Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Karla L. Ewalt"'
Autor:
Eleni Tzima, Karla L. Ewalt, Hua Zhang, Paul Schimmel, James E. Faber, Xiang-Lei Yang, Gang Cheng
Publikováno v:
American Journal of Physiology-Regulatory, Integrative and Comparative Physiology. 295:R1138-R1146
Mini-tyrosyl-tRNA synthetase (mini-TyrRS), the N-terminal domain of tyrosyl-tRNA synthetase, is a recently identified protein released by endothelial cells that exhibits angiogenic and leukocyte chemoattractant, ELR-motif (Glu-Leu-Arg)-dependent acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2d79142e1567386aee9ba3f6b20dd66
https://doi.org/10.1152/ajpregu.90519.2008
https://doi.org/10.1152/ajpregu.90519.2008
Autor:
Bonnie M. Slike, Mili Kapoor, Xiang-Lei Yang, David A. Cheresh, Francella J. Otero, Paul Schimmel, Ricardo F. Frausto, Alison Bates, Karla L. Ewalt, Hiro Tsuruta
Publikováno v:
Chemistry & Biology. 14(12):1323-1333
SummaryDisease-causing mutations occur in genes for aminoacyl tRNA synthetases. That some mutations are dominant suggests a gain of function. Native tRNA synthetases, such as tyrosyl-tRNA synthetase (TyrRS) and tryptophanyl-tRNA synthetase, catalyze
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e250729d99646ec8b832959bd877fae4
Autor:
Min Guo, Xiang-Lei Yang, Francella J. Otero, Karla L. Ewalt, Duncan E. McRee, Mili Kapoor, Robert J. Skene, Paul Schimmel
Publikováno v:
Structure. 15(7):793-805
Higher eukaryote tRNA synthetases have expanded functions with roles in the assembly of biological systems. New functions come from enlarged, more differentiated structures that were adapted to fit with the essential aminoacylation function. How thos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::809be7e5f13344bd63d447b9f6e4dd26
Autor:
Manal A. Swairjo, Xiang-Lei Yang, Caroline Köhrer, Karla L. Ewalt, Paul Schimmel, Jianming Liu, Uttam L. RajBhandary, Duncan E. McRee, Francella J. Otero, Robert J. Skene
Publikováno v:
The EMBO Journal. 25:2919-2929
Aminoacylation of tRNA is the first step of protein synthesis. Here, we report the co-crystal structure of human tryptophanyl-tRNA synthetase and tRNATrp. This enzyme is reported to interact directly with elongation factor 1alpha, which carries charg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c10556b26460b49892fdfae69446033d
https://doi.org/10.1038/sj.emboj.7601154
https://doi.org/10.1038/sj.emboj.7601154
Autor:
Karla L. Ewalt, Francella J. Otero, Bonnie M. Slike, Xiang-Lei Yang, Paul Schimmel, Jianming Liu
Publikováno v:
Biochemistry. 44:4216-4221
In cellular environments, coupled hydrolytic reactions are used to force efficient product formation in enzyme-catalyzed reactions. In the first step of protein synthesis, aminoacyl-tRNA synthetases react with amino acid and ATP to form an enzyme-bou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f609e4eee0111ccd12b4cdd1c6625060
https://doi.org/10.1021/bi048116l
https://doi.org/10.1021/bi048116l
Publikováno v:
Trends in Biochemical Sciences. 29:250-256
Human tyrosyl-tRNA synthetase (TyrRS) and tryptophanyl-tRNA synthetase (TrpRS) are closely related, dual function enzymes that act in protein biosynthesis and angiogenesis. The recent crystallographic structures of these two enzymes show that they ad
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b96393741a0f6da76a8c8029e6e9d28
https://doi.org/10.1016/j.tibs.2004.03.002
https://doi.org/10.1016/j.tibs.2004.03.002
Autor:
Martin A. Schwartz, Karla L. Ewalt, Paul Schimmel, Eleni Tzima, Mohammad Irani-Tehrani, John S. Reader
Publikováno v:
Proceedings of the National Academy of Sciences. 100:14903-14907
Human tryptophanyl-tRNA synthetase (TrpRS) is active in translation and angiogenesis. In particular, an N-terminally truncated fragment, T2-TrpRS, that is closely related to a natural splice variant is a potent antagonist of vascular endothelial grow
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1552511b41c210bcf26360f6cb940b50
https://doi.org/10.1073/pnas.2436330100
https://doi.org/10.1073/pnas.2436330100
Autor:
Lawrence Kleiman, Karin Musier-Forsyth, Paul Schimmel, Kiyotaka Shiba, Alan Rein, Karla L. Ewalt, Hassan Javanbakht, Sunghoon Kim, Rebecca C. Craven, Shan Cen
Publikováno v:
Journal of Virology. 76:13111-13115
The tRNAs used to prime reverse transcription in human immunodeficiency virus type 1 (HIV-1), Rous sarcoma virus (RSV), and Moloney murine leukemia virus (Mo-MuLV) are \batchmode \documentclass[fleqn,10pt,legalpaper]{article} \usepackage{amssymb} \us
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e9f8742fc61af92767ead2f25510a49
https://doi.org/10.1128/jvi.76.24.13111-13115.2002
https://doi.org/10.1128/jvi.76.24.13111-13115.2002
Publikováno v:
Biochemistry. 41:14232-14237
Aminoacyl-tRNA synthetases catalyze the attachment of amino acids to their cognate tRNAs. A link was recently established between protein biosynthesis and cytokine signal transduction. Human tyrosyl-tRNA synthetase can be split into two fragments, ea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8150b4560fb617a62820f34a3f71104c
https://doi.org/10.1021/bi0205395
https://doi.org/10.1021/bi0205395
Autor:
David A. Cheresh, Michael I. Dorrell, Karla L. Ewalt, Karen Kinder, Atsushi Otani, John Hood, Bonnie M. Slike, Paul Schimmel, Martin Friedlander
Publikováno v:
Proceedings of the National Academy of Sciences. 99:178-183
Pathological angiogenesis contributes directly to profound loss of vision associated with many diseases of the eye. Recent work suggests that human tyrosyl- and tryptophanyl-tRNA synthetases (TrpRS) link protein synthesis to signal transduction pathw
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4753c35e15d3a1942b3058acd93f176
https://doi.org/10.1073/pnas.012601899
https://doi.org/10.1073/pnas.012601899