Evidence map›Paper›PMID 35503380›Full record

ReviewCellular and molecular life sciences : CMLS2022

Nucleolin: a cell portal for viruses, bacteria, and toxins.

Fiorella Tonello, Maria Lina Massimino, Caterina Peggion

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Review
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  9. Exploring Therapeutic Targets From Spreading Patterns Against Respiratory Syncytial Virus.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
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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

3 authors.

Fiorella TonelloCNR of Italy, Neuroscience Institute, viale G. Colombo 3, 35131, Padua, Italy. fiorella.tonello@cnr.it.ORCID http://orcid.org/0000-0001-8935-8938
Maria Lina MassiminoCNR of Italy, Neuroscience Institute, viale G. Colombo 3, 35131, Padua, Italy.
Caterina PeggionDepartment of Biomedical Sciences, University of Padua, Via Ugo Bassi, 58/B, 35131, Padua, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The main localization of nucleolin is the nucleolus, but this protein is present in multiple subcellular sites, and it is unconventionally secreted. On the cell surface, nucleolin acts as a receptor for various viruses, some bacteria, and some toxins. Aim of this review is to discuss the characteristics that make nucleolin able to act as receptor or co-receptor of so many and different pathogens. The important features that emerge are its multivalence, and its role as a bridge between the cell surface and the nucleus. Multiple domains, short linear motifs and post-translational modifications confer and modulate nucleolin ability to interact with nucleic acids, with proteins, but also with carbohydrates and lipids. This modular multivalence allows nucleolin to participate in different types of biomolecular condensates and to move to various subcellular locations, where it can act as a kind of molecular glue. It moves from the nucleus to the cell surface and can accompany particles in the reverse direction, from the cell surface into the nucleus, which is the destination of several pathogens to manipulate the cell in their favour.

Indexed as

PhosphoproteinsVirusesBacteriaCell NucleolusNucleolinRNA-Binding ProteinsNucleolinPhosphoproteinsRNA-Binding ProteinsCancerGlycosylationInfectious diseasesNeurodegenerative diseasesPhase separationSnake venom toxins

Identifiers

PMID35503380
PMCPMC9064852

What OpenQuestion holds

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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.