Evidence map›Paper›PMID 27387600›Full record

ArticleJournal of labelled compounds & radiopharmaceuticals2016

A chemical synthesis of a multiply

Wenhui Zhang, Qingfeng Pan, Anthony S Serianni

Abstract read
In one paragraph

Article in Journal of labelled compounds & radiopharmaceuticals, 2016. 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
–field-weighted citation impact
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.

  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

3 authors.

Wenhui ZhangDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, USA.
Qingfeng PanOmicron Biochemicals, Inc., South Bend, IN, USA.
Anthony S SerianniDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, USA.

Funding

NCI NIH HHS HHSN261201500020C
6 · The paper itself

Abstract

As covalent modifiers of proteins, high-mannose N-glycans are important in maintaining protein structure and function in vivo. The conformations of these glycans can be studied by nuclear magnetic resonance spectroscopy using spin-spin couplings (J-couplings; scalar couplings) and other nuclear magnetic resonance parameters that are sensitive to the geometries of their constituent glycosidic linkages and other mobile elements in their structures. These analyses often require

Indexed as

Carbon IsotopesChemistry Techniques, SyntheticIsotope LabelingMannosePolysaccharidesCarbon IsotopesMannosePolysaccharides13C-labelingchemical synthesishexasaccharidehigh-mannose N-glycanNMR

Identifiers

PMID27387600
PMCPMC5177528

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.