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Relevant bibliographies by topics / Prolyl-tRNA synthetase

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Journal articles
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Conference papers

Academic literature on the topic 'Prolyl-tRNA synthetase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Prolyl-tRNA synthetase"

1

Jacquin-Becker, Clarisse, Ivan Ahel, Alexandre Ambrogelly, Benfang Ruan, Dieter Söll, and Constantinos Stathopoulos. "Cysteinyl-tRNA formation and prolyl-tRNA synthetase." FEBS Letters 514, no. 1 (2002): 34–36. http://dx.doi.org/10.1016/s0014-5793(02)02331-1.

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Hahn, Hyunggu, Sang Ho Park, Hyun-Jung Kim, Sunghoon Kim, and Byung Woo Han. "The DRS–AIMP2–EPRS subcomplex acts as a pivot in the multi-tRNA synthetase complex." IUCrJ 6, no. 5 (2019): 958–67. http://dx.doi.org/10.1107/s2052252519010790.

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Aminoacyl-tRNA synthetases (ARSs) play essential roles in protein biosynthesis as well as in other cellular processes, often using evolutionarily acquired domains. For possible cooperativity and synergistic effects, nine ARSs assemble into the multi-tRNA synthetase complex (MSC) with three scaffold proteins: aminoacyl-tRNA synthetase complex-interacting multifunctional proteins 1, 2 and 3 (AIMP1, AIMP2 and AIMP3). X-ray crystallographic methods were implemented in order to determine the structure of a ternary subcomplex of the MSC comprising aspartyl-tRNA synthetase (DRS) and two glutathione S

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3

Cen, Shan, Hassan Javanbakht, Sunghoon Kim, et al. "Retrovirus-Specific Packaging of Aminoacyl-tRNA Synthetases with Cognate Primer tRNAs." Journal of Virology 76, no. 24 (2002): 13111–15. http://dx.doi.org/10.1128/jvi.76.24.13111-13115.2002.

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ABSTRACT 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} \usepackage{amsfonts} \usepackage{amsmath} \pagestyle{empty} \begin{document} \(tRNA_{3}^{Lys}\) \end{document} , tRNATrp, and tRNAPro, respectively. Using antibodies to the three cognate human aminoacyl-tRNA synthetases, we found that only lysyl-tRNA synthetase (LysRS) is present in HIV-1, only tryptophanyl-tRNA synthetase (TrpRS) is present

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Eswarappa, Sandeep M., Alka A. Potdar, Sarthak Sahoo, Santhosh Sankar, and Paul L. Fox. "Metabolic origin of the fused aminoacyl-tRNA synthetase, glutamyl-prolyl-tRNA synthetase." Journal of Biological Chemistry 293, no. 49 (2018): 19148–56. http://dx.doi.org/10.1074/jbc.ra118.004276.

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Sampath, Prabha, Barsanjit Mazumder, Vasudevan Seshadri, et al. "Noncanonical Function of Glutamyl-Prolyl-tRNA Synthetase." Cell 119, no. 2 (2004): 195–208. http://dx.doi.org/10.1016/j.cell.2004.09.030.

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6

Ambrogelly, Alexandre, Satwik Kamtekar, Constantinos Stathopoulos, Dexter Kennedy, and Dieter Söll. "Asymmetric behavior of archaeal prolyl-tRNA synthetase." FEBS Letters 579, no. 27 (2005): 6017–22. http://dx.doi.org/10.1016/j.febslet.2005.09.025.

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7

Son, Jonghyeon, Eun Hye Lee, Minyoung Park, et al. "Conformational changes in human prolyl-tRNA synthetase upon binding of the substrates proline and ATP and the inhibitor halofuginone." Acta Crystallographica Section D Biological Crystallography 69, no. 10 (2013): 2136–45. http://dx.doi.org/10.1107/s0907444913020556.

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Aminoacyl-tRNA synthetases recognize cognate amino acids and tRNAs from their noncognate counterparts and catalyze the formation of aminoacyl-tRNAs. Halofuginone (HF), a coccidiostat used in veterinary medicine, exerts its effects by acting as a high-affinity inhibitor of the enzyme glutamyl-prolyl-tRNA synthetase (EPRS). In order to elucidate the precise molecular basis of this inhibition mechanism of human EPRS, the crystal structures of the prolyl-tRNA synthetase domain of human EPRS (hPRS) at 2.4 Å resolution (hPRS-apo), ofhPRS complexed with ATP and the substrate proline at 2.3 Å resoluti

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8

Del Monte, U., S. Capaccioli, G. Neri Cini, R. Perego, R. Caldini, and M. Chevanne. "Effects of liver regeneration on tRNA contents and aminoacyl-tRNA synthetase activities and sedimentation patterns." Biochemical Journal 236, no. 1 (1986): 163–69. http://dx.doi.org/10.1042/bj2360163.

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The tRNA content and aminoacyl-tRNA synthetases of regenerating liver in the phase of rapid growth were compared with those of livers from both intact and sham-operated rats. At 48 h after hepatectomy, the amount of active tRNA (called ‘total acceptor capacity’) is significantly higher in regenerating liver than in control livers, owing to a general, possibly not uniform, increase in the various tRNA families, which suggests that it may contribute to the increased protein synthesis and to decreased protein degradation as well. The activities of most, but not of all, aminoacyl-tRNA synthetases

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9

Liu, Ziwei, Oscar Vargas-Rodriguez, Yuki Goto, et al. "Homologous trans-editing factors with broad tRNA specificity prevent mistranslation caused by serine/threonine misactivation." Proceedings of the National Academy of Sciences 112, no. 19 (2015): 6027–32. http://dx.doi.org/10.1073/pnas.1423664112.

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Aminoacyl-tRNA synthetases (ARSs) establish the rules of the genetic code, whereby each amino acid is attached to a cognate tRNA. Errors in this process lead to mistranslation, which can be toxic to cells. The selective forces exerted by species-specific requirements and environmental conditions potentially shape quality-control mechanisms that serve to prevent mistranslation. A family of editing factors that are homologous to the editing domain of bacterial prolyl-tRNA synthetase includes the previously characterized trans-editing factors ProXp-ala and YbaK, which clear Ala-tRNAPro and Cys-tR

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Kim, Yeonjin, Mark S. Sundrud, Changqian Zhou, et al. "Aminoacyl-tRNA synthetase inhibition activates a pathway that branches from the canonical amino acid response in mammalian cells." Proceedings of the National Academy of Sciences 117, no. 16 (2020): 8900–8911. http://dx.doi.org/10.1073/pnas.1913788117.

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Signaling pathways that sense amino acid abundance are integral to tissue homeostasis and cellular defense. Our laboratory has previously shown that halofuginone (HF) inhibits the prolyl-tRNA synthetase catalytic activity of glutamyl-prolyl-tRNA synthetase (EPRS), thereby activating the amino acid response (AAR). We now show that HF treatment selectively inhibits inflammatory responses in diverse cell types and that these therapeutic benefits occur in cells that lack GCN2, the signature effector of the AAR. Depletion of arginine, histidine, or lysine from cultured fibroblast-like synoviocytes

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Dissertations / Theses on the topic "Prolyl-tRNA synthetase"

1

Oshule, Paul Sifuna. "Biochemical Characterization of Trypanosoma cruzi Prolyl-tRNA Synthetase." University of Toledo / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=toledo1388662531.

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Chen, Lin. "Characterization of Prolyl-tRNA Synthetase, YbaK, and ProXp-ala Editing Mechanism." The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu148053070268849.

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Das, Mom. "Mechanistic Studies of Class II Bacterial Prolyl-tRNA Synthetase and YbaK Editing." The Ohio State University, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=osu1337922934.

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Sackes, Zubeyde. "Probing Editing Domain Conformational Changes Upon E. coli Prolyl-tRNA Synthetase•YbaK Complex Formation." The Ohio State University, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=osu1291022397.

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5

Tanimoto, Akiko. "Investigation of the Editing Mechanism of Prolyl-tRNA Synthetase and Characterization of RNase P Variants by Mass Spectrometry." The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu1471848969.

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6

Sanford, Brianne. "Role of Coupled Dynamics and a Strictly Conserved Lysine Residue in the Function of Bacterial Prolyl-tRNA Synthetase and Substrate Binding by a Related trans-Editing Enzyme ProXp-ala." The Ohio State University, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=osu1397645941.

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7

Eriani, Gilbert. "Recherche des elements structuraux des aspartyl-, prolyl- et arginyl-trna synthetases impliques dans leurs activites catalytiques." Université Louis Pasteur (Strasbourg) (1971-2008), 1990. http://www.theses.fr/1990STR13042.

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Les domaines fonctionnels de plusieurs aminoacyl-trna synthetases (aars) ont ete etudies par essentiellement deux grandes approches: par mutagenese des genes et analyse de l'effet sur les constantes catalytiques, et par la determination de nouvelles sequences d'aars dans le but de mettre en evidence, par comparaison de sequence, des homologies voir des motifs consensus tres conserves pouvant refleter leur importance fonctionnelle. L'asprs de levure a ainsi ete sondee par differentes methodes de modification de la proteine dont les resultats nous conduisent a proposer un modele dans lequel site

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8

Khang, Nguyen Viet, and 阮越康. "Bacillus thuringiensis possesses two prolyl-tRNA synthetase genes of distinct origins." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/62b57j.

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碩士<br>國立中央大學<br>生命科學系<br>106<br>Prolyl-tRNA synthetase (ProRS) is a class II synthetase which, according to sequence analysis, occurs in various organisms with one of two distinct structural architectures: prokaryotic-like and eukaryotic-like. While most of bacteria contain only one prokaryotic-like ProRS gene, Bacillus thuringiensis possesses two ProRS genes: proS1 and proS2. Intriguingly, both genes have different origins in which the expression of proS1 is much higher than that of proS2. Based on cognate tRNAPro identity elements, proS1 is supposed to be constitutive, whereas the function o

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Chen, Ting-Chun, and 陳亭均. "Glutamyl-prolyl-tRNA synthetase and its related complex regulate ER stress-induced cytotoxicity." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/4r2q84.

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10

Yang, Tsu Hao, and 楊祖豪. "Glutamyl-prolyl-tRNA synthetase and its associated proteins dictate ER stress-induced cytotoxicity." Thesis, 2016. http://ndltd.ncl.edu.tw/handle/65122398469942267401.

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Conference papers on the topic "Prolyl-tRNA synthetase"

1

Lee, C. H., D. W. Kim, M. Cho, et al. "Glutamyl-Prolyl-tRNA-Synthetase as a Novel Biomarker for Idiopathic Pulmonary Fibrosis." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a2275.

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2

Park, M. Y., J. Heo, Y. K. Kim, et al. "Safety, Tolerability and Pharmacokinetics/Pharmacodynamic Assessment of an Oral, Selective Prolyl-tRNA Synthetase Inhibitor, DWN12088, for the Treatment of Idiopathic Pulmonary Fibrosis in Healthy Subjects." In American Thoracic Society 2021 International Conference, May 14-19, 2021 - San Diego, CA. American Thoracic Society, 2021. http://dx.doi.org/10.1164/ajrccm-conference.2021.203.1_meetingabstracts.a1897.

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