Evidence map›Paper›PMID 35320522›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Introducing

Mária Raics, István Timári, László Szilágyi, Hans-Joachim Gabius, Katalin E Kövér

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. 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
3.5field-weighted citation impact, top 8% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Exploring Sulfur Sites in Proteins via Triple-ResonanceJournal of the American Chemical Society · 2023
    Article
  2. Article
  3. Pharmaceutics · 2022
    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

5 authors at 2 institutions in 2 countries.

Mária RaicsDepartment of Inorganic and Analytical Chemistry, University of Debrecen, Debrecen, Hungary.
István TimáriDepartment of Inorganic and Analytical Chemistry, University of Debrecen, Debrecen, Hungary.
László SzilágyiDepartment of Organic Chemistry, University of Debrecen, Debrecen, Hungary.
Hans-Joachim GabiusInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Munich, Germany. gabius@tiph.vetmed.uni-muenchen.de.
Katalin E KövérDepartment of Inorganic and Analytical Chemistry, University of Debrecen, Debrecen, Hungary. kover@science.unideb.hu.
University of Debrecen · HULudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Their emerging nature as multifunctional effectors explains the large interest to monitor glycan binding to galectins and to define bound-state conformer(s) of their ligands in solution. Basically, NMR spectroscopy facilitates respective experiments. Towards developing new and even better approaches for these purposes, extending the range of exploitable isotopes beyond

Indexed as

CarbohydratesGalectinsGlycosidesLigandsMagnetic Resonance SpectroscopyCarbohydratesGalectinsGlycosidesLigands77Se NMRGalectinHSQMBCSelenoglycosideThiodigalactoside

Identifiers

PMID35320522
OpenAlexW4221055209

What OpenQuestion holds

Textmetadata
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.