA helicasesR01GM108617 · NIGMS · UNIVERSITY OF IOWA · PI SPIES, MARIA · 2014 to 2018
$1.6M
NIGMS NIH HHS R01 GM108617
6 · The paper itself

Abstract

The DNA strand exchange protein RAD51 facilitates the central step in homologous recombination, a process fundamentally important for accurate repair of damaged chromosomes, restart of collapsed replication forks, and telomere maintenance. The active form of RAD51 is a nucleoprotein filament that assembles on single-stranded DNA (ssDNA) at the sites of DNA damage. The c-Abl tyrosine kinase and its oncogenic counterpart BCR-ABL fusion kinase phosphorylate human RAD51 on tyrosine residues 54 and 315. We combined biochemical reconstitutions of the DNA strand exchange reactions with total internal reflection fluorescence microscopy to determine how the two phosphorylation events affect the biochemical activities of human RAD51 and properties of the RAD51 nucleoprotein filament. By mimicking RAD51 tyrosine phosphorylation with a nonnatural amino acid, p-carboxymethyl-l-phenylalanine (pCMF), we demonstrated that Y54 phosphorylation enhances the RAD51 recombinase activity by at least two different mechanisms, modifies the RAD51 nucleoprotein filament formation, and allows RAD51 to compete efficiently with ssDNA binding protein RPA. In contrast, Y315 phosphorylation has little effect on the RAD51 activities. Based on our work and previous cellular studies, we propose a mechanism underlying RAD51 activation by c-Abl/BCR-ABL kinases.

Indexed as

Biological MimicryDNADNA-Binding ProteinsDNA, Single-StrandedEnzyme ActivationHomologous RecombinationHumansHydrolysisModels, MolecularMutationNucleoproteinsPhosphorylationPhosphotyrosineProtein ConformationProtein MultimerizationProto-Oncogene Proteins c-ablDNADNA-Binding ProteinsDNA, Single-StrandedNucleoproteinsPhosphotyrosineProto-Oncogene Proteins c-ablRad51 RecombinaseRecombinant Proteinsc-Abl tyrosine kinasehomologous recombinationphosphorylationRAD51 recombinasesingle-molecule total internal reflection fluorescence microscopy

Identifiers

PMID27671650
PMCPMC5068273
OpenAlexW2527218799

What OpenQuestion holds

Textmetadata
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.