Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Martha A. Lovato"'
Autor:
Martha A. Lovato, Manal A. Swairjo, Robert J. Skene, Francella J. Otero, Lluís Ribas de Pouplana, Xiang-Lei Yang, Paul Schimmel, Duncan E. McRee
Publikováno v:
Molecular cell. 13(6)
Early work on aminoacylation of alanine-specific tRNA (tRNA(Ala)) by alanyl-tRNA synthetase (AlaRS) gave rise to the concept of an early "second genetic code" imbedded in the acceptor stems of tRNAs. A single conserved and position-specific G:U base
The genetic code is defined by the specific aminoacylations of tRNAs by aminoacyl-tRNA synthetases. Although the synthetases are widely conserved through evolution, aminoacylation of a given tRNA is often system specific-a synthetase from one source
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a035e425a022a9826e96d60abf80514e
https://europepmc.org/articles/PMC125604/
https://europepmc.org/articles/PMC125604/
Publikováno v:
The Journal of biological chemistry. 275(36)
In the yeast Saccharomyces cerevisiae, two genes (GRS1 and GRS2) encode glycyl-tRNA synthetase (GlyRS1 and GlyRS2, respectively). 59% of the sequence of GlyRS2 is identical to that of GlyRS1. Others have proposed that GRS1 and GRS2 encode the cytopla
Autor:
Seiichi P. T. Matsuda, José-Luis Giner, Martha A. Lovato, Michael J. R. Segura, Elizabeth A. Hart
Publikováno v:
The Journal of biological chemistry. 275(18)
Plants and certain protists use cycloeucalenol cycloisomerase (EC 5.5.1.9) to convert pentacyclic cyclopropyl sterols to conventional tetracyclic sterols. We used a novel complementation strategy to clone a cycloeucalenol cycloisomerase cDNA. Express
Autor:
Eugenio L. de Hostos, Kimberly A. Foster, William K. Wilson, Michelle M. Meyer, Seiichi P. T. Matsuda, Wei Gu, Martha A. Lovato, Sharotka M. Godzina
Publikováno v:
Lipids. 35(3)
Cycloartenol synthase converts oxidosqualene to cycloartenol, the first carbocyclic intermediate en route to sterols in plants and many protists. Presented here is the first cycloartenol synthase gene identified from a protist, the cellular slime mol
Publikováno v:
Biochemistry. 38(31)
Fatty acid amide hydrolase (FAAH) is a membrane-bound enzyme responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide. FAAH's primary structure identifies this enzyme as a member of a diverse group of alk