Evidence map›Paper›PMID 32758356›Full record

ArticleeLife2020

How to measure and evaluate binding affinities.

Inga Jarmoskaite, Ishraq AlSadhan, Pavanapuresan P Vaidyanathan, Daniel Herschlag

Abstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 294 papers.

0numbers the graph read from it
0cells of the map it votes in
294citing 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

294 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
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  5. Article
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  7. Article
  8. Protein-Ratio Rheostats: Integrating Stoichiometry, Abundance, and Binding Affinity in Cellular Function.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
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  16. Amplicon/Protein Bead Display enables quantitativebioRxiv : the preprint server for biology · 2026
    Article
  17. Article
  18. Article
  19. Article
  20. Article

234 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

4 authors.

Inga Jarmoskaite *Department of Biochemistry, Stanford University, Stanford, United States.ORCID https://orcid.org/0000-0001-5847-5867
Ishraq AlSadhan *Department of Biochemistry, Stanford University, Stanford, United States.
Pavanapuresan P Vaidyanathan *Department of Biochemistry, Stanford University, Stanford, United States.
Daniel HerschlagDepartment of Biochemistry, Stanford University, Stanford, United States.ORCID https://orcid.org/0000-0002-4685-1973

Funding

Fundamental Studies of RNA Conformational ThermodynamicsR01GM132899 · NIGMS · STANFORD UNIVERSITY · PI AL-HASHIMI, HASHIM M, HERSCHLAG, DANIEL · 2019 to 2022
$2.7M
NIGMS NIH HHS R01 GM132899NIH HHS R01 GM132899
6 · The paper itself

Abstract

Quantitative measurements of biomolecule associations are central to biological understanding and are needed to build and test predictive and mechanistic models. Given the advances in high-throughput technologies and the projected increase in the availability of binding data, we found it especially timely to evaluate the current standards for performing and reporting binding measurements. A review of 100 studies revealed that in most cases essential controls for establishing the appropriate incubation time and concentration regime were not documented, making it impossible to determine measurement reliability. Moreover, several reported affinities could be concluded to be incorrect, thereby impacting biological interpretations. Given these challenges, we provide a framework for a broad range of researchers to evaluate, teach about, perform, and clearly document high-quality equilibrium binding measurements. We apply this framework and explain underlying fundamental concepts through experimental examples with the RNA-binding protein Puf4.

Indexed as

Protein BindingThermodynamicsCase-Control StudiesKineticsLigandsReproducibility of ResultsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsLigandsPUF4 protein, S cerevisiaeRNA-Binding ProteinsSaccharomyces cerevisiae Proteinsbinding affinitybiochemistrychemical biologydissociation constantkineticsnoneprotein‐ligand interactionRNA binding proteinthermodynamics

Identifiers

PMID32758356
PMCPMC7452723

What OpenQuestion holds

Textmetadata
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.