Evidence map›Paper›PMID 21237304›Full record

ReviewAnalytica chimica acta2011

Methods for measuring aptamer-protein equilibria: a review.

Meng Jing, Michael T Bowser

Abstract readReview
In one paragraph

Review in Analytica chimica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing 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

64 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Kinetic and Thermodynamic Analyses of RNA-Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. Dissociation Constant (KSmall methods · 2025
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. In vitro selection of aptamers and their applications.Nature reviews. Methods primers · 2023
    Article
  20. Article

4 more citing papers are in PubMed but not listed here.

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

2 authors.

Meng JingUniversity of Minnesota, Department of Chemistry, 207 Pleasant St. SE, Minneapolis, MN 55455-0431, USA.
Michael T Bowser

Funding

Microfluidic Selection of AptamersR01GM063533 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI BOWSER, MICHAEL T · 2002 to 2015
$3.7M
NIGMS NIH HHS R01 GM063533NIGMS NIH HHS R01GM063533
6 · The paper itself

Abstract

Aptamers are single stranded DNA or RNA molecules that have been selected using in vitro techniques to bind target molecules with high affinity and selectivity, rivaling antibodies in many ways. In order to use aptamers in research and clinical applications, a thorough understanding of aptamer-target binding is necessary. In this article, we review methods for assessing aptamer-protein binding using separation based techniques such as dialysis, ultrafiltration, gel and capillary electrophoresis, and HPLC; as well as mixture based techniques such as fluorescence intensity and anisotropy, UV-vis absorption and circular dichroism, surface plasmon resonance, and isothermal titration calorimetry. For each method the principle, range of application and important features, such as sample consumption, experimental time and complexity, are summarized and compared.

Indexed as

Aptamers, NucleotideCalorimetryChromatography, High Pressure LiquidCircular DichroismElectrophoresis, CapillaryProtein BindingProteinsSpectrometry, FluorescenceSpectrophotometry, UltravioletSurface Plasmon ResonanceAptamers, NucleotideProteins

Identifiers

PMID21237304
PMCPMC3026478

What OpenQuestion holds

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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.