Evidence map›Paper›PMID 28534482›Full record

ArticleNature communications2017

An engineered high affinity Fbs1 carbohydrate binding protein for selective capture of N-glycans and N-glycopeptides.

Minyong Chen, Xiaofeng Shi, Rebecca M Duke, Cristian I Ruse, Nan Dai, Christopher H Taron, James C Samuelson

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 50 citations in OpenAlex.

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  12. Metabolic precision labeling enables selective probing of O-linkedProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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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 1 institution in 1 country.

Minyong ChenNew England Biolabs Inc., 240 County Road, Ipswich, Massachusetts 01938, USA.
Xiaofeng ShiNew England Biolabs Inc., 240 County Road, Ipswich, Massachusetts 01938, USA.
Rebecca M DukeNew England Biolabs Inc., 240 County Road, Ipswich, Massachusetts 01938, USA.
Cristian I RuseNew England Biolabs Inc., 240 County Road, Ipswich, Massachusetts 01938, USA.
Nan DaiNew England Biolabs Inc., 240 County Road, Ipswich, Massachusetts 01938, USA.
Christopher H TaronNew England Biolabs Inc., 240 County Road, Ipswich, Massachusetts 01938, USA.
James C SamuelsonNew England Biolabs Inc., 240 County Road, Ipswich, Massachusetts 01938, USA.
New England Biolabs (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A method for selective and comprehensive enrichment of N-linked glycopeptides was developed to facilitate detection of micro-heterogeneity of N-glycosylation. The method takes advantage of the inherent properties of Fbs1, which functions within the ubiquitin-mediated degradation system to recognize the common core pentasaccharide motif (Man3GlcNAc2) of N-linked glycoproteins. We show that Fbs1 is able to bind diverse types of N-linked glycomolecules; however, wild-type Fbs1 preferentially binds high-mannose-containing glycans. We identified Fbs1 variants through mutagenesis and plasmid display selection, which possess higher affinity and improved recovery of complex N-glycomolecules. In particular, we demonstrate that the Fbs1 GYR variant may be employed for substantially unbiased enrichment of N-linked glycopeptides from human serum. Most importantly, this highly efficient N-glycopeptide enrichment method enables the simultaneous determination of N-glycan composition and N-glycosites with a deeper coverage (compared to lectin enrichment) and improves large-scale N-glycoproteomics studies due to greatly reduced sample complexity.

Indexed as

Cell Cycle ProteinsElectrophoresis, Polyacrylamide GelF-Box ProteinsFetuinsGenetic VariationGlycopeptidesGlycoproteinsGlycosylationHumansImmunoglobulin GLectinsMannoseMutagenesisMutationNerve Tissue ProteinsPlasmidsCell Cycle ProteinsF-Box ProteinsFBXO2 protein, humanFetuinsGlycopeptidesGlycoproteinsImmunoglobulin GLectinsMannoseNerve Tissue ProteinsPolysaccharidesribonuclease BRibonucleasesSaltsTrypsin

Identifiers

PMID28534482
PMCPMC5457524
OpenAlexW2617922043

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.