K. Kumaki

发表

Role of the Dnmt3 family in de novo methylation of imprinted and repetitive sequences during male germ cell development in the mouse.

Y. Kohara, E. Li, M. Nozaki, 2007, Human molecular genetics.

Determination of 22-oxacalcitriol, a new analog of 1alpha,25-dihydroxyvitamin D3, in human serum by liquid chromatography-mass spectrometry.

K. Kumaki, M. Ishigai, Y. Asoh, 1998, Journal of chromatography. B, Biomedical sciences and applications.

Neoplastic Transformation of Normal Rat Embryo Fibroblasts by a Mutated p53 and an Activated ras Oncogene Induces Parathyroid Hormone-related Peptide Gene Expression and Causes Hypercalcemia in Nude Mice(*)

T. Motokura, E. Ogata, K. Ikeda, 1995, The Journal of Biological Chemistry.

Genetic differences in induction of cytosol reduced-NAD(P):menadione oxidoreductase and microsomal aryl hydrocarbon hydroxylase in the mouse.

D. Nebert, K. Kumaki, J. Shire, 1977, The Journal of biological chemistry.

Induction of Aryl Hydrocarbon Hydroxylase Activity in Various Cell Cultures by 2,3,7,8-Tetrachlorodibenzo-p-dioxin

D. Nebert, K. Kumaki, A. Niwa, 1975 .

Genetic expression of aryl hydrocarbon hydroxylase activity in the mouse. Distinction between the "responsive" homozygote and heterozygote at the Ah locus.

D. Nebert, A. Poland, K. Kumaki, 1975, Archives of Biochemistry and Biophysics.

The [53–63] amino acid portion of the parathyroid hormone molecule is essential for the stimulatory effect of carboxyl-terminal PTH fragments on alkaline phosphatase activity in dexamethasone-treated rat osteoblastic osteosarcoma cells, ROS 17/2.8

K. Chihara, T. Fujita, S. Sakakibara, 1994, Journal of Bone and Mineral Metabolism.

Binding of the carboxyl-terminal fragments of human parathyroid hormone to rat osteoblastic cells ROS 17/2.8

E. Ogata, K. Chihara, S. Sakakibara, 1994, Journal of Bone and Mineral Metabolism.

Circular dichroism studies on the binding of type I substrates and reverse type I compounds to rabbit liver microsomal cytochrome P-450.

D. Nebert, K. Kumaki, H. Shichi, 1978, Chemico-biological interactions.

Mechanism for the nonlinear pharmacokinetics of erythropoietin in rats.

Y. Kato, K. Kumaki, H. Kamiyama, 1997, The Journal of pharmacology and experimental therapeutics.

Characteristics of mass spectrometric analyses coupled to gas chromatography and liquid chromatography for 22-oxacalcitriol, a vitamin D3 analog, and related compounds.

K. Kumaki, M. Ishigai, Y. Ishitani, 1997, Journal of chromatography. B, Biomedical sciences and applications.

Distribution of 1,25-dihydroxyvitamin D3[22-oxa] in vivo receptor binding in adult and developing skin

W. Stumpf, K. Kumaki, N. Hayakawa, 2005, Archives of Dermatological Research.

W. Stumpf, K. Kumaki, N. Hayakawa, 1998, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

In vivo metabolism off the vitamin D analog, 22-oxacalcitriol: Evidence for side-chain truncation and 17-hydroxylation

K. Kumaki, M. Ishigai, Y. Ishitani, 1998, The Journal of Steroid Biochemistry and Molecular Biology.

The 69-84 amino acid region of the parathyroid hormone molecule is essential for the interaction of the hormone with the binding sites with carboxyl-terminal specificity.

K. Chihara, T. Fujita, T. Kimura, 1996, Endocrinology.

Comparative EPR study on high-spin ferric porphine complexes and cytochrome P-450 having rhombic character.

D. Nebert, M. Sato, K. Kumaki, 1977, Biochimica et biophysica acta.

Differential induction of murine Ah locus-associated monooxygenase activities in rabbit liver and kidney.

S. Thorgeirsson, A. Boobis, D. Nebert, 1975, Biochemical pharmacology.

DIFFERENTIAL TIME COURSE OF INDUCTION OF 1α,25-DIHYDROXYVITAMIN D3-24-HYDROXYLASE mRNA EXPRESSION IN RATS BY 1α,25-DIHYDROXYVITAMIN D3 AND ITS ANALOGS

K. Kumaki, T. Furuichi, Y. Ohyama, 1997 .

Molecular Cloning and Expression of Serum Calcium- decreasing Factor (Caldecrin) (*)

T. Saheki, M. Akiyama, M. Tomomura, 1995, The Journal of Biological Chemistry.

Spectral evidence for weak ligand in sixth position of hepatic microsomal cytochrome P-450 low spin ferric iron in vivo.

D. Nebert, K. Kumaki, 1978, Pharmacology.

Effect of acyl residues of hydroxamic acids on urease inhibition.

K. Kobashi, K. Kumaki, J. Hase, 1971, Biochimica et biophysica acta.

ASSOCIATION ON TYPE I, TYPE II, AND REVERSE TYPE I DIFFERENCE SPECTRA WITH ABSOLUTE SPIN STATE OF CYTOCHROME P-450 IRON

D. Nebert, K. Kumaki, H. Kon, 1977 .

Correlation of type I, type II, and reverse type I difference spectra with absolute changes in spin state of hepatic microsomal cytochrome P-450 iron from five mammalian species.

D W Nebert, D. Nebert, M. Sato, 1978, The Journal of biological chemistry.

Evidence for the uptake of a vitamin D analogue (OCT) by a human carcinoma and its effect of suppressing the transcription of parathyroid hormone-related peptide gene in vivo.

E. Ogata, K. Ikeda, K. Kumaki, 1994, The Journal of biological chemistry.

Pharmacokinetics of erythropoietin in genetically anemic mice.

Y. Kato, Y Kato, Y Sugiyama, 1998, Drug metabolism and disposition: the biological fate of chemicals.

A comparison between daily and thrice-weekly i.v. administration of 1,25-dihydroxy-22-oxavitamin D(3) regarding suppression of parathyroid hormone secretion and calcaemic action in uraemic rats.

E. Slatopolsky, K. Kurokawa, M. Fukagawa, 2002, Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association.

1,25-Dihydroxyvitamin D3 and 22-oxa-1,25-dihydroxyvitamin D3 in vivo nuclear receptor binding in developing bone during endochondral and intramembranous ossification

W. Stumpf, Y. Tsuchiya, K. Kumaki, 1994, Histochemistry.

Measuring Methods for Ultra-Low Light Intensity and Their Application to Extra-Weak Spontaneous Bioluminescence from Living Tissues

H. Inaba, K. Kumaki, K. Mizuno, 1973 .

Immunological response to repeated administration of recombinant human erythropoietin in rats: biphasic effect on its pharmacokinetics.

Y. Kato, K. Kumaki, H. Kamiyama, 1997, Drug metabolism and disposition: the biological fate of chemicals.