Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Nina, Moor"'
Publikováno v:
International Journal of Biomedicine, Vol 9, Iss Suppl_1, Pp S26-S26 (2019)
Background: Base excision DNA repair (BER) is very efficient process that involves the action of many enzymes and accessory proteins to correct the most common DNA lesions usually induced by ionizing irradiation and oxidative stress. Coordination of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f330c6ac6d9be8ac9e63097c3e0094e
http://ijbm.org/articles/IJBM_2019_9_S1_P21.pdf
http://ijbm.org/articles/IJBM_2019_9_S1_P21.pdf
Publikováno v:
Protein Science. 25:618-626
Mitochondria are considered as the primary source of reactive oxygen species (ROS) in nearly all eukaryotic cells during respiration. The harmful effects of these compounds range from direct neurotoxicity to incorporation into proteins producing aber
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e8fc44176693b201abe060a2990b5c57
https://doi.org/10.1002/pro.2855
https://doi.org/10.1002/pro.2855
Publikováno v:
Proceedings of the National Academy of Sciences. 112:3967-3972
At the amino acid binding and recognition step, phenylalanyl-tRNA synthetase (PheRS) faces the challenge of discrimination between cognate phenylalanine and closely similar noncognate tyrosine. Resampling of Tyr-tRNA Phe to PheRS increasing the numbe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4426ed35e90e52b3beab54af91e1281d
https://doi.org/10.1073/pnas.1414852112
https://doi.org/10.1073/pnas.1414852112
Autor:
Ekaterine, Kartvelishvili, Dmitry, Tworowski, Hilary, Vernon, Nina, Moor, Jing, Wang, Lee-Jun, Wong, Zofia, Chrzanowska-Lightowlers, Mark, Safro
Publikováno v:
Protein Science : A Publication of the Protein Society
Mutations in the mitochondrial aminoacyl‐tRNA synthetases (mtaaRSs) can cause profound clinical presentations, and have manifested as diseases with very selective tissue specificity. To date most of the mtaaRS mutations could be phenotypically reco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::08f2f7d22478b5eab5380302ffcc9988
https://pubmed.ncbi.nlm.nih.gov/28419689
https://pubmed.ncbi.nlm.nih.gov/28419689
Publikováno v:
Chemistry & Biology. 18:1221-1229
Summary Aminoacyl-tRNA synthetases exert control over the accuracy of translation by selective pairing the correct amino acids with their cognate tRNAs, and proofreading the misacylated products. Here we show that three existing, structurally differe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef0439f000019b2544e14c0a3891763b
https://doi.org/10.1016/j.chembiol.2011.08.008
https://doi.org/10.1016/j.chembiol.2011.08.008
Publikováno v:
Structure. 18(3):343-353
The existence of three types of phenylalanyl-tRNA synthetase (PheRS), bacterial (alphabeta)(2), eukaryotic/archaeal cytosolic (alphabeta)(2), and mitochondrial alpha, is a prominent example of structural diversity within the aaRS family. PheRSs have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84895820c5e0c8afee8415fc10f6468d
Publikováno v:
Structure. 16(7):1095-1104
All class II aminoacyl-tRNA synthetases (aaRSs) are known to be active as functional homodimers, homotetramers, or heterotetramers. However, multimeric organization is not a prerequisite for phenylalanylation activity, as monomeric mitochondrial phen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcdd91372b4dbbae91bb28673a2b287d
Publikováno v:
Protein science : a publication of the Protein Society. 25(3)
Mitochondria are considered as the primary source of reactive oxygen species (ROS) in nearly all eukaryotic cells during respiration. The harmful effects of these compounds range from direct neurotoxicity to incorporation into proteins producing aber
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9ddfe93025c57eb0c6b0217e13186813
https://pubmed.ncbi.nlm.nih.gov/26645192
https://pubmed.ncbi.nlm.nih.gov/26645192
Publikováno v:
Biochemistry. 42:10697-10708
The interaction of human phenylalanyl-tRNA synthetase, a eukaryotic prototype with an unknown three-dimensional structure, with the tRNA(Phe) acceptor end was studied by s(4)U-induced affinity cross-linking with human tRNA(Phe) derivatives site-speci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbced72ad077746fb8c02d3d5ab7ab5c
https://doi.org/10.1021/bi034732q
https://doi.org/10.1021/bi034732q