Evidence map›Paper›PMID 29532137›Full record

ArticleEuropean biophysics journal : EBJ2018

Interaction studies of a protein and carbohydrate system using an integrated approach: a case study of the miniagrin-heparin system.

Trushar R Patel, Tabot M D Besong, Markus Meier, Kevin McEleney, Stephen E Harding, Donald J Winzor, Jörg Stetefeld

Abstract read
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In one paragraph

Article in European biophysics journal : EBJ, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 44% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

7 authors at 4 institutions in 3 countries.

Trushar R PatelDepartment of Chemistry and Biochemistry, Alberta RNA Research and Training Institute, University of Lethbridge, 4401 University Drive, Lethbridge, AB, T1K 3M4, Canada. trushar.patel@uleth.ca.ORCID http://orcid.org/0000-0003-0627-2923
Tabot M D BesongNational Centre for Macromolecular Hydrodynamics, University of Nottingham, Sutton Bonington, LE12 5RsD, UK.ORCID http://orcid.org/0000-0002-3572-1428
Markus MeierDepartment of Chemistry, University of Manitoba, Winnipeg, MB, R3T 2N2, Canada.ORCID http://orcid.org/0000-0003-1068-746X
Kevin McEleneyDepartment of Chemistry, University of Manitoba, Winnipeg, MB, R3T 2N2, Canada.
Stephen E HardingNational Centre for Macromolecular Hydrodynamics, University of Nottingham, Sutton Bonington, LE12 5RsD, UK.ORCID http://orcid.org/0000-0002-7798-9692
Donald J WinzorSchool of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, QLD, 4072, Australia.
Jörg StetefeldDepartment of Chemistry, University of Manitoba, Winnipeg, MB, R3T 2N2, Canada. jorg.stetefeld@umanitoba.ca.ORCID http://orcid.org/0000-0003-1478-3248
University of Manitoba · CAUniversity of Nottingham · GBThe University of Queensland · AUUniversity of Lethbridge · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The major challenges in biophysical characterization of human protein-carbohydrate interactions are obtaining monodispersed preparations of human proteins that are often post-translationally modified and lack of detection of carbohydrates by traditional detection systems. Light scattering (dynamic and static) techniques offer detection of biomolecules and their complexes based on their size and shape, and do not rely on chromophore groups (such as aromatic amino acid sidechains). In this study, we utilized dynamic light scattering, analytical ultracentrifugation and small-angle X-ray scattering techniques to investigate the solution properties of a complex resulting from the interaction between a 15 kDa heparin preparation and miniagrin, a miniaturized version of agrin. Results from dynamic light scattering, sedimentation equilibrium, and sedimentation velocity experiments signify the formation of a monodisperse complex with 1:1 stoichiometry, and low-resolution structures derived from the small-angle X-ray scattering measurements implicate an extended conformation for a side-by-side miniagrin‒heparin complex.

Indexed as

AgrinHEK293 CellsHeparinHumansHydrodynamicsModels, MolecularProtein BindingProtein ConformationAgrinHeparinAgrinAnalytical ultracentrifugationDynamic light scatteringHeparinSmall-angle X-ray scattering

Identifiers

PMID29532137
OpenAlexW2794264713

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.