Maria Rosaria Cera
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Explore the profile of Maria Rosaria Cera including associated specialties, affiliations and a list of published articles.
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11
Citations
335
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Recent Articles
1.
Cera M, Bastianello G, Purushothaman D, Andronache A, Ascione F, Robusto M, et al.
Sci Rep
. 2024 Dec;
14(1):30786.
PMID: 39730498
Targeting nuclear mechanics is emerging as a promising therapeutic strategy for sensitizing cancer cells to immunotherapy. Inhibition of the mechano-sensory kinase ATR leads to mechanical vulnerability of cancer cells, causing...
2.
Brambillasca S, Cera M, Andronache A, Dey S, Faga G, Fancelli D, et al.
Biomed Pharmacother
. 2024 Jun;
177:116991.
PMID: 38906021
Macropinocytosis is a cellular process that enables cells to engulf extracellular material, such as nutrients, growth factors, and even whole cells. It is involved in several physiological functions as well...
3.
Cavallo F, Troglio F, Faga G, Fancelli D, Shyti R, Trattaro S, et al.
Mol Autism
. 2020 Nov;
11(1):88.
PMID: 33208191
Background: Autism spectrum disorder (ASD) is a highly prevalent neurodevelopmental condition affecting almost 1% of children, and represents a major unmet medical need with no effective drug treatment available. Duplication...
4.
Romussi A, Cappa A, Vianello P, Brambillasca S, Cera M, Dal Zuffo R, et al.
ACS Med Chem Lett
. 2020 May;
11(5):754-759.
PMID: 32435381
Lysine-specific demethylase 1 (LSD1 or KDM1A) is a FAD-dependent enzyme that acts as a transcription corepressor or coactivator by regulating the methylation status of histone H3 lysines K4 and K9,...
5.
Trifiro P, Cappa A, Brambillasca S, Botrugno O, Cera M, Dal Zuffo R, et al.
Future Med Chem
. 2017 Jul;
9(11):1161-1174.
PMID: 28722470
Background: Histone lysine demethylases (KDMs) are well-recognized targets in oncology drug discovery. They function at the post-translation level controlling chromatin conformation and gene transcription. KDM1A is a flavin adenine dinucleotide-dependent...
6.
Nguyen T, Cera M, Pinto A, Lo Presti L, Hamel E, Conti P, et al.
Mol Cancer Ther
. 2012 Mar;
11(5):1103-11.
PMID: 22442310
Tumor resistance to antitubulin drugs resulting from P-glycoprotein (Pgp) drug-efflux activity, increased expression of the βIII tubulin isotype, and alterations in the drug-binding sites are major obstacles in cancer therapy....
7.
Bottos A, Destro E, Rissone A, Graziano S, Cordara G, Assenzio B, et al.
Proc Natl Acad Sci U S A
. 2009 Nov;
106(49):20782-7.
PMID: 19926856
Unlike other neuronal counterparts, primary synaptic proteins are not known to be involved in vascular physiology. Here, we demonstrate that neurexins and neuroligins, which constitute large and complex families of...
8.
Cera M, Fabbri M, Molendini C, Corada M, Orsenigo F, Rehberg M, et al.
J Cell Sci
. 2009 Jan;
122(Pt 2):268-77.
PMID: 19118219
The membrane-associated adhesion molecule JAM-A is required for neutrophil infiltration in inflammatory or ischemic tissues. JAM-A expressed in both endothelial cells and neutrophils has such a role, but the mechanism...
9.
Vetrano S, Rescigno M, Cera M, Correale C, Rumio C, Doni A, et al.
Gastroenterology
. 2008 Jun;
135(1):173-84.
PMID: 18514073
Background & Aims: Junctional adhesion molecule-A (JAM-A) is localized at the tight junctions and controls leukocyte migration into the tissues. However, its functional role in inflammatory bowel disease (IBD) is...
10.
Corada M, Chimenti S, Cera M, Vinci M, Salio M, Fiordaliso F, et al.
Proc Natl Acad Sci U S A
. 2005 Jul;
102(30):10634-9.
PMID: 16027360
Junctional Adhesion Molecule-A (JAM-A) is a transmembrane adhesive protein expressed at endothelial junctions and in leukocytes. Here we report that JAM-A is required for the correct infiltration of polymorphonuclear leukocytes...