Zobrazeno 1 - 10
of 51
pro vyhledávání: '"Serena Faggiano"'
Autor:
Monica Cozzi, Mariacristina Failla, Eleonora Gianquinto, Sandra Kovachka, Valeria Buoli Comani, Carlotta Compari, Omar De Bei, Roberta Giaccari, Francesco Marchesani, Marialaura Marchetti, Luca Ronda, Barbara Rolando, Massimo Baroni, Gabriele Cruciani, Barbara Campanini, Stefano Bettati, Serena Faggiano, Loretta Lazzarato, Francesca Spyrakis
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-21 (2024)
Abstract Human hemoglobin (Hb) is the preferred iron source of Staphylococcus aureus. This pathogenic bacterium exploits a sophisticated protein machinery called Iron-regulated surface determinant (Isd) system to bind Hb, extract and internalize heme
Externí odkaz:
https://doaj.org/article/f9ef68fdb4844b4a8556175d108cfb76
Publikováno v:
Data in Brief, Vol 22, Iss , Pp 158-163 (2019)
We investigated the pH dependence of the fluorescence spectra of ADIFAB (FFA Sciences), a probe used for the quantification of free fatty acids (FFA). Data reports the change in the emission peak of ADIFAB and in the affinity for FFA as a function of
Externí odkaz:
https://doaj.org/article/706a1135efcf429f8689b19e7fecf7bb
Autor:
Samanta Raboni, Marialaura Marchetti, Serena Faggiano, Barbara Campanini, Stefano Bruno, Francesco Marchesani, Marilena Margiotta, Andrea Mozzarelli
Publikováno v:
Frontiers in Molecular Biosciences, Vol 5 (2019)
Human serine racemase is a pyridoxal 5′-phosphate (PLP)-dependent dimeric enzyme that catalyzes the reversible racemization of L-serine and D-serine and their dehydration to pyruvate and ammonia. As D-serine is the co-agonist of the N-methyl-D-aspa
Externí odkaz:
https://doaj.org/article/0eca15e56cf1458e9bf2eb561a4bb0cf
Autor:
Serena Faggiano, Annalisa Pastore
Publikováno v:
Cells, Vol 3, Iss 2, Pp 639-656 (2014)
Protein ubiquitination is an important post-translational modification involved in several essential signalling pathways. It has different effects on the target protein substrate, i.e., it can trigger the degradation of the protein in the proteasome,
Externí odkaz:
https://doaj.org/article/652139bd63ae4e5e99bc92f73b8b327b
Autor:
Rajesh P Menon, Suran Nethisinghe, Serena Faggiano, Tommaso Vannocci, Human Rezaei, Sally Pemble, Mary G Sweeney, Nicholas W Wood, Mary B Davis, Annalisa Pastore, Paola Giunti
Publikováno v:
PLoS Genetics, Vol 9, Iss 7, p e1003648 (2013)
At least nine dominant neurodegenerative diseases are caused by expansion of CAG repeats in coding regions of specific genes that result in abnormal elongation of polyglutamine (polyQ) tracts in the corresponding gene products. When above a threshold
Externí odkaz:
https://doaj.org/article/160e066247634585a377f084b98468ee
Autor:
Andrea Mozzarelli, Luca Ronda, Stefano Bettati, Stefania Abbruzzetti, Stefano Bruno, Cristiano Viappiani, Serena Faggiano
Publikováno v:
Molecular aspects of medicine 84 (2022). doi:10.1016/j.mam.2021.101050
info:cnr-pdr/source/autori:Faggiano S.; Ronda L.; Bruno S.; Abbruzzetti S.; Viappiani C.; Bettati S.; Mozzarelli A./titolo:From hemoglobin allostery to hemoglobin-based oxygen carriers/doi:10.1016%2Fj.mam.2021.101050/rivista:Molecular aspects of medicine/anno:2022/pagina_da:/pagina_a:/intervallo_pagine:/volume:84
info:cnr-pdr/source/autori:Faggiano S.; Ronda L.; Bruno S.; Abbruzzetti S.; Viappiani C.; Bettati S.; Mozzarelli A./titolo:From hemoglobin allostery to hemoglobin-based oxygen carriers/doi:10.1016%2Fj.mam.2021.101050/rivista:Molecular aspects of medicine/anno:2022/pagina_da:/pagina_a:/intervallo_pagine:/volume:84
Hemoglobin (Hb) plays its vital role through structural and functional properties evolutionarily optimized to work within red blood cells, i.e., the tetrameric assembly, well-defined oxygen affinity, positive cooperativity, and heterotropic allosteri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab77ca5f9796c8dc983abaf3337058bf
http://www.scopus.com/inward/record.url?eid=2-s2.0-85119276611&partnerID=q2rCbXpz
http://www.scopus.com/inward/record.url?eid=2-s2.0-85119276611&partnerID=q2rCbXpz
Autor:
Roberta Giaccari, Stefano Bruno, Andrea Mozzarelli, Barbara Campanini, Stefano Bettati, Serena Faggiano, Francesco Marchesani, Annalisa Michielon
Publikováno v:
Biochimica et biophysica acta. Proteins and proteomics 1869 (2021). doi:10.1016/j.bbapap.2020.140544
info:cnr-pdr/source/autori:Michielon A.; Marchesani F.; Faggiano S.; Giaccari R.; Campanini B.; Bettati S.; Mozzarelli A.; Bruno S./titolo:Human serine racemase is inhibited by glyceraldehyde 3-phosphate, but not by glyceraldehyde 3-phosphate dehydrogenase/doi:10.1016%2Fj.bbapap.2020.140544/rivista:Biochimica et biophysica acta. Proteins and proteomics/anno:2021/pagina_da:/pagina_a:/intervallo_pagine:/volume:1869
info:cnr-pdr/source/autori:Michielon A.; Marchesani F.; Faggiano S.; Giaccari R.; Campanini B.; Bettati S.; Mozzarelli A.; Bruno S./titolo:Human serine racemase is inhibited by glyceraldehyde 3-phosphate, but not by glyceraldehyde 3-phosphate dehydrogenase/doi:10.1016%2Fj.bbapap.2020.140544/rivista:Biochimica et biophysica acta. Proteins and proteomics/anno:2021/pagina_da:/pagina_a:/intervallo_pagine:/volume:1869
Murine serine racemase (SR), the enzyme responsible for the biosynthesis of the neuromodulator d-serine, was reported to form a complex with glyceraldehyde 3-phosphate dehydrogenase (GAPDH), resulting in SR inhibition. In this work, we investigated t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05d93787ebaaa444d4a26667a7548ff7
http://www.cnr.it/prodotto/i/456405
http://www.cnr.it/prodotto/i/456405
Autor:
Roberta Giaccari, Francesco Marchesani, Carlotta Compari, Emilia Fisicaro, Andrea Mozzarelli, Barbara Campanini, Stefano Bettati, Stefano Bruno, Serena Faggiano
Publikováno v:
International journal of molecular sciences
23 (2022). doi:10.3390/ijms23094959
info:cnr-pdr/source/autori:Giaccari R.; Marchesani F.; Compari C.; Fisicaro E.; Mozzarelli A.; Campanini B.; Bettati S.; Bruno S.; Faggiano S./titolo:Human Serine Racemase Weakly Binds the Third PDZ Domain of PSD-95/doi:10.3390%2Fijms23094959/rivista:International journal of molecular sciences (Print)/anno:2022/pagina_da:/pagina_a:/intervallo_pagine:/volume:23
International Journal of Molecular Sciences; Volume 23; Issue 9; Pages: 4959
23 (2022). doi:10.3390/ijms23094959
info:cnr-pdr/source/autori:Giaccari R.; Marchesani F.; Compari C.; Fisicaro E.; Mozzarelli A.; Campanini B.; Bettati S.; Bruno S.; Faggiano S./titolo:Human Serine Racemase Weakly Binds the Third PDZ Domain of PSD-95/doi:10.3390%2Fijms23094959/rivista:International journal of molecular sciences (Print)/anno:2022/pagina_da:/pagina_a:/intervallo_pagine:/volume:23
International Journal of Molecular Sciences; Volume 23; Issue 9; Pages: 4959
Human serine racemase (hSR) is a pyridoxal-5′-phosphate (PLP)-dependent dimer that catalyzes the formation of D-serine from L-serine, as well as the dehydration of both L- and D-serine to pyruvate and ammonia. As D-serine is a co-agonist of N-methy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b14ee4a36dd67d12aba0a1c22d08b9e
https://doi.org/10.3390/ijms23094959
https://doi.org/10.3390/ijms23094959
Autor:
Serena Faggiano, Francesca Spyrakis, Andrea Mozzarelli, Stefano Bruno, Barbara Campanini, Ida Autiero, Annalisa Michielon, Eleonora Gianquinto, Stefano Bettati, Francesco Marchesani
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::319890b43b5770e638913a9ea541d1d9
https://doi.org/10.1111/febs.15645/v2/response1
https://doi.org/10.1111/febs.15645/v2/response1
Autor:
Riccardo Percudani, Luca Ronda, Marialaura Marchetti, Serena Faggiano, Stefano Bettati, Anastasia Liuzzi
Publikováno v:
Sensors and actuators. B, Chemical
255 (2018): 2820–2828. doi:10.1016/j.snb.2017.09.099
info:cnr-pdr/source/autori:Marchetti M, Ronda L, Faggiano S, Liuzzi A, Percudani R, Bettati S/titolo:Fluorescence quantification of allantoin in biological samples by cap-immobilized allantoinase%2Fresorcinol assay/doi:10.1016%2Fj.snb.2017.09.099/rivista:Sensors and actuators. B, Chemical (Print)/anno:2018/pagina_da:2820/pagina_a:2828/intervallo_pagine:2820–2828/volume:255
255 (2018): 2820–2828. doi:10.1016/j.snb.2017.09.099
info:cnr-pdr/source/autori:Marchetti M, Ronda L, Faggiano S, Liuzzi A, Percudani R, Bettati S/titolo:Fluorescence quantification of allantoin in biological samples by cap-immobilized allantoinase%2Fresorcinol assay/doi:10.1016%2Fj.snb.2017.09.099/rivista:Sensors and actuators. B, Chemical (Print)/anno:2018/pagina_da:2820/pagina_a:2828/intervallo_pagine:2820–2828/volume:255
Allantoin, the final product of urate degradation in non-hominoid mammals, forms in vivo through an enzyme-dependent pathway whose restoration has been proposed for the treatment of hyperuricemic conditions. Non-enzymatic urate oxidation to allantoin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d4d22ecffed058b47b421ac93661974
https://doi.org/10.1016/j.snb.2017.09.099
https://doi.org/10.1016/j.snb.2017.09.099