@article{Artusi2015, abstract = {Guanine-rich nucleic acids can fold into G-quadruplexes, secondary structures implicated in important regulatory functions at the genomic level in humans, prokaryotes and viruses. The remarkably high guanine content of the Herpes Simplex Virus-1 (HSV-1) genome prompted us to investigate both the presence of G-quadruplex forming sequences in the viral genome and the possibility to target them with G-quadruplex ligands to obtain anti-HSV-1 effects with a novel mechanism of action. Using biophysical, molecular biology and antiviral assays, we showed that the HSV-1 genome displays multiple clusters of repeated sequences that form very stable G-quadruplexes. These sequences are mainly located in the inverted repeats of the HSV-1 genome. Treatment of HSV-1 infected cells with the G-quadruplex ligand BRACO-19 induced inhibition of virus production. BRACO-19 was able to inhibit Taq polymerase processing at G-quadruplex forming sequences in the HSV-1 genome, and decreased intracellular viral DNA in infected cells. The last step targeted by BRACO-19 was viral DNA replication, while no effect on virus entry in the cells was observed. This work, presents the first evidence of extended G-quadruplex sites in key regions of the HSV-1 genome, indicates the possibility to block viral DNA replication by G-quadruplex-ligand and therefore provides a proof of concept for the use of G-quadruplex ligands as new anti-herpetic therapeutic options.}, author = {Artusi, Sara and Nadai, Matteo and Perrone, Rosalba and Biasolo, Maria Angela and Palù, Giorgio and Flamand, Louis and Calistri, Arianna and Richter, Sara N.}, doi = {10.1016/j.antiviral.2015.03.016}, journal = {Antiviral Research}, month = {jun}, pages = {123-131}, title = {The Herpes Simplex Virus-1 genome contains multiple clusters of repeated G-quadruplex: Implications for the antiviral activity of a G-quadruplex ligand}, url = {https://doi.org/10.1016/j.antiviral.2015.03.016}, volume = {118}, year = {2015} } @article{DeNicola2016, abstract = {AbstractThe long terminal repeat (LTR) of the proviral human immunodeficiency virus (HIV)-1 genome is integral to virus transcription and host cell infection. The guanine-rich U3 region within the LTR promoter, previously shown to form G-quadruplex structures, represents an attractive target to inhibit HIV transcription and replication. In this work, we report the structure of a biologically relevant G-quadruplex within the LTR promoter region of HIV-1. The guanine-rich sequence designated LTR-IV forms a well-defined structure in physiological cationic solution. The nuclear magnetic resonance (NMR) structure of this sequence reveals a parallel-stranded G-quadruplex containing a single-nucleotide thymine bulge, which participates in a conserved stacking interaction with a neighboring single-nucleotide adenine loop. Transcription analysis in a HIV-1 replication competent cell indicates that the LTR-IV region may act as a modulator of G-quadruplex formation in the LTR promoter. Consequently, the LTR-IV G-quadruplex structure presented within this work could represent a valuable target for the design of HIV therapeutics.}, author = {DeNicola, B. and De Nicola, Beatrice and Lech, Christopher J. and Heddi, Brahim and Regmi, Sagar and Frasson, Ilaria and Perrone, Rosalba and Richter, Sara N. and Phan, Anh Tuân}, doi = {10.1093/nar/gkw432}, journal = {Nucleic Acids Research}, month = {jun}, pages = {6442-6451}, title = {Structure and possible function of a G-quadruplex in the long terminal repeat of the proviral HIV-1 genome}, url = {https://doi.org/10.1093/nar/gkw432}, volume = {44}, year = {2016} } @article{Doria2016, author = {Doria, Filippo and Nadai, Matteo and Costa, Giosuè and Sattin, Giovanna and Gallati, Caroline and Bergamaschi, Greta and Moraca, Federica and Alcaro, Stefano and Freccero, Mauro and Richter, Sara N.}, doi = {10.1002/ejoc.201600757}, journal = {European Journal of Organic Chemistry}, month = {oct}, pages = {4824-4833}, title = {Extended Naphthalene Diimides with Donor/Acceptor Hydrogen-Bonding Properties Targeting G-Quadruplex Nucleic Acids: Extended Naphthalene Diimides with Donor/Acceptor Hydrogen-Bonding Properties Targeting G-Quadruplex Nucleic Acids}, url = {https://oadoi.org/10.1002/ejoc.201600757}, volume = {2016}, year = {2016} } @article{Doria2017, abstract = {Aggregation, red-NIR emission and light-up upon nucleic acid G-quadruplex binding have been investigated for a prototype core-extended naphthalene diimide, which is capable of fast cellular entry and nucleolar localization. Both high-level colocalization with an anti-G-quadruplex antibody and nucleolin displacement reveal that the compound targets and thus makes visible nuclear DNA G-quadruplexes.}, author = {Doria, F. and Nadai, M. and Zuffo, M. and Perrone, R. and Freccero, M. and Richter, S. N.}, doi = {10.1039/c6cc08492c}, journal = {Chemical Communications}, month = {jan}, pages = {2268-2271}, title = {A red-NIR fluorescent dye detecting nuclear DNA G-quadruplexes: in vitro analysis and cell imaging}, url = {http://pubs.rsc.org/en/content/articlepdf/2017/cc/c6cc08492c}, volume = {53}, year = {2017} } @article{Doria2019, author = {Doria, Filippo and Salvati, Erica and Pompili, Luca and Pirota, Valentina and D'Angelo, Carmen and Manoli, Francesco and Nadai, Matteo and Richter, Sara N. and Biroccio, Annamaria and Manet, Ilse and Freccero, Mauro}, doi = {10.1002/chem.201900766}, journal = {Chemistry - A European Journal}, month = {aug}, pages = {11085-11097}, title = {Dyads of G‐Quadruplex Ligands Triggering DNA Damage Response and Tumour Cell Growth Inhibition at Subnanomolar Concentration}, url = {https://oadoi.org/10.1002/chem.201900766}, volume = {25}, year = {2019} } @article{Frasson2016, author = {Frasson, Ilaria and Bettanello, Sabrina and De Canale, Ettore and Richter, Sara N. and Palù, Giorgio}, doi = {10.1186/s13099-016-0110-8}, journal = {Gut Pathogens}, month = {jun}, title = {Serotype epidemiology and multidrug resistance patterns of Salmonella enterica infecting humans in Italy}, url = {https://doi.org/10.1186/s13099-016-0110-8}, volume = {8}, year = {2016} } @article{Frasson2024, abstract = {Abstract The high mutation rate of SARS-CoV-2 leads to the emergence of multiple variants, some of which are resistant to vaccines and drugs targeting viral elements. Targeting host dependency factors, e.g. cellular proteins required for viral replication, would help prevent resistance. However, it remains unclear whether different SARS-CoV-2 variants induce conserved cellular responses and exploit the same core host factors. To this end, we compared three variants of concern and found that the host transcriptional response was conserved, differing only in kinetics and magnitude. Through CRISPR screening, we identified host genes required for infection by each variant. Most of the genes were shared by multiple variants. We validated our hits with small molecules and repurposed Food and Drug Administration-approved drugs. All the drugs were highly active against all the variants tested, including new variants that emerged during the study (Delta and Omicron). Mechanistically, we identified reactive oxygen species production as a key step in early virus replication. Antioxidants such as N-acetyl cysteine (NAC) were effective against all the variants in both human lung cells and a humanised mouse model. Our study supports the use of available antioxidant drugs, such as NAC, as a general and effective anti-COVID-19 approach.}, author = {Frasson, Ilaria and Diamante, Linda and Zangrossi, Manuela and Carbognin, Elena and Dalla Pietà, Anna and Pietà, A. D. and Penna, Alessandro and Rosato, Antonio and Verin, Ranieri and Torrigiani, Filippo and Salata, Cristiano and Dizanzo, Marìa Paula and Vaccaro, Lorenzo and Cacchiarelli, Davide and Richter, Sara N. and Montagner, Marco and Martello, Graziano}, doi = {10.1093/jmcb/mjae004}, journal = {Journal of Molecular Cell Biology}, month = {feb}, title = {Identification of druggable host dependency factors shared by multiple SARS-CoV-2 variants of concern}, url = {https://doi.org/10.1093/jmcb/mjae004}, year = {2024} } @article{Lago2016, abstract = {BACKGROUND: G-quadruplexes (G4s) are four-stranded nucleic acid structures that form in G-rich sequences. Nucleolin (NCL) is a cellular protein reported for its functions upon G4 recognition, such as induction of neurodegenerative diseases, tumor and virus mechanisms activation. We here aimed at defining NCL/G4 binding determinants. METHODS: Electrophoresis mobility shift assay was used to detect NCL/G4 binding; circular dichroism to assess G4 folding, topology and stability; dimethylsulfate footprinting to detect G bases involved in G4 folding. RESULTS: The purified full-length human NCL was initially tested on telomeric G4 target sequences to allow for modulation of loop, conformation, length, G-tract number, stability. G4s in promoter regions with more complex sequences were next employed. We found that NCL binding to G4s heavily relies on G4 loop length, independently of the conformation and oligonucleotide/loop sequence. Low stability G4s are preferred. When alternative G4 conformations are possible, those with longer loops are preferred upon binding to NCL, even if G-tracts need to be spared from G4 folding. CONCLUSIONS: Our data provide insight into how G4s and the associated proteins may control the ON/OFF molecular switch to several pathological processes, including neurodegeneration, tumor and virus activation. Understanding these regulatory determinants is the first step towards the development of targeted therapies. GENERAL SIGNIFICANCE: The indication that NCL binding preferentially stimulates and induces folding of G4s containing long loops suggests NCL ability to modify the overall structure and steric hindrance of the involved nucleic acid regions. This protein-induced modification of the G4 structure may represent a cellular mechanosensor mechanism to molecular signaling and disease pathogenesis.}, author = {Lago, Sara and Tosoni, Elena and Nadai, Matteo and Palumbo, Manlio and Richter, Sara N.}, doi = {10.1016/j.bbagen.2016.11.036}, journal = {BBA - General Subjects}, month = {jan}, pages = {1371-1381}, title = {The cellular protein nucleolin preferentially binds long-looped G-quadruplex nucleic acids}, url = {https://oadoi.org/10.1016/j.bbagen.2016.11.036}, volume = {1861}, year = {2016} } @article{Lavezzo2018, author = {Lavezzo, Enrico and Berselli, Michele and Frasson, Ilaria and Perrone, Rosalba and Palù, Giorgio and Brazzale, Alessandra R. and Richter, Sara N. and Toppo, Stefano}, doi = {10.1371/journal.pcbi.1006675}, journal = {PLoS Computational Biology}, month = {jun}, pages = {e1006675}, title = {G-quadruplex forming sequences in the genome of all known human viruses: a comprehensive guide}, url = {https://doi.org/10.1371/journal.pcbi.1006675}, volume = {14}, year = {2018} } @article{Lopergolo2014, author = {Lopergolo, Alessia and Perrone, Rosalba and Tortoreto, Monica and Doria, Filippo and Beretta, Giovanni L. and Zuco, Valentina and Freccero, Mauro and Grazia Borrello, Maria and Borrello, Maria Grazia and Lanzi, Cinzia and Richter, Sara N. and Ricther, Sara N. and Zaffaroni, Nadia and Folini, Marco}, doi = {10.18632/oncotarget.10105}, journal = {Oncotarget}, month = {nov}, pages = {49649-49663}, title = {Targeting of RET oncogene by naphthalene diimide-mediated gene promoter G-quadruplex stabilization exerts anti-tumor activity in oncogene-addicted human medullary thyroid cancer}, url = {https://doi.org/10.18632/oncotarget.10105}, volume = {7}, year = {2014} } @article{Nadai2014, author = {Nadai, Matteo and Cimino‑Reale, Graziella and Sattin, Giovanna and Doria, Filippo and Butovskaya, Elena and Zaffaroni, Nadia and Freccero, Mauro and Palumbo, Manlio and Richter, Sara N. and Folini, Marco}, doi = {10.3892/ijo.2014.2723}, journal = {International Journal of Oncology}, month = {oct}, title = {Assessment of gene promoter G‑quadruplex binding and modulation by a naphthalene diimide derivative in tumor cells}, url = {http://www.spandidos-publications.com/ijo/46/1/369/download}, year = {2014} } @article{Nadai2014_2, author = {Nadai, Matteo and Doria, Filippo and Germani, Luca and Richter, Sara N. and Freccero, Mauro}, doi = {10.1002/chem.201405215}, journal = {Chemistry - A European Journal}, month = {dec}, pages = {2330-2334}, title = {A Photoreactive G-Quadruplex Ligand Triggered by Green Light}, url = {https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fchem.201405215}, volume = {21}, year = {2014} } @article{Perrone2014, author = {Perrone, R. and Butovskaya, E. and Daelemans, D. and Palu, G. and Pannecouque, C. and Richter, S. N.}, doi = {10.1093/jac/dku280}, journal = {Journal of Antimicrobial Chemotherapy}, month = {aug}, pages = {3248-3258}, title = {Anti-HIV-1 activity of the G-quadruplex ligand BRACO-19}, url = {https://academic.oup.com/jac/article-pdf/69/12/3248/2444939/dku280.pdf}, volume = {69}, year = {2014} } @incollection{Perrone2015, author = {Perrone, Rosalba and Artusi, Sara and Butovskaya, Elena and Nadai, Matteo and Pannecouque, Christophe and Richter, Sara N.}, doi = {10.1007/978-3-319-11776-8_50}, journal = {Ifmbe Proceedings}, month = {jan}, pages = {207-210}, title = {G-Quadruplexes in the Human Immunodeficiency Virus-1 and Herpes Simplex Virus-1: New Targets for Antiviral Activity by Small Molecules}, url = {https://oadoi.org/10.1007/978-3-319-11776-8_50}, year = {2015} } @article{Perrone2015_2, abstract = {We have previously reported that stabilization of the G-quadruplex structures in the HIV-1 Long Terminal Repeat (LTR) promoter suppresses viral transcription. Here we sought to develop new G-quadruplex ligands to be exploited as antiviral compounds by enhancing binding towards the viral G-quadruplex structures. We synthesized naphthalene diimide derivatives with a lateral expansion of the aromatic core. The new compounds were able to bind/stabilize the G-quadruplex to a high extent and some of them displayed clear-cut selectivity towards the viral G-quadruplexes with respect to the human telomeric G-quadruplexes. This feature translated into low nanomolar anti-HIV-1 activity towards two viral strains and encouraging selectivity indexes. The selectivity depended on specific recognition of LTR loop residues; the mechanism of action was ascribed to inhibition of LTR promoter activity in cells. This is the first example of G-quadruplex ligands that show increased selectivity towards the viral G-quadruplexes and display remarkable antiviral activity.}, author = {Perrone, Rosalba and Doria, Filippo and Butovskaya, Elena and Frasson, Ilaria and Botti, Silvia and Scalabrin, Matteo and Lago, Sara and Grande, Vincenzo and Nadai, Matteo and Freccero, Mauro and Richter, Sara N.}, doi = {10.1021/acs.jmedchem.5b01283}, journal = {Journal of Medicinal Chemistry}, month = {nov}, pages = {9639-9652}, title = {Synthesis, Binding and Antiviral Properties of Potent Core-Extended Naphthalene Diimides Targeting the HIV-1 Long Terminal Repeat Promoter G-Quadruplexes}, url = {https://doi.org/10.1021/acs.jmedchem.5b01283}, volume = {58}, year = {2015} } @article{Perrone2016, author = {Perrone, Rosalba and Butovskaya, Elena and Lago, Sara and Garzino-Demo, Alfredo and Pannecouque, Christophe and Palù, Giorgio and Richter, Sara N.}, doi = {10.1016/j.ijantimicag.2016.01.016}, journal = {International Journal of Antimicrobial Agents}, month = {mar}, pages = {311-316}, title = {The G-quadruplex-forming aptamer AS1411 potently inhibits HIV-1 attachment to the host cell}, url = {https://doi.org/10.1016/j.ijantimicag.2016.01.016}, volume = {47}, year = {2016} } @article{Rocca2016, abstract = {Background Recent findings demonstrated that, in mammalian cells, telomere DNA (Tel) is transcribed into telomeric repeat-containing RNA (TERRA), which is involved in fundamental biological processes, thus representing a promising anticancer target. For this reason, the discovery of dual (as well as selective) Tel/TERRA G-quadruplex (G4) binders could represent an innovative strategy to enhance telomerase inhibition. Methods Initially, docking simulations of known Tel and TERRA active ligands were performed on the 3D coordinates of bimolecular G4 Tel DNA (Tel2) and TERRA (TERRA2). Structure-based pharmacophore models were generated on the best complexes and employed for the virtual screening of ~ 257,000 natural compounds. The 20 best candidates were submitted to biophysical assays, which included circular dichroism and mass spectrometry at different K+ concentrations. Results Three hits were here identified and characterized by biophysical assays. Compound 7 acts as dual Tel2/TERRA2 G4-ligand at physiological KCl concentration, while hits 15 and 17 show preferential thermal stabilization for Tel2 DNA. The different molecular recognition against the two targets was also discussed. Conclusions Our successful results pave the way to further lead optimization to achieve both increased selectivity and stabilizing effect against TERRA and Tel DNA G4s. General significance The current study combines for the first time molecular modelling and biophysical assays applied to bimolecular DNA and RNA G4s, leading to the identification of innovative ligand chemical scaffolds with a promising anticancer profile. This article is part of a Special Issue entitled "G-quadruplex" Guest Editor: Dr. Concetta Giancola and Dr. Daniela Montesarchio.}, author = {Rocca, Roberta and Moraca, Federica and Costa, Giosuè and Nadai, Matteo and Scalabrin, Matteo and Talarico, Carmine and Distinto, Simona and Maccioni, Elias and Ortuso, Francesco and Artese, Anna and Alcaro, Stefano and Richter, Sara N.}, doi = {10.1016/j.bbagen.2016.12.023}, journal = {BBA - General Subjects}, month = {jan}, pages = {1329-1340}, title = {Identification of G-quadruplex DNA/RNA binders: Structure-based virtual screening and biophysical characterization}, url = {https://oadoi.org/10.1016/j.bbagen.2016.12.023}, volume = {1861}, year = {2016} } @article{Rocca2022, abstract = {In mammalian cells, telomerase transcribes telomeres in large G-rich non-coding RNA, known as telomeric repeat-containing RNA (TERRA), which folds into noncanonical nucleic acid secondary structures called G-quadruplexes (G4s). Since TERRA G4 has been shown to be involved in telomere length and translation regulation, it could provide valuable insight into fundamental biological processes, such as cancer growth, and TERRA G4 binders could represent an innovative strategy for cancer treatment. In this work, the three best candidates identified in our previous virtual screening campaign on bimolecular DNA/RNA G4s were investigated on the monomolecular Tel DNA and TERRA G4s by means of molecular modelling simulations and in vitro and in cell analysis. The results obtained in this work highlighted the stabilizing power of all the three candidates on TERRA G4. In particular, the two compounds characterized by a chromene scaffold were selective TERRA G4 binders, while the compound with a naphthyridine core acted as a dual Tel/TERRA G4-binder. A biophysical investigation by circular dichroism confirmed the relative stabilization efficiency of the compounds towards TERRA and Tel G4s. The TERRA G4 stabilizing hits showed good antiproliferative activity against colorectal and lung adenocarcinoma cell lines. Lead optimization to increase TERRA G4 stabilization may provide new powerful tools against cancer.}, author = {Rocca, Roberta and Scionti, Francesca and Nadai, Matteo and Moraca, Federica and Maruca, Annalisa and Costa, Giosuè and Catalano, Raffaella and Juli, Giada and Di Martino, Maria Teresa and Ortuso, Francesco and Alcaro, Stefano and Tagliaferri, Pierosandro and Tassone, Pierfrancesco and Richter, Sara N. and Artese, Anna}, doi = {10.3390/ph15050548}, journal = {Pharmaceuticals}, month = {apr}, pages = {548}, title = {Chromene Derivatives as Selective TERRA G-Quadruplex RNA Binders with Antiproliferative Properties}, url = {https://doi.org/10.3390/ph15050548}, volume = {15}, year = {2022} } @article{Tosoni2015, abstract = {AbstractFolding of the LTR promoter into dynamic G-quadruplex conformations has been shown to suppress its transcriptional activity in HIV-1. Here we sought to identify the proteins that control the folding of this region of proviral genome by inducing/stabilizing G-quadruplex structures. The implementation of electrophorethic mobility shift assay and pull-down experiments coupled with mass spectrometric analysis revealed that the cellular protein nucleolin is able to specifically recognize G-quadruplex structures present in the LTR promoter. Nucleolin recognized with high affinity and specificity the majority, but not all the possible G-quadruplexes folded by this sequence. In addition, it displayed greater binding preference towards DNA than RNA G-quadruplexes, thus indicating two levels of selectivity based on the sequence and nature of the target. The interaction translated into stabilization of the LTR G-quadruplexes and increased promoter silencing activity; in contrast, disruption of nucleolin binding in cells by both siRNAs and a nucleolin binding aptamer greatly increased LTR promoter activity. These data indicate that nucleolin possesses a specific and regulated activity toward the HIV-1 LTR promoter, which is mediated by G-quadruplexes. These observations provide new essential insights into viral transcription and a possible low mutagenic target for antiretroviral therapy.}, author = {Tosoni, Elena and Frasson, Ilaria and Scalabrin, Matteo and Perrone, Rosalba and Butovskaya, Elena and Nadai, Matteo and Palù, Giorgio and Fabris, Dan and Richter, Sara N.}, doi = {10.1093/nar/gkv897}, journal = {Nucleic Acids Research}, month = {sep}, pages = {8884-8897}, title = {Nucleolin stabilizes G-quadruplex structures folded by the LTR promoter and silences HIV-1 viral transcription}, url = {http://dx.doi.org/10.1093/nar/gkv897}, volume = {43}, year = {2015} } @article{Żołnowska2017, abstract = {Tuberculosis (TB) remains a serious health problem responsible to cause millions of deaths annually. The scenario becomes alarming when it is evaluated that the number of new drugs does not increase proportionally to the emergence of resistance to the current therapy. Furoxan derivatives, known as nitric oxide (NO) donors, have been described to exhibit antitubercular activity. Herein, a novel series of hybrid furoxan derivatives (1,2,5-oxadiazole 2-N-oxide) (compounds 4a-c, 8a-c and 14a-c) were designed, synthesized and evaluated in vitro against Mycobacterium tuberculosis (MTB) H37Rv (ATCC 27294) and a clinical isolate MDR-TB strain. The furoxan derivatives have exhibited MIC90 values ranging from 1.03 to 62 mM (H37Rv) and 7.0e50.0 mM (MDR-TB). For the most active compounds (8c, 14a, 14b and 14c) the selectivity index ranged from 3.78 to 52.74 (MRC-5 cells) and 1.25e34.78 (J774A.1 cells). In addition, it was characterized for those compounds logPo/w values between 2.1 and 2.9. All compounds were able to release NO at levels ranging from 0.16 to 44.23%. Among the series, the phenylsulfonyl furoxan derivatives (compounds 14a-c) were the best NO-donor with the lowest MIC90 values. The most active compound (14c) was also stable at different pHs (5.0 and 7.4). In conclusion, furoxan derivatives were identified as new promising compounds useful to treat tuberculosis.}, author = {Żołnowska, Beata and Řezáčová, Pavlína and Zamagni, Alice and Wűnsch, Bernhard and Zaffaroni, Nadia and Wilkinson, Shane M. and Wong, R. S.-M. and Wong, W.-Y. and Wamhoff, Eike-Christian and Wang, Q.-W. and Werz, Oliver and van Kuijk, Simon J. A. and de Souza, Paula Carolina and van Gisbergen, Marike W. and Yaromina, Ala and dos Santos, Jean Leandro and Winum, Jean-Yves and Vistoli, Giulio and Visentin, Sonja and Viola, Giampietro and Vincenzi, Fabrizio and Vullo, Daniela and Valgimigli, Luca and Urban, Ernst and Tömböly, Csaba and Valacchi, Giuseppe and Varani, Katia and Tuccinardi, Tiziano and Tutone, Marco and Varano, Flavia and Tesei, Anna and Tesoriere, Luisa and Terenzi, Alessio and Szafrański, Krzysztof and Sławiński, Jarosław and Thomas, Ajiroghene and Tayebee, Reza and Tolomeo, Manlio and Sticozzi, Claudia and Spiliotopoulos, Dimitrios and Spanò, Virginia and Spinello, Angelo and Tenci, Barbara and Supuran, Claudiu T. and Serpe, Loredana and Romagnoli, Romeo and Soukup, Ondrej and Schinelli, Sergio and Shen, Bin and Selleri, Silvia and Sissi, Claudia and Secci, Daniela and Schiaffino Ortega, Santiago and Ramshini, Hassan and Schepmann, Dirk and Alafeefy, Ahmed M. and Fernandes, Guilherme Felipe dos Santos and Sautebin, Lidia and Saponaro, Giulia and Giorgis, Marta and Salvador, Alessia and Rui, Marta and De Luca, Laura and Rossi, Daniela and Pibiri, Ivana and Riganti, Chiara and Scherrmann, Marie-Christine and Federico, Stephanie and Schillaci, Domenico and Ibrahim, Hany S. and Ruggiero, Emanuela and Parvathaneni, Nanda Kumar and Salvadori, Severo and Lolli, Marco Lucio and Falsini, Matteo and Rossi, Antonietta and Rizzo, Roberta and Baraldi, Pier Giovanni and Bonardi, Alessandro and Richter, Sara N. and Ruoho, Arnold and Awadallah, Fadi M. and Poli, Daniela and De Lucia, Daniela and Krasavin, Mikhail and Ahmad, Rehan and De Monte, Celeste and Congiu, Cenzo and Rolando, Barbara and Martorana, Annamaria and Aghazadeh Tabrizi, Mojgan and Ghorab, Mostafa M. and Di Capua, Angela and Ciancetta, Antonella and Buemi, Maria Rosa and Parrino, Barbara and Niemans, Raymon and Ellena, Silvano and Ciancimino, Cristina and Brogi, Simone and Lam, P.-L. and Allam, Heba Abdelrasheed and Mancuso, Francesca and Perlikowska, Renata and Abate, Carmen and Prencipe, Filippo and Tosco, Paolo and Gentile, Carla and Lucio, Oscar Méndez and Cascioferro, Stella and Piekielna, Justyna and Rao, Angela and Ferro, Stefania and Redenti, Sara and Onnis, Valentina and Raffa, Demetrio and Kimatrai Salvador, Maria and Carbone, Anna and El-Waei, Tamer A. and Del Bello, Fabio and Lentini, Laura and Brindisi, Margherita and Marino, Leonardo Biancolino and Abdulla, Maha and Banister, Samuel D. and Mannini, Benedetta and Eldehna, Wagdy M. and Marra, Annamaria and Maggio, Benedetta and Carradori, Simone and Bonifazi, Alessandro and Porta, Nicola and Mahmoud, Walaa R. and Cilibrasi, Vincenzo and Rondanin, Riccardo and Musio, Biagia and Barbero, Nadia and Lopez-Cara, Luisa Carlota and De Simone, Angela and Bartolini, Manuela and Betti, Marco and Perricone, Ugo and Paolillo, Mayra and Catarzi, Daniela and Cappelli, Andrea and Gentilucci, Luca and Fares, Mohamed and Abo-Ashour, Mahmoud F. and Deplano, Alessandro and Chegaev, Konstantin and Frasson, Ilaria and Beinat, Corinne and Bender, Andreas and Cheng, G. Y.-M. and Hanna, Mona M. and Simoni, Daniele and Giallombardo, Daniele and Brzozowski, Zdzisław and Damiano, Francesca M. and Korsakov, Mikhail and Giorgioni, Gianfabio and Baschieri, Andrea and Bruno, Elvira and Oliva, Paola and Khodayari, Kaveh and Pogorzelska, Aneta and Foglietta, Federica and Montalbano, Alessandra and Piccionello, Antonio Palumbo and Pati, Maria Laura and Apperley, Kim Y. P. and De Marco, Rossella and Listing, Monika and Lam, K.-H. and Carta, Fabrizio and Ceruso, Mariangela and Curti, Daniela and Raimondi, Maria Valeria and Petrelli, Riccardo and Di Cesare Mannelli, Lorenzo and Guglielmo, Stefano and Chen, Huan Huan and Al-Tamimi, Abdul-Malek S. and Doria, Filippo and Baraldi, Stefania and Abbas, Safinaz E. and Gallucci, Giulia and Alsaid, Mansour S. and Dorogov, Mikhail and Prandini, Federica and Bian, Z.-X. and Nocentini, Alessio and Bartolotta, Roberta and Pace, Simona and Dennhardt, Sophie and Spalluto, Giampiero and Cerlesi, Maria Camilla and Ghigo, Dario and Pugliese, Anna Maria and Cortesi, Michela and Pastorin, Giorgia and Guardigni, Melissa and Ghabbour, Hazem A. and Cusimano, Maria Grazia and Pastorekova, Silvia and Marconi, Veronica and Ebrahim-Habibi, Azadeh and Bartoli, Cecilia and Quaglia, Wilma and D'Ascenzio, Melissa and Eissa, Ibrahim H. and Pedata, Felicita and Montanari, Serena and Lazzarato, Loretta and Barraja, Paola and Brancale, Andrea and Ho, C.-L. and Koeberle, Andreas and Attanzio, Alessandro and Gallo, Maria Pia and Calo, Girolamo and Melfi, Raffaella and Hamel, Ernest and Abou-Seri, Sahar M. and Berardi, Francesco and Altomare, Angela and Gratteri, Paola and Pinato, Odra and Laurini, Erik and Kobrlova, Tereza and Chaurasia, Shilpi and Cacciari, Barbara and Chojnacki, Jarosław and Del Prete, Sonia and Nissan, Yassin M. and Ferla, Salvatore and Prosa, Nicolò and Maftei, Daniela and Dal Ben, Diego and Feng, Y.-H. and Ghelardini, Carla and Garscha, Ulrike and Nadai, Matteo and Brożewicz, Kamil and Al-Obaid, Omar and Lolli, Graziano and Ismael, Omnia E. and Levi, Renzo and Pricl, Sabrina and Pospíšilová, Klára and Grimaudo, Stefania and Palumbo, Manlio and Moghaddasi, Azam Sadat and Pennati, Marzia and Artali, Roberto and Falcicchio, Aurelia and Da Pozzo, Eleonora and Oz, Beyza Ecem and Rademacher, Christoph and Balzarini, Jan and Gambari, R. and Plescia, Fabiana and Giorgi, Gianluca and Beretta, Giovanni and Marabello, Domenica and Mavlyutov, Timur and Ibrahim, Eslam S. and Cirrincione, Girolamo and Angeli, Andrea and Manachini, Barbara and Klotz, Karl Norbert and Abdel-Aziz, Hatem A. and Capasso, Clemente and Lauricella, Marianna and Negri, Lucia and Chung, Man Chin and Fruttero, Roberta and Pace, Andrea and Palchetti, Ilaria and Andrisano, Vincenza and Mingoia, Francesco and Barolo, Claudia and Pipitone, Rosaria Maria and Diana, Patrizia and Matucci, Rosanna and Brynda, Jiří and Dubois, Ludwig J. and Giordani, Antonio and Liekens, Sandra and Folini, Marco and Dedeoglu, Nurcan and Arafa, Reem K. and Martini, Claudia and Manfredini, Stefano and Chimirri, Alba and Lo, Y.-H. and Freccero, Mauro and Elaasser, Mahmoud M. and Keillor, Jeffrey W. and Guo, Lian-Wang and Abou El Ella, Dalal A. and Bettazzi, Francesca and Barone, Giampaolo and Guler, Ozen Ozensoy and Martinelli, Adriano and Mattiuzzo, Elena and Matyus, Peter and Poce, Giovanna and Moro, Stefano and Lattanzi, Roberta and Al-Kahtani, Abdulla A. and Pavan, Fernando Rogério and D’Anneo, Antonella and Meli, Maria and Canaparo, Roberto and Kluczyk, Alicja and Chin, Frederick T. and Almerico, Anna Maria and Caflisch, Amedeo and Basso, Giuseppe and Basso, Manuela and Pace, Vittorio and Balogh, Balázs and Biava, Mariangela and Milelli, Andrea and Collina, Simona and Kassiou, Michael and Di Leonardo, Aldo and Piergentili, Alessandro and Janecka, Anna and Chui, C.-H. and Ley, Steven V. and Anzini, Maurizio and Chiti, Fabrizio and Daidone, Giuseppe and Lambin, Philippe and Gitto, Rosaria and Colotta, Vittoria and Lauria, Antonino and Balboni, Gianfranco and Gasco, Alberto}, doi = {10.1016/j.ejmech.2018.04.016}, journal = {European Journal of Medicinal Chemistry}, month = {jun}, pages = {523-549}, title = {Discovery of BAZ2A Bromodomain Ligands}, url = {http://doi.org/10.1016/j.ejmech.2016.10.037}, volume = {142}, year = {2017} }