Ibes a fast system for the production of soluble, tetrameric and glycosylated recombinant neuraminidase using optimized NA-expressing vectors in mammalian cells. The rNAs are enzymatically active and able to induce functional antibodies, demonstrating their prospective as a tool for the screening of new NA inhibitors, for the development of novel diagnostic tools, and for structural research, as a non-exhaustive list of attainable applications. The development of standardized ELLA based on these enzymatically active rNA may well enable routine NA immunity analysis in typical influenza vaccine clinical trials enabling better characterization of your immune response in the course of vaccination or infection.PLOS 1 | DOI:ten.1371/journal.pone.0135474 August 17,15 /Recombinant Neuraminidase Production, Characterization and Use in ELLASupporting InformationS1 Fig. Various sequence alignment of influenza neuraminidases.Ethyl 4-chloroacetoacetate uses Structure-based amino acid sequence alignment with the complete A/turkey/Turkey/01/2005, A/California/07/2009 and A/ Caledonia/22/99 N1 NAs, A/Wyoming/3/2003 N2 NA and B/Malaysia/2506/2004 and B/Florida/4/2006 B NAs.936637-97-7 Chemical name Secondary structure components refer to the crystal structure of the A/Vietnam/1203/04 (H5N1) NA globular head (PDB 2HTY). Identical residues are shown using a red background, whereas related residues are shown in red and highlighted with blue boxes (http:// espript.ibcp.fr/ESPript/ESPript/). (TIF)AcknowledgmentsThe authors would prefer to thanks Novartis Animal Care facility and Miguela Vieru for formulating the recombinant proteins.Author ContributionsConceived and created the experiments: MP IF AB YU SB FL JLT ECS DM RC. Performed the experiments: MP IF GA FG RC. Analyzed the information: MP IF AB YU FG FL DM RC. Contributed reagents/materials/analysis tools: AB DM. Wrote the paper: MP IF SB DM RC.
JNCI J Natl Cancer Inst (2016) 108(7): djvdoi:10.1093/jnci/djv435 Initial published on the web February five, 2016 ArticlearticleAntitumor Activity of BRAF Inhibitor and IFN Mixture in BRAF-Mutant MelanomaFrancesco Sabbatino*, Yangyang Wang*, GiosuScognamiglio, Elvira Favoino, Steven A. Feldman, Vincenzo Villani, Keith T. Flaherty, Sjoerd Nota, Diana Giannarelli, Ester Simeone, Anna M. Anniciello, Giuseppe Palmieri, Stefano Pepe, Gerardo Botti, Paolo A. Ascierto, Cristina R.PMID:35670838 Ferrone, Soldano FerroneDepartment of Surgery (FS, YW, EF, VV, CRF, SF), Department of Health-related Oncology (KTF), and Department of Orthopaedic Surgery (SN, SF), Massachusetts Basic Hospital, Harvard Medical School, Boston, MA; Unit of Pathology (GS, AMA, GB) and Unit of Melanoma, Cancer Immunotherapy and Innovative Therapy (ES, PAA), Istituto Nazionale Tumori, Fondazione “G. Pascale,” Naples, Italy; Surgery Branch, National Cancer Institute, National Institutes of Wellness, Bethesda, MD (SAF); Biostatistics Unit, Regina Elena National Cancer Institute, Roma, Italy (DG); Unit of Cancer Genetics, Institute of Biomolecular Chemistry, National Investigation Council, Sassari, Italy (GP); Department of Medicine and Surgery, University of Salerno, Baronissi, Salerno, Italy (FS, SP). Current affiliation: Laboratory of Cellular and Molecular Biology, National Institute for Digestive Illnesses, I.R.C.C.S. “Saverio de Bellis,” Castellana Grotte (BA), Italy (EF). *Authors contributed equally to this perform. Correspondence to: Soldano Ferrone M.D., Ph.D., Division of Surgery, Massachusetts General Hospital, Harvard Health-related College, 55 Fruit Street, Boston, MA 02114 (e-mail: [email protected]).Abstr.
