Ion channels, chloride channels, calcium signaling, drug discovery, cystic fibrosis
218
Scopus Publications
Scopus Publications
Evaluation of ATP12A and NFKBIZ as potential markers of inflammatory status in cystic fibrosis airway epithelial cells Caterina Allegretta, Daniela Guidone, Silvia Boscia, Laura Pisano, Silvia Ricci, Chiara Azzari, Cristina Fevola, Martina De Santis, Fabiana Ciciriello, Enza Montemitro, Daniela Dolce, Giulio Cabrini, Luis J. V. Galietta, Vito Terlizzi, Onofrio Laselva Inflammation Research, 2026 Background People with Cystic Fibrosis (pwCF) are prone to bacterial lung infections with P. aeruginosa , which have been linked to chronic inflammation in the lung. Although the highly effective CFTR modulator therapy (Elexacaftor-Tezacaftor-Ivacaftor, ETI) has dramatically improved respiratory outcomes in pwCF, airway inflammation and bacterial colonization persist in the upper and lower respiratory tracts. Methods We investigated the effect of ETI in both plasma and fresh primary nasal epithelial (HNE) cells obtained from pwCF pre- and post-three months of ETI treatment. Given that inflammation has been shown to upregulate NFKBIZ and the ATP12A proton pump, we measured their levels in fresh HNE cells and in cultured HNE cells exposed to clinical exoproducts (EXO) of P. aeruginosa or other inflammatory stimuli. Results ELISA analysis revealed a significant reduction of IL-6, IL-8, and IL-17C in both plasma and HNE cells after ETI treatment. NFKBIZ and ATP12A expression was increased after infection and inflammatory stimuli in CF bronchial epithelial (CFBE) and HNE cells, and this increase was reduced by Dimethyl-Fumarate, an anti-inflammatory drug. Conclusions These preclinical studies, using patient-derived tissues, suggest that NFKBIZ and ATP12A may play a relevant role in the pathophysiology and inflammatory response of the CF airway epithelium.
A critical analysis on ENaC inhibitors, unravelling molecular medicinal insights and promising research roadmap in the treatment of cystic fibrosis Fabiana Lo Mascolo, Alessandra Lipani, Stefano Giuffrida, Marilia Barreca, Roberta Bivacqua, Virginia Spanò, Maria Valeria Raimondi, Alessandra Montalbano, Anna Borrelli, Arianna Venturini, Daniela Guidone, Michele Genovese, Luis J.V. Galietta, Paola Barraja European Journal of Medicinal Chemistry, 2026 channel (ENaC) has emerged as a pharmacologically attractive approach to counteract airway dehydration. Due to adverse effects caused by systemic ENaC inhibition, and in particular related to potassium homeostasis, medicinal chemistry efforts have focused on inhaled, lung-restricted inhibitors. This review examines the evolution of direct ENaC blockers from early amiloride-like compounds to more advanced clinical candidates, emphasizing the medicinal chemistry principles that enabled improved airway selectivity. In particular, the optimization process progressively shifted to a multi-parameter strategy integrating persistent positive charge, increased polarity, reduced lipophilicity and low epithelial permeability, in order to decrease pulmonary absorption, prolong lung retention and reduce systemic exposure. In this context, special attention is given to positively charged acylguanidine mimetics, including quaternary amines and N-alkylated benzimidazoles. Overall, the field shows that for inhaled ENaC inhibitors, therapeutic success depends not only on nanomolar target potency, but on achieving sustained local airway exposure with minimal renal liability.
Functional correction of the untreatable CFTR 1717-1G>A mutation through mRNA- and sgRNA-optimized base editing Alessandro Umbach, Annalisa Santini, Mattijs Bulcaen, Daniela Guidone, Giulia Maule, Daniele Arosio, Irene Carrozzo, Matteo Ciciani, Enrica Brugnara, Anabela Ramalho, François Vermeulen, Luis J. V. Galietta, Marianne S. Carlon, Anna Cereseto Science Translational Medicine, 2026 The 1717-1G>A is a prevalent splicing mutation causing cystic fibrosis (CF) for which no pharmacological treatments have been approved. This mutation disrupts a canonical 3′ AG splice acceptor site in the cystic fibrosis transmembrane conductance regulator ( CFTR ) gene, leading to severe RNA missplicing, which prevents the correct synthesis of the encoded protein. In this study, we developed an adenine base editing (ABE) strategy to efficiently correct the 1717-1G>A mutation. By using the ABE9 base editor with the protospacer adjacent motif–relaxed Streptococcus pyogenes clustered regularly interspaced short palindromic repeats (CRISPR)–CRISPR-associated protein 9 (Cas9) variant SpRY, we obtained up to 30% editing with limited bystander effects in a human embryonic kidney (HEK) 293–based cellular model. Through systematic optimizations of the ABE system, delivered by electroporation of base editor messenger RNA (mRNA) and single guide RNA (sgRNA), we demonstrated genetic repair of the 1717-1G>A mutation in airway epithelial cells and intestinal organoids derived from people with CF. Functional analysis was performed by measuring short-circuit current in air-liquid interface (ALI) culture and by assessing forskolin-induced swelling (FIS) in intestinal organoids, which revealed restoration of CFTR channel activity. These results highlight SpRY-ABE9 as a potential genome editing strategy to permanently correct the CFTR 1717-1G>A mutation and restore CFTR function.
Modulators of anion channels and transporters as alternative therapeutic agents to normalize airway surface liquid in cystic fibrosis Alessandra Lipani, Fabiana Lo Mascolo, Stefano Giuffrida, Marilia Barreca, Roberta Bivacqua, Virginia Spanò, Maria Valeria Raimondi, Anna Borrelli, Arianna Venturini, Daniela Guidone, Michele Genovese, Alessandra Montalbano, Luis J.V. Galietta, Paola Barraja European Journal of Medicinal Chemistry, 2026 Cystic fibrosis (CF) is characterized by impaired chloride and bicarbonate secretion due to mutations in the CFTR gene which codes for a plasma membrane anion channel. Defective anion transport in CF is particularly severe in the respiratory system, with impairment of mucociliary clearance, mucus accumulation, and airway obstruction. Pharmacological CFTR modulators, able to rescue mutant CFTR trafficking and gating, have improved the clinical condition of many CF patients, particularly those with F508del mutation. However, there is a substantial number of patients with mutations unresponsive to CFTR modulators. This unmet need has prompted the exploration of alternative therapies to target the basic defect in CF. This review provides a comprehensive overview covering the years 2010-2025 of most prominent advances in the identification of small-molecule inhibitors and activators targeting three potential contributors to airway epithelium ion homeostasis: pendrin (SLC26A4), SLC26A9, and TMEM16A (ANO1). These molecules may represent potential therapeutic agents and/or be important tools of research to understand the pathophysiological role of their target. For pendrin, high-throughput screening yielded novel classes of potent and selective inhibitors including tetrahydropyrazolopyridines and pyrazolo-thiophenesulfonamides. SAR analysis led to the discovery of lead compounds PDSinh-A01 and PDSinh-C01 showing significant activity and favorable drug-like properties. Additionally, 5-benzyloxy-2-methylbenzofuran compounds have emerged as promising candidates with increased activity and favourable drug-like properties. Though SLC26A9 involvement in chloride secretion remains debated, the identification of the potent and selective inhibitor S9-A13 revealed the role of this transporter in ASL pH regulation via bicarbonate modulation. Pharmacological potentiation of TMEM16A, a calcium activated chloride channel, could be a way to bypass the defective anion transport in CF. To achieve this goal, the ETX001 compound was identified and progressed to clinical trials. TMEM16A inhibitors, such as MONNA, Ani9, and 2-acylaminocycloalkylthiophene derivatives, have been also identified and represent tools of research to assess the role of TMEM16A in different organs and tissues. Overall, the efforts towards the development of modulators of alternative ion channels and transporters opens new avenues for improving mucociliary clearance in CF. • Defective chloride transport due to CFTR loss-of-function is the basic defect in cystic fibrosis (CF) • Pharmacological modulators can restore CFTR function but this is not possible in patients with undruggable mutations • Other anion channels and transporters can be considered as alternative targets in CF • The drug-discovery process of small-molecule inhibitors/activators targeting SLC26A4, SLC26A9 and TMEM16A anion channels/transporters is discussed • SLC26A4 inhibitors may counteract electrolyte/water absorption and improve airway surface hydration • TMEM16A potentiators can be useful to stimulate chloride secretion and bypass CFTR defect whereas inhibitors represent important tools of research to understand TMEM16A role
Esc peptides and derivatives potentiate the activity of CFTR with gating defects and display antipseudomonal activity in cystic fibrosis-like lung disease Loretta Ferrera, Floriana Cappiello, Arianna Venturini, Hexin Lu, Bruno Casciaro, Giacomo Cappella, Giulio Bontempi, Alessandra Corrente, Raffaele Strippoli, Federico Zara, Y. Peter Di, Luis J. V. Galietta, Mattia Mori, Maria Luisa Mangoni Cellular and Molecular Life Sciences, 2025 Cystic fibrosis (CF) is a rare disease caused by mutations in the gene encoding the CF transmembrane conductance regulator (CFTR), a chloride channel with an important role in the airways. Despite the clinical efficacy of present modulators in restoring the activity of defective CFTR, there are patients who show persistent pulmonary infections, mainly due to Pseudomonas aeruginosa. Recently, we reported an unprecedented property of antimicrobial peptides i.e. Esc peptides, which consists in their ability to act as potentiators of CFTR carrying the most common mutation (the loss of phenylalanine 508) affecting protein folding, trafficking and gating. In this work, by electrophysiology experiments and computational studies, the capability of these peptides and de-novo designed analogs was demonstrated to recover the function of other mutated forms of CFTR which severely affect the channel gating (G551D and G1349D). This is presumably due to direct interaction of the peptides with the nucleotide binding domains (NBDs) of CFTR, followed by a novel local phenomenon consisting in distancing residues located at the cytosolic side of the NBDs interface, thus stabilizing the open conformation of the pore at its cytosolic end. The most promising peptides for the dual antimicrobial and CFTR potentiator activities were also shown to display antipseudomonal activity in conditions mimicking the CF pulmonary ion transport and mucus obstruction, with a higher efficacy than the clinically used colistin. These studies should assist in development of novel drugs for lung pathology in CF, with dual CFTR potentiator and large spectrum antibiotic activities.
Quantitative characterisation of extracellular vesicles designed to decoy or compete with SARS-CoV-2 reveals differential mode of action across variants of concern and highlights the diversity of Omicron Melanie Schürz, Isabel Pagani, Eva Klinglmayr, Heloisa Melo Benirschke, Martin Mayora Neto, Luis J. V. Galietta, Arianna Venturini, Nicoletta Pedemonte, Valeria Capurro, Sandra Laner-Plamberger, Christoph Grabmer, Essi Emminger, Martin Wolf, Marianne Steiner, Cyrus Kohlmetz, Niklas Mayr, Liliia Paniushkina, Katharina Schallmoser, Dirk Strunk, Hans Brandstetter, Martin Hintersteiner, Nigel Temperton, Elisa Vicenzi, Nicole Meisner-Kober Cell Communication and Signaling, 2025 BACKGROUND: The converging biology between enveloped viruses and extracellular vesicles (EVs) has raised interest in the application of engineered EVs as antiviral therapeutics. Following the recent COVID-19 pandemic, EVs engineered with either the ACE2-receptor or Spike-protein have been proposed as strategy to either decoy SARS-CoV-2, or to compete with its cell entry. For generic use as a platform for future pandemic preparedness, a systematic and quantitative comparison of both strategies is required to assess their limitations and benefits across different variants of concern. METHODS: Here we generated EVs decorated with either the ACE2-receptor or the Spike-protein of (Wuhan)-SARS-CoV-2 and used single vesicle imaging for in-depth quantitative characterisation. These vesicles were then systematically tested for anti-viral activity across SARS-CoV-2 variants of concern using both, pseudotype and live virus cellular infection models including primary human bronchial and nasal explants. RESULTS: Spike-protein EVs or ACE2-EVs recovered from transiently transfected HEK293T cells comprised only a small fraction of the EV secretome (5% or 20%, respectively) and were primarily derived from the plasma membrane rather than multivesicular bodies. Redirecting intracellular trafficking of the Spike protein by mutating its transmembrane or subcellular localisation domains did not increase the yields of Spike-EVs. Both types of vesicles inhibited SARS-CoV-2 (D614G) in a dose dependent manner with kinetics and immunohistochemistry consistent with an inhibition at the initial cell entry stage. ACE2-EVs were more potent than Spike-EVs and at least 500-1000 times more potent than soluble antibodies in a pseudotype model. Surprisingly, ACE2-EVs switched from an inhibitory to an enhancer activity for the Omicron BA.1 variant whereas Spike-EVs retained their activity across all variants of concern. CONCLUSIONS: While our data show that both types of engineered EVs potently inhibit SARS-CoV, the decoy versus competition strategy may result in diverging outcomes when considering viral evolution into new variants of concern. While Spike-EVs retain their competition for receptor binding even against higher affinity viral Spike mutations, the formation of complexes between ACE2-EVs and the virus may not only result in inhibition by decoy. As EVs are actively internalised by cells themselves, they may shuttle the virus into cells, resulting in a productive alternative cell entry route for variants such as Omicron, that diverge from strict plasma membrane protease cleavage to the use of endosomal proteases for release of their genome.
In silico, in vitro and ex vivo characterization of cystic fibrosis transmembrane conductance regulator pathogenic variants localized in the fourth intracellular loop and their rescue by modulators Emanuela Pesce, Valeria Tomati, Valeria Capurro, Mariateresa Lena, Cristina Pastorino, Miro Astore, Serdar Kuyucak, Benoit Chevalier, Elvira Sondo, Federico Cresta, Alice Dighero, Vito Terlizzi, Cristina Fevola, Stefano Costa, Maria Cristina Lucanto, Valeria Daccò, Laura Claut, Francesca Ficili, Benedetta Fabrizzi, Renata Bocciardi, Federico Zara, Carlo Castellani, Luis J. V. Galietta, Shafagh A. Waters, Alexandre Hinzpeter, Nicoletta Pedemonte British Journal of Pharmacology, 2025 Background and PurposeCystic fibrosis (CF) is due to loss‐of‐function variants of the CF transmembrane conductance regulator (CFTR) channel. The most effective treatment for people with CF carrying the F508del mutation is the triple combination of elexacaftor–tezacaftor–ivacaftor (ETI). ETI can correct the underlying defect(s) in other CFTR mutants. The use of disease‐relevant predictive models such as patient‐derived human nasal epithelial cells allow to investigate the response to CFTR modulators of specific genotypes, possibly supporting patients' access to treatment.Experimental ApproachUsing computational, biochemical and functional methodologies, a detailed analysis of selected variants in the intracellular loop 4 (ICL4) to understand their impact on CFTR structure and function.Key ResultsMutations affecting L1065, R1066 and L1077 compromise structural stability of CFTR. Analyses of single variants expressed heterologously in immortalized bronchial cells showed that, upon ETI, rescued activity for both L1065P and R1066C was close to 50% of the wild‐type CFTR activity. Biochemical studies of ICL4 variants expression pattern in CFBE41o‐cells, following treatment for 24 h, demonstrate the appearance of the mature, fully glycosylated band, with no changes in the immature band. Finally, our study provides evidence in primary nasal cells from a cohort of people with CF that L1065P and R1066C can be effectively rescued by ETI up to 25%–45% of the activity measured in non‐CF epithelia.Conclusion and ImplicationsAlthough the observed rescue for L1065P and R1066C was smaller than that of the F508del, it should fall in a range predicted, by various studies, to provide a clinical benefit.
Sodium-Coupled Monocarboxylate Absorption in the Airway Epithelium Is Facilitated by the SLC5A8 Co-Transporter Anita Guequen, Bárbara Tapia‐Balladares, Tábata Apablaza, Daniela Guidone, Nátali Cárcamo‐Lemus, Sandra Villanueva, Pamela Y. Sandoval, Luis J. V. Galietta, Carlos A. Flores Acta Physiologica, 2025 AimAmino acids, sugars, short‐chain fatty acids (SCFA), vitamins, and other small molecules compose the extracellular metabolome on the airway lumen surface, but how the airway epithelium deals with these molecules has not been deeply studied. Due to the broad spectrum of metabolites transported by SLC5A8 and SLC5A12, we aim to determine if they are functionally expressed and participate in the absorption of Na+, short‐chain fatty acids, and monocarboxylates in mouse and human airway epithelium.MethodsTracheas isolated from male or female mice and human bronchial epithelial cells (HBECs) were used for electrophysiological studies in the Ussing chamber and to detect members of the SLC16 family by RT‐PCR and bulk RNAseq. Additionally, cell lines expressing the human and murine SLC5A8 transporter were employed for uptake studies using a fluorescent lactate probe.ResultsWe showed for the first time that human and murine airway epithelium express a functional SLC5A8 transporter, facilitating the absorption of glucose metabolites and SCFAs. The Na+‐coupled monocarboxylate transport was not additive with ENaC‐mediated Na+ absorption in mouse trachea. We observed that valproate acts as an inhibitor of the murine but not of the human SLC5A8 transporter.ConclusionsOur results demonstrate that several metabolites derived from bacterial and cellular metabolism can be transported from the airway lumen into the epithelial cells, participating in a homeostatic relation of the tissue with its environment.
The apical mucus layer alters the pharmacological properties of the airway epithelium Daniela Guidone, Martina de Santis, Emanuela Pesce, Valeria Capurro, Nicoletta Pedemonte, Luis J. V. Galietta Journal of Physiology, 2025 Electrogenic transepithelial ion transport can be measured with the short‐circuit current technique. Such experiments are frequently used to evaluate the activity of the cystic fibrosis transmembrane conductance regulator (CFTR), a cAMP‐activated chloride channel that is defective in cystic fibrosis, one of the most frequent genetic diseases. Typically, CFTR activity is estimated from the effect of CFTRinh‐172, a selective CFTR inhibitor. Unexpectedly, we found that CFTRinh‐172, in addition to PPQ‐102, another CFTR inhibitor, caused only partial inhibition of CFTR function, particularly in epithelia in pro‐inflammatory conditions, which are characterized by abundant mucus secretion. We hypothesized that the mucus layer was responsible for the poor activity of CFTR inhibitors. Therefore, we treated the epithelial surface with the reducing agent dithiothreitol to remove mucus. Removal of mucus, confirmed by immunofluorescence, resulted in highly enhanced sensitivity of CFTR to pharmacological inhibition. Our results show that the mucus layer represents an important barrier whose presence limits the activity of pharmacological agents. This is particularly relevant for CFTR and the evaluation of therapeutic approaches for correction of the basic defect in cystic fibrosis. imageKey points Activity of the cAMP‐activated cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel can be evaluated by measuring the inhibition elicited by the selective blockers CFTRinh‐172 and PPQ‐102. In short‐circuit current recordings on human airway epithelia, CFTR inhibitors had only a partial effect on cAMP‐dependent chloride secretion, suggesting the possible contribution of other ion channels. The mucus layer covering the epithelial surface was removed with the reducing agent dithiothreitol. Treatment of epithelia with dithiothreitol markedly improved the efficacy of CFTR inhibitors. The partial effect of CFTR inhibitors might be explained by the presence of the mucus layer acting as a barrier.
Distinct Responses of Cystic Fibrosis Epithelial Cells to SARS-CoV-2 and Influenza A Virus Isabel Pagani, Arianna Venturini, Valeria Capurro, Alessandro Nonis, Silvia Ghezzi, Mariateresa Lena, Beatriz Alcalá-Franco, Fabrizio Gianferro, Daniela Guidone, Carla Colombo, Nicoletta Pedemonte, Alessandra Bragonzi, Cristina Cigana, Luis J. V. Galietta, Elisa Vicenzi American Journal of Respiratory Cell and Molecular Biology, 2025 The coronavirus disease (COVID-19) pandemic has underscored the impact of viral infections on individuals with cystic fibrosis (CF). Initial observations suggested lower COVID-19 rates among CF populations; however, subsequent clinical data have presented a more complex scenario. This study aimed to investigate how bronchial epithelial cells from individuals with and without CF, including various CFTR (CF transmembrane conductance regulator) mutations, respond to in vitro infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants and SARS-CoV. Comparisons with the influenza A virus (IAV) were included based on evidence that patients with CF experience heightened morbidity from IAV infection. Our findings showed that CF epithelial cells exhibited reduced replication of SARS-CoV-2, regardless of the type of CFTR mutation or SARS-CoV-2 variant, as well as the original 2003 SARS-CoV. In contrast, these cells displayed more efficient IAV replication than non-CF cells. Interestingly, the reduced susceptibility to SARS-CoV-2 in CF was not linked to the expression of ACE2 (angiotensin-converting enzyme 2) receptor or to CFTR dysfunction, as pharmacological treatments to restore CFTR function did not normalize the viral response. Both SARS-CoV-2 infection and CFTR function influenced the concentrations of certain cytokines and chemokines, although these effects were not correlated. Overall, this study reveals a unique viral response in CF epithelial cells, characterized by reduced replication for some viruses like SARS-CoV-2, while showing increased susceptibility to others, such as IAV. This research offers a new perspective on CF and viral interactions, emphasizing the need for further investigation into the mechanisms underlying these differences.
Beyond Trikafta: new models to assess tissue dependent rescue of N1303K-CFTR Iwona Pranke, Valeria Capurro, Benoit Chevalier, Emanuela Pesce, Valeria Tomati, Cristina Pastorino, Mairead Kelly-Aubert, Aurelie Hatton, Elise Dreano, Mariateresa Lena, Renata Bocciardi, Federico Zara, Stefano Pantano, Vito Terlizzi, Cristina Lucanto, Stefano Costa, Laura Claut, Valeria Daccò, Piercarlo Poli, Massimo Maschio, Benedetta Fabrizzi, Nicole Caporelli, Marco Cipolli, Sonia Volpi, Frederique Chedevergne, Laure Cosson, Julie Macey, Sophie Ramel, Laurence Weiss, Dominique Grenet, Laurence Le Clainche-Viala, Benoit Douvry, Bruno Ravoninjatovo, Camille Audousset, Aurélie Tatopoulos, Bénédicte Richaud-Thiriez, Melissa Baravalle, Guillaume Thouvenin, Guillaume Labbé, Marie Mittaine, Philippe Reix, Isabelle Durieu, Julie Mankikian, Stéphanie Bui, Thao Nguyen-Khoa, Karim Khoukh, Clémence Martin, Jennifer Da Silva, Paola De Carli, Carlo Castellani, Federico Cresta, Luis Galietta, Anne Guillemaut, Emmanuelle Girodon, Natacha Remus, Mathis Bulcaen, Marjolein Ensinck, Miroslaw Zajac, Marianne Carlon, Jean LeBihan, Pierre-Régis Burgel, Isabelle Sermet-Gaudelus, Alexandre Hinzpeter, Nicoletta Pedemonte Frontiers in Pharmacology, 2025
Pharmacological rescue of the G85E CFTR variant by preclinical and approved modulators Valeria Tomati, Valeria Capurro, Emanuela Pesce, Cristina Pastorino, Elvira Sondo, Mariateresa Lena, Anna Borrelli, Federico Cresta, Stefano Pantano, Francesca Collini, Pietro Ripani, Vito Terlizzi, Cristina Fevola, Stefano Costa, Maria Cristina Lucanto, Federico Zara, Tiziano Bandiera, Renata Bocciardi, Carlo Castellani, Luis J. V. Galietta, Nicoletta Pedemonte Frontiers in Pharmacology, 2024
Novel tricyclic pyrrolo-quinolines as pharmacological correctors of the mutant CFTR chloride channel Mario Renda, Marilia Barreca, Anna Borrelli, Virginia Spanò, Alessandra Montalbano, Maria Valeria Raimondi, Roberta Bivacqua, Ilaria Musante, Paolo Scudieri, Daniela Guidone, Martina Buccirossi, Michele Genovese, Arianna Venturini, Tiziano Bandiera, Paola Barraja, Luis J. V. Galietta Scientific Reports, 2023
Partial rescue of f508del-cftr stability and trafficking defects by double corrector treatment Valeria Capurro, Valeria Tomati, Elvira Sondo, Mario Renda, Anna Borrelli, Cristina Pastorino, Daniela Guidone, Arianna Venturini, Alessandro Giraudo, Sine Mandrup Bertozzi, Ilaria Musante, Fabio Bertozzi, Tiziano Bandiera, Federico Zara, Luis J. V. Galietta, Nicoletta Pedemonte International Journal of Molecular Sciences, 2021
Current development of CFTR potentiators in the last decade Virginia Spanò, Arianna Venturini, Michele Genovese, Marilia Barreca, Maria Valeria Raimondi, Alessandra Montalbano, Luis J.V. Galietta, Paola Barraja European Journal of Medicinal Chemistry, 2020
Light-responsive microRNA miR-211 targets Ezrin to modulate lysosomal biogenesis and retinal cell clearance Federica Naso, Daniela Intartaglia, Danila Falanga, Chiara Soldati, Elena Polishchuk, Giuliana Giamundo, Paola Tiberi, Elena Marrocco, Paolo Scudieri, Chiara Di Malta, Ivana Trapani, Edoardo Nusco, Francesco Giuseppe Salierno, Enrico Maria Surace, Luis JV Galietta, Sandro Banfi, Alberto Auricchio, Andrea Ballabio, Diego Luis Medina, Ivan Conte EMBO Journal, 2020
Discovery of a picomolar potency pharmacological corrector of the mutant CFTR chloride channel Nicoletta Pedemonte, Fabio Bertozzi, Emanuela Caci, Federico Sorana, Paolo Di Fruscia, Valeria Tomati, Loretta Ferrera, Alejandra Rodríguez-Gimeno, Francesco Berti, Emanuela Pesce, Elvira Sondo, Ambra Gianotti, Paolo Scudieri, Tiziano Bandiera, Luis J. V. Galietta Science Advances, 2020
Bioactive Thymosin Alpha-1 Does Not Influence F508del-CFTR Maturation and Activity Andrea Armirotti, Valeria Tomati, Elizabeth Matthes, Guido Veit, Deborah M. Cholon, Puay-Wah Phuan, Clarissa Braccia, Daniela Guidone, Martina Gentzsch, Gergely L. Lukacs, Alan S. Verkman, Luis J. V. Galietta, John W. Hanrahan, Nicoletta Pedemonte Scientific Reports, 2019
Two CFTR mutations within codon 970 differently impact on the chloride channel functionality Felice Amato, Paolo Scudieri, Ilaria Musante, Valeria Tomati, Emanuela Caci, Marika Comegna, Sabrina Maietta, Francesca Manzoni, Antonella Miriam Di Lullo, Elke Wachter, Eef Vanderhelst, Vito Terlizzi, Cesare Braggion, Giuseppe Castaldo, Luis J. V. Galietta Human Mutation, 2019
Thymosin α-1 does not correct F508del-CFTR in cystic fibrosis airway epithelia Valeria Tomati, Emanuela Caci, Loretta Ferrera, Emanuela Pesce, Elvira Sondo, Deborah M. Cholon, Nancy L. Quinney, Susan E. Boyles, Andrea Armirotti, Roberto Ravazzolo, Luis J.V. Galietta, Martina Gentzsch, Nicoletta Pedemonte Jci Insight, 2018
The role of pendrin in the airways: Links with asthma and copd Kenji Izuhara, Shoichi Suzuki, Charity Nofziger, Masahiro Ogawa, Shoichiro Ohta, Yasuhiro Nanri, Yasutaka Mitamura, Tomohito Yoshihara, Nicoletta Pedemonte, Luis J. V. Galietta, Markus Paulmichl Role of Pendrin in Health and Disease Molecular and Functional Aspects of the Slc26a4 Anion Exchanger, 2017
CFTR pharmacology Olga Zegarra-Moran, Luis J. V. Galietta Cellular and Molecular Life Sciences, 2017
Goblet Cell Hyperplasia Requires High Bicarbonate Transport to Support Mucin Release Giulia Gorrieri, Paolo Scudieri, Emanuela Caci, Marco Schiavon, Valeria Tomati, Francesco Sirci, Francesco Napolitano, Diego Carrella, Ambra Gianotti, Ilaria Musante, Maria Favia, Valeria Casavola, Lorenzo Guerra, Federico Rea, Roberto Ravazzolo, Diego Di Bernardo, Luis J. V. Galietta Scientific Reports, 2016
Unravelling druggable signalling networks that control F508del-CFTR proteostasis Ramanath Narayana Hegde, Seetharaman Parashuraman, Francesco Iorio, Fabiana Ciciriello, Fabrizio Capuani, Annamaria Carissimo, Diego Carrella, Vincenzo Belcastro, Advait Subramanian, Laura Bounti, Maria Persico, Graeme Carlile, Luis Galietta, David Y Thomas, Diego Di Bernardo, Alberto Luini Elife, 2015
Upregulation of TMEM16A protein in bronchial epithelial cells by bacterial pyocyanin Emanuela Caci, Paolo Scudieri, Emma Di Carlo, Patrizia Morelli, Silvia Bruno, Ida De Fino, Alessandra Bragonzi, Ambra Gianotti, Elvira Sondo, Loretta Ferrera, Alessandro Palleschi, Luigi Santambrogio, Roberto Ravazzolo, Luis J. V. Galietta Plos One, 2015
DOG1 regulates growth and IGFBP5 in gastrointestinal stromal tumors Susanne Simon, Florian Grabellus, Loretta Ferrera, Luis Galietta, Benjamin Schwindenhammer, Thomas Mühlenberg, Georg Taeger, Grant Eilers, Juergen Treckmann, Frank Breitenbuecher, Martin Schuler, Takahiro Taguchi, Jonathan A. Fletcher, Sebastian Bauer Cancer Research, 2013
Altered expression of ano1 variants in human diabetic gastroparesis Amelia Mazzone, Cheryl E. Bernard, Peter R. Strege, Arthur Beyder, Luis J.V. Galietta, Pankaj J. Pasricha, James L. Rae, Henry P. Parkman, David R. Linden, Joseph H. Szurszewski, Tamas Ördög, Simon J. Gibbons, Gianrico Farrugia Journal of Biological Chemistry, 2011
Alternative splicing at a NAGNAG acceptor site as a novel phenotype modifier Alexandre Hinzpeter, Abdel Aissat, Elvira Sondo, Catherine Costa, Nicole Arous, Christine Gameiro, Natacha Martin, Agathe Tarze, Laurence Weiss, Alix de Becdelièvre, Bruno Costes, Michel Goossens, Luis J. Galietta, Emmanuelle Girodon, Pascale Fanen Plos Genetics, 2010
Gelsolin secretion in interleukin-4-treated bronchial epithelia and in asthmatic airways Giovanni Candiano, Maurizio Bruschi, Nicoletta Pedemonte, Emanuela Caci, Sabrina Liberatori, Luca Bini, Carlo Pellegrini, Mario Viganò, Brian J. O'Connor, Tak H. Lee, Luis J. V. Galietta, Olga Zegarra-Moran American Journal of Respiratory and Critical Care Medicine, 2005
Effect of inflammatory stimuli on airway ion transport. Luis J. V. Galietta, Chiara Folli, Emanuela Caci, Nicoletta Pedemonte, Alessandro Taddei, Roberto Ravazzolo, Olga Zegarra-Moran Proceedings of the American Thoracic Society, 2004
Correction of delF508-CFTR activity with benzo(c)quinolizinium compounds through facilitation of its processing in cystic fibrosis airway cells Journal of Cell Science, 2001
Molecular genetics. Research and clinical activity Gaslini, 2001
Properties of CFTR activated by the xanthine derivative X-33 in human airway Calu-3 cells Laurence Bulteau, Renaud Dérand, Yvette Mettey, Thierry Métayé, M. Rachel Morris, Ceinwen M. McNeilly, Chiara Folli, Luis J. V. Galietta, Olga Zegarra-Moran, Malcolm M. C. Pereira, Chantal Jougla, Robert L. Dormer, Jean-Michel Vierfond, Michel Joffre, Frédéric Becq American Journal of Physiology Cell Physiology, 2000
Development of substituted benzo[c]quinolizinium compounds as novel activators of the cystic fibrosis chloride channel Frédéric Becq, Yvette Mettey, Mike A. Gray, Luis J.V. Galietta, Robert L. Dormer, Marc Merten, Thierry Métayé, Valérie Chappe, Cécie Marvingt-Mounir, Olga Zegarra-Moran, Robert Tarran, Laurence Bulteau, Renaud Dérand, Malcome M.C. Pereira, Margaret A. McPherson, Christian Rogier, Michel Joffre, Barry E. Argent, Denis Sarrouilhe, Wafa Kammouni, Catherine Figarella, Bernard Verrier, Maurice Gola, Jean-Michel Vierfond Journal of Biological Chemistry, 1999
