Evidence map›Paper›PMID 35347133›Full record

ArticleNature communications2022

Structural basis of R-loop recognition by the S9.6 monoclonal antibody.

Charles Bou-Nader, Ankur Bothra, David N Garboczi, Stephen H Leppla, Jinwei Zhang

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

55 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
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  3. NAT10-dependent NCell reports · 2026
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  15. ADAR1 RNA-Editing Enzyme Regulates Telomeric R-Loop Formation.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  16. Article
  17. Article
  18. International journal of molecular sciences · 2025
    Article
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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

5 authors at 2 institutions in 1 country.

Charles Bou-NaderLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD, 20892, USA.ORCID http://orcid.org/0000-0003-0955-0204
Ankur BothraLaboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, MD, 20892, USA.
David N GarbocziStructural Biology Section, Research Technologies Branch, National Institute of Allergy and Infectious Diseases, Bethesda, MD, 20892, USA.
Stephen H LepplaLaboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, MD, 20892, USA. sleppla@niaid.nih.gov.
Jinwei ZhangLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD, 20892, USA. jinwei.zhang@nih.gov.ORCID http://orcid.org/0000-0002-2114-173X
National Institute of Allergy and Infectious Diseases · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Noncoding RNA structures and interactions in cellular stress responses and immunityZIADK075136 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI ZHANG, JINWEI · 2016 to 2025
$23.2M
SARS CoV2 Studies in the Microbial Pathogenesis Section/LPDZIAAI001283 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI LEPPLA, STEPHEN · 2020 to 2024
$536k
Intramural NIH HHS ZIA DK075136
6 · The paper itself

Abstract

R-loops are ubiquitous, dynamic nucleic-acid structures that play fundamental roles in DNA replication and repair, chromatin and transcription regulation, as well as telomere maintenance. The DNA-RNA hybrid-specific S9.6 monoclonal antibody is widely used to map R-loops. Here, we report crystal structures of a S9.6 antigen-binding fragment (Fab) free and bound to a 13-bp hybrid duplex. We demonstrate that S9.6 exhibits robust selectivity in binding hybrids over double-stranded (ds) RNA and in categorically rejecting dsDNA. S9.6 asymmetrically recognizes a compact epitope of two consecutive RNA nucleotides via their 2'-hydroxyl groups and six consecutive DNA nucleotides via their backbone phosphate and deoxyribose groups. Recognition is mediated principally by aromatic and basic residues of the S9.6 heavy chain, which closely track the curvature of the hybrid minor groove. These findings reveal the molecular basis for S9.6 recognition of R-loops, detail its binding specificity, identify a new hybrid-recognition strategy, and provide a framework for S9.6 protein engineering.

Indexed as

Antibodies, MonoclonalR-Loop StructuresDNANucleic Acid ConformationNucleotidesRNARNA, Double-StrandedAntibodies, MonoclonalDNANucleotidesRNARNA, Double-Stranded

Identifiers

PMID35347133
PMCPMC8960830
OpenAlexW4220886629

What OpenQuestion holds

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LicenceCC BY
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.