Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Toshifumi Ueda"'
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 82(8):1327-1334
In Archaea and Bacteria, surface layer (S-layer) proteins form the cell envelope and are involved in cell protection. In the present study, a putative S-layer protein was purified from the crude extract of Pyrococcus horikoshii using affinity chromat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20889974001daaae6dd654a1ea13b894
https://nagasaki-u.repo.nii.ac.jp/records/1335
https://nagasaki-u.repo.nii.ac.jp/records/1335
Publikováno v:
Biochemical and Biophysical Research Communications. 493:1063-1068
Ribonuclease P (RNase P) is an endoribonuclease involved in maturation of the 5′-end of tRNA. We found previously that RNase P in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 consists of a catalytic RNase P RNA (PhopRNA) and five protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe179d14ec988705b6d87604973ba5ad
https://doi.org/10.1016/j.bbrc.2017.09.085
https://doi.org/10.1016/j.bbrc.2017.09.085
Publikováno v:
Biochemical and Biophysical Research Communications. 482:68-74
Ribonuclease P (RNase P) is a ribonucleoprotein that catalyzes the processing of 5′ leader sequences of precursor tRNAs (pre-tRNA). RNase P proteins PhoRpp21 and PhoRpp29 in the hyperthermophilic archaeon Pyrococcus horikoshii, homologs of human nu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfffea3ea57df2e7c241c165a636e6b4
https://doi.org/10.1016/j.bbrc.2016.10.142
https://doi.org/10.1016/j.bbrc.2016.10.142
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 79:952-959
The ribonuclease P (RNase P) proteins TkoPop5 and TkoRpp30, homologs of human Pop5 and Rpp30, respectively, in the hyperthermophilic archaeon Thermococcus kodakarensis were prepared and characterized with respect to pre-tRNA cleavage activity using t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fcf96078678d28a3b824e8fe42d34a8e
https://doi.org/10.1080/09168451.2014.1003130
https://doi.org/10.1080/09168451.2014.1003130
Publikováno v:
RNA Metabolism and Gene Expression in Archaea ISBN: 9783319657943
Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5′-leader sequence of precursor tRNA (pre-tRNA) and other small RNAs in all phylogenetic domains. A characteristic feature of archaeal RNase P RNAs is that th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e08c163d370cbe208ba170517adef66
https://doi.org/10.1007/978-3-319-65795-0_7
https://doi.org/10.1007/978-3-319-65795-0_7
Autor:
Makoto Kimura, Toshifumi Ueda, Kohsuke Hazeyama, Etsuko Nishimoto, Takashi Nakashima, Masato Ishihara, Yoshimitsu Kakuta
Publikováno v:
Biochemical and Biophysical Research Communications. 440:594-598
Ribonuclease P (RNase P) is a ribonucleoprotein complex essential for the processing of 5' leader sequences of precursor tRNAs (pre-tRNA). PhoPop5 is an archaeal homolog of human RNase P protein hPop5 involved in the activation of RNase P RNA (PhopRN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::975e6d0b7d54e090dde5dfd5c976a631
https://doi.org/10.1016/j.bbrc.2013.09.140
https://doi.org/10.1016/j.bbrc.2013.09.140
Characterization of the peripheral structures of archaeal RNase P RNA from Pyrococcus horikoshii OT3
Autor:
Makoto Kimura, Toshifumi Ueda, Hiroki Yamaguchi, Mitsuru Miyanoshita, Takashi Nakashima, Yoshimitsu Kakuta
Publikováno v:
Journal of Biochemistry. 155:25-33
Ribonuclease P (RNase P) is a ubiquitous trans-acting ribozyme that processes the 5' leader sequence of precursor tRNA (pre-tRNA). The secondary structure of RNase P RNA (PhopRNA) in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 has severa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4baad643c7473aea4bcce918e18bb5db
https://doi.org/10.1093/jb/mvt092
https://doi.org/10.1093/jb/mvt092
Publikováno v:
High Pressure Research. 33:258-264
The small heat shock proteins (sHSPs) solubilize thermo-denatured proteins without adenosine triphosphate energy consumption to facilitate protein refolding. sHSP20.8 is one of the silkworm (Bombyx mori) sHSPs having only one cystein in the N-termina
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::44687a4eab634c7edfe51ef118fda0f4
https://doi.org/10.1080/08957959.2013.773324
https://doi.org/10.1080/08957959.2013.773324
Autor:
Sonoko Ishino, Makoto Kimura, Yoshizumi Ishino, Toshifumi Ueda, Kotaro Suematsu, Yoshimitsu Kakuta, Takashi Nakashima, Yutaka Kawarabayasi
Publikováno v:
Biochemical and biophysical research communications. 468(4)
Ribonuclease P (RNase P) catalyzes the processing of 5' leader sequences of tRNA precursors in all three phylogenetic domains. RNase P also plays an essential role in non-tRNA biogenesis in bacterial and eukaryotic cells. For archaeal RNase Ps, addit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::512120725086fb8e63e7528de63f5c3d
https://pubmed.ncbi.nlm.nih.gov/26551464
https://pubmed.ncbi.nlm.nih.gov/26551464
Autor:
Masato Hamasaki, Takashi Nakashima, Toshifumi Ueda, Makoto Kimura, Kohsuke Hazeyama, Yoshimitsu Kakuta, Fumihiko Iwasaki
Publikováno v:
Journal of biochemistry. 159(1)
PhoPop5 and PhoRpp30 in the hyperthermophilic archaeon Pyrococcus horikoshii, homologues of human ribonuclease P (RNase P) proteins hPop5 and Rpp30, respectively, fold into a heterotetramer [PhoRpp30-(PhoPop5)2-PhoRpp30], which plays a crucial role i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d98645b547546694168273042b65bea
https://pubmed.ncbi.nlm.nih.gov/26152732
https://pubmed.ncbi.nlm.nih.gov/26152732