Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Reeder, Robinson"'
Publikováno v:
Journal for ImmunoTherapy of Cancer, Vol 11, Iss Suppl 1 (2023)
Externí odkaz:
https://doaj.org/article/6b40c7704f8148d7b60e87401a1f5e3a
Autor:
Ben N. Christopher, Reeder Robinson, Leticia Reyes, Lena Golick, Ashton Basar, Nathan Dolloff
Publikováno v:
Cancer Research. 82:C035-C035
Pancreatic Ductal Adenocarcinoma (PDAC) has a 5-year survival rate of only 10%, and limited treatment options exist. Immune checkpoint inhibitors are effective in a variety of cancer types; however, the complex immunosuppressive tumor microenvironmen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1b14abfc121d9efa7a39dcbf36e6ecc8
https://doi.org/10.1158/1538-7445.panca22-c035
https://doi.org/10.1158/1538-7445.panca22-c035
Publikováno v:
The FASEB Journal. 35
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::db89912d4594e7eb28ab8944c919f416
https://doi.org/10.1096/fasebj.2021.35.s1.00166
https://doi.org/10.1096/fasebj.2021.35.s1.00166
The ornithine hydroxylase known as SidA is a class B flavin monooxygenase that catalyzes the first step in the biosynthesis of hydroxamate-containing siderophores in Aspergillus fumigatus. Crystallographic studies of SidA revealed that the FAD underg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3f674109addec67d0db17f8c9e1e237
https://hdl.handle.net/10919/107583
https://hdl.handle.net/10919/107583
Publikováno v:
Protein Science. 28:90-99
Siderophore A (SidA) from Aspergillus fumigatus is a flavin‐containing monooxygenase that hydroxylates ornithine (Orn) at the amino group of the side chain. Lysine (Lys) also binds to the active site of SidA; however, hydroxylation is not efficient
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79343864e3e6f958d274fdc35b793396
https://doi.org/10.1002/pro.3487
https://doi.org/10.1002/pro.3487
Autor:
Pedro Rodriguez, Camelia Adly, Heba Abdelwahab, S. A. El-Sohaimy, Reeder Robinson, Pablo Sobrado
Publikováno v:
Archives of Biochemistry and Biophysics. 606:180-188
l -lysine ( l -Lys) N6-monooxygenase (NbtG), from Nocardia farcinica, is a flavin-dependent enzyme that catalyzes the hydroxylation of l -Lys in the presence of oxygen and NAD(P)H in the biosynthetic pathway of the siderophore nocobactin. NbtG displa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a11f2b47815517674a8ede34943e2759
https://doi.org/10.1016/j.abb.2016.08.004
https://doi.org/10.1016/j.abb.2016.08.004
Autor:
Nicholas D. Keul, Howard Robinson, Claudia Binda, Andrea Mattevi, Pedro J. Rodriguez, Julia S. Martin del Campo, Pablo Sobrado, Reeder Robinson
Publikováno v:
Journal of Biological Chemistry. 290:12676-12688
N-Hydroxylating monooxygenases are involved in the biosynthesis of iron-chelating hydroxamate-containing siderophores that play a role in microbial virulence. These flavoenzymes catalyze the NADPH- and oxygen-dependent hydroxylation of amines such as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83b3752d27fd0c2d3829b1ea9cb47cd9
https://doi.org/10.1074/jbc.m114.629485
https://doi.org/10.1074/jbc.m114.629485
Autor:
Michael Fedkenheuer, Stefano Franceschini, Jacob Ellerbrock, Pedro J. Rodriguez, Pablo Sobrado, Reeder Robinson, Elvira Romero, Maria Paulina Echandi, Julia S. Martin del Campo
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1844:778-784
Siderophore A (SidA) is a flavin-dependent monooxygenase that catalyzes the NAD(P)H- and oxygen-dependent hydroxylation of ornithine in the biosynthesis of siderophores in Aspergillus fumigatus and is essential for virulence. SidA can utilize both NA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1c011957d1510e515f53188d014d915
https://doi.org/10.1016/j.bbapap.2014.02.005
https://doi.org/10.1016/j.bbapap.2014.02.005
Publikováno v:
Archives of Biochemistry and Biophysics. 532:46-53
Flavin-dependent monooxygenase (FMO) from Methylophaga sp. strain SK1 catalyzes the NADPH- and oxygen-dependent hydroxylation of a number of xenobiotics. Reduction of the flavin cofactor by NADPH is required for activation of molecular oxygen. The ro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b07554fb26cf6303ef91789e7036d5b
https://doi.org/10.1016/j.abb.2013.01.004
https://doi.org/10.1016/j.abb.2013.01.004
Autor:
Heba, Abdelwahab, Reeder, Robinson, Pedro, Rodriguez, Camelia, Adly, Sohby, El-Sohaimy, Pablo, Sobrado
Publikováno v:
Archives of biochemistry and biophysics. 606
l-lysine (l-Lys) N(6)-monooxygenase (NbtG), from Nocardia farcinica, is a flavin-dependent enzyme that catalyzes the hydroxylation of l-Lys in the presence of oxygen and NAD(P)H in the biosynthetic pathway of the siderophore nocobactin. NbtG displays
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::93c3f9befa388d6ba673a3c7ce415b15
https://pubmed.ncbi.nlm.nih.gov/27503802
https://pubmed.ncbi.nlm.nih.gov/27503802