Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Rosalida Leone"'
Autor:
Aaron R. Hansen, Michael Chisamore, Helen Zhou, Ezra E.W. Cohen, Marc S. Ballas, Kelly Bell, Danny Rischin, Hisham Mehanna, Carlos Baccan, Rosalida Leone, Sapna Yadavilli, Thomas S. Stanton, Catherine E. Ellis, Axel Hoos, Min Hee Hong, David C. Turner, Helen Chen
Publikováno v:
Journal of Clinical Oncology. 38:TPS6591-TPS6591
TPS6591 Background: Pembrolizumab as part of first-line treatment for patients (pts) with R/M HNSCC has improved survival. However, in order to further improve outcomes in this population investigation of rational combinations targeting different mec
Autor:
Stefano Mangani, Luca Costantino, Rosaria Luciani, Flavio Di Pisa, Samuele Calò, Stefania Ferrari, Cecilia Pozzi, Susan Sammak, Rosalida Leone, M. Paola Costi
Thymidylate synthase (TS) is a target for antifolate-based chemotherapies of microbial and human diseases. Here, ligand-based, synthetic, and X-ray crystallography studies led to the discovery of 6-(3-cyanobenzoyloxy)-2-oxo-2H-naphto[1,8-bc]furan, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::327cb7b4a33102f834aadd455264633c
http://pubs.acs.org/doi/abs/10.1021/jm4014086
http://pubs.acs.org/doi/abs/10.1021/jm4014086
Autor:
Sandra Lazzari, Stefano Mangani, Maria Paola Costi, Cecilia Pozzi, Rosaria Luciani, Laura Cancian, Rosalida Leone, Stefania Ferrari
To identify specific bacterial thymidylate synthase (TS) inhibitors, we exploited phenolphthalein (PTH), which inhibits both bacterial and human enzymes. The X-ray crystal structure of Lactobacillus casei TS (LcTS) that binds PTH showed multiple bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11fb80778ea9827181cb8c501fc35dbb
http://hdl.handle.net/11365/32730
http://hdl.handle.net/11365/32730
Autor:
Maria Cristina Thaller, Stefano Mangani, Emilia Cappelletti, Gianluca Lentini, Rosalida Leone, Manuela Benvenuti
Publikováno v:
Journal of molecular biology. 384(2)
AphA is a magnesium-dependent, bacterial class B acid phosphatase that catalyzes the hydrolysis of a variety of phosphoester substrates and belongs to the DDDD superfamily of phosphohydrolases. The recently reported crystal structure of AphA from Esc
Autor:
Rosalida Leone, Vanna Micheli, Gian Maria Rossolini, Claudio Passariello, Stefano Mangani, Costantino Forleo, Maria Cristina Thaller, Serena Schippa
The AphA enzyme of Escherichia coli, a molecular class B periplasmic phosphatase that belongs to the DDDD superfamily of phosphohydrolases, was purified and subjected to biochemical characterization. Kinetic analysis with several substrates revealed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f465d9ecb3b33354dab72a04e72a89c
http://hdl.handle.net/2108/37930
http://hdl.handle.net/2108/37930
Autor:
Rosalida Leone, Fabio Polticelli, Maurizio Botta, Fabrizio Manetti, Federico Corelli, Paraskevi Tavladoraki, Alessandra Cona
Maize polyamine oxidase (MPAO), the only member of the polyamine oxidase (PAO) family whose three-dimensional structure is known, is characterized by a 30 A long U-shaped catalytic tunnel located between the substrate binding domain and the FAD. To s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32775eb381af833e5efa8938cb5d507d
https://hdl.handle.net/11590/150200
https://hdl.handle.net/11590/150200