Zobrazeno 1 - 10
of 233
pro vyhledávání: '"Uttam L. RajBhandary"'
Autor:
Robert A. Zimmermann
Publikováno v:
Science. 271:1240-1241
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::073ee729dad650825b55bb1f70719a3e
https://doi.org/10.1126/science.271.5253.1240
https://doi.org/10.1126/science.271.5253.1240
Autor:
K Musierforsyth
Publikováno v:
Trends in Biochemical Sciences. 21:322
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::42f0308c128026d4c827d42b6e73e811
https://doi.org/10.1016/0968-0004(96)80840-1
https://doi.org/10.1016/0968-0004(96)80840-1
Autor:
Maarten Vercruysse, Caroline Köhrer, Yang Shen, Sandra Proulx, Anubrata Ghosal, Bryan W. Davies, Uttam L. RajBhandary, Graham C. Walker
Publikováno v:
mBio, Vol 7, Iss 6 (2016)
ABSTRACT YbeY is part of a core set of RNases in Escherichia coli and other bacteria. This highly conserved endoribonuclease has been implicated in several important processes such as 16S rRNA 3′ end maturation, 70S ribosome quality control, and re
Externí odkaz:
https://doaj.org/article/17b5a820c273493788ed9a01f2254ec3
Autor:
Maarten Vercruysse, Caroline Köhrer, Bryan W Davies, Markus F F Arnold, John J Mekalanos, Uttam L RajBhandary, Graham C Walker
Publikováno v:
PLoS Pathogens, Vol 10, Iss 6, p e1004175 (2014)
YbeY, a highly conserved protein, is an RNase in E. coli and plays key roles in both processing of the critical 3' end of 16 S rRNA and in 70 S ribosome quality control under stress. These central roles account for YbeY's inclusion in the postulated
Externí odkaz:
https://doaj.org/article/8e4590c6719e487eb48619c2b1082155
Autor:
Sven Niehues, Julia Bussmann, Georg Steffes, Ines Erdmann, Caroline Köhrer, Litao Sun, Marina Wagner, Kerstin Schäfer, Guangxia Wang, Sophia N. Koerdt, Morgane Stum, Sumit Jaiswal, Uttam L. RajBhandary, Ulrich Thomas, Hermann Aberle, Robert W. Burgess, Xiang-Lei Yang, Daniela Dieterich, Erik Storkebaum
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-1 (2016)
Nature Communications 6: Article number: 7520 (2015); Published: 3 July 2015; Updated: 21 January 2016. The authors inadvertently omitted Sumit Jaiswal, who was originally included in the Acknowledgements section of this Article and contributed to th
Externí odkaz:
https://doaj.org/article/d78a9b87a531477386b0c8affd38d9a5
Publikováno v:
Other repository
N-Formylation of the Met-tRNA Met by the nuclearly encoded mitochondrial methionyl-tRNA formyltransferase (MTFMT) has been found to be a key determinant of protein synthesis initiation in mitochondria. In humans, mutations in the MTFMTgene result in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f15e3b3f23fa7a8ad6bd2f4af21b3a53
https://doi.org/10.1074/jbc.ra118.003838
https://doi.org/10.1074/jbc.ra118.003838
Autor:
Moore, Peter B.
Publikováno v:
Chemistry & Biology. (6):365
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::32d34a96dfa5c63cc9dd7281aa980730
Publikováno v:
The Journal of biological chemistry. 293(39)
N-Formylation of the Met-tRNA(Met) by the nuclearly encoded mitochondrial methionyl-tRNA formyltransferase (MTFMT) has been found to be a key determinant of protein synthesis initiation in mitochondria. In humans, mutations in the MTFMT gene result i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::62944c5c14e53745828c7890bee325bc
https://pubmed.ncbi.nlm.nih.gov/30087118
https://pubmed.ncbi.nlm.nih.gov/30087118
Autor:
Caroline Köhrer, Akesh Sinha, Michael H.W. Weber, Isao Masuda, Uttam L. RajBhandary, Ya-Ming Hou, Vamsi K. Mootha
Publikováno v:
Journal of Biological Chemistry. 289:32729-32741
N-Formylation of initiator methionyl-tRNA (Met-tRNA(Met)) by methionyl-tRNA formyltransferase (MTF) is important for translation initiation in bacteria, mitochondria, and chloroplasts. Unlike all other translation systems, the metazoan mitochondrial
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3174d635ce9cfdfacb73eb397959be8
https://doi.org/10.1074/jbc.m114.610626
https://doi.org/10.1074/jbc.m114.610626
Autor:
Clement T Y Chan, Paul H. Blum, I. Ramesh Babu, Debabrata Mandal, Uttam L. RajBhandary, Dan Su, Masayasu Kuwahara, Caroline Köhrer, Yuchen Liu, Dieter Söll, Peter C. Dedon
Publikováno v:
RNA. 20:177-188
Most archaea and bacteria use a modified C in the anticodon wobble position of isoleucine tRNA to base pair with A but not with G of the mRNA. This allows the tRNA to read the isoleucine codon AUA without also reading the methionine codon AUG. To und
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05b3d10de9e65c0a81f3fd5adf833cd3
https://doi.org/10.1261/rna.042358.113
https://doi.org/10.1261/rna.042358.113