N. Hayashi

发表

Heme mediates derepression of Maf recognition element through direct binding to transcription repressor Bach1

S Shibahara, O. Nakajima, S. Shibahara, 2001, The EMBO journal.

Conserved structure, regulatory elements, and transcriptional regulation from the GATA-1 gene testis promoter.

J. D. Engel, E. Ito, S. Takahashi, 1997, Journal of biochemistry.

Identification of Bach2 as a B‐cell‐specific partner for small Maf proteins that negatively regulate the immunoglobulin heavy chain gene 3′ enhancer

L. Madisen, M. Groudine, H. Nakauchi, 1998, The EMBO journal.

Differential Regulation of Coproporphyrinogen Oxidase Gene Between Erythroid and Nonerythroid Cells

Masayuki Yamamoto, T. Nagai, A. Kobayashi, 1998 .

Differential regulation of coproporphyrinogen oxidase gene between erythroid and nonerythroid cells.

S. Takahashi, T. Nagai, A. Kobayashi, 1998, Blood.

Cloning and characterization of a novel erythroid cell-derived CNC family transcription factor heterodimerizing with the small Maf family proteins

K. Itoh, K. Igarashi, N. Hayashi, 1995, Molecular and cellular biology.

Oxygen equilibrium of hemoglobin Hiroshima.

N. Hayashi, G. Kikuchi, K. Mihara, 1968, Biochemical and biophysical research communications.

Expression of GATA transcription factors in myelogenous and lymphoblastic leukemia cells.

M. Minegishi, N. Hayashi, M. Yamamoto, 1997, International journal of hematology.

Lysine 129 of CD38 (ADP-ribosyl Cyclase/Cyclic ADP-ribose Hydrolase) Participates in the Binding of ATP to Inhibit the Cyclic ADP-ribose Hydrolase*

S. Takasawa, N. Hayashi, H. Munakata, 1997, The Journal of Biological Chemistry.

Molecular defect in human erythropoietic protoporphyria with fatal liver failure

Masayuki Yamamoto, Kyoichi Inoue, S. Taketani, 1993, Human Genetics.

Novel regulation of δ-aminolevulinate synthase in the rat harderian gland

K. Goto, Masayuki Yamamoto, T. Nagai, 1997 .

Cloning of a coproporphyrinogen oxidase promoter regulatory element binding protein.

S. Takahashi, K. Furuyama, K. Igarashi, 2000, Biochemical and biophysical research communications.

Molecular Cloning and Functional Characterization of a New Cap’n’ Collar Family Transcription Factor Nrf3*

T. Toki, E. Ito, K. Igarashi, 1999, The Journal of Biological Chemistry.

Conditional expression of the ubiquitous transcription factor MafK induces erythroleukemia cell differentiation.

K. Itoh, K. Igarashi, N. Hayashi, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Regulation of synthesis and intracellular translocation of delta-aminolevulinate synthase by heme and its relation to the heme saturation of tryptophan pyrrolase in rat liver.

N. Hayashi, M. Yamamoto, G. Kikuchi, 1981, Archives of biochemistry and biophysics.

Regulation by heme of synthesis and intracellular translocation of δ-aminolevulinate synthase in the liver

N. Hayashi, G. Kikuchi, 1981, Molecular and Cellular Biochemistry.

Translational inhibition by heme of the synthesis of hepatic delta-aminolevulinate synthase in a cell-free system.

N. Hayashi, M. Yamamoto, G. Kikuchi, 1983, Biochemical and biophysical research communications.

Evidence for the transcriptional inhibition by heme of the synthesis of delta-aminolevulinate synthase in rat liver.

N. Hayashi, M. Yamamoto, G. Kikuchi, 1982, Biochemical and biophysical research communications.

and Aorta-Gonads and Mesonephros Region The Mouse GATA-2 Gene is Expressed in the Para-Aortic Splanchnopleura

J. D. Engel, J. Engel, Masayuki Yamamoto, 2013 .

Heme deficiency in erythroid lineage causes differentiation arrest and cytoplasmic iron overload

O. Nakajima, K. Furuyama, S. Sassa, 1999, The EMBO journal.

Pyridoxine refractory X-linked sideroblastic anemia caused by a point mutation in the erythroid 5-aminolevulinate synthase gene.

T. Nagai, K. Furuyama, N. Hayashi, 1997, Blood.

Erythroleukemia differentiation. Distinctive responses of the erythroid-specific and the nonspecific delta-aminolevulinate synthase mRNA.

S. Sassa, N. Hayashi, M. Yamamoto, 1991, The Journal of biological chemistry.

Absence of C282Y and H63D mutations of the hemochromatosis gene in Japanese patients with sideroblastic anemia

K. Furuyama, K. Anderson, S. Sassa, 1999, American journal of hematology.

Relation of the extra-sequence of the precursor form of chicken liver delta-aminolevulinate synthase to its quaternary structure and catalytic properties.

N. Hayashi, G. Kikuchi, N. Watanabe, 1984, Archives of biochemistry and biophysics.

Regulation of NF-E2 Activity in Erythroleukemia Cell Differentiation*

T. Nagai, K. Furuyama, K. Igarashi, 1998, The Journal of Biological Chemistry.

Expression of c-erbB-2 in human esophageal carcinoma cells: overexpression correlated with gene amplification or with GATA-3 transcription factor expression.

H. Sasano, T. Yamamoto, N. Hayashi, 1993, Anticancer research.

OXYGEN EQUILIBRIUM OF HEMOGLOBIN M-IWATE.

N. Hayashi, G. Kikuchi, A. Tamura, 1964, Biochimica et biophysica acta.

ON THE REACTIVITY OF HEMOGLOBIN MIWATE.

N. Hayashi, G. Kikuchi, Y. Motokawa, 1964, Archives of biochemistry and biophysics.

Mechanism of allylisopropylacetamide-induced increase of delta-aminolevulinate synthetase in liver mitochondria. IV. Accumulation of the enzyme in the soluble fraction of rat liver.

B. Yoda, N. Hayashi, G. Kikuchi, 1969, Archives of biochemistry and biophysics.

Cell‐free synthesis of rat liver δ‐aminolevulinate synthase and possible occurrence of processing of the enzyme protein in the course of its translocation from the cytosol into the mitochondrial matrix

N. Hayashi, G. Kikuchi, K. Yamauchi, 1980, FEBS letters.

An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements.

K. Itoh, Y. Katoh, T. Chiba, 1997, Biochemical and biophysical research communications.

Inhibition by hemin of in vitro translocation of chicken liver delta-aminolevulinate synthase into mitochondria.

N. Hayashi, G. Kikuchi, N. Watanabe, 1983, Biochemical and biophysical research communications.

Mechanism of allylisopropylacetamide-induced increase of -aminolevulinate synthetase in liver mitochondria. V. Mechanism of regulation by hemin of the level of -aminolevulinate synthetase in rat liver mitochondria.

N. Hayashi, G. Kikuchi, Y. Kurashima, 1972, Archives of biochemistry and biophysics.

Mechanism of allylisopropylacetamide-induced increase of delta-aminolevulinate synthetase in liver mitochondria. II. Effects of hemin and bilirubin on enzyme induction.

B. Yoda, N. Hayashi, G. Kikuchi, 1968, Journal of biochemistry.

Bach proteins belong to a novel family of BTB-basic leucine zipper transcription factors that interact with MafK and regulate transcription through the NF-E2 site

K. Itoh, K. Igarashi, N. Hayashi, 1996, Molecular and cellular biology.

Two chronic myelogenous leultaemia cell lines which represent different stages of erythroid differentiation

Masayuki Yamamoto, T. Nagai, K. Furuyama, 1993, British journal of haematology.

A Combinatorial Code for Gene Expression Generated by Transcription Factor Bach2 and MAZR (MAZ-Related Factor) through the BTB/POZ Domain

Masayuki Yamamoto, Masayuki Yamamoto, K. Igarashi, 2000, Molecular and Cellular Biology.

, the BTB / POZ Domain and MAZR ( MAZ-Related Factor ) through Generated by Transcription Factor Bach 2 A Combinatorial Code for Gene Expression

Masayuki Yamamoto, K. Igarashi, A. Kobayashi, 1999 .

GATA-1 transcription is controlled by distinct regulatory mechanisms during primitive and definitive erythropoiesis.

J. D. Engel, N. Hayashi, M. Yamamoto, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Long range interaction of cis‐DNA elements mediated by architectural transcription factor Bach1

J. D. Engel, K Takeyasu, K. Igarashi, 1999, Genes to cells : devoted to molecular & cellular mechanisms.

Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins

Ken Itoh, Masayuki Yamamoto, K. Itoh, 1994, Nature.

Synthesis and Translocation of Mitochondrial Matrix Enzymes in Higher Animals with Special Reference to δ-Aminolevulinate Synthase

N. Hayashi, G. Kikuchi, 1982 .

Erythropoietin-dependent induction of hemoglobin synthesis in a cytokine-dependent cell line M-TAT.

M. Minegishi, T. Nagai, N. Hayashi, 1994, The Journal of biological chemistry.

delta-Aminolevulinate synthase isozymes in the liver and erythroid cells of chicken.

N. Hayashi, G. Kikuchi, N. Watanabe, 1983, Biochemical and biophysical research communications.

Arrest in Primitive Erythroid Cell Development Caused by Promoter-specific Disruption of the GATA-1 Gene*

N. Hayashi, M. Yamamoto, H. Motohashi, 1997, The Journal of Biological Chemistry.

A novel mutation of the erythroid‐specific δ‐aminolaevulinate synthase gene in a patient with X‐linked sideroblastic anaemia

Masayuki Yamamoto, K. Furuyama, S. Sassa, 1999, British journal of haematology.

R411C mutation of the ALAS2 gene encodes a pyridoxine‐responsive enzyme with low activity

Masayuki Yamamoto, K. Furuyama, S. Sassa, 1998, British journal of haematology.

Transcription factor GATA-2 is expressed in erythroid, early myeloid, and CD34+ human leukemia-derived cell lines.

J. D. Engel, T. Nagai, H. Ishihara, 1994, Blood.

Activity and Expression of Murine Small Maf Family Protein MafK (*)

K. Itoh, K. Igarashi, N. Hayashi, 1995, The Journal of Biological Chemistry.

Alternative Promoters Regulate Transcription of the Mouse GATA-2 Gene*

H. Ishihara, N. Hayashi, N. Minegishi, 1998, The Journal of Biological Chemistry.

The mouse GATA-2 gene is expressed in the para-aortic splanchnopleura and aorta-gonads and mesonephros region.

J. D. Engel, S. Takahashi, S. Kawauchi, 1999, Blood.

Human erythropoietic protoporphyria: identification of a mutation at the splice donor site of intron 7 causing exon 7 skipping of the ferrochelatase gene.

S. Taketani, N. Hayashi, M. Yamamoto, 1993, Human molecular genetics.

Sequential activation of genes for heme pathway enzymes during erythroid differentiation of mouse Friend virus-transformed erythroleukemia cells.

R. Morimoto, S. Shibahara, H. de Verneuil, 1991, Biochimica et biophysica acta.

Translocation of delta-aminolevulinate synthase from the cytosol to the mitochondria and its regulation by hemin in the rat liver.

N. Hayashi, G. Kikuchi, K. Yamauchi, 1980, The Journal of biological chemistry.

Oxidative Stress Abolishes Leptomycin B-sensitive Nuclear Export of Transcription Repressor Bach2 That Counteracts Activation of Maf Recognition Element*

N. Kudo, Minoru Yoshida, K. Igarashi, 2000, The Journal of Biological Chemistry.

Structural determination and characterization of a 40 kDa protein isolated from rat 40 S ribosomal subunit

S. Takasawa, N. Hayashi, H. Yonekura, 1994, FEBS letters.

The Addition of Bisecting N-Acetylglucosamine Residues to E-cadherin Down-regulates the Tyrosine Phosphorylation of β-Catenin*

Y. Matsuzawa, N. Hayashi, N. Taniguchi, 2001, The Journal of Biological Chemistry.

Involvement of the transcriptional factor GATA-1 in regulation of expression of coproporphyrinogen oxidase in mouse erythroleukemia cells.

S. Taketani, N. Hayashi, M. Yamamoto, 1997, Biochemical and biophysical research communications.

Reduced synthesis of 5-aminolevulinate dehydratase in styrene-treated rats.

N. Hayashi, A. Koizumi, M. Ikeda, 1986, Biochimica et biophysica acta.

5-Aminolevulinate synthase expression and hemoglobin synthesis in a human myelogenous leukemia cell line.

T. Nagai, K. Furuyama, S. Sassa, 1997, Journal of biochemistry.

An immunochemical study of δ-aminolevulinate synthase and δ-aminolevulinate dehydratase in liver and erythroid cells of rat☆

Masayuki Yamamoto, N. Hayashi, H. Fujita, 1986 .

Effects of hemin on the synthesis and intracellular translocation of delta-aminolevulinate synthase in the liver of rats treated with 3,5-dicarbethoxy-1,4-dihydrocollidine.

N. Hayashi, G. Kikuchi, K. Yamauchi, 1980, Journal of biochemistry.

Purification and some properties of delta-aminolevulinate synthase from the rat liver cytosol fraction and immunochemical identity of the cytosolic enzyme and the mitochondrial enzyme.

N. Hayashi, G. Kikuchi, M. Nakakuki, 1980, The Journal of biological chemistry.

Role of the heme regulatory motif in the heme-mediated inhibition of mitochondrial import of 5-aminolevulinate synthase.

K. Furuyama, N. Hayashi, T. Nakatani, 2004, Journal of biochemistry.

Immunochemical studies of the turnover of delta-aminolevulinate synthase in rat liver mitochondria and the effect of hemin on it.

N. Hayashi, G. Kikuchi, M. Terasawa, 1980, Journal of biochemistry.

Secretion of tetrain, a Tetrahymena cysteine protease, as a mature enzyme and its identification as a member of the cathepsin L subfamily.

T. Kosaka, H. Hosoya, N. Hayashi, 1998, European journal of biochemistry.

Mechanism of inhibition by hemin of increase of delta-aminolevulinate synthetase in liver mitochondria.

N. Hayashi, G. Kikuchi, Y. Kurashima, 1970, Journal of biochemistry.

Difference in molecular sizes of delta-aminolevulinate synthetases in the soluble and mitochondrial fractions of rat liver.

B. Yoda, N. Hayashi, G. Kikuchi, 1970, Journal of biochemistry.

Effects of administration of cobalt chloride and cobalt protoporphyrin on delta-aminolevulinate synthase in rat liver.

N. Hayashi, G. Kikuchi, J. Igarashi, 1978, Journal of biochemistry.

The promoter of mouse transcription repressor bach1 is regulated by Sp1 and trans-activated by Bach1.

E. Ito, S. Nishimura, K. Igarashi, 2001, Journal of Biochemistry (Tokyo).

delta-Aminolevulinate synthetases in the liver cytosol fraction and mitochondria of mice treated with allylisopropylacetamide and 3,5-dicarbethoxyl-1,4-dihydrocollidine.

N. Hayashi, G. Kikuchi, J. Igarashi, 1976, Journal of biochemistry.

A novel mutation of the erythroid‐specific δ‐aminolevulinate synthase gene in a patient with non‐inherited pyridoxine‐responsive sideroblastic anemia

K. Furuyama, S. Sassa, N. Hayashi, 1999, American journal of hematology.

Studies on relationships between structure and function of hemoglobin M-Iwate.

N. Hayashi, G. Kikuchi, Y. Motokawa, 1966, The Journal of biological chemistry.

Isolation of recombinant cDNAs encoding chicken erythroid delta-aminolevulinate synthase.

J. D. Engel, J. Dodgson, N. Yew, 1985, Proceedings of the National Academy of Sciences of the United States of America.

Purification and structure of rat erythroid-specific delta-aminolevulinate synthase.

T. Nagai, N. Hayashi, M. Yamamoto, 1993, Journal of biochemistry.