Evidence map›Paper›PMID 33889819›Full record

ArticleiScience2021

Aberrant sialylation in a patient with a

Luisa Sturiale, Marie-Cécile Nassogne, Angelo Palmigiano, Angela Messina, Immacolata Speciale, Rosangela Artuso, Gaetano Bertino, Nicole Revencu, Xavier Stephénne, Cristina De Castro and 4 more

Open access · goldAbstract read
In one paragraph

Article in iScience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

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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

14 authors at 6 institutions in 2 countries.

Luisa SturialeCNR, Institute for Polymers, Composites and Biomaterials, IPCB, 95126 Catania, Italy.
Marie-Cécile NassognePediatric Neurology Unit, Cliniques Universitaires Saint-Luc, Université Catholique de Louvain, 1200 Brussels, Belgium.
Angelo PalmigianoCNR, Institute for Polymers, Composites and Biomaterials, IPCB, 95126 Catania, Italy.
Angela MessinaCNR, Institute for Polymers, Composites and Biomaterials, IPCB, 95126 Catania, Italy.
Immacolata SpecialeDepartment of Chemical Sciences, University of Naples Federico II, 80100 Naples, Italy.
Rosangela ArtusoMedical Genetics Unit, Meyer Children's University Hospital, 50100 Florence, Italy.
Gaetano BertinoHepatology Unit, A.O.U. Policlinico-Vittorio Emanuele, Department of Clinical and Experimental Medicine, University of Catania, 95100 Catania, Italy.
Nicole RevencuCenter for Human Genetics, Cliniques Universitaires Saint-Luc, Université Catholique de Louvain, 1200 Brussels, Belgium.
Xavier StephénneService de Gastro-Entérologie et Hépatologie Pédiatrique, Cliniques Universitaires Saint-Luc, Université Catholique de Louvain, 1200 Brussels, Belgium.
Cristina De CastroDepartment of Agricultural Sciences, University of Naples Federico II, 80055 Portici, Italy.
Gert MatthijsDepartment of Human Genetics, Laboratory for Molecular Diagnosis, KU Leuven, 3000 Leuven, Belgium.
Rita BaroneCNR, Institute for Polymers, Composites and Biomaterials, IPCB, 95126 Catania, Italy.
Jaak JaekenCenter for Metabolic Diseases, UZ and KU Leuven, 3000 Leuven, Belgium.
Domenico GarozzoCNR, Institute for Polymers, Composites and Biomaterials, IPCB, 95126 Catania, Italy.
Institute of Polymers, Composites and Biomaterials · ITCliniques Universitaires Saint-Luc · BEFederico II University Hospital · ITKU Leuven · BEUniversity of Catania · ITMeyer Children's Hospital · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation is a fundamental post-translational modification of proteins that boosts their structural diversity providing subtle and specialized biological properties and functions. All those genetic diseases due to a defective glycan biosynthesis and attachment to the nascent glycoproteins fall within the wide area of congenital disorders of glycosylation (CDG), mostly causing multisystem involvement. In the present paper, we detailed the unique serum N-glycosylation of a CDG-candidate patient with an unexplained neurological phenotype and liver adenomatosis harboring a recurrent pathogenic

Indexed as

Biological SciencesGlycomicsProteomics

Identifiers

PMID33889819
PMCPMC8050382
OpenAlexW3136937303

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.