Bohren KM - Search Results

1

Characterization of the human aldehyde reductase gene and promoter.

Barski OA, Gabbay KH, Bohren KM. Barski OA, et al. Among authors: bohren km. Genomics. 1999 Sep 1;60(2):188-98. doi: 10.1006/geno.1999.5915. Genomics. 1999. PMID: 10486210

2

Catalytic effectiveness of human aldose reductase. Critical role of C-terminal domain.

Bohren KM, Grimshaw CE, Gabbay KH. Bohren KM, et al. J Biol Chem. 1992 Oct 15;267(29):20965-70. J Biol Chem. 1992. PMID: 1400412 Free article.

3

An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications.

Wilson DK, Bohren KM, Gabbay KH, Quiocho FA. Wilson DK, et al. Among authors: bohren km. Science. 1992 Jul 3;257(5066):81-4. doi: 10.1126/science.1621098. Science. 1992. PMID: 1621098

4

Expression of human aldose and aldehyde reductases. Site-directed mutagenesis of a critical lysine 262.

Bohren KM, Page JL, Shankar R, Henry SP, Gabbay KH. Bohren KM, et al. J Biol Chem. 1991 Dec 15;266(35):24031-7. J Biol Chem. 1991. PMID: 1748675 Free article.

5

The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases.

Bohren KM, Bullock B, Wermuth B, Gabbay KH. Bohren KM, et al. J Biol Chem. 1989 Jun 5;264(16):9547-51. J Biol Chem. 1989. PMID: 2498333 Free article.

6

Human carbonyl reductase. Nucleotide sequence analysis of a cDNA and amino acid sequence of the encoded protein.

Wermuth B, Bohren KM, Heinemann G, von Wartburg JP, Gabbay KH. Wermuth B, et al. Among authors: bohren km. J Biol Chem. 1988 Nov 5;263(31):16185-8. J Biol Chem. 1988. PMID: 3141401 Free article.

7

Human aldose reductase: rate constants for a mechanism including interconversion of ternary complexes by recombinant wild-type enzyme.

Grimshaw CE, Bohren KM, Lai CJ, Gabbay KH. Grimshaw CE, et al. Among authors: bohren km. Biochemistry. 1995 Nov 7;34(44):14356-65. doi: 10.1021/bi00044a012. Biochemistry. 1995. PMID: 7578039

8

Human aldose reductase: subtle effects revealed by rapid kinetic studies of the C298A mutant enzyme.

Grimshaw CE, Bohren KM, Lai CJ, Gabbay KH. Grimshaw CE, et al. Among authors: bohren km. Biochemistry. 1995 Nov 7;34(44):14366-73. doi: 10.1021/bi00044a013. Biochemistry. 1995. PMID: 7578040

9

Human aldose reductase: pK of tyrosine 48 reveals the preferred ionization state for catalysis and inhibition.

Grimshaw CE, Bohren KM, Lai CJ, Gabbay KH. Grimshaw CE, et al. Among authors: bohren km. Biochemistry. 1995 Nov 7;34(44):14374-84. doi: 10.1021/bi00044a014. Biochemistry. 1995. PMID: 7578041

10

Mechanism of human aldehyde reductase: characterization of the active site pocket.

Barski OA, Gabbay KH, Grimshaw CE, Bohren KM. Barski OA, et al. Among authors: bohren km. Biochemistry. 1995 Sep 5;34(35):11264-75. doi: 10.1021/bi00035a036. Biochemistry. 1995. PMID: 7669785

A H112Q mutant aldehyde reductase exhibited a substantial decrease in catalytic efficiency (kcat/Km) for hydrophilic (average 150-fold) and aromatic substrates (average 4200-fold) and 50-fold higher IC50 values for a variety of inhibitors than that of the wild-type enzyme. …

A H112Q mutant aldehyde reductase exhibited a substantial decrease in catalytic efficiency (kcat/Km) for hydrophilic (average 150-fol …

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