Evidence map›Paper›PMID 33998795›Full record

ArticleThe journal of physical chemistry. B2021

Nanomolar Pulse Dipolar EPR Spectroscopy in Proteins: Cu

Katrin Ackermann, Joshua L Wort, Bela E Bode

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
8.0field-weighted citation impact, top 3% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Binding Affinity Determines the Success of Endogenous CuThe journal of physical chemistry letters · 2026
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  16. Pulse dipolar EPR for determining nanomolar binding affinities.Chemical communications (Cambridge, England) · 2022
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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 1 institution in 1 country.

Katrin AckermannEaStChem School of Chemistry, Biomedical Sciences Research Complex, Centre of Magnetic Resonance, University of St Andrews, North Haugh, St Andrews KY16 9ST, Scotland.ORCID 0000-0003-1632-0503
Joshua L WortEaStChem School of Chemistry, Biomedical Sciences Research Complex, Centre of Magnetic Resonance, University of St Andrews, North Haugh, St Andrews KY16 9ST, Scotland.
Bela E BodeEaStChem School of Chemistry, Biomedical Sciences Research Complex, Centre of Magnetic Resonance, University of St Andrews, North Haugh, St Andrews KY16 9ST, Scotland.ORCID 0000-0002-3384-271X
University of St Andrews · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M010996/1Biotechnology and Biological Sciences Research Council BB/R013780/1Wellcome Trust 099149Wellcome Trust 099149/Z/12/ZWellcome Trust 204821Wellcome Trust 204821/Z/16/Z
6 · The paper itself

Abstract

The study of ever more complex biomolecular assemblies implicated in human health and disease is facilitated by a suite of complementary biophysical methods. Pulse dipolar electron paramagnetic resonance spectroscopy (PDS) is a powerful tool that provides highly precise geometric constraints in frozen solutions; however, the drive toward PDS at physiologically relevant sub-μM concentrations is limited by the currently achievable concentration sensitivity. Recently, PDS using a combination of nitroxide- and Cu

Indexed as

Nitrogen OxidesProteinsElectron Spin Resonance SpectroscopyHumansSpin LabelsNitrogen OxidesnitroxylProteinsSpin Labels

Identifiers

PMID33998795
PMCPMC7611071
OpenAlexW3161781161

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.