Evidence map›Paper›PMID 40750744›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

Metabolic

Shunli Pan, Noriyoshi Manabe, Yoshiki Yamaguchi

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Shunli PanDivision of Structural Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Medical and Pharmaceutical University, Sendai, Japan.
Noriyoshi ManabeDivision of Structural Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Medical and Pharmaceutical University, Sendai, Japan.
Yoshiki YamaguchiDivision of Structural Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Medical and Pharmaceutical University, Sendai, Japan. yyoshiki@tohoku-mpu.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The atomic description of glycosylated proteins is essential for gaining an understanding of the physiological roles of protein glycosylation. X-ray crystallographic and cryo-EM analyses currently play a central role in the 3D structural determination of biological macromolecules. 3D structural information of glycosylated proteins remains limited due to the weak or absent electron densities of the glycan parts. Solution nuclear magnetic resonance (NMR) analysis is unique in that the conformation and dynamics of the glycan part can be obtained experimentally at atomic resolution. The sensitivity of NMR can be greatly enhanced through

Indexed as

Immunoglobulin AImmunoglobulin Fc FragmentsIsotope LabelingNuclear Magnetic Resonance, BiomolecularCarbon RadioisotopesHumansPolysaccharidesCarbon RadioisotopesImmunoglobulin AImmunoglobulin Fc FragmentsPolysaccharides13C-labelingFcGlycoproteinImmunoglobulin ASite-directed mutagenesisSite-specific assignmentTransient expression

Identifiers

PMID40750744

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.