Evidence map›Paper›PMID 35114109›Full record

ArticleCell chemical biology2022

Generation of an anticoagulant aptamer that targets factor V/Va and disrupts the FVa-membrane interaction in normal and COVID-19 patient samples.

Erin E Soule, Haixiang Yu, Lyra Olson, Ibtehaj Naqvi, Shekhar Kumar, Sriram Krishnaswamy, Bruce A Sullenger

Open access · bronzeAbstract read
In one paragraph

Article in Cell chemical biology, 2022. 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
1.6field-weighted citation impact, top 16% 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, 12 citations in OpenAlex.

  1. Advances in aptamer technology for target-based drug discovery.Journal of pharmaceutical analysis · 2026
    Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. 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

7 authors at 3 institutions in 1 country.

Erin E SouleDepartment of Pharmacology & Cancer Biology, Duke University, Durham, NC 27710, USA; Department of Surgery, Duke University Medical Center, Durham, NC 27710, USA.
Haixiang YuDepartment of Surgery, Duke University Medical Center, Durham, NC 27710, USA.
Lyra OlsonDepartment of Pharmacology & Cancer Biology, Duke University, Durham, NC 27710, USA; Department of Surgery, Duke University Medical Center, Durham, NC 27710, USA.
Ibtehaj NaqviDepartment of Surgery, Duke University Medical Center, Durham, NC 27710, USA.
Shekhar KumarThe Children's Hospital of Philadelphia, Division of Hematology, Department of Pediatrics, The University of Pennsylvania, Perelman School of Medicine, Philadelphia, PA 19104, USA.
Sriram KrishnaswamyThe Children's Hospital of Philadelphia, Division of Hematology, Department of Pediatrics, The University of Pennsylvania, Perelman School of Medicine, Philadelphia, PA 19104, USA.
Bruce A SullengerDepartment of Pharmacology & Cancer Biology, Duke University, Durham, NC 27710, USA; Department of Surgery, Duke University Medical Center, Durham, NC 27710, USA. Electronic address: bruce.sullenger@duke.edu.
Duke University · USChildren's Hospital of Philadelphia · USDuke Medical Center · US

Funding

Translating Mechanistic Insights into Intrinsic Xase FunctionP01HL139420 · NHLBI · CHILDREN'S HOSP OF PHILADELPHIA · PI Sriram Krishnaswamy · 2018 to 2026
$22.4M
Medical Scientist Training Program Training GrantT32GM145449 · NIGMS · DUKE UNIVERSITY · PI Christopher D Kontos · 2022 to 2026
$6.6M
NHLBI NIH HHS P01 HL139420NIGMS NIH HHS T32 GM145449
6 · The paper itself

Abstract

Coagulation cofactors profoundly regulate hemostasis and are appealing targets for anticoagulants. However, targeting such proteins has been challenging because they lack an active site. To address this, we isolate an RNA aptamer termed T18.3 that binds to both factor V (FV) and FVa with nanomolar affinity and demonstrates clinically relevant anticoagulant activity in both plasma and whole blood. The aptamer also shows synergy with low molecular weight heparin and delivers potent anticoagulation in plasma collected from patients with coronavirus disease 2019 (COVID-19). Moreover, the aptamer's anticoagulant activity can be rapidly and efficiently reversed using protamine sulfate, which potentially allows fine-tuning of aptamer's activity post-administration. We further show that the aptamer achieves its anticoagulant activity by abrogating FV/FVa interactions with phospholipid membranes. Our success in generating an anticoagulant aptamer targeting FV/Va demonstrates the feasibility of using cofactor-binding aptamers as therapeutic protein inhibitors and reveals an unconventional working mechanism of an aptamer by interrupting protein-membrane interactions.

Indexed as

Amino Acid SequenceAnticoagulantsAptamers, NucleotideBase PairingBinding SitesBlood CoagulationCell MembraneCOVID-19COVID-19 Drug TreatmentFactor VFactor VaHeparin, Low-Molecular-WeightHumansImmune SeraModels, MolecularNucleic Acid ConformationAnticoagulantsAptamers, NucleotideFactor VFactor VaHeparin, Low-Molecular-WeightImmune SeraProtaminesanticoagulantaptamerCOVID-19factor V/Vaprotein inhibitorprotein-membrane interactionthrombosis

Identifiers

PMID35114109
PMCPMC8808741
OpenAlexW4210497525

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.