Zobrazeno 1 - 10
of 87
pro vyhledávání: '"Steen V. Petersen"'
Autor:
Ann Huysseune, Ulrike G. Larsen, Daria Larionova, Cecilie L. Matthiesen, Steen V. Petersen, Marc Muller, P. Eckhard Witten
Publikováno v:
Biomolecules, Vol 13, Iss 12, p 1780 (2023)
DAF-FM DA is widely used as a live staining compound to show the presence of nitric oxide (NO) in cells. Applying this stain to live zebrafish embryos is known to indicate early centers of bone formation, but the precise (cellular) location of the si
Externí odkaz:
https://doaj.org/article/693f2f7bbcea4a379779e7d4e17538f4
Publikováno v:
Redox Biology, Vol 26, Iss , Pp - (2019)
Superoxide dismutase 3 (SOD3) is an extracellular enzyme with the capacity to modulate extracellular redox conditions by catalyzing the dismutation of superoxide to hydrogen peroxide. In addition to synthesis and release of this extracellular protein
Externí odkaz:
https://doaj.org/article/e7178fb2b25d409599965ce39c498cff
Autor:
Dennis V. Pedersen, Trine A. F. Gadeberg, Caroline Thomas, Yong Wang, Nicolas Joram, Rasmus K. Jensen, Sofia M. M. Mazarakis, Margot Revel, Carine El Sissy, Steen V. Petersen, Kresten Lindorff-Larsen, Steffen Thiel, Nick S. Laursen, Véronique Fremeaux-Bacchi, Gregers R. Andersen
Publikováno v:
Frontiers in Immunology, Vol 10 (2019)
Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system. Here we present two crystal structures of FP and two structure
Externí odkaz:
https://doaj.org/article/ac896c2448754a3fb20a2396a833fbe7
Publikováno v:
Redox Biology, Vol 1, Iss 1, Pp 24-31 (2013)
Superoxide dismutase (EC-SOD) controls the level of superoxide in the extracellular space by catalyzing the dismutation of superoxide into hydrogen peroxide and molecular oxygen. In addition, the enzyme reacts with hydrogen peroxide in a peroxidase r
Externí odkaz:
https://doaj.org/article/a48dbe0df21a48f18685a2b2e26fdbb4
Autor:
Jan J. Enghild, Esben S. Sørensen, Ida Bregenov, Carsten Scavenius, Gitte N Schytte, Katarzyna Kjøge, Brian Christensen, Steen V. Petersen
Publikováno v:
Schytte, G N, Christensen, B, Bregenov, I, Kjøge, K, Scavenius, C, Petersen, S V, Enghild, J J & Sørensen, E S 2020, ' FAM20C phosphorylation of the RGDSVVYGLR motif in osteopontin inhibits interaction with the αvβ3 integrin ', Journal of Cellular Biochemistry, vol. 121, no. 12, pp. 4809-4818 . https://doi.org/10.1002/jcb.29708
Osteopontin (OPN) is a ubiquitously expressed, multifunctional, and highly phosphorylated protein. OPN contains two neighboring integrin-binding motifs, RGD and SVVYGLR, which mediate interaction with cells. Phosphorylation and proteolytic processing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80e2a04a8dfddfc1e7221fa3cc9022d0
https://doi.org/10.1002/jcb.29708
https://doi.org/10.1002/jcb.29708
Publikováno v:
Abd El-Maksoud, A A, Cheng, W, Petersen, S V, Pandiselvam, R & Guo, Z 2022, ' Covalent phenolic acid-grafted β-lactoglobulin conjugates : Synthesis, characterization, and evaluation of their multifunctional properties ', LWT, vol. 172, 114215 . https://doi.org/10.1016/j.lwt.2022.114215
In our work, covalent conjugates of β-Lactoglobulin (βLg) with different phenolic acids (PhAs) including caffeic (CA), ferulic (FA), sinapic (SA), and gallic (GA) acids were synthesized by using carbodiimide chemistry. The resulting βLg-PhA conjug
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0c09bcba6893851b15aecba7d8b0735
https://doi.org/10.1016/j.lwt.2022.114215
https://doi.org/10.1016/j.lwt.2022.114215
Autor:
Claus Oxvig, Ulrike G. Larsen, Jan J. Enghild, Ebbe Toftgaard Poulsen, Kasper Kjaer-Sorensen, Cecilie Linneberg Matthiesen, Annemarie Brüel, Steen V. Petersen, Astrid S. Torslev, Jesper Skovhus Thomsen, Lili Hu
Publikováno v:
Matthiesen, C L, Hu, L, Torslev, A S, Poulsen, E T, Larsen, U G, Kjaer-Sorensen, K, Thomsen, J S, Brüel, A, Enghild, J J, Oxvig, C & Petersen, S V 2021, ' Superoxide dismutase 3 is expressed in bone tissue and required for normal bone homeostasis and mineralization ', Free Radical Biology and Medicine, vol. 164, pp. 399-409 . https://doi.org/10.1016/j.freeradbiomed.2021.01.027
Superoxide dismutase 3 (SOD3) is an extracellular protein with the capacity to convert superoxide into hydrogen peroxide, an important secondary messenger in redox regulation. To investigate the utility of zebrafish in functional studies of SOD3 and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::136ff5e56d25f2e668189fc1df9e1427
https://pure.au.dk/portal/da/publications/superoxide-dismutase-3-is-expressed-in-bone-tissue-and-required-for-normal-bone-homeostasis-and-mineralization(67f93f18-385d-4678-9979-bf863f5237a0).html
https://pure.au.dk/portal/da/publications/superoxide-dismutase-3-is-expressed-in-bone-tissue-and-required-for-normal-bone-homeostasis-and-mineralization(67f93f18-385d-4678-9979-bf863f5237a0).html
Publikováno v:
Petersen, S V, Poulsen, N B, Matthiesen, C L & Vilhardt, F 2021, ' Novel and converging ways of NOX2 and SOD3 in trafficking and redox signaling in macrophages ', Antioxidants, vol. 10, no. 2, 172 . https://doi.org/10.3390/antiox10020172
Antioxidants
Petersen, S V, Poulsen, N B, Matthiesen, C L & Vilhardt, F 2021, ' Novel and converging ways of NOX2 and SOD3 in trafficking and redox signaling in macrophages ', Antioxidants, vol. 10, no. 2, 172, pp. 1-16 . https://doi.org/10.3390/antiox10020172
Antioxidants, Vol 10, Iss 172, p 172 (2021)
Antioxidants
Petersen, S V, Poulsen, N B, Matthiesen, C L & Vilhardt, F 2021, ' Novel and converging ways of NOX2 and SOD3 in trafficking and redox signaling in macrophages ', Antioxidants, vol. 10, no. 2, 172, pp. 1-16 . https://doi.org/10.3390/antiox10020172
Antioxidants, Vol 10, Iss 172, p 172 (2021)
Macrophages and related tissue macrophage populations use the classical NADPH oxidase (NOX2) for the regulated production of superoxide and derived oxidants for pathogen combat and redox signaling. With an emphasis on macrophages, we discuss how sort
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9f582bbcebb0de402b391cbefbb0e94
https://pure.au.dk/portal/da/publications/novel-and-converging-ways-of-nox2-and-sod3-in-trafficking-and-redox-signaling-in-macrophages(f20c088d-905e-486a-95cd-7910c77407a0).html
https://pure.au.dk/portal/da/publications/novel-and-converging-ways-of-nox2-and-sod3-in-trafficking-and-redox-signaling-in-macrophages(f20c088d-905e-486a-95cd-7910c77407a0).html
Autor:
Jacob Flyvholm Cramer, Peder Madsen, Lone Tjener Pallesen, Camilla Gustafsen, Claus Munck Petersen, Steen V. Petersen, Søren Thirup
Publikováno v:
Molecular and Cellular Biology
Pallesen, L T, Gustafsen, C, Cramer, J, Petersen, S V, Thirup, S S, Madsen, P & Petersen, C M 2020, ' PAK kinases targets sortilin and modulates its sorting ', Molecular and Cellular Biology, vol. 40, no. 3, e00411-19 . https://doi.org/10.1128/MCB.00411-19
Pallesen, L T, Gustafsen, C, Cramer, J, Petersen, S V, Thirup, S S, Madsen, P & Petersen, C M 2020, ' PAK kinases targets sortilin and modulates its sorting ', Molecular and Cellular Biology, vol. 40, no. 3, e00411-19 . https://doi.org/10.1128/MCB.00411-19
The multifunctional type 1 receptor sortilin is involved in endocytosis and intracellular transport of ligands. The short intracellular domain of sortilin binds several cytoplasmic adaptor proteins (e.g., the AP-1 complex and GGA1 to -3), most of whi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e08197a4c91b050e8bce077ec5045f1
http://europepmc.org/articles/PMC6965034
http://europepmc.org/articles/PMC6965034
Superoxide dismutase 3 (SOD3 or EC-SOD) is the only scavenger of superoxide in the extracellular space allowing for the catalyzed dismutation of the superoxide radical into hydrogen peroxide. The activity and distribution of the enzyme are regulated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ef12c029d42ad89a87613815d0817250
https://doi.org/10.1016/b978-0-12-818606-0.00012-2
https://doi.org/10.1016/b978-0-12-818606-0.00012-2