Evidence map›Paper›PMID 38322727›Full record

ArticleJournal of applied crystallography2024

Using XAS to monitor radiation damage in real time and post-analysis, and investigation of systematic errors of fluorescence XAS for Cu-bound amyloid-β.

Ruwini S K Ekanayake, Victor A Streltsov, Stephen P Best, Christopher T Chantler

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of applied crystallography, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

4 authors.

Ruwini S K EkanayakeSchool of Physics, University of Melbourne, Australia.ORCID https://orcid.org/0000-0002-5255-1969
Victor A StreltsovSchool of Physics, University of Melbourne, Australia.ORCID https://orcid.org/0000-0002-7846-4396
Stephen P BestSchool of Chemistry, University of Melbourne, Australia.ORCID https://orcid.org/0000-0002-9399-3560
Christopher T ChantlerSchool of Physics, University of Melbourne, Australia.ORCID https://orcid.org/0000-0001-6608-0048

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

X-ray absorption spectroscopy (XAS) is a promising technique for determining structural information from sensitive biological samples, but high-accuracy X-ray absorption fine structure (XAFS) requires corrections of systematic errors in experimental data. Low-temperature XAS and room-temperature X-ray absorption spectro-electrochemical (XAS-EC) measurements of N-truncated amyloid-β samples were collected and corrected for systematic effects such as dead time, detector efficiencies, monochromator glitches, self-absorption, radiation damage and noise at higher wavenumber (

Indexed as

dead-time correctionEXAFSextended X-ray absorption fine structureN-truncated amyloid pepidesradiation damageXAS-ECX-ray absorption spectro-electrochemical measurements

Identifiers

PMID38322727
PMCPMC10840304

What OpenQuestion holds

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LicenceCC BY
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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.