Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Michael C. Kiel"'
Autor:
Sayeed Sameera, Leah Dziopa, Vega Beatriz, Michael C. Kiel, Adebobola Imeh-Nathaniel, Adam Brager, Thomas I. Nathaniel, Dana Baier
Publikováno v:
Brain Research Bulletin. 85:385-395
With a highly organized stereotypic behavior and a simplified neuronal system that is characterized by cellular modularity, crayfish (Orconectes rusticus) represents an excellent model that we used in this study to explore how a drug-conditioned-cue
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::473ae5d2a121a96e69327eba0101c3d9
https://doi.org/10.1016/j.brainresbull.2011.04.003
https://doi.org/10.1016/j.brainresbull.2011.04.003
Publikováno v:
Biochemistry. 43:12728-12740
Ribosome recycling factor (RRF) and elongation factor-G (EF-G) are jointly essential for recycling bacterial ribosomes following termination of protein synthesis. Here we present equilibrium and rapid kinetic measurements permitting formulation of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::317bdf958eed1fd09b4b8b40d6604e45
https://doi.org/10.1021/bi048927p
https://doi.org/10.1021/bi048927p
Autor:
Robert A. Grassucci, T.M. Booth, Go Hirokawa, Michael C. Kiel, Christian M. T. Spahn, Rajendra K. Agrawal, Akira Kaji, Manjuli R. Sharma, Joachim Frank
Publikováno v:
Proceedings of the National Academy of Sciences. 101:8900-8905
After the termination step of protein synthesis, a deacylated tRNA and mRNA remain associated with the ribosome. The ribosome-recycling factor (RRF), together with elongation factor G (EF-G), disassembles this posttermination complex into mRNA, tRNA,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5fcdc27c598865dbb005f8bf80ee542
https://doi.org/10.1073/pnas.0401904101
https://doi.org/10.1073/pnas.0401904101
Publikováno v:
Journal of Biological Chemistry. 278:48041-48050
Elongation factor G (EF-G) and ribosome recycling factor (RRF) disassemble post-termination complexes of ribosome, mRNA, and tRNA. RRF forms stable complexes with 70 S ribosomes and 50 S ribosomal subunits. Here, we show that EF-G releases RRF from 7
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ccf14c221eb97ef60e7b0e8407f8e65
https://doi.org/10.1074/jbc.m304834200
https://doi.org/10.1074/jbc.m304834200
Publikováno v:
Cell. 111(1):129-140
Ribosome recycling factor (RRF) disassembles posttermination complexes in conjunction with elongation factor EF-G, liberating ribosomes for further rounds of translation. The striking resemblance of its L-shaped structure to that of tRNA has suggeste
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ce3cf2fe188e4dde120193395b160d6
Publikováno v:
Microbiology and Molecular Biology Reviews. 66:460-485
SUMMARYCurrent X-ray diffraction and cryoelectron microscopic data of ribosomes of eubacteria have shed considerable light on the molecular mechanisms of translation. Structural studies of the protein factors that activate ribosomes also point to man
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f731d734ab0626c034b9f6da7050611b
https://doi.org/10.1128/mmbr.66.3.460-485.2002
https://doi.org/10.1128/mmbr.66.3.460-485.2002
Autor:
Gota Kawai, Aiko Muto, Akira Kaji, Hideko Kaji, Kazuei Igarashi, Go Hirokawa, Michael C. Kiel
Publikováno v:
Journal of Biological Chemistry. 277:35847-35852
The prokaryotic post-termination ribosomal complex is disassembled by ribosome recycling factor (RRF) and elongation factor G. Because of the structural similarity of RRF and tRNA, we compared the biochemical characteristics of RRF binding to ribosom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8c01029d2133102aa81e205c368ca0c
https://doi.org/10.1074/jbc.m206295200
https://doi.org/10.1074/jbc.m206295200
Autor:
Kazuei Igarashi, Aiko Muto, Anders Liljas, Go Hirokawa, Michael C. Kiel, V. Samuel Raj, Akira Kaji, Maria Selmer, Hideko Kaji
Publikováno v:
The EMBO Journal. 21(9):2272-2281
Ribosome recycling factor (RRF) together with elongation factor G (EF-G) disassembles the post- termination ribosomal complex. Inhibitors of translocation, thiostrepton, viomycin and aminoglycosides, inhibited the release of tRNA and mRNA from the po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a54f1c4421cee177b4e3f90fab44ef2b
https://opac.ll.chiba-u.jp/da/curator/900021119/
https://opac.ll.chiba-u.jp/da/curator/900021119/
Autor:
Ravinder Valadri, Manuel Ramos, Vincent Yi Fong Su, Po-Hong Liu, Huijun Li, Qi Shi, Michael C. Kiel, Chien-Wen Yang, Lisa Thomas, Thomas Roe
Publikováno v:
Medicine
Background: Troponin I is one of the most commonly tested biochemical markers in the emergency room (ER) and in the hospital setting. Besides coronary artery disease (CAD), demand ischemia with underlying tachycardia, anemia, hypertensive emergency,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8573874ded57831350781b089cd057b9
https://doi.org/10.1097/md.0000000000008027
https://doi.org/10.1097/md.0000000000008027
Autor:
Michael C. Kiel, M. Clelia Ganoza
Publikováno v:
European Journal of Biochemistry. 268:278-286
The gene encoding ribosome-bound ATPase (RbbA), which occurs bound to 70S ribosomes and 30S subunits, has been identified. The amino-acid sequence of RbbA reveals the presence of two ATP-binding domains in the N-terminal half of the protein. RbbA har
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ff91f99a4dec8202a6d969d618884628
https://doi.org/10.1046/j.1432-1033.2001.01873.x
https://doi.org/10.1046/j.1432-1033.2001.01873.x