-
1
-
-
0028609781
-
+ channel beta subunits belong to an NAD(P)H-dependent oxidoreductase superfamily
-
+ channel beta subunits belong to an NAD(P)H-dependent oxidoreductase superfamily. Cell 79 (1994) 1133-1135
-
(1994)
Cell
, vol.79
, pp. 1133-1135
-
-
McCormack, T.1
McCormack, K.2
-
2
-
-
0030821699
-
Comparative anatomy of the aldo-keto reductase superfamily
-
Jez J.M., Bennett M.J., Schlegel B.P., Lewis M., and Penning T.M. Comparative anatomy of the aldo-keto reductase superfamily. Biochem. J. 326 (1997) 625-636
-
(1997)
Biochem. J.
, vol.326
, pp. 625-636
-
-
Jez, J.M.1
Bennett, M.J.2
Schlegel, B.P.3
Lewis, M.4
Penning, T.M.5
-
3
-
-
0032567505
-
Coexpression of the KCNA3B gene product with Kv1.5 leads to a novel A-type potassium
-
Leicher T., Bahring R., Isbrandt D., and Pongs O. Coexpression of the KCNA3B gene product with Kv1.5 leads to a novel A-type potassium. J. Biol. Chem. 273 (1998) 35095-35101
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 35095-35101
-
-
Leicher, T.1
Bahring, R.2
Isbrandt, D.3
Pongs, O.4
-
10
-
-
59049083667
-
Catalytic activity of the beta-subunits of the voltage-gated potassium channels and its regulation by pyridine nucleotides
-
Weiner H., Maser E., Lindahl R., and Plapp B. (Eds), Purdue University Press, West Lafayette, Indiana
-
Tipparaju S.M., Bhatnagar A., and Barski O.A. Catalytic activity of the beta-subunits of the voltage-gated potassium channels and its regulation by pyridine nucleotides. In: Weiner H., Maser E., Lindahl R., and Plapp B. (Eds). Enzymology and Molecular Biology of Carbonyl Metabolism (2006), Purdue University Press, West Lafayette, Indiana 401-410
-
(2006)
Enzymology and Molecular Biology of Carbonyl Metabolism
, pp. 401-410
-
-
Tipparaju, S.M.1
Bhatnagar, A.2
Barski, O.A.3
-
11
-
-
33744970273
-
Modulation of voltage-dependent Shaker family potassium channels by an aldo-keto reductase
-
Weng J., Cao Y., Moss N., and Zhou M. Modulation of voltage-dependent Shaker family potassium channels by an aldo-keto reductase. J. Biol. Chem. 281 (2006) 15194-15200
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 15194-15200
-
-
Weng, J.1
Cao, Y.2
Moss, N.3
Zhou, M.4
-
12
-
-
50149118166
-
Catalytic mechanism and substrate specificity of the beta-subunit of the voltage-gated potassium channel
-
Tipparaju S.M., Barski O.A., Srivastava S., and Bhatnagar A. Catalytic mechanism and substrate specificity of the beta-subunit of the voltage-gated potassium channel. Biochemistry 47 (2008) 8840-8854
-
(2008)
Biochemistry
, vol.47
, pp. 8840-8854
-
-
Tipparaju, S.M.1
Barski, O.A.2
Srivastava, S.3
Bhatnagar, A.4
-
13
-
-
43749106478
-
Functional coupling between the Kv1.1 channel and aldoketoreductase Kvbeta1
-
Pan Y., Weng J., Cao Y., Bhosle R.C., and Zhou M. Functional coupling between the Kv1.1 channel and aldoketoreductase Kvbeta1. J. Biol. Chem. 283 (2008) 8634-8642
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 8634-8642
-
-
Pan, Y.1
Weng, J.2
Cao, Y.3
Bhosle, R.C.4
Zhou, M.5
-
14
-
-
0028837692
-
Human aldose reductase: rate constants for a mechanism including interconversion of ternary complexes by recombinant wild-type enzyme
-
Grimshaw C.E., Bohren K.M., Lai C.J., and Gabbay K.H. Human aldose reductase: rate constants for a mechanism including interconversion of ternary complexes by recombinant wild-type enzyme. Biochemistry 34 (1995) 14356-14365
-
(1995)
Biochemistry
, vol.34
, pp. 14356-14365
-
-
Grimshaw, C.E.1
Bohren, K.M.2
Lai, C.J.3
Gabbay, K.H.4
-
15
-
-
0026701774
-
Studies on pig muscle aldose reductase. Kinetic mechanism and evidence for a slow conformational change upon coenzyme binding
-
Kubiseski T.J., Hyndman D.J., Morjana N.A., and Flynn T.G. Studies on pig muscle aldose reductase. Kinetic mechanism and evidence for a slow conformational change upon coenzyme binding. J Biol. Chem. 267 (1992) 6510-6517
-
(1992)
J Biol. Chem.
, vol.267
, pp. 6510-6517
-
-
Kubiseski, T.J.1
Hyndman, D.J.2
Morjana, N.A.3
Flynn, T.G.4
-
16
-
-
0026719692
-
An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications
-
Wilson D.K., Bohren K.M., Gabbay K.H., and Quiocho F.A. An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257 (1992) 81-84
-
(1992)
Science
, vol.257
, pp. 81-84
-
-
Wilson, D.K.1
Bohren, K.M.2
Gabbay, K.H.3
Quiocho, F.A.4
-
17
-
-
0017184389
-
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
-
Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
-
(1976)
Anal. Biochem.
, vol.72
, pp. 248-254
-
-
Bradford, M.M.1
-
18
-
-
0035969828
-
Binding of pyridine coenzymes to the beta-subunit of the voltage sensitive potassium channels
-
Liu S.Q., Jin H., Zacarias A., Srivastava S., and Bhatnagar A. Binding of pyridine coenzymes to the beta-subunit of the voltage sensitive potassium channels. Chem. Biol. Interact. 130-132 (2001) 955-962
-
(2001)
Chem. Biol. Interact.
, vol.130-132
, pp. 955-962
-
-
Liu, S.Q.1
Jin, H.2
Zacarias, A.3
Srivastava, S.4
Bhatnagar, A.5
-
19
-
-
0015608091
-
Equilibrium binding of nicotinamide nucleotides to lactate dehydrogenases
-
Stinson R.A., and Holbrook J.J. Equilibrium binding of nicotinamide nucleotides to lactate dehydrogenases. Biochem. J. 131 (1973) 719-728
-
(1973)
Biochem. J.
, vol.131
, pp. 719-728
-
-
Stinson, R.A.1
Holbrook, J.J.2
-
20
-
-
0029103124
-
Mechanism of human aldehyde reductase: characterization of the active site pocket
-
Barski O.A., Gabbay K.H., Grimshaw C.E., and Bohren K.M. Mechanism of human aldehyde reductase: characterization of the active site pocket. Biochemistry 34 (1995) 11264-11275
-
(1995)
Biochemistry
, vol.34
, pp. 11264-11275
-
-
Barski, O.A.1
Gabbay, K.H.2
Grimshaw, C.E.3
Bohren, K.M.4
-
21
-
-
33751096178
-
Multiple steps determine the overall rate of the reduction of 5alpha-dihydrotestosterone catalyzed by human type 3 3alpha-hydroxysteroid dehydrogenase: implications for the elimination of androgens
-
Jin Y., and Penning T.M. Multiple steps determine the overall rate of the reduction of 5alpha-dihydrotestosterone catalyzed by human type 3 3alpha-hydroxysteroid dehydrogenase: implications for the elimination of androgens. Biochemistry 45 (2006) 13054-13063
-
(2006)
Biochemistry
, vol.45
, pp. 13054-13063
-
-
Jin, Y.1
Penning, T.M.2
-
22
-
-
0035964171
-
Transient-state and steady-state kinetic studies of the mechanism of NADH-dependent aldehyde reduction catalyzed by xylose reductase from the yeast Candida tenuis
-
Nidetzky B., Klimacek M., and Mayr P. Transient-state and steady-state kinetic studies of the mechanism of NADH-dependent aldehyde reduction catalyzed by xylose reductase from the yeast Candida tenuis. Biochemistry 40 (2001) 10371-10381
-
(2001)
Biochemistry
, vol.40
, pp. 10371-10381
-
-
Nidetzky, B.1
Klimacek, M.2
Mayr, P.3
-
23
-
-
35148871936
-
-
Taylor and Francis Group, LLC, New York, NY 10016, USA
-
Cook P.F., and Cleland W.W. Enzyme Kinetics and Mechanism (2007), Taylor and Francis Group, LLC, New York, NY 10016, USA
-
(2007)
Enzyme Kinetics and Mechanism
-
-
Cook, P.F.1
Cleland, W.W.2
-
24
-
-
0028229517
-
Overexpression and mutagenesis of the cDNA for rat liver 3alpha-hydroxysteroid/dihydrodiol dehydrogenase. Role of cysteines and tyrosines in catalysis
-
Pawlowski J.E., and Penning T.M. Overexpression and mutagenesis of the cDNA for rat liver 3alpha-hydroxysteroid/dihydrodiol dehydrogenase. Role of cysteines and tyrosines in catalysis. J. Biol. Chem. 269 (1994) 13502-13510
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 13502-13510
-
-
Pawlowski, J.E.1
Penning, T.M.2
-
25
-
-
0026531024
-
Novel NADPH-binding domain revealed by the crystal structure of aldose reductase
-
Rondeau J.M., Tete-Favier F., Podjarny A., Reymann J.M., Barth P., Biellmann J.F., and Moras D. Novel NADPH-binding domain revealed by the crystal structure of aldose reductase. Nature 355 (1992) 469-472
-
(1992)
Nature
, vol.355
, pp. 469-472
-
-
Rondeau, J.M.1
Tete-Favier, F.2
Podjarny, A.3
Reymann, J.M.4
Barth, P.5
Biellmann, J.F.6
Moras, D.7
|