Wilfred (Fred) R. Hagen
Affiliations: | Delft University of Technology, Delft, Zuid-Holland, Netherlands |
Area:
EnzymologyWebsite:
http://www.bt.tudelft.nl/over-faculteit/afdelingen/biotechnologie/people/enzymologie/profdr-wr-fred-hagen/Google:
"Wilfred (Fred) Hagen"Mean distance: 9.67 | S | N | B | C | P |
Parents
Sign in to add mentor| Simon P.J. Albracht | grad student | 1982 | Amsterdam | |
| Edward Charles Slater | grad student | 1982 | Amsterdam | |
| (EPR spectroscopy of metalloproteins; with emphasis on respiratory complexes) | ||||
| Cees Veeger | post-doc | 1985 | Wageningen University | |
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Publications
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| van der Weel L, As KS, Dekker WJC, et al. (2018) ZraP, the most prominent zinc protein under zinc stress conditions has no direct role in in-vivo zinc tolerance in Escherichia coli. Journal of Inorganic Biochemistry. 192: 98-106 |
| Srour B, Strampraad MJF, Hagen WR, et al. (2018) Refolding kinetics of cytochrome c studied with microsecond timescale continuous-flow UV-vis spectroscopy and rapid freeze-quench EPR. Journal of Inorganic Biochemistry. 184: 42-49 |
| van Schie MMCH, Ebrahimi KH, Hagen WR, et al. (2017) Fast and accurate enzyme activity measurements using a chip-based microfluidic calorimeter. Analytical Biochemistry. 544: 57-63 |
| Mitić S, Strampraad MJF, Hagen WR, et al. (2017) Microsecond time-scale kinetics of transient biochemical reactions. Plos One. 12: e0185888 |
| Hagen WR, Hagedoorn PL, Honarmand Ebrahimi K. (2017) The workings of ferritin: a crossroad of opinions. Metallomics : Integrated Biometal Science |
| Ebrahimi KH, Bill E, Hagedoorn PL, et al. (2017) Spectroscopic evidence for the presence of a high-valent Fe(IV) species in the ferroxidase reaction of an archaeal ferritin. Febs Letters |
| Ebrahimi KH, Bill E, Hagedoorn PL, et al. (2016) Spectroscopic evidence for the role of a site of the di-iron catalytic center of ferritins in tuning the kinetics of Fe(ii) oxidation. Molecular Biosystems |
| Duine JA, Strampraad MJ, Hagen WR, et al. (2016) The cooperativity effect in the reaction of soluble quinoprotein (PQQ-containing) glucose dehydrogenase is not due to subunit interaction but to substrate-assisted catalysis. The Febs Journal |
| Vertregt F, Torrelo G, Trunk S, et al. (2016) EPR Study of Substrate Binding to Mn(II) in Hydroxynitrile Lyase from Granulicella tundricola Acs Catalysis. 6: 5081-5085 |
| Ebrahimi KH, Hagedoorn PL, Jacobs D, et al. (2015) Accurate label-free reaction kinetics determination using initial rate heat measurements. Scientific Reports. 5: 16380 |