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Arc is a flexible modular protein capable of reversible self-oligomerization.
Myrum C, Baumann A, Bustad HJ, Flydal MI, Mariaule V, Alvira S, Cuéllar J, Haavik J, Soulé J, Valpuesta JM, Márquez JA, Martinez A, Bramham CR. Myrum C, et al. Among authors: martinez a. Biochem J. 2015 May 15;468(1):145-58. doi: 10.1042/BJ20141446. Biochem J. 2015. PMID: 25748042 Free PMC article.
EPR and 1H-NMR spectroscopic studies on the paramagnetic iron at the active site of phenylalanine hydroxylase and its interaction with substrates and inhibitors.
Martínez A, Andersson KK, Haavik J, Flatmark T. Martínez A, et al. Eur J Biochem. 1991 Jun 15;198(3):675-82. doi: 10.1111/j.1432-1033.1991.tb16066.x. Eur J Biochem. 1991. PMID: 1646718 Free article.
The EPR-detectable iron of the bovine enzyme was found to be present as a high-spin form (S = 5/2) in different ligand field symmetries depending on medium conditions (buffer ions) and the presence of ligands known to bind at the active site. ...The results support our rec …
The EPR-detectable iron of the bovine enzyme was found to be present as a high-spin form (S = 5/2) in different ligand field symmetri …
Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Isolation and characterization of the wild-type enzyme.
Martinez A, Knappskog PM, Olafsdottir S, Døskeland AP, Eiken HG, Svebak RM, Bozzini M, Apold J, Flatmark T. Martinez A, et al. Biochem J. 1995 Mar 1;306 ( Pt 2)(Pt 2):589-97. doi: 10.1042/bj3060589. Biochem J. 1995. PMID: 7887915 Free PMC article.
8,245 results