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Dive into the research topics where Masanori Ogawa is active.

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Featured researches published by Masanori Ogawa.


FEBS Letters | 1997

Hedgehog and patched gene expression in adult ocular tissues

Takashi Takabatake; Masanori Ogawa; Tadashi C. Takahashi; Makoto Mizuno; Mitsumasa Okamoto; Kazuhito Takeshima

We analysed the expression of members of the hh gene family in adult ocular tissues of newt, frog and mouse by RT‐PCR method. Shh displayed restricted expression in the neural retina that was conserved in each species analyzed. X‐bhh, X‐chh and mouse Ihh were detected in the iris and in the retinal pigment epithelium, while mouse Dhh was detected additionally in the neural retina and faintly in the cornea. We also found that two types of ptc genes, potential hh targets and receptors, were expressed in these tissues, suggesting the presence of active hh signalling there.


Mechanisms of Development | 2000

Distinct expression of two types of Xenopus Patched genes during early embryogenesis and hindlimb development.

Takashi Takabatake; Tadashi C. Takahashi; Yuka Takabatake; Kazuto Yamada; Masanori Ogawa; Kazuhito Takeshima

Patched (Ptc) is a putative twelve transmembrane domain protein that is both a Hedgehog (Hh) receptor and transcriptional target of Hh. In this study, we isolated Xenopus Ptc cDNAs, Ptc-1 and Ptc-2, and carried out comparative analyses on their expression patterns. The putative Ptc-2 protein has a long C-terminal extension that has similarities in both length and sequence to those of Ptc-1 proteins in mouse, chick and human. In both early embryogenesis and hindlimb development, Ptc-2 expression is restricted to cells that receive a Hh signal, a pattern similar to that of Gli-1. Ptc-1, however, shows a broader distribution, mainly non-overlapping with that of Ptc-2. Despite the difference in their expression patterns, both are induced in animal cap explants synergistically by Shh and Noggin, showing a conserved regulation in their activation mechanisms.


Development Genes and Evolution | 1997

Metamorphic change in EP37 expression: members of the βγ-crystallin superfamily in newt

Masanori Ogawa; Takashi Takabatake; Tadashi C. Takahashi; Kazuhito Takeshima

Abstractu2002EP37 is an epidermis-specific protein found in the developing embryo of the Japanese newt, Cynops pyrrhogaster. Our previous study predicted the presence of genes homologous to EP37, which show temporary shared expression at the turn of metamorphosis. In this study, we isolated and characterized three cDNAs encoding novel EP37 homologues; two from the skin of an adult newt and the other from swimming larva. Conceptual translation of the open reading frames of these cDNAs predicted proteins carrying βγ-crystallin motifs and putative calcium-binding sites, both of which are features shared by the originally identified EP37 (EP37L1), as well as a spore coat protein of Myxococcus xanthus, protein S. Immunoblot analyses and immunohistochemical studies indicated that two of the EP37 proteins, EP37L1 and EP37L2, are exclusively expressed in the epidermis (skein cells) including the figures of Eberth at premetamorphic stages. During and after metamorphosis, the expression of EP37 proteins was mainly observed in cutaneous glands, and a molecular transition to the adult types of EP37, EP37A1 and EP37A2, occurred. These observations suggest that EP37 proteins play an important role in construction of integumental tissues and adaptation to the aquatic or amphibious environment.


Mechanisms of Development | 2001

Corrigendum to “Distinct expression of two types of Xenopus Patched genes during early embryogenesis and hindlimb development” [Mech. Dev. 98 (2000) 99–104]

Takashi Takabatake; Tadashi C. Takahashi; Yuka Takabatake; Kazuto Yamada; Masanori Ogawa; Kazuhito Takeshima

Corrigendum to aDistinct expression of two types of Xenopus Patched genes during early embryogenesis and hindlimb developmento [Mech. Dev. 98 (2000) 99±104] Takashi Takabatake, Tadashi C. Takahashi, Yuka Takabatake, Kazuto Yamada, Masanori Ogawa, Kazuhito Takeshima* Radioisotope Research Center, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan Biohistory Research Hall, Takatsuki, Osaka 569-1125, Japan Graduate School of Human Informatics, Nagoya University, Chikusa, Nagoya 464-8601, Japan


Experimental Cell Research | 2002

Phosphorylation-Dependent Migration of Retinoblastoma Protein into the Nucleolus Triggered by Binding to Nucleophosmin/B23

Masaharu Takemura; Fumiharu Ohoka; Marinela Perpelescu; Masanori Ogawa; Hidenobu Matsushita; Tomoyuki Takaba; Tetsu Akiyama; Hayato Umekawa; Yukio Furuichi; Peter R. Cook; Shonen Yoshida


Biochemical and Biophysical Research Communications | 1996

ACTIVATION OF TWO CYNOPS GENES, FORK HEAD AND SONIC HEDGEHOG, IN ANIMAL CAP EXPLANTS

Takashi Takabatake; Tadashi C. Takahashi; Kunio Inoue; Masanori Ogawa; Kazuhito Takeshima


Development Growth & Differentiation | 1998

Isolation and characterization of a gene expressed mainly in the gastric epithelium, a novel member of the ep37 family that belongs to the betagamma-crystallin superfamily

Masanori Ogawa; Tadashi C. Takahashi; Takashi Takabatake; Kazuhito Takeshima


Journal of Biological Chemistry | 2001

O-helix Mutant T664P of Thermus aquaticus DNA Polymerase I ALTERED CATALYTIC PROPERTIES FOR INCORPORATION OF INCORRECT NUCLEOTIDES BUT NOT CORRECT NUCLEOTIDES

Aki Tosaka; Masanori Ogawa; Shonen Yoshida; Motoshi Suzuki


Journal of Biological Chemistry | 2003

Distinct Function of Conserved Amino Acids in the Fingers of Saccharomyces cerevisiae DNA Polymerase α

Masanori Ogawa; Siripan Limsirichaikul; Atsuko Niimi; Shigenori Iwai; Shonen Yoshida; Motoshi Suzuki


Nucleic Acids Research | 2001

Arg660Ser mutation in Thermus aquaticus DNA polymerase I suppresses T→C transitions: implication of wobble base pair formation at the nucleotide incorporation step

Katsushi Yoshida; Aki Tosaka; Hiroyuki Kamiya; Takashi Murate; Hiroshi Kasai; Yuji Nimura; Masanori Ogawa; Shonen Yoshida; Motoshi Suzuki

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