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M Lehnerer

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Journal of Biochemical Toxicology|October 1, 1995
Some aspects of the role of cytochrome P-450 isozymes in the N-oxidative transformation of secondary and tertiary amine compoundsP Hlavica, M Lehnerer
Plant Molecular Biology|June 1, 1990
Mitochondrial malate dehydrogenase from watermelon: sequence of cDNA clones and primary structure of the higher-plant precursor proteinC Gietl, M Lehnerer, O Olsen
The Biochemical Journal|September 15, 1996
Histidine residues in rabbit liver microsomal cytochrome P-450 2B4 control electron transfer from NADPH-cytochrome P-450 reductase and cytochrome b5P Hlavica, M Lehnerer, M Eulitz
European Journal of Biochemistry|September 15, 1994
Chemical modification of Tyr34 and Tyr129 in rabbit liver microsomal cytochrome b5 affects interaction with cytochrome P-450 2B4P Hlavica, J Kellermann, I Golly, et al.
Human & Experimental Toxicology|August 1, 1997
Primary aromatic amines: their N-oxidative bioactivationP Hlavica, I Golly, M Lehnerer, et al.
Biochemical and Biophysical Research Communications|January 28, 1999
Some properties of mitochondrial adrenodoxin associated with its nonconventional electron donor function toward rabbit liver microsomal cytochrome P450 2B4M Lehnerer, J Schulze, R Bernhardt, et al.
Biochemical and Biophysical Research Communications|April 25, 2000
Residue 285 in cytochrome P450 2B4 lacking the NH(2)-terminal hydrophobic sequence has a role in the functional association of NADPH-cytochrome P450 reductaseJ Schulze, K Tschöp, M Lehnerer, et al.
Biochemistry and Molecular Biology International|June 12, 1998
Amino acid residue 250 has a functional role in the assembly of rabbit liver microsomal cytochrome P450 2B4J Schulze, M Lehnerer, D F Lewis, et al.
Biochimica Et Biophysica Acta|August 17, 1995
Rabbit liver cytochrome P-450 2B5: high-level expression of the full-length protein in Escherichia coli, purification, and catalytic activityM Lehnerer, J Schulze, A Petzold, et al.
Journal of Biochemistry|March 25, 2000
Identification of key residues in rabbit liver microsomal cytochrome P450 2B4: importance in interactions with NADPH-cytochrome P450 reductaseM Lehnerer, J Schulze, K Achterhold, et al.
Pageof 2

Showing results (1-10 of 15) with videos related to

Sort By:
Pageof 2
Journal of Biochemical Toxicology|October 1, 1995
Some aspects of the role of cytochrome P-450 isozymes in the N-oxidative transformation of secondary and tertiary amine compoundsP Hlavica, M Lehnerer
Plant Molecular Biology|June 1, 1990
Mitochondrial malate dehydrogenase from watermelon: sequence of cDNA clones and primary structure of the higher-plant precursor proteinC Gietl, M Lehnerer, O Olsen
The Biochemical Journal|September 15, 1996
Histidine residues in rabbit liver microsomal cytochrome P-450 2B4 control electron transfer from NADPH-cytochrome P-450 reductase and cytochrome b5P Hlavica, M Lehnerer, M Eulitz
European Journal of Biochemistry|September 15, 1994
Chemical modification of Tyr34 and Tyr129 in rabbit liver microsomal cytochrome b5 affects interaction with cytochrome P-450 2B4P Hlavica, J Kellermann, I Golly, et al.
Human & Experimental Toxicology|August 1, 1997
Primary aromatic amines: their N-oxidative bioactivationP Hlavica, I Golly, M Lehnerer, et al.
Biochemical and Biophysical Research Communications|January 28, 1999
Some properties of mitochondrial adrenodoxin associated with its nonconventional electron donor function toward rabbit liver microsomal cytochrome P450 2B4M Lehnerer, J Schulze, R Bernhardt, et al.
Biochemical and Biophysical Research Communications|April 25, 2000
Residue 285 in cytochrome P450 2B4 lacking the NH(2)-terminal hydrophobic sequence has a role in the functional association of NADPH-cytochrome P450 reductaseJ Schulze, K Tschöp, M Lehnerer, et al.
Biochemistry and Molecular Biology International|June 12, 1998
Amino acid residue 250 has a functional role in the assembly of rabbit liver microsomal cytochrome P450 2B4J Schulze, M Lehnerer, D F Lewis, et al.
Biochimica Et Biophysica Acta|August 17, 1995
Rabbit liver cytochrome P-450 2B5: high-level expression of the full-length protein in Escherichia coli, purification, and catalytic activityM Lehnerer, J Schulze, A Petzold, et al.
Journal of Biochemistry|March 25, 2000
Identification of key residues in rabbit liver microsomal cytochrome P450 2B4: importance in interactions with NADPH-cytochrome P450 reductaseM Lehnerer, J Schulze, K Achterhold, et al.
Pageof 2