Evidence map›Paper›PMID 30611426›Full record

ArticleMethods in enzymology2019

The Preparation and Solution NMR Spectroscopy of Human Glycoproteins Is Accessible and Rewarding.

Adam W Barb, Daniel J Falconer, Ganesh P Subedi

Abstract read
In one paragraph

Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. A comprehensive assessment of selective amino acidJournal of biomolecular NMR · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Glycan structures and their interactions with proteins. A NMR view.Current opinion in structural biology · 2020
    Review
  10. Glycans in drug discovery.MedChemComm · 2019
    Review
  11. Review
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.

Adam W BarbRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, United States. Electronic address: abarb@iastate.edu.
Daniel J FalconerRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, United States.
Ganesh P SubediRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, United States.
Iowa State University · US

Funding

Mechanism and engineering of IgG-based monoclonal antibody/receptor interactionsR01GM115489 · NIGMS · UNIVERSITY OF GEORGIA · PI BARB, ADAM WESLEY · 2015 to 2019
$1.4M
NIGMS NIH HHS R01 GM115489
6 · The paper itself

Abstract

The majority of proteins excreted by human cells and borne at the cell surface are modified with carbohydrates. Glycoproteins mediate a wide range of processes and adopt fundamental roles in many diseases. The carbohydrates covalently attached to proteins during maturation in the cell directly impact protein structure and function as integral and indispensable components. However, the ability to study the structure of glycoproteins to high resolution was historically limited by technical barriers including a limited availability of appropriate recombinant protein expression platforms, limited methods to generate compositional homogeneity, and difficulties analyzing glycoprotein composition. Furthermore, glycoproteins and in particular the glycan moieties themselves often exhibit a high degree of conformational heterogeneity. Solution NMR spectroscopy is a powerful tool to study biological macromolecules that is capable of characterizing mobile elements of molecules with atomic-level resolution. Methods to express glycoproteins, incorporate stable isotope labels, and analyze glycoproteins have recently opened new avenues to prepare and investigate glycoproteins. These methods are accessible to many laboratories with experience expressing and purifying proteins from prokaryotic expression hosts.

Indexed as

AcetylgalactosamineCarbohydrate SequenceCell LineChromatography, AffinityGene ExpressionGlycoproteinsGlycosylationHEK293 CellsHumansHydrophobic and Hydrophilic InteractionsImmunoglobulin Fc FragmentsImmunoglobulin GIsotope LabelingNuclear Magnetic Resonance, BiomolecularSerineSpectrometry, Mass, Electrospray IonizationAcetylgalactosamineGlycoproteinsImmunoglobulin Fc FragmentsImmunoglobulin GSerineThreonineGlycan remodelingGlycoprotein expressionGlycosylhydrolaseGlycosyltransferaseHEK293N-glycoproteinO-glycoprotein

Identifiers

PMID30611426
PMCPMC6462349
OpenAlexW2892807821

What OpenQuestion holds

Textmetadata
LicenceTDM
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.