Evidence map›Paper›PMID 18398007›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Molecular assembly for high-performance bivalent nucleic acid inhibitor.

Youngmi Kim, Zehui Cao, Weihong Tan

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
8.0field-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

60 citing papers in PubMed, 190 citations in OpenAlex.

  1. Size-Dependent Ultrasound Activation of Thrombin Catalytic Activity by Mechano-Nanoswitches.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Binding Revisited-Avidity in Cellular Function and Signaling.Frontiers in molecular biosciences · 2020
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. 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

3 authors at 2 institutions in 1 country.

Youngmi KimCenter for Research at the Bio/nano Interface, Department of Chemistry, University of Florida Genetics Institute, Shands Cancer Center, and McKnight Brain Institute, University of Florida, Gainesville, FL 32611-7200, USA.
Zehui Cao
Weihong Tan
University of Florida Health · USStanford University · US

Funding

PathologyU54NS058185 · NINDS · LOVELACE BIOMEDICAL & ENVIRONMENTAL RESEARCH INSTITUTE · PI BOGGS, SUSAN ESTHER · 2006 to 2010
$18.4M
Development of molecular probes for biomedical applicationsR01GM079359 · NIGMS · UNIVERSITY OF FLORIDA · PI TAN, WEIHONG · 2007 to 2016
$2.3M
NIGMS NIH HHS R01 GM079359NINDS NIH HHS U54 NS058185
6 · The paper itself

Abstract

It is theorized that multivalent interaction can result in better affinity and selectivity than monovalent interaction in the design of high-performance ligands. Accordingly, biomolecular engineers are increasingly taking advantage of multivalent interactions to fabricate novel molecular assemblies, resulting in new functions for ligands or enhanced performance of existing ligands. Substantial efforts have been expended in using small molecules or epitopes of antibodies for designing multifunctional or better-performing ligands. However, few attempts to use nucleic acid aptamers as functional domains have been reported. In this study, we explore the design of bivalent nucleic acid ligands by using thrombin and its aptamers as the model by which to evaluate its functions. By assembling two thrombin-binding aptamers with optimized design parameters, this assembly has resulted in the successful development of a nucleic acid-based high-performance bivalent protein inhibitor. Our experimentation proved (i) that the simultaneous binding of two aptamers after linkage achieved 16.6-fold better inhibition efficiency than binding of the monovalent ligand and (ii) that such an improvement originated from changes in the kinetics of the binding interactions, with a k(off) rate approximately 1/50 as fast. In addition, the newly generated aptamer assembly is an excellent anticoagulant reagent when tested with different samples. Because this optimized ligand design offers a simple and noninvasive means of accomplishing higher performance from known functional aptamers, it holds promise as a potent antithrombin agent in the treatment of various diseases related to abnormal thrombin activities.

Indexed as

Drug DesignAntidotesAptamers, NucleotideFluorescence Resonance Energy TransferHumansKineticsProtein BindingAntidotesAptamers, Nucleotidethrombin aptamer

Identifiers

PMID18398007
PMCPMC2311377
OpenAlexW2012130949

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.