Antonio Maraver (0000-0002-5527-5680)

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Antonio Maraver was born in Madrid in 1973. He has been working in international prestigious research centers all over the world as: CNB (Madrid, Spain), The Scripps Research Institute (San Diego, USA), Turku University (Turku, Finland), The Skirball Institute of Biomolecular Medicine, NYU (New York, USA) and CNIO (Madrid, Spain). Since January 2015 he is group leader of the "Oncogenic pathways in lung cancer" laboratory at IRCM (Montpellier, France).

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Montpellier University: Montpellier, FR

2015-04-21 to 2015-11-24 | HDR

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Antonio Maraver

https://orcid.org/0000-0002-5527-5680

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Education and qualifications (3)

Montpellier University: Montpellier, FR

Universidad Autonoma de Madrid Facultad de Ciencias: Madrid, Madrid, ES

Universidad de Alcala de Henares Facultad de Biologia: Alcala de Henares, Madrid, ES

Works (34)

Partial role of volatile organic compounds in behavioural responses of mice to bedding from cancer-affected congeners

RIP140 regulates HES1 oscillatory expression and mitogenic activity in colon cancer cells

Odours of cancerous mouse congeners: detection and attractiveness

Farnesyltransferase inhibition overcomes the adaptive resistance to osimertinib in EGFR-mutant NSCLC

Fibroblast-derived prolargin is a tumor suppressor in hepatocellular carcinoma

Mouse Modeling Dissecting Macrophage-Breast Cancer Communication Uncovered Roles of PYK2 in Macrophage Recruitment and Breast Tumorigenesis.

Generation and Characterization of a New Preclinical Mouse Model of EGFR-Driven Lung Cancer with MET-Induced Osimertinib Resistance

Tumor-Antagonizing Fibroblasts Secrete Prolargin as Tumor Suppressor in Hepatocellular Carcinoma

Spleen plays a major role in DLL4-driven acute T-cell lymphoblastic leukemia.

Notch inhibition overcomes resistance to tyrosine kinase inhibitors in EGFR-driven lung adenocarcinoma.

The evolution of resistance and tolerance as cancer defences.

An oligoclonal antibody durably overcomes resistance of lung cancer to third-generation EGFR inhibitors.

Troponin-I enhances and is required for oncogenic overgrowth

Bladder cancer and the Notch pathway

Targeting γ-secretases protect against angiotensin II-induced cardiac hypertrophy

NOTCH pathway inactivation promotes bladder cancer progression

Characterization of two distinct lymphoproliferative diseases caused by ectopic expression of the Notch ligand DLL4 on T cells.

Programmed cell senescence during mammalian embryonic development.

SIRT1 promotes thyroid carcinogenesis driven by PTEN deficiency.

EMT and induction of miR-21 mediate metastasis development in Trp53-deficient tumours.

Notching up a new therapeutic strategy for non-small cell lung carcinoma (NSCLC).

Therapeutic effect of γ-secretase inhibition in KrasG12V-driven non-small cell lung carcinoma by derepression of DUSP1 and inhibition of ERK.

Anti-aging activity of the Ink4/Arf locus.

Telomerase reverse transcriptase delays aging in cancer-resistant mice.

The Arf/p53 pathway in cancer and aging.

Effect of presenilins in the apoptosis of thymocytes and homeostasis of CD8+ T cells.

Delayed ageing through damage protection by the Arf/p53 pathway.

Regulatory T cells inhibit stable contacts between CD4+ T cells and dendritic cells in vivo.

The C-terminal domain of the pVP2 precursor is essential for the interaction between VP2 and VP3, the capsid polypeptides of infectious bursal disease virus.

The oligomerization domain of VP3, the scaffolding protein of infectious bursal disease virus, plays a critical role in capsid assembly.

Identification and molecular characterization of the RNA polymerase-binding motif of infectious bursal disease virus inner capsid protein VP3.

C terminus of infectious bursal disease virus major capsid protein VP2 is involved in definition of the T number for capsid assembly.

VP5, the nonstructural polypeptide of infectious bursal disease virus, accumulates within the host plasma membrane and induces cell lysis.

VP1, the putative RNA-dependent RNA polymerase of infectious bursal disease virus, forms complexes with the capsid protein VP3, leading to efficient encapsidation into virus-like particles.

Peer review (7 reviews for 2 publications/grants)