Evidence map›Paper›PMID 36012353›Full record

ReviewInternational journal of molecular sciences2022

The Key Role of Lysosomal Protease Cathepsins in Viral Infections.

Melania Scarcella, Danila d'Angelo, Mariangela Ciampa, Simona Tafuri, Luigi Avallone, Luigi Michele Pavone, Valeria De Pasquale

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
13.8field-weighted citation impact, top 1% 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

44 citing papers in PubMed, 78 citations in OpenAlex.

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  12. Molecular mechanisms of SARS-CoV-2 entry: implications for biomedical strategies.Microbiology and molecular biology reviews : MMBR · 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

7 authors at 1 institution in 1 country.

Melania ScarcellaDepartment of Molecular Medicine and Medical Biotechnology, Medical School, University of Naples Federico II, Via S. Pansini n. 5, 80131 Naples, Italy.ORCID 0000-0002-1975-1328
Danila d'AngeloDepartment of Veterinary Medicine and Animal Productions, University of Naples Federico II, Via Delpino 1, 80137 Naples, Italy.ORCID 0000-0003-2903-4039
Mariangela CiampaDepartment of Molecular Medicine and Medical Biotechnology, Medical School, University of Naples Federico II, Via S. Pansini n. 5, 80131 Naples, Italy.ORCID 0000-0002-9700-3480
Simona TafuriDepartment of Veterinary Medicine and Animal Productions, University of Naples Federico II, Via Delpino 1, 80137 Naples, Italy.ORCID 0000-0002-2154-4205
Luigi AvalloneDepartment of Veterinary Medicine and Animal Productions, University of Naples Federico II, Via Delpino 1, 80137 Naples, Italy.
Luigi Michele PavoneDepartment of Molecular Medicine and Medical Biotechnology, Medical School, University of Naples Federico II, Via S. Pansini n. 5, 80131 Naples, Italy.ORCID 0000-0002-5145-7428
Valeria De PasqualeDepartment of Veterinary Medicine and Animal Productions, University of Naples Federico II, Via Delpino 1, 80137 Naples, Italy.ORCID 0000-0001-5285-1980
University of Naples Federico II · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cathepsins encompass a family of lysosomal proteases that mediate protein degradation and turnover. Although mainly localized in the endolysosomal compartment, cathepsins are also found in the cytoplasm, nucleus, and extracellular space, where they are involved in cell signaling, extracellular matrix assembly/disassembly, and protein processing and trafficking through the plasma and nuclear membrane and between intracellular organelles. Ubiquitously expressed in the body, cathepsins play regulatory roles in a wide range of physiological processes including coagulation, hormone secretion, immune responses, and others. A dysregulation of cathepsin expression and/or activity has been associated with many human diseases, including cancer, diabetes, obesity, cardiovascular and inflammatory diseases, kidney dysfunctions, and neurodegenerative disorders, as well as infectious diseases. In viral infections, cathepsins may promote (1) activation of the viral attachment glycoproteins and entry of the virus into target cells; (2) antigen processing and presentation, enabling the virus to replicate in infected cells; (3) up-regulation and processing of heparanase that facilitates the release of viral progeny and the spread of infection; and (4) activation of cell death that may either favor viral clearance or assist viral propagation. In this review, we report the most relevant findings on the molecular mechanisms underlying cathepsin involvement in viral infection physiopathology, and we discuss the potential of cathepsin inhibitors for therapeutical applications in viral infectious diseases.

Indexed as

CathepsinsVirus DiseasesEndopeptidasesHumansLysosomesPeptide HydrolasesCathepsinsEndopeptidasesPeptide Hydrolasescathepsinsinfectionphysiopathologytherapyviruses

Identifiers

PMID36012353
PMCPMC9409221
OpenAlexW4291465467

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.