Evidence map›Paper›PMID 29462882›Full record

ReviewInternational journal of molecular sciences2018

Glycosylation as a Main Regulator of Growth and Death Factor Receptors Signaling.

Inês Gomes Ferreira, Michela Pucci, Giulia Venturi, Nadia Malagolini, Mariella Chiricolo, Fabio Dall'Olio

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

67 citing papers in PubMed, 121 citations in OpenAlex.

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7 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Inês Gomes FerreiraDepartment of Experimental, Diagnostic and Specialty Medicine (DIMES), General Pathology Building, University of Bologna, 40126 Bologna, Italy. ines.gomesferreira@unibo.it.
Michela PucciDepartment of Experimental, Diagnostic and Specialty Medicine (DIMES), General Pathology Building, University of Bologna, 40126 Bologna, Italy. michela.pucci3@unibo.it.
Giulia VenturiDepartment of Experimental, Diagnostic and Specialty Medicine (DIMES), General Pathology Building, University of Bologna, 40126 Bologna, Italy. giulia.venturi13@unibo.it.
Nadia MalagoliniDepartment of Experimental, Diagnostic and Specialty Medicine (DIMES), General Pathology Building, University of Bologna, 40126 Bologna, Italy. nadia.malagolini@unibo.it.
Mariella ChiricoloDepartment of Experimental, Diagnostic and Specialty Medicine (DIMES), General Pathology Building, University of Bologna, 40126 Bologna, Italy. mariella.chiricolo@unibo.it.
Fabio Dall'OlioDepartment of Experimental, Diagnostic and Specialty Medicine (DIMES), General Pathology Building, University of Bologna, 40126 Bologna, Italy. fabio.dallolio@unibo.it.ORCID 0000-0001-9384-2845
University of Bologna · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation is a very frequent and functionally important post-translational protein modification that undergoes profound changes in cancer. Growth and death factor receptors and plasma membrane glycoproteins, which upon activation by extracellular ligands trigger a signal transduction cascade, are targets of several molecular anti-cancer drugs. In this review, we provide a thorough picture of the mechanisms bywhich glycosylation affects the activity of growth and death factor receptors in normal and pathological conditions. Glycosylation affects receptor activity through three non-mutually exclusive basic mechanisms: (1) by directly regulating intracellular transport, ligand binding, oligomerization and signaling of receptors; (2) through the binding of receptor carbohydrate structures to galectins, forming a lattice thatregulates receptor turnover on the plasma membrane; and (3) by receptor interaction with gangliosides inside membrane microdomains. Some carbohydrate chains, for example core fucose and β1,6-branching, exert a stimulatory effect on all receptors, while other structures exert opposite effects on different receptors or in different cellular contexts. In light of the crucial role played by glycosylation in the regulation of receptor activity, the development of next-generation drugs targeting glyco-epitopes of growth factor receptors should be considered a therapeutically interesting goal.

Indexed as

Apoptosis Regulatory ProteinsFucoseGalectinsGlycosylationHumansLigandsReceptors, Death DomainSignal TransductionApoptosis Regulatory ProteinsFucoseGalectinsLigandsReceptors, Death Domaincancergalectinsgangliosidesglycosylationgrowth factor receptorssignal transduction

Identifiers

PMID29462882
PMCPMC5855802
OpenAlexW2793169963

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.