Evidence map›Paper›PMID 34299586›Full record

ArticleMolecules (Basel, Switzerland)2021

Glycosylation States on Intact Proteins Determined by NMR Spectroscopy.

Audra A Hargett, Aaron M Marcella, Huifeng Yu, Chao Li, Jared Orwenyo, Marcos D Battistel, Lai-Xi Wang, Darón I Freedberg

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

8 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Glycoprotein molecular dynamics analysis: SARS-CoV-2 spike glycoprotein case study.Advances in protein chemistry and structural biology · 2022
    Article
  8. 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

8 authors at 2 institutions in 1 country.

Audra A HargettCenter for Biologics Evaluation and Review, Laboratory of Bacterial Polysaccharides, Food and Drug Administration (FDA), Silver Spring, MD 20993, USA.
Aaron M MarcellaCenter for Biologics Evaluation and Review, Laboratory of Bacterial Polysaccharides, Food and Drug Administration (FDA), Silver Spring, MD 20993, USA.
Huifeng YuCenter for Biologics Evaluation and Review, Laboratory of Bacterial Polysaccharides, Food and Drug Administration (FDA), Silver Spring, MD 20993, USA.
Chao LiDepartment of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA.ORCID 0000-0002-8090-2017
Jared OrwenyoDepartment of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA.
Marcos D BattistelCenter for Biologics Evaluation and Review, Laboratory of Bacterial Polysaccharides, Food and Drug Administration (FDA), Silver Spring, MD 20993, USA.
Lai-Xi WangDepartment of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA.
Darón I FreedbergCenter for Biologics Evaluation and Review, Laboratory of Bacterial Polysaccharides, Food and Drug Administration (FDA), Silver Spring, MD 20993, USA.ORCID 0000-0003-1991-5174
Center for Biologics Evaluation and Research · USUniversity of Maryland, College Park · US

Funding

Covergent Chemoenzymatic Synthesis of Glycopeptides and GlycoproteinsR01GM080374 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI WANG, LAI-XI · 2007 to 2021
$3.9M
NIGMS NIH HHS R01 GM080374
6 · The paper itself

Abstract

Protein glycosylation is important in many organisms for proper protein folding, signaling, cell adhesion, protein-protein interactions, and immune responses. Thus, effectively determining the extent of glycosylation in glycoprotein therapeutics is crucial. Up to now, characterizing protein glycosylation has been carried out mostly by liquid chromatography mass spectrometry (LC-MS), which requires careful sample processing, e.g., glycan removal or protein digestion and glycopeptide enrichment. Herein, we introduce an NMR-based method to better characterize intact glycoproteins in natural abundance. This non-destructive method relies on exploiting differences in nuclear relaxation to suppress the NMR signals of the protein while maintaining glycan signals. Using RNase B Man5 and RNase B Man9, we establish reference spectra that can be used to determine the different glycoforms present in heterogeneously glycosylated commercial RNase B.

Indexed as

Nuclear Magnetic Resonance, BiomolecularGlycoproteinsGlycosylationMannoseRibonucleasesGlycoproteinsMannoseribonuclease BRibonucleasesglycoproteinglycosylated proteinsheteronuclear NMRHSQC-TOCSYnatural abundanceT2 filter

Identifiers

PMID34299586
PMCPMC8303171
OpenAlexW3183231933

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.