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Items: 1 to 20 of 61

1.
A Mutant of Yeast with a Defective Methionyl-Trna Synthetase
Calvin S. McLaughlin, Leland H. Hartwell
Genetics. 1969 Mar; 61(3): 557–566. doi: 10.1093/genetics/61.3.557
PMCID:
PMC1212224
SummaryPDF–566K
2.
Proofreading in vivo: editing of homocysteine by methionyl-tRNA synthetase in the yeast Saccharomyces cerevisiae.
H Jakubowski
EMBO J. 1991 Mar; 10(3): 593–598. doi: 10.1002/j.1460-2075.1991.tb07986.x
PMCID:
PMC452689
SummaryPage BrowsePDF–1.1M
3.
Primary structure of the Saccharomyces cerevisiae gene for methionyl-tRNA synthetase.
P Walter, J Gangloff, J Bonnet, Y Boulanger, J P Ebel, F Fasiolo
Proc Natl Acad Sci U S A. 1983 May; 80(9): 2437–2441. doi: 10.1073/pnas.80.9.2437
PMCID:
PMC393840
SummaryPage BrowsePDF–863K
4.
Strategy for the mass spectrometric verification and correction of the primary structures of proteins deduced from their DNA sequences.
B W Gibson, K Biemann
Proc Natl Acad Sci U S A. 1984 Apr; 81(7): 1956–1960. doi: 10.1073/pnas.81.7.1956
PMCID:
PMC345415
SummaryPage BrowsePDF–1.0M
5.
MARS variant associated with both recessive interstitial lung and liver disease and dominant Charcot-Marie-Tooth disease
Jonathan Rips, Rebecca Meyer-Schuman, Oded Breuer, Reuven Tsabari, Avraham Shaag, Shoshana Revel-Vilk, Shimon Reif, Orly Elpeleg, Anthony Antonellis, Tamar Harel
Eur J Med Genet. Author manuscript; available in PMC 2019 Oct 1.
Published in final edited form as: Eur J Med Genet. 2018 Oct; 61(10): 616–620. Published online 2018 Apr 12. doi: 10.1016/j.ejmg.2018.04.005
PMCID:
PMC6133759
AbstractArticlePDF–477K
6.
Biallelic Mutations of Methionyl-tRNA Synthetase Cause a Specific Type of Pulmonary Alveolar Proteinosis Prevalent on Réunion Island
Alice Hadchouel, Thomas Wieland, Matthias Griese, Enrico Baruffini, Bettina Lorenz-Depiereux, Laurent Enaud, Elisabeth Graf, Jean Christophe Dubus, Sonia Halioui-Louhaichi, Aurore Coulomb, Christophe Delacourt, Gertrud Eckstein, Ralf Zarbock, Thomas Schwarzmayr, François Cartault, Thomas Meitinger, Tiziana Lodi, Jacques de Blic, Tim M. Strom
Am J Hum Genet. 2015 May 7; 96(5): 826–831. doi: 10.1016/j.ajhg.2015.03.010
PMCID:
PMC4570277
AbstractArticlePDF–1008K
7.
Modulating the Structure and Function of an Aminoacyl-tRNA Synthetase Cofactor by Biotinylation
Chih-Yao Chang, Chia-Pei Chang, Shruti Chakraborty, Shao-Win Wang, Yi-Kuan Tseng, Chien-Chia Wang
J Biol Chem. 2016 Aug 12; 291(33): 17102–17111. Published online 2016 Jun 21. doi: 10.1074/jbc.M116.734343
PMCID:
PMC5016114
AbstractArticlePDF–1.9M
8.
Quaternary structure of the yeast Arc1p-aminoacyl-tRNA synthetase complex in solution and its compaction upon binding of tRNAs
Christine Koehler, Adam Round, Hannes Simader, Dietrich Suck, Dmitri Svergun
Nucleic Acids Res. 2013 Jan; 41(1): 667–676. Published online 2012 Nov 17. doi: 10.1093/nar/gks1072
PMCID:
PMC3592460
AbstractArticlePDF–5.6M
9.
Misacylation of tRNA with methionine in Saccharomyces cerevisiae
Elizabeth Wiltrout, Jeffrey M. Goodenbour, Mathieu Fréchin, Tao Pan
Nucleic Acids Res. 2012 Nov; 40(20): 10494–10506. Published online 2012 Aug 30. doi: 10.1093/nar/gks805
PMCID:
PMC3488245
AbstractArticlePDF–8.2M
10.
Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes
Hannes Simader, Michael Hothorn, Christine Köhler, Jerome Basquin, George Simos, Dietrich Suck
Nucleic Acids Res. 2006; 34(14): 3968–3879. Published online 2006 Aug 12. doi: 10.1093/nar/gkl560
PMCID:
PMC1557820
AbstractArticlePDF–2.0M
11.
The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases.
G Simos, A Segref, F Fasiolo, K Hellmuth, A Shevchenko, M Mann, E C Hurt
EMBO J. 1996 Oct 1; 15(19): 5437–5448.
PMCID:
PMC452286
SummaryPage BrowsePDF–3.1M
12.
The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p
Kyriaki Galani, Helge Großhans, Karina Deinert, Eduard C. Hurt, George Simos
EMBO J. 2001 Dec 3; 20(23): 6889–6898. doi: 10.1093/emboj/20.23.6889
PMCID:
PMC125769
AbstractArticlePDF–375K
13.
A Los1p-independent pathway for nuclear export of intronless tRNAs in Saccharomycescerevisiae
Wenqin Feng, Anita K. Hopper
Proc Natl Acad Sci U S A. 2002 Apr 16; 99(8): 5412–5417. doi: 10.1073/pnas.082682699
PMCID:
PMC122783
AbstractArticlePDF–361K
14.
Nuclear tRNA aminoacylation and its role in nuclear export of endogenous tRNAs in Saccharomycescerevisiae
Srimonti Sarkar, Abul K. Azad, Anita K. Hopper
Proc Natl Acad Sci U S A. 1999 Dec 7; 96(25): 14366–14371. doi: 10.1073/pnas.96.25.14366
PMCID:
PMC24442
AbstractArticlePDF–295K
15.
Reversible, specific, active aggregates of endogenous proteins assemble upon heat stress
Edward W.J. Wallace, Jamie L. Kear-Scott, Evgeny V. Pilipenko, Michael H. Schwartz, Pawel R. Laskowski, Alexandra E. Rojek, Christopher D. Katanski, Joshua A. Riback, Michael F. Dion, Alexander M. Franks, Edoardo M. Airoldi, Tao Pan, Bogdan A. Budnik, D. Allan Drummond
Cell. Author manuscript; available in PMC 2016 Sep 10.
Published in final edited form as: Cell. 2015 Sep 10; 162(6): 1286–1298. doi: 10.1016/j.cell.2015.08.041
PMCID:
PMC4567705
AbstractArticlePDF–3.2M
16.
Comprehensive characterization of mRNAs associated with yeast cytosolic aminoacyl-tRNA synthetases
Shahar Garin, Ofri Levi, Megan E. Forrest, Anthony Antonellis, Yoav S. Arava
RNA Biol. 2021; 18(12): 2605–2616. Published online 2021 Jun 10. doi: 10.1080/15476286.2021.1935116
PMCID:
PMC8632134
AbstractArticlePDF–3.3M
17.
A Protein–Protein Interaction Analysis Suggests a Wide Range of New Functions for the p21-Activated Kinase (PAK) Ste20
Ifeoluwapo Matthew Joshua, Meng Lin, Ariestia Mardjuki, Alessandra Mazzola, Thomas Höfken
Int J Mol Sci. 2023 Nov; 24(21): 15916. Published online 2023 Nov 2. doi: 10.3390/ijms242115916
PMCID:
PMC10647699
AbstractArticlePDF–5.4M
18.
Pseudouridine-mediated translation control of mRNA by methionine aminoacyl tRNA synthetase
Ofri Levi, Yoav S Arava
Nucleic Acids Res. 2021 Jan 11; 49(1): 432–443. Published online 2020 Dec 10. doi: 10.1093/nar/gkaa1178
PMCID:
PMC7797078
AbstractArticlePDF–3.3M
19.
The Hsp70 homolog Ssb and the 14-3-3 protein Bmh1 jointly regulate transcription of glucose repressed genes in Saccharomyces cerevisiae
Volker Hübscher, Kaivalya Mudholkar, Marco Chiabudini, Edith Fitzke, Tina Wölfle, Dietmar Pfeifer, Friedel Drepper, Bettina Warscheid, Sabine Rospert
Nucleic Acids Res. 2016 Jul 8; 44(12): 5629–5645. Published online 2016 Mar 21. doi: 10.1093/nar/gkw168
PMCID:
PMC4937304
AbstractArticlePDF–8.3M
20.
The elongation factor eEF3 (Yef3) interacts with mRNA in a translation independent manner
Nitzan Samra, Avigail Atir-Lande, Lilach Pnueli, Yoav Arava
BMC Mol Biol. 2015; 16: 17. Published online 2015 Sep 24. doi: 10.1186/s12867-015-0045-5
PMCID:
PMC4582935
AbstractArticlePDF–2.1M

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