Evidence map›Paper›PMID 33228060›Full record

ReviewCells2020

Mechanisms of Action of EGFR Tyrosine Kinase Receptor Incorporated in Extracellular Vesicles.

Laura C Zanetti-Domingues, Scott E Bonner, Marisa L Martin-Fernandez, Veronica Huber

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 37 citations in OpenAlex.

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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

4 authors at 3 institutions in 2 countries.

Laura C Zanetti-DominguesCentral Laser Facility, Research Complex at Harwell, Rutherford Appleton Laboratory, Didcot OX11 0FA, UK.ORCID 0000-0003-0514-3185
Scott E BonnerThe Wood Lab, Department of Paediatrics, University of Oxford, Oxford OX1 3QX, UK.ORCID 0000-0003-2361-9968
Marisa L Martin-FernandezCentral Laser Facility, Research Complex at Harwell, Rutherford Appleton Laboratory, Didcot OX11 0FA, UK.ORCID 0000-0001-5496-6300
Veronica HuberUnit of Immunotherapy of Human Tumors, Fondazione IRCCS Istituto Nazionale dei Tumori, 20133 Milan, Italy.ORCID 0000-0001-6304-3575
Rutherford Appleton Laboratory · GBFondazione IRCCS Istituto Nazionale dei Tumori · ITUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M011224/1
6 · The paper itself

Abstract

EGFR and some of the cognate ligands extensively traffic in extracellular vesicles (EVs) from different biogenesis pathways. EGFR belongs to a family of four homologous tyrosine kinase receptors (TKRs). This family are one of the major drivers of cancer and is involved in several of the most frequent malignancies such as non-small cell lung cancer, breast cancer, colorectal cancer and ovarian cancer. The carrier EVs exert crucial biological effects on recipient cells, impacting immunity, pre-metastatic niche preparation, angiogenesis, cancer cell stemness and horizontal oncogene transfer. While EV-mediated EGFR signalling is important to EGFR-driven cancers, little is known about the precise mechanisms by which TKRs incorporated in EVs play their biological role, their stoichiometry and associations to other proteins relevant to cancer pathology and EV biogenesis, and their means of incorporation in the target cell. In addition, it remains unclear whether different subtypes of EVs incorporate different complexes of TKRs with specific functions. A raft of high spatial and temporal resolution methods is emerging that could solve these and other questions regarding the activity of EGFR and its ligands in EVs. More importantly, methods are emerging to block or mitigate EV activity to suppress cancer progression and drug resistance. By highlighting key findings and areas that remain obscure at the intersection of EGFR signalling and EV action, we hope to cross-fertilise the two fields and speed up the application of novel techniques and paradigms to both.

Indexed as

Epithelial-Mesenchymal TransitionExtracellular VesiclesHumansReceptor Protein-Tyrosine KinasesSignal TransductionTumor MicroenvironmentReceptor Protein-Tyrosine KinasescancerEpidermal Growth Factor Receptor (EGFR)epithelial-to-mesenchymal transition (EMT)EV heterogeneityextracellular vesicles (EVs)ExTRAcrine signallingimmune suppressionmicroenvironment subversiontherapy resistancetumour microenvironment

Identifiers

PMID33228060
PMCPMC7699420
OpenAlexW3105949291

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.