Evidence map›Paper›PMID 12889655›Full record

ReviewJournal of inherited metabolic disease2003

Mass spectrometric analysis of glycans in elucidating the pathogenesis of CDG type IIx .

P B Mills, K Mills, N Mian, B G Winchester, P T Clayton

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Journal of inherited metabolic disease, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

9 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. 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

5 authors at 2 institutions in 1 country.

P B MillsBiochemistry, Endocrinology and Metabolism Unit, Institute of Child Health at Great Ormond Street Hospital, University College London, UK.
K Mills
N Mian
B G Winchester
P T Clayton
Great Ormond Street Hospital · GBUniversity College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The majority of secreted or membrane-bound proteins are glycosylated. The glycans attached to glycoproteins can affect a range of physicochemical and biological properties of the glycoprotein and appropriate glycosylation is essential for many normal cellular functions, with aberrant glycosylation often leading to disease. This short review briefly outlines the methodology used to release glycans from proteins and analyse them by mass spectrometry. The technology is illustrated by the description of a rapid and sensitive method for profiling glycoproteins of patients with congenital disorders of glycosylation type II. This methodology can rapidly pinpoint the defective step(s) in the processing pathway of N-linked glycans, thereby focusing the biochemical analyses that need to be performed to define the genetic basis of these diseases.

Indexed as

Congenital Disorders of GlycosylationGlycoproteinsHumansPolysaccharidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationGlycoproteinsPolysaccharides

Identifiers

PMID12889655
OpenAlexW1501242798

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.