Susan A. Martinis
Affiliations: | University of Houston, Houston, TX, United States |
Area:
BiochemistryGoogle:
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Children
Sign in to add traineeTommie L. Lincecum | grad student | 2003 | University of Houston |
Richard S. Mursinna | grad student | 2003 | University of Houston |
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Publications
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Baymiller M, Nordick B, Forsyth CM, et al. (2022) Tissue-specific alternative splicing separates the catalytic and cell signaling functions of human leucyl-tRNA synthetase. The Journal of Biological Chemistry. 101757 |
Weitzel CS, Li L, Zhang C, et al. (2020) Duplication of leucyl-tRNA synthetase in an archaeal extremophile may play a role in adaptation to variable environmental conditions. The Journal of Biological Chemistry |
Son K, You JS, Yoon MS, et al. (2019) Nontranslational function of leucyl-tRNA synthetase regulates myogenic differentiation and skeletal muscle regeneration. The Journal of Clinical Investigation. 130 |
Stephen J, Nampoothiri S, Banerjee A, et al. (2018) Loss of function mutations in VARS encoding cytoplasmic valyl-tRNA synthetase cause microcephaly, seizures, and progressive cerebral atrophy. Human Genetics |
Kim JH, Lee C, Lee M, et al. (2017) Control of leucine-dependent mTORC1 pathway through chemical intervention of leucyl-tRNA synthetase and RagD interaction. Nature Communications. 8: 732 |
Zhao H, Martinis S. (2016) Isolation of bacterial compartments to track movement of protein synthesis factors. Methods (San Diego, Calif.) |
Zhao H, Palencia A, Seiradake E, et al. (2015) Analysis of the Resistance Mechanism of a Benzoxaborole Inhibitor Reveals Insight into the Leucyl-tRNA Synthetase Editing Mechanism. Acs Chemical Biology. 10: 2277-85 |
Pang YL, Poruri K, Martinis SA. (2014) tRNA synthetase: tRNA aminoacylation and beyond. Wiley Interdisciplinary Reviews. Rna. 5: 461-80 |
Yao P, Poruri K, Martinis SA, et al. (2014) Non-catalytic regulation of gene expression by aminoacyl-tRNA synthetases. Topics in Current Chemistry. 344: 167-87 |
Li L, Palencia A, Lukk T, et al. (2013) Leucyl-tRNA synthetase editing domain functions as a molecular rheostat to control codon ambiguity in Mycoplasma pathogens. Proceedings of the National Academy of Sciences of the United States of America. 110: 3817-22 |