Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Simon Dieterich"'
Autor:
Tina Nybo, Simon Dieterich, Luke F. Gamon, Christine Y. Chuang, Astrid Hammer, Gerald Hoefler, Ernst Malle, Adelina Rogowska-Wrzesinska, Michael J. Davies
Publikováno v:
Redox Biology, Vol 20, Iss , Pp 496-513 (2019)
Basement membranes are specialized extracellular matrices that underlie arterial wall endothelial cells, with laminin being a key structural and biologically-active component. Hypochlorous acid (HOCl), a potent oxidizing and chlorinating agent, is fo
Externí odkaz:
https://doaj.org/article/a949ff32f513463fadbe717ec77d6b45
Publikováno v:
Redox Biology, Vol 28, Iss , Pp - (2020)
Iodide ions (I−) are an essential dietary mineral, and crucial for mental and physical development, fertility and thyroid function. I− is also a high affinity substrate for the heme enzyme myeloperoxidase (MPO), which is involved in bacterial cel
Externí odkaz:
https://doaj.org/article/d505c1cd5e26413fa23c31bd840c490a
Publikováno v:
Redox Biology, Vol 28, Iss, Pp-(2020)
Gamon, L F, Dieterich, S, Ignasiak, M T, Schrameyer, V & Davies, M J 2020, ' Iodide modulates protein damage induced by the inflammation-associated heme enzyme myeloperoxidase ', Redox Biology, vol. 28, 101331 . https://doi.org/10.1016/j.redox.2019.101331
Redox Biology
Gamon, L F, Dieterich, S, Ignasiak, M T, Schrameyer, V & Davies, M J 2020, ' Iodide modulates protein damage induced by the inflammation-associated heme enzyme myeloperoxidase ', Redox Biology, vol. 28, 101331 . https://doi.org/10.1016/j.redox.2019.101331
Redox Biology
Iodide ions (I−) are an essential dietary mineral, and crucial for mental and physical development, fertility and thyroid function. I− is also a high affinity substrate for the heme enzyme myeloperoxidase (MPO), which is involved in bacterial cel
Autor:
Michael J. Davies, Christine Y. Chuang, Astrid Hammer, Simon Dieterich, Luke F. Gamon, Adelina Rogowska-Wrzesinska, Tina Nybo, Ernst Malle, Gerald Hoefler
Publikováno v:
Nybo, T, Dieterich, S, Gamon, L F, Chuang, C Y, Hammer, A, Hoefler, G, Malle, E, Rogowska-Wrzesinska, A & Davies, M J 2019, ' Chlorination and oxidation of the extracellular matrix protein laminin and basement membrane extracts by hypochlorous acid and myeloperoxidase ', Redox Biology, vol. 20, pp. 496-513 . https://doi.org/10.1016/j.redox.2018.10.022
Redox Biology, Vol 20, Iss, Pp 496-513 (2019)
Redox Biology
Redox Biology, Vol 20, Iss, Pp 496-513 (2019)
Redox Biology
Basement membranes are specialized extracellular matrices that underlie arterial wall endothelial cells, with laminin being a key structural and biologically-active component. Hypochlorous acid (HOCl), a potent oxidizing and chlorinating agent, is fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbabf82455fc551721050f1ce060d7ec
https://curis.ku.dk/ws/files/229271387/OA_Chlorination_and_oxidation_of_the_extracellular_matrix_protein_laminin.pdf
https://curis.ku.dk/ws/files/229271387/OA_Chlorination_and_oxidation_of_the_extracellular_matrix_protein_laminin.pdf
Publikováno v:
Free Radical Biology and Medicine. 120:S24
Iodide ions (I-) are an essential dietary mineral, and crucial for mental and physical development, fertility and thyroid function. I- is also a high affinity substrate for the heme enzyme myeloperoxidase (MPO), which is involved in both bacterial ce
Publikováno v:
Journal of Statistical Mechanics: Theory and Experiment. 2009:P07013
For systems in an externally controllable time-dependent potential, the optimal protocol minimizes the mean work spent in a finite-time transition between given initial and final values of a control parameter. For an initially thermalized ensemble, w
Publikováno v:
LETTERS IN MATHEMATICAL PHYSICS
We formulate a correspondence between affine and projective special K\"ahler manifolds of the same dimension. As an application, we show that, under this correspondence, the affine special K\"ahler manifolds in the image of the rigid r-map are mapped
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b796b1a622fa5d34928c4f2b47277e9b
http://livrepository.liverpool.ac.uk/3009526/1/1702.02400v1.pdf
http://livrepository.liverpool.ac.uk/3009526/1/1702.02400v1.pdf