Evidence map›Paper›PMID 38256263›Full record

ArticleInternational journal of molecular sciences2024

Targeted Proteomics Reveals Quantitative Differences in Low-Abundance Glycosyltransferases of Patients with Congenital Disorders of Glycosylation.

Roman Sakson, Lars Beedgen, Patrick Bernhard, K Merve Alp, Nicole Lübbehusen, Ralph Röth, Beate Niesler, Marcin Luzarowski, Olga Shevchuk, Matthias P Mayer and 2 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

12 authors at 4 institutions in 1 country.

Roman SaksonZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Alliance, 69120 Heidelberg, Germany.ORCID 0000-0002-9698-0773
Lars BeedgenCenter for Child and Adolescent Medicine, Department Pediatrics I, Heidelberg University, 69120 Heidelberg, Germany.
Patrick BernhardInstitute for Surgical Pathology, Medical Center-University of Freiburg, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany.ORCID 0000-0003-1593-9769
K Merve AlpMax Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), 13125 Berlin, Germany.ORCID 0000-0001-9919-9838
Nicole LübbehusenZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Alliance, 69120 Heidelberg, Germany.
Ralph RöthnCounter Core Facility, Institute of Human Genetics, University Hospital Heidelberg, 69120 Heidelberg, Germany.
Beate NieslernCounter Core Facility, Institute of Human Genetics, University Hospital Heidelberg, 69120 Heidelberg, Germany.
Marcin LuzarowskiZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Alliance, 69120 Heidelberg, Germany.
Olga ShevchukDepartment of Immunodynamics, Institute of Experimental Immunology and Imaging, University Hospital Essen, 45147 Essen, Germany.ORCID 0000-0003-1150-7344
Matthias P MayerZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Alliance, 69120 Heidelberg, Germany.
Christian ThielCenter for Child and Adolescent Medicine, Department Pediatrics I, Heidelberg University, 69120 Heidelberg, Germany.
Thomas RuppertZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Alliance, 69120 Heidelberg, Germany.ORCID 0000-0001-9152-2266
Heidelberg University · DEEssen University Hospital · DEMax Delbrück Center · DEUniversity of Freiburg · DE

Funding

Deutsche Forschungsgemeinschaft RU 747/1-2Deutsche Forschungsgemeinschaft TH1461/7-1
6 · The paper itself

Abstract

Protein glycosylation is an essential post-translational modification in all domains of life. Its impairment in humans can result in severe diseases named congenital disorders of glycosylation (CDGs). Most of the glycosyltransferases (GTs) responsible for proper glycosylation are polytopic membrane proteins that represent challenging targets in proteomics. We established a multiple reaction monitoring (MRM) assay to comprehensively quantify GTs involved in the processes of

Indexed as

Congenital Disorders of GlycosylationGlycosyltransferasesGlycosylationHumansMannosyltransferasesMembrane ProteinsProtein Processing, Post-TranslationalProteomicsALG11 protein, humanGlycosyltransferasesMannosyltransferasesMembrane Proteinscongenital disorders of glycosylationendoplasmic reticulumglycosylationMRMnCounterproteomicsSkyline

Identifiers

PMID38256263
PMCPMC10816918
OpenAlexW4390972373

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.