Zobrazeno 1 - 10
of 53
pro vyhledávání: '"Jean-Pierre Waller"'
Publikováno v:
2018 Conference on Precision Electromagnetic Measurements (CPEM 2018)
2018 Conference on Precision Electromagnetic Measurements (CPEM 2018), Jul 2018, Paris, France. pp.1-2, ⟨10.1109/CPEM.2018.8501040⟩
2018 Conference on Precision Electromagnetic Measurements (CPEM 2018), Jul 2018, Paris, France. pp.1-2, ⟨10.1109/CPEM.2018.8501040⟩
This paper presents a long-range absolute distance meter working at 1550 nm. This instrument, based on off-the-shelf fiber-optic components from the telecommunications industry, has been evaluated in term of performances thanks to measurement campaig
Autor:
Yuri Motorin, Jean-Pierre Waller
Publikováno v:
Biochimie. 80:579-590
Cysteinyl-tRNA synthetase (CRS) from rabbit liver was purified 8300-fold to a constant specific activity. SDS-PAGE revealed the presence of two polypeptides of 86 kDa and 92 kDa, in the proportions of 60% and 40% respectively. The SDS-electrophoretic
Publikováno v:
Biochimie. 79:731-740
Cysteinyl-tRNA synthetase (CRS) from Saccharomyces cerevisiae was purified 2300-fold with a yield of 33%, to high-specific activity (kcal4.3 s−1 at 25°C for the aminoacylation of yeast tRNACys). SDS-PAGE revealed a single polypeptide corresponding
Publikováno v:
Journal of Biological Chemistry. 269:2086-2092
Valyl-tRNA synthetase from mammalian cells is isolated exclusively as a complex with elongation factor (EF) 1H (the "heavy" form of eukaryotic EF-1, composed of subunits alpha, beta, gamma, and delta). In a previous study, the 140-kDa valyl-tRNA synt
Publikováno v:
Biochimie. 74:195-205
The high-M(r) aminoacyl-tRNA synthetase complex previously purified from sheep liver differed from those isolated from several other mammalian sources by the absence of prolyl-tRNA synthetase activity and the presence of glutamyl tRNA synthetase as a
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1996, 271 (46), pp.29295-29303. ⟨10.1074/jbc.271.46.29295⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1996, 271 (46), pp.29295-29303. ⟨10.1074/jbc.271.46.29295⟩
International audience; Cytoplasmic aspartyl-tRNA synthetase from mammals is one of the components of a multienzyme complex comprising nine synthetase activities. The presence of an amino-terminal extension composed of about 40 residues is a characte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5aed8995cc0a86d2bc63d1b214ce6c11
https://hal.archives-ouvertes.fr/hal-03276099/document
https://hal.archives-ouvertes.fr/hal-03276099/document
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 1995, 34 (2), pp.569-576. ⟨10.1021/bi00002a023⟩
Biochemistry, American Chemical Society, 1995, 34 (2), pp.569-576. ⟨10.1021/bi00002a023⟩
International audience; Conformational studies were performed on the synthetic tricosapeptide N-acetyl-SKKALKKLQKEQEKQRKKEERAL-amide, representing the highly basic segment (residues 30-52) of the N-terminal extension of yeast cytoplasmic aspartyl-tRN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c6acb8d623249b55e1cfee3bfc8c67b
https://hal-pasteur.archives-ouvertes.fr/pasteur-03276092
https://hal-pasteur.archives-ouvertes.fr/pasteur-03276092
Autor:
Sophie Quevillon, Fabrice Agou, Guillaume Bec, Myriam Lazard, Marc Mirande, Pierre Kerjan, Jean-Pierre Waller
Publikováno v:
The Translational Apparatus ISBN: 9781461360216
The aminoacyl-tRNA synthetases are a family of ubiquitous enzymes that function at an essential step in the translation of the genetic information. These enzymes are responsible for the accurate esterification of amino acids to the corresponding tRNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::13b9acbf5bff98db4da2e286fba03472
https://doi.org/10.1007/978-1-4615-2407-6_62
https://doi.org/10.1007/978-1-4615-2407-6_62
Autor:
Marc Mirande, Jean-Pierre Waller
Publikováno v:
Journal of Biological Chemistry. 263:18443-18451
The nucleotide sequence of a 3.6-kilobase pair DNA fragment containing the structural gene for yeast cytoplasmic lysyl-tRNA synthetase (KRS1) and its flanking regions was determined. The encoded protein of 67,881 kDa displays a cluster of 11 lysines
Autor:
Jean-Pierre Waller, Marc Mirande
Publikováno v:
Journal of Biological Chemistry. 264:842-847
A cDNA clone encoding rat liver aspartyl-tRNA synthetase was isolated by probing a lambda gt11 recombinant cDNA expression library with antibodies directed against the corresponding polypeptide from sheep liver. The 1930-base pairs-long cDNA insert a