Evidence map›Paper›PMID 35650588›Full record

ReviewCell communication and signaling : CCS2022

Phospholipid scramblase 1: a protein with multiple functions via multiple molecular interactors.

Jessica Dal Col, Marìa Julia Lamberti, Annunziata Nigro, Vincenzo Casolaro, Elisabetta Fratta, Agostino Steffan, Barbara Montico

Open access · goldAbstract readReviewVideo-Audio Media
In one paragraph

Review in Cell communication and signaling : CCS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Trial
  2. Review
  3. METTL7A-Dependent mMedComm · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. IFN-inducible human phospholipid scramblase 1 (PLSCR1) protein restricts HIV-1 infection by inhibiting membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Phospholipid scramblase 1: a frontline defense against viral infections.Frontiers in cellular and infection microbiology · 2025
    Review
  17. Proteomics analysis of soluble secreted proteins ofFrontiers in cellular and infection microbiology · 2025
    Article
  18. Article
  19. Article
  20. TargetingVaccines · 2024
    Review
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 3 institutions in 2 countries.

Jessica Dal ColDepartment of Medicine, Surgery and Dentistry "Scuola Medica Salernitana", University of Salerno, Baronissi, Italy. jdalcol@unisa.it.
Marìa Julia LambertiDepartment of Medicine, Surgery and Dentistry "Scuola Medica Salernitana", University of Salerno, Baronissi, Italy.
Annunziata NigroDepartment of Medicine, Surgery and Dentistry "Scuola Medica Salernitana", University of Salerno, Baronissi, Italy.
Vincenzo CasolaroDepartment of Medicine, Surgery and Dentistry "Scuola Medica Salernitana", University of Salerno, Baronissi, Italy.
Elisabetta FrattaDivision of Immunopathology and Cancer Biomarkers, Centro Di Riferimento Oncologico di Aviano (CRO), IRCCS, Aviano, Italy.
Agostino SteffanDivision of Immunopathology and Cancer Biomarkers, Centro Di Riferimento Oncologico di Aviano (CRO), IRCCS, Aviano, Italy.
Barbara MonticoDivision of Immunopathology and Cancer Biomarkers, Centro Di Riferimento Oncologico di Aviano (CRO), IRCCS, Aviano, Italy. bmontico@cro.it.
University of Salerno · ITCentro di Riferimento Oncologico · ITIstituti di Ricovero e Cura a Carattere Scientifico · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phospholipid scramblase 1 (PLSCR1) is the most studied protein of the scramblase family. Originally, it was identified as a membrane protein involved in maintaining plasma membrane asymmetry. However, studies conducted over the past few years have shown the involvement of PLSCR1 in several other cellular pathways. Indeed, PLSCR1 is not only embedded in the plasma membrane but is also expressed in several intracellular compartments where it interacts with a diverse repertoire of effectors, mediators, and regulators contributing to distinct cellular processes. Although most PLSCR1 interactors are thought to be cell-type specific, PLSCR1 often exerts its regulatory functions through shared mechanisms, including the trafficking of different molecules within intracellular vesicles such as endosomes, liposomes, and phagosomes. Intriguingly, besides endogenous proteins, PLSCR1 was also reported to interact with exogenous viral proteins, thereby regulating viral uptake and spread. This review aims to summarize the current knowledge about the multiple roles of PLSCR1 in distinct cellular pathways. Video Abstract.

Indexed as

Phospholipid Transfer ProteinsBiological TransportCell MembranePhospholipid Transfer ProteinsCell deathInflammationPLSCR1Protein–protein interactionVirus

Identifiers

PMID35650588
PMCPMC9158361
OpenAlexW4281894550

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.