| Year |
Citation |
Score |
| 2020 |
Chihade J. Mitochondrial aminoacyl-tRNA synthetases. The Enzymes. 48: 175-206. PMID 33837704 DOI: 10.1016/bs.enz.2020.07.003 |
0.515 |
|
| 2020 |
Kuhle B, Chihade J, Schimmel P. Relaxed sequence constraints favor mutational freedom in idiosyncratic metazoan mitochondrial tRNAs. Nature Communications. 11: 969. PMID 32080176 DOI: 10.1038/S41467-020-14725-Y |
0.604 |
|
| 2019 |
González-Serrano LE, Chihade JW, Sissler M. When a common biological role does not imply common disease outcomes: Disparate pathology linked to human mitochondrial aminoacyl-tRNA synthetases. The Journal of Biological Chemistry. PMID 30647134 DOI: 10.1074/Jbc.Rev118.002953 |
0.527 |
|
| 2019 |
Kennicott H, McCurdy C, Makori J, Chihade J. Pathogenic Mutations in a Human Mitochondrial Enzyme Affect Protein Stability The Faseb Journal. 33. DOI: 10.1096/fasebj.2019.33.1_supplement.630.5 |
0.368 |
|
| 2018 |
Hilander T, Zhou XL, Konovalova S, Zhang FP, Euro L, Chilov D, Poutanen M, Chihade J, Wang ED, Tyynismaa H. Editing activity for eliminating mischarged tRNAs is essential in mammalian mitochondria. Nucleic Acids Research. 46: 849-860. PMID 29228266 DOI: 10.1093/Nar/Gkx1231 |
0.58 |
|
| 2016 |
Fernández-Millán P, Schelcher C, Chihade J, Masquida B, Giegé P, Sauter C. Transfer RNA: From pioneering crystallographic studies to contemporary tRNA biology. Archives of Biochemistry and Biophysics. 602: 95-105. PMID 26968773 DOI: 10.1016/J.Abb.2016.03.005 |
0.448 |
|
| 2015 |
Euro L, Konovalova S, Asin-Cayuela J, Tulinius M, Griffin H, Horvath R, Taylor RW, Chinnery PF, Schara U, Thorburn DR, Suomalainen A, Chihade J, Tyynismaa H. Structural modeling of tissue-specific mitochondrial alanyl-tRNA synthetase (AARS2) defects predicts differential effects on aminoacylation. Frontiers in Genetics. 6: 21. PMID 25705216 DOI: 10.3389/Fgene.2015.00021 |
0.507 |
|
| 2006 |
Hati S, Ziervogel B, Sternjohn J, Wong FC, Nagan MC, Rosen AE, Siliciano PG, Chihade JW, Musier-Forsyth K. Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in "selective release" of noncognate amino acids. The Journal of Biological Chemistry. 281: 27862-72. PMID 16864571 DOI: 10.1074/Jbc.M605856200 |
0.576 |
|
| 2001 |
Lovato MA, Chihade JW, Schimmel P. Translocation within the acceptor helix of a major tRNA identity determinant. The Embo Journal. 20: 4846-53. PMID 11532948 DOI: 10.1093/Emboj/20.17.4846 |
0.528 |
|
| 2000 |
Chihade JW, Brown JR, Schimmel PR, Ribas De Pouplana L. Origin of mitochondria in relation to evolutionary history of eukaryotic alanyl-tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America. 97: 12153-7. PMID 11035802 DOI: 10.1073/Pnas.220388797 |
0.639 |
|
| 1999 |
Chihade JW, Schimmel P. Assembly of a catalytic unit for RNA microhelix aminoacylation using nonspecific RNA binding domains Proceedings of the National Academy of Sciences of the United States of America. 96: 12316-12321. PMID 10535919 DOI: 10.1073/Pnas.96.22.12316 |
0.523 |
|
| 1998 |
Chihade JW, Hayashibara K, Shiba K, Schimmel P. Strong Selective Pressure To Use G:U To Mark an RNA Acceptor Stem for Alanine† Biochemistry. 37: 9193-9202. PMID 9636067 DOI: 10.1021/Bi9804636 |
0.688 |
|
| 1996 |
Chihade JW, Horne DA. Single nucleotide modulation of uridine to pseudouridine rearrangement in transfer RNA catalyzed by pseudouridine synthase I. Journal of Molecular Recognition : Jmr. 9: 524-7. PMID 9174935 DOI: 10.1002/(Sici)1099-1352(199634/12)9:5/6<524::Aid-Jmr295>3.0.Co;2-4 |
0.588 |
|
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