Knappskog PM - Search Results

1

Crystallization and preliminary diffraction analysis of a truncated homodimer of human phenylalanine hydroxylase.

Erlandsen H, Martinez A, Knappskog PM, Haavik J, Hough E, Flatmark T. Erlandsen H, et al. Among authors: knappskog pm. FEBS Lett. 1997 Apr 7;406(1-2):171-4. doi: 10.1016/s0014-5793(97)00259-7. FEBS Lett. 1997. PMID: 9109411 Free article.

2

Phosphorylation of recombinant human phenylalanine hydroxylase: effect on catalytic activity, substrate activation and protection against non-specific cleavage of the fusion protein by restriction protease.

Døskeland AP, Martinez A, Knappskog PM, Flatmark T. Døskeland AP, et al. Among authors: knappskog pm. Biochem J. 1996 Jan 15;313 ( Pt 2)(Pt 2):409-14. doi: 10.1042/bj3130409. Biochem J. 1996. PMID: 8573072 Free PMC article.

3

Structure/function relationships in human phenylalanine hydroxylase. Effect of terminal deletions on the oligomerization, activation and cooperativity of substrate binding to the enzyme.

Knappskog PM, Flatmark T, Aarden JM, Haavik J, Martínez A. Knappskog PM, et al. Eur J Biochem. 1996 Dec 15;242(3):813-21. doi: 10.1111/j.1432-1033.1996.0813r.x. Eur J Biochem. 1996. PMID: 9022714 Free article.

4

Effect of mutations at Cys237 on the activation state and activity of human phenylalanine hydroxylase.

Knappskog PM, Martínez A. Knappskog PM, et al. FEBS Lett. 1997 Jun 2;409(1):7-11. doi: 10.1016/s0014-5793(97)00465-1. FEBS Lett. 1997. PMID: 9199493 Free article.

5

Domain structure and stability of human phenylalanine hydroxylase inferred from infrared spectroscopy.

Chehin R, Thorolfsson M, Knappskog PM, Martinez A, Flatmark T, Arrondo JL, Muga A. Chehin R, et al. Among authors: knappskog pm. FEBS Lett. 1998 Jan 30;422(2):225-30. doi: 10.1016/s0014-5793(97)01596-2. FEBS Lett. 1998. PMID: 9490012 Free article.

6

Tryptophan fluorescence of human phenylalanine hydroxylase produced in Escherichia coli.

Knappskog PM, Haavik J. Knappskog PM, et al. Biochemistry. 1995 Sep 19;34(37):11790-9. doi: 10.1021/bi00037a017. Biochemistry. 1995. PMID: 7547912

7

The PKU mutation S349P causes complete loss of catalytic activity in the recombinant phenylalanine hydroxylase enzyme.

Knappskog PM, Eiken HG, Martinez A, Flatmark T, Apold J. Knappskog PM, et al. Hum Genet. 1995 Feb;95(2):171-3. doi: 10.1007/BF00209396. Hum Genet. 1995. PMID: 7860062

8

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. Among authors: knappskog pm. Biochem J. 1995 Mar 1;306 ( Pt 2)(Pt 2):589-97. doi: 10.1042/bj3060589. Biochem J. 1995. PMID: 7887915 Free PMC article.

9

PKU mutation G46S is associated with increased aggregation and degradation of the phenylalanine hydroxylase enzyme.

Eiken HG, Knappskog PM, Apold J, Flatmark T. Eiken HG, et al. Among authors: knappskog pm. Hum Mutat. 1996;7(3):228-38. doi: 10.1002/(SICI)1098-1004(1996)7:3<228::AID-HUMU7>3.0.CO;2-6. Hum Mutat. 1996. PMID: 8829656

10

PKU mutation (D143G) associated with an apparent high residual enzyme activity: expression of a kinetic variant form of phenylalanine hydroxylase in three different systems.

Knappskog PM, Eiken HG, Martínez A, Bruland O, Apold J, Flatmark T. Knappskog PM, et al. Hum Mutat. 1996;8(3):236-46. doi: 10.1002/(SICI)1098-1004(1996)8:3<236::AID-HUMU7>3.0.CO;2-7. Hum Mutat. 1996. PMID: 8889583

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