Evidence map›Paper›PMID 25291143›Full record

ReviewMolecular therapy. Nucleic acids2014

Nucleic Acid Ligands With Protein-like Side Chains: Modified Aptamers and Their Use as Diagnostic and Therapeutic Agents.

John C Rohloff, Amy D Gelinas, Thale C Jarvis, Urs A Ochsner, Daniel J Schneider, Larry Gold, Nebojsa Janjic

Open access · goldAbstract readReview
In one paragraph

Review in Molecular therapy. Nucleic acids, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 298 papers.

0numbers the graph read from it
0cells of the map it votes in
298citing papers in PubMed
13.8field-weighted citation impact, top 1% 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

298 citing papers in PubMed, 533 citations in OpenAlex.

  1. Trial
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  10. Innovations in Aptamer Technology: SELEX To Intelligent Molecular Engineering and Clinical Translation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  11. Review
  12. Article
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  14. Observational
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238 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

7 authors at 1 institution in 1 country.

John C RohloffSomaLogic, Inc., Boulder, Colorado, USA.
Amy D GelinasSomaLogic, Inc., Boulder, Colorado, USA.
Thale C JarvisSomaLogic, Inc., Boulder, Colorado, USA.
Urs A OchsnerSomaLogic, Inc., Boulder, Colorado, USA.
Daniel J SchneiderSomaLogic, Inc., Boulder, Colorado, USA.
Larry GoldSomaLogic, Inc., Boulder, Colorado, USA.
Nebojsa JanjicSomaLogic, Inc., Boulder, Colorado, USA.
SomaLogic (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Limited chemical diversity of nucleic acid libraries has long been suspected to be a major constraining factor in the overall success of SELEX (Systematic Evolution of Ligands by EXponential enrichment). Despite this constraint, SELEX has enjoyed considerable success over the past quarter of a century as a result of the enormous size of starting libraries and conformational richness of nucleic acids. With judicious introduction of functional groups absent in natural nucleic acids, the "diversity gap" between nucleic acid-based ligands and protein-based ligands can be substantially bridged, to generate a new class of ligands that represent the best of both worlds. We have explored the effect of various functional groups at the 5-position of uracil and found that hydrophobic aromatic side chains have the most profound influence on the success rate of SELEX and allow the identification of ligands with very low dissociation rate constants (named Slow Off-rate Modified Aptamers or SOMAmers). Such modified nucleotides create unique intramolecular motifs and make direct contacts with proteins. Importantly, SOMAmers engage their protein targets with surfaces that have significantly more hydrophobic character compared with conventional aptamers, thereby increasing the range of epitopes that are available for binding. These improvements have enabled us to build a collection of SOMAmers to over 3,000 human proteins encompassing major families such as growth factors, cytokines, enzymes, hormones, and receptors, with additional SOMAmers aimed at pathogen and rodent proteins. Such a large and growing collection of exquisite affinity reagents expands the scope of possible applications in diagnostics and therapeutics.

Identifiers

PMID25291143
PMCPMC4217074
OpenAlexW2066356596

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.