Zobrazeno 1 - 6
of 6
pro vyhledávání: '"S Z Wahab"'
Publikováno v:
Journal of Biological Chemistry. 267:13440-13445
The Escherichia coli enzyme tRNA(m1G)methyltransferase, one of a group of post-transcription tRNA-modifying enzymes, shows remarkable specificity in selecting the tRNA species and the specific guanosine base to be methylated. To examine the structura
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::72cef366782e32dcf439af607914b799
https://doi.org/10.1016/s0021-9258(18)42230-2
https://doi.org/10.1016/s0021-9258(18)42230-2
Publikováno v:
The Journal of biological chemistry. 267(19)
The Escherichia coli enzyme tRNA(m1G)methyltransferase, one of a group of post-transcription tRNA-modifying enzymes, shows remarkable specificity in selecting the tRNA species and the specific guanosine base to be methylated. To examine the structura
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::aab4471e8d7b46c461c5a2074d7d3fa9
https://pubmed.ncbi.nlm.nih.gov/1618846
https://pubmed.ncbi.nlm.nih.gov/1618846
Publikováno v:
Journal of Biological Chemistry. 260:5286-5289
An 18 S multienzyme complex of aminoacyl-tRNA synthetases is found to be active in the synthesis of diadenosine-5',5'''-P1,P4-tetraphosphate (AppppA). Most of the activity is attributed to lysyl-tRNA synthetase in the complex. Free lysyl-tRNA synthet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1b41635890f471c41cc3d2d1e6aafc92
https://doi.org/10.1016/s0021-9258(18)89019-6
https://doi.org/10.1016/s0021-9258(18)89019-6
Autor:
S. Z. Wahab, D. C. H. Yang
Publikováno v:
Journal of Biological Chemistry. 260:12735-12739
Lysyl-tRNA synthetase, dissociated from the multienzyme complexes of aminoacyl-tRNA synthetases from rat liver, was previously found to be 6-fold more active than the synthetase complex in the enzymatic synthesis of P1,P4-bis(5'-adenosyl)tetraphospha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::06ab4036bed82254df1960c7fd308fe4
https://doi.org/10.1016/s0021-9258(17)38937-8
https://doi.org/10.1016/s0021-9258(17)38937-8
Autor:
S Z, Wahab, D C, Yang
Publikováno v:
The Journal of biological chemistry. 260(23)
Lysyl-tRNA synthetase, dissociated from the multienzyme complexes of aminoacyl-tRNA synthetases from rat liver, was previously found to be 6-fold more active than the synthetase complex in the enzymatic synthesis of P1,P4-bis(5'-adenosyl)tetraphospha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::93e0eb70add4e9d3f1da2eafefc1d4bc
https://pubmed.ncbi.nlm.nih.gov/2995387
https://pubmed.ncbi.nlm.nih.gov/2995387
Autor:
S Z, Wahab, D C, Yang
Publikováno v:
The Journal of biological chemistry. 260(9)
An 18 S multienzyme complex of aminoacyl-tRNA synthetases is found to be active in the synthesis of diadenosine-5',5'''-P1,P4-tetraphosphate (AppppA). Most of the activity is attributed to lysyl-tRNA synthetase in the complex. Free lysyl-tRNA synthet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::06f1cc5b7f45b7fe448670cbf6967ea5
https://pubmed.ncbi.nlm.nih.gov/3988754
https://pubmed.ncbi.nlm.nih.gov/3988754