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pro vyhledávání: '"Michael C. Marvin"'
Publikováno v:
American Journal of Physics. 87:527-534
An ongoing need exists for the creation of interdisciplinary working groups in the sciences and development of pedagogical approaches to content themes that tie together different scientific disciplines. The work described here addresses this need th
Publikováno v:
Nature Structural & Molecular Biology. 22:611-617
Phosphorylation of the spliceosome is essential for RNA splicing, yet how and to what extent kinase signaling affects splicing have not been defined on a genome-wide basis. Using a chemical genetic approach, we show in Schizosaccharomyces pombe that
Publikováno v:
RNA. 17:1429-1440
Ribonuclease P (RNase P) is an essential endoribonuclease for which the best-characterized function is processing the 5′ leader of pre-tRNAs. Compared to bacterial RNase P, which contains a single small protein subunit and a large catalytic RNA sub
Autor:
John R. Yates, Sandra Clauder-Münster, Scott C. Walker, Lars M. Steinmetz, David R. Engelke, Ali Sarkeshik, Michael C. Marvin
Publikováno v:
RNA. 17:1441-1450
Ribonuclease P (RNase P) is an essential endoribonuclease that catalyzes the cleavage of the 5′ leader of pre-tRNAs. In addition, a growing number of non-tRNA substrates have been identified in various organisms. RNase P varies in composition, as b
Autor:
David R. Engelke, Michael C. Marvin
Publikováno v:
Journal of Cellular Biochemistry. 108:1244-1251
The "RNA World" hypothesis suggests that life developed from RNA enzymes termed ribozymes, which carry out reactions without assistance from proteins. Ribonuclease (RNase) P is one ribozyme that appears to have adapted these origins to modern cellula
Autor:
David R. Engelke, Michael C. Marvin
Publikováno v:
RNA Biology. 6:40-42
Ribonuclease P (RNase P) is an essential enzyme that catalyzes the 5' endonucleolytic cleavage of precursor transfer RNAs (pre-tRNAs). It is found in all phylogenetic domains: bacteria, archaea and eukaryotes. The bacterial enzyme consists of a singl
Publikováno v:
Biophysical Journal. 98(3)
Ribonuclease P (RNase P) is an essential RNA enzyme found in all phylogenetic domains that is best known for catalyzing the 5’ endonucleolytic cleavage of precursor transfer RNAs (pre-tRNAs). In bacteria, the enzyme consists of a single, catalytic
Publikováno v:
Ribonuclease P ISBN: 9781441911414
Ribonuclease P (RNase P) is an essential endonuclease that catalyzes the cleavage of the 5′ leader sequence from precursor tRNAs (pre-tRNAs). Most forms of RNase P are ribonucleoproteins and the bacterial enzyme possesses a single catalytic RNA and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fec30bf10e4536027d6db134c2980207
https://doi.org/10.1007/978-1-4419-1142-1_10
https://doi.org/10.1007/978-1-4419-1142-1_10
Autor:
Michael C. Marvin, Peter C. D. Macpherson, Xiang Jiao Yang, Eric Meadows, William Klein, Huibin Tang, Daniel Goldman
Publikováno v:
Molecular biology of the cell. 20(4)
Muscle activity contributes to formation of the neuromuscular junction and affects muscle metabolism and contractile properties through regulated gene expression. However, the mechanisms coordinating these diverse activity-regulated processes remain