Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Alessandro Foti"'
Publikováno v:
Journal of Maps, Vol 19, Iss 1 (2023)
ABSTRACTIn this paper we show data from new detailed geological-structural field surveys, integrated with preliminary photogrammetric analysis, presented in a 1:10,000 scale geological map. The field-based investigations covered an area of about 60-k
Externí odkaz:
https://doaj.org/article/2ca1d64330e843cc99b5ae96ee51e255
Autor:
Sadia Sultana, Mary E. Crompton, Kennadi Meurer, Olivia Jankiewicz, Grace H. Morales, Colton Johnson, Elise Horbach, Kevin Pierre Hoffmann, Pooja Kr, Ritika Shah, Greg M. Anderson, Nathan T. Mortimer, Jonathan E. Schmitz, Maria Hadjifrangiskou, Alessandro Foti, Jan-Ulrik Dahl
Publikováno v:
mBio, Vol 13, Iss 5 (2022)
ABSTRACT The ability to overcome stressful environments is critical for pathogen survival in the host. One challenge for bacteria is the exposure to reactive chlorine species (RCS), which are generated by innate immune cells as a critical part of the
Externí odkaz:
https://doaj.org/article/c20bbfc91ae248aaafac1e32f859b9ee
Autor:
Cristiano Mota, Mariam Esmaeeli, Catarina Coelho, Teresa Santos‐Silva, Martin Wolff, Alessandro Foti, Silke Leimkühler, Maria João Romão
Publikováno v:
FEBS Open Bio, Vol 9, Iss 5, Pp 925-934 (2019)
Human aldehyde oxidase (hAOX1) is a molybdenum enzyme with high toxicological importance, but its physiological role is still unknown. hAOX1 metabolizes different classes of xenobiotics and is one of the main drug‐metabolizing enzymes in the liver,
Externí odkaz:
https://doaj.org/article/a305ef19af68434e80950374136dd979
Publikováno v:
PLoS ONE, Vol 12, Iss 7, p e0182061 (2017)
Aldehyde oxidases (AOXs) are molybdo-flavoenzymes characterized by broad substrate specificity, oxidizing aromatic/aliphatic aldehydes into the corresponding carboxylic acids and hydroxylating various heteroaromatic rings. The enzymes use oxygen as t
Externí odkaz:
https://doaj.org/article/ec753ec5a6d3441291394730e373077d
Publikováno v:
Immunity. 54:1377-1391
Neutrophils are immune cells with unusual biological features that furnish potent antimicrobial properties. These cells phagocytose and subsequently kill prokaryotic and eukaryotic organisms very efficiently. Importantly, it is not only their ability
Autor:
Jan-Ulrik Dahl, Pooja Kr, Sadia Sultana, Elise Horbach, Ritika Shah, Jonathan E. Schmitz, Kennadi LeDoux, Mary E. Crompton, Nathan T. Mortimer, Kevin Pierre Hoffmann, Maria Hadjifrangiskou, Alessandro Foti, Colton Johnson, Grace H. Morales, Greg M. Anderson, Olivia Jankiewicz
The ability to overcome stressful environments is critical for pathogen survival in the host. One challenge for bacteria is the exposure to reactive chlorine species (RCS), which are generated by innate immune cells as critical part of the oxidative
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1b77d7dfe7174c6916f6fec787ae552f
https://doi.org/10.1101/2021.08.31.458474
https://doi.org/10.1101/2021.08.31.458474
Publikováno v:
Infect Immun
Neutrophils kill invading microbes and therefore represent the first line of defense of the innate immune response. Activated neutrophils assemble NADPH oxidase to convert substantial amounts of molecular oxygen into superoxide, which, after dismutat
Autor:
Martin Wolff, Cristiano Mota, Mariam Esmaeeli, Silke Leimkühler, Maria João Romão, Catarina Coelho, Alessandro Foti, Teresa Santos-Silva
Publikováno v:
FEBS Open Bio
'FEBS Open Bio ', vol: 9, pages: 925-934 (2019)
'FEBS Open Bio ', vol: 9, pages: 925-934 (2019)
This work was supported by the Applied Molecular Biosciences Unit-UCIBIO which is financed by national funds from FCT/MCTES (UID/Multi/04378/2019), Project PTDC/BBB-BEP/1185/2014 and Grant SFRH/BPD/ 84581/2012 (CC). SL thanks the Deutsche Forschungsg
Autor:
Catarina Coelho, Maria João Romão, Tobias Hartmann, Teresa Santos-Silva, Silke Leimkühler, Alessandro Foti
Publikováno v:
Nature Chemical Biology. 11:779-783
Aldehyde oxidase (AOX) is a xanthine oxidase (XO)-related enzyme with emerging importance due to its role in the metabolism of drugs and xenobiotics. We report the first crystal structures of human AOX1, substrate free (2.6-angstrom resolution) and i