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Glucose utilization by tumor cells: the enzyme hexokinase autophosphorylates both its N- and C-terminal halves.
Arora KK, Pedersen PL. Arora KK, et al. Arch Biochem Biophys. 1993 Aug 1;304(2):515-8. doi: 10.1006/abbi.1993.1384. Arch Biochem Biophys. 1993. PMID: 8346927 No abstract available.
Structure/function relationships in hexokinase. Site-directed mutational analyses and characterization of overexpressed fragments implicate different functions for the N- and C-terminal halves of the enzyme.
Arora KK, Filburn CR, Pedersen PL. Arora KK, et al. J Biol Chem. 1993 Aug 25;268(24):18259-66. J Biol Chem. 1993. PMID: 8349702
Four amino acid residues, Ser603, Asp657, Glu708, and Glu742, located in the C-terminal half of the tumor mitochondrial enzyme have been shown to be essential for enzyme function (Arora, K. ...
Four amino acid residues, Ser603, Asp657, Glu708, and Glu742, located in the C-terminal half of the tumor mitochondrial enzyme have been sho …
Glucokinase of Escherichia coli: induction in response to the stress of overexpressing foreign proteins.
Arora KK, Pedersen PL. Arora KK, et al. Arch Biochem Biophys. 1995 Jun 1;319(2):574-8. doi: 10.1006/abbi.1995.1333. Arch Biochem Biophys. 1995. PMID: 7786044
Glucose phosphorylation. Interaction of a 50-amino acid peptide of yeast hexokinase with trinitrophenyl ATP.
Arora KK, Shenbagamurthi P, Fanciulli M, Pedersen PL. Arora KK, et al. J Biol Chem. 1990 Mar 25;265(9):5324-8. J Biol Chem. 1990. PMID: 2318895
Glucose phosphorylation in tumor cells. Cloning, sequencing, and overexpression in active form of a full-length cDNA encoding a mitochondrial bindable form of hexokinase.
Arora KK, Fanciulli M, Pedersen PL. Arora KK, et al. J Biol Chem. 1990 Apr 15;265(11):6481-8. J Biol Chem. 1990. PMID: 2318862
In rapidly growing tumor cells exhibiting high glucose catabolic rates, the enzyme hexokinase is markedly elevated and bound in large amounts (50-80% of the total cell activity) to the outer mitochondrial membrane (Arora, K.K., and Pedersen, P.L. (1988) J. ...
In rapidly growing tumor cells exhibiting high glucose catabolic rates, the enzyme hexokinase is markedly elevated and bound in large amount …
Hexokinase receptors: preferential enzyme binding in normal cells to nonmitochondrial sites and in transformed cells to mitochondrial sites.
Arora KK, Parry DM, Pedersen PL. Arora KK, et al. J Bioenerg Biomembr. 1992 Feb;24(1):47-53. doi: 10.1007/BF00769530. J Bioenerg Biomembr. 1992. PMID: 1506408 Review.
Glucose phosphorylation. Site-directed mutations which impair the catalytic function of hexokinase.
Arora KK, Filburn CR, Pedersen PL. Arora KK, et al. J Biol Chem. 1991 Mar 25;266(9):5359-62. J Biol Chem. 1991. PMID: 2005085
Significantly, studies on the hepatoma enzyme conducted in this laboratory (Arora, K.K., Fanciulli, M., and Pedersen, P.L. (1990) J. ...
Significantly, studies on the hepatoma enzyme conducted in this laboratory (Arora, K.K., Fanciulli, M., and Pedersen, P.L. (1990) J. …
Expression and function of the gonadotropin-releasing hormone receptor are dependent on a conserved apolar amino acid in the third intracellular loop.
Chung HO, Yang Q, Catt KJ, Arora KK. Chung HO, et al. Among authors: arora kk. J Biol Chem. 1999 Dec 10;274(50):35756-62. doi: 10.1074/jbc.274.50.35756. J Biol Chem. 1999. PMID: 10585457
Mediation of cyclic AMP signaling by the first intracellular loop of the gonadotropin-releasing hormone receptor.
Arora KK, Krsmanovic LZ, Mores N, O'Farrell H, Catt KJ. Arora KK, et al. J Biol Chem. 1998 Oct 2;273(40):25581-6. doi: 10.1074/jbc.273.40.25581. J Biol Chem. 1998. PMID: 9748222
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