Evidence map›Paper›PMID 40750740›Full record

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

The Glycoworld: Glycoproteins in Nature: A General Overview of the Different Roles That Glycoproteins Exert in Living Organism.

Maria Pia Lenza, Cristina Di Carluccio, Antonio Molinaro, Alba Silipo, Roberta Marchetti

Abstract readReview
PubMed Publisher
In one paragraph

Review 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. 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

5 authors.

Maria Pia Lenza *Department of Chemical Sciences, University of Naples Federico II, Naples, Italy.
Cristina Di Carluccio *Department of Chemical Sciences, University of Naples Federico II, Naples, Italy.
Antonio MolinaroDepartment of Chemical Sciences, University of Naples Federico II, Naples, Italy.
Alba SilipoDepartment of Chemical Sciences, University of Naples Federico II, Naples, Italy.
Roberta MarchettiDepartment of Chemical Sciences, University of Naples Federico II, Naples, Italy. Roberta.marchetti@unina.it.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation is an important post-translational modification of proteins, lipids and other biomolecules, essential in a plethora of physiopathological processes. It plays a significant role in protein folding, stability, trafficking, and recognition events, impacting cellular communication, immune response, development, and disease progression.The great diversity and heterogeneity of glycans structures, assembled and remodeled by a complex machinery of glycosyltransferases and glycosidases, indeed, encodes several information that is context-dependent due to the cell-specific patterns of glycosylation.In this chapter, we will discuss the protein glycosylation pathway in eukaryotes, procaryotes and viruses. Examples of glycoproteins functions in different species are also reported to highlight the crucial roles of glycans in diverse biological processes in almost all living organisms.

Indexed as

GlycoproteinsAnimalsGlycosylationGlycosyltransferasesHumansPolysaccharidesProtein Processing, Post-TranslationalVirusesGlycoproteinsGlycosyltransferasesPolysaccharidesArchaeaEukaryotesGlycanGlycoconjugatesGlycoproteinsGlycosaminoglycanGlycosylationN-glycanO-glycanProkaryotesProteoglycansVirus

Identifiers

PMID40750740

What Socratic 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 Socratic graph.