Knappskog PM - Search Results

1

Urea-induced denaturation of human phenylalanine hydroxylase.

Kleppe R, Uhlemann K, Knappskog PM, Haavik J. Kleppe R, et al. Among authors: knappskog pm. J Biol Chem. 1999 Nov 19;274(47):33251-8. doi: 10.1074/jbc.274.47.33251. J Biol Chem. 1999. PMID: 10559199 Free article.

2

A de novo phenylketonuria mutation: ATG (Met) to ATA (Ile) in the start codon of the phenylalanine hydroxylase gene.

Eiken HG, Knappskog PM, Apold J, Skjelkvåle L, Boman H. Eiken HG, et al. Among authors: knappskog pm. Hum Mutat. 1992;1(5):388-91. doi: 10.1002/humu.1380010507. Hum Mutat. 1992. PMID: 1301947

3

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

4

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

5

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.

6

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.

7

DGGE analysis as supplement to SSCP analysis of the phenylalanine hydroxylase gene: detection of eight (one de novo, seven inherited) of nine remaining Norwegian PKU mutations.

Eiken HG, Knappskog PM, Guldberg P, Apold J. Eiken HG, et al. Among authors: knappskog pm. Hum Mutat. 1996;8(1):19-22. doi: 10.1002/(SICI)1098-1004(1996)8:1<19::AID-HUMU2>3.0.CO;2-K. Hum Mutat. 1996. PMID: 8807331 No abstract available.

8

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

9

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

10

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.

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