Výsledky vyhledávání - "Harumi Hosaka"

Crystal Structure of Aminomethyltransferase in Complex with Dihydrolipoyl-H-Protein of the Glycine Cleavage System

Autor: Kazuko Fujiwara, Nobuo Maita, Akiyasu C. Yoshizawa, Harumi Hosaka, Hisaaki Taniguchi, Atsushi Nakagawa, Kazuko Okamura-Ikeda

Publikováno v: Journal of Biological Chemistry. 285:18684-18692

Aminomethyltransferase, a component of the glycine cleavage system termed T-protein, reversibly catalyzes the degradation of the aminomethyl moiety of glycine attached to the lipoate cofactor of H-protein, resulting in the production of ammonia, 5,10

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::53b52b259d8495c98f30a3acc50931e2
https://doi.org/10.1074/jbc.m110.110718

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Structure and Evolution of the 23S rRNA Binding Domain of Protein L2

Autor: Atsushi Nakagawa, Harumi Hosaka, Makoto Kimura, Masae Taniguchi, Takashi Nakashima, Isao Tanaka

Publikováno v: The Ribosome

This chapter focuses on the crystal structure of the RNA binding domain of BstL2, and discusses its structure from functional and evolutionary points of view. Site-directed mutagenesis of Arg86 or Arg155 significantly diminished RNA binding affinity,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0276295457364611f093c038252849db
https://doi.org/10.1128/9781555818142.ch9

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The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome

Autor: Harumi Hosaka, Makoto Kimura, Takashi Nakashima, Masae Taniguchi, Atsushi Nakagawa, Isao Tanaka

Publikováno v: The EMBO Journal. 18:1459-1467

Ribosomal protein L2 is the largest protein component in the ribosome. It is located at or near the peptidyl transferase center and has been a prime candidate for the peptidyl transferase activity. It binds directly to 23S rRNA and plays a crucial ro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fcf2fddb93bfa16724cdb09715c568f4
https://doi.org/10.1093/emboj/18.6.1459

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Matching the crystallographic structure of ribosomal protein S7 to a three-dimensional model of the 16S ribosomal RNA

Autor: Atsushi Nakagawa, Richard Brimacombe, Isao Tanaka, Harumi Hosaka, Soichi Wakatsuki, Florian Mueller

Publikováno v: RNA. 4:542-550

Two recently published but independently derived structures, namely the X-ray crystallographic structure of ribosomal protein S7 and the "binding pocket" for this protein in a three-dimensional model of the 16S rRNA, have been correlated with one ano

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61f152a8c4ced957bb24f346c61761c7
https://doi.org/10.1017/s1355838298972004

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A new protein complex promoting the assembly of Rad51 filaments

Autor: Miki Shinohara, Hiroyuki Sasanuma, Maki S. Tawaramoto, Eri Sanda, Jessica P. Lao, Akira Shinohara, Harumi Hosaka, Neil Hunter, Mamoru Suzuki, Eiki Yamashita, Atsushi Nakagawa

Publikováno v: Nature communications. 4

During homologous recombination, eukaryotic RecA homologue Rad51 assembles into a nucleoprotein filament on single-stranded DNA to catalyse homologous pairing and DNA-strand exchange with a homologous template. Rad51 nucleoprotein filaments are highl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bfe9e49b76678ed4be9c61dabd17dee
https://pubmed.ncbi.nlm.nih.gov/23575680

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Global Conformational Change Associated with the Two-step Reaction Catalyzed by Escherichia coli Lipoate-Protein Ligase A*

Autor: Hisaaki Taniguchi, Atsushi Nakagawa, Harumi Hosaka, Nobuo Maita, Kazuko Okamura-Ikeda, Kazuko Fujiwara

This research was originally published in Journal of Biological Chemistry. Kazuko Fujiwara, Nobuo Maita, Harumi Hosaka, Kazuko Okamura-Ikeda, Atsushi Nakagawa Hisaaki Taniguchi. Global conformational change associated with the two-step reaction catal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d037bf6680bcccfa5c17853f322fe0e5
https://europepmc.org/articles/PMC2843243/

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Targeting AMAP1 and cortactin binding bearing an atypical src homology 3/proline interface for prevention of breast cancer invasion and metastasis

Autor: Tsutomu Agatsuma, Hisataka Sabe, Chitose Oneyama, Ken-ichi Akagi, Takahisa Ikegami, Masato Okada, Masaki Morishige, Ari Hashimoto, Hiromi Wada, Mayumi Hirose, Eiji Ogawa, Shigeru Hashimoto, Atsuko Yamada, Hirofumi Nakano, Atsushi Nakagawa, Harumi Hosaka, Hidenori Kobayashi

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 103(18)

Invasive potentials of carcinomas greatly contribute to their metastasis, which is a major threat in most cancers. We have recently shown that Arf6 plays a pivotal role in breast cancer invasive activities and identified AMAP1 as an effector of GTP-A

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba9a75ff504cdca2a9c6afda0def5aad
https://pubmed.ncbi.nlm.nih.gov/16636290

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