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  • Author: Avalos JL
  • References

Author: Avalos JL


References 27 references


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  • Kichuk T and Avalos JL (2025) Shape Matters: The Utility and Analysis of Altered Yeast Mitochondrial Morphology in Health, Disease, and Biotechnology. Int J Mol Sci 26(5) PMID:40076772
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  • Suresh P, et al. (2025) Growth inhibition of Saccharomyces cerevisiae by SUMO-specific nanobodies. Sci Rep 15(1):18368 PMID:40419540
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  • Tang AY, et al. (2025) Anti-Pdc1p Nanobody as a Genetically Encoded Inhibitor of Ethanol Production Enables Dual Transcriptional and Post-translational Controls of Yeast Fermentations. ACS Synth Biol 14(4):1072-1083 PMID:40098243
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  • Kichuk T, et al. (2024) Using MitER for 3D analysis of mitochondrial morphology and ER contacts. Cell Rep Methods 4(1):100692 PMID:38232737
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  • Tang AY, et al. (2024) Light-Induced Nanobody-Mediated Targeted Protein Degradation for Metabolic Flux Control. ACS Synth Biol 13(12):4110-4118 PMID:39527810
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  • Wegner SA and Avalos JL (2024) Mevalonate secretion is not mediated by a singular non-essential transporter in Saccharomyces cerevisiae. Biotechnol Notes 5:140-150 PMID:39498316
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  • Hoffman SM, et al. (2022) Light-Controlled Fermentations for Microbial Chemical and Protein Production. J Vis Exp PMID:35404352
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  • Zhang Y, et al. (2022) Biosensor for branched-chain amino acid metabolism in yeast and applications in isobutanol and isopentanol production. Nat Commun 13(1):270 PMID:35022416
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  • Hoffman SM, et al. (2021) Cellulosic biofuel production using emulsified simultaneous saccharification and fermentation (eSSF) with conventional and thermotolerant yeasts. Biotechnol Biofuels 14(1):157 PMID:34274018
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  • Lalwani MA, et al. (2021) Optogenetic Control of Microbial Consortia Populations for Chemical Production. ACS Synth Biol 10(8):2015-2029 PMID:34351122
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  • Wegner SA, et al. (2021) Engineering acetyl-CoA supply and ERG9 repression to enhance mevalonate production in Saccharomyces cerevisiae. J Ind Microbiol Biotechnol 48(9-10) PMID:34351398
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  • Zhao EM, et al. (2021) Optogenetic Amplification Circuits for Light-Induced Metabolic Control. ACS Synth Biol 10(5):1143-1154 PMID:33835777
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  • Duran L, et al. (2020) ¡Viva la mitochondria!: harnessing yeast mitochondria for chemical production. FEMS Yeast Res 20(6) PMID:32592388
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  • Hammer SK and Avalos JL (2020) Corrigendum to "Uncovering the role of branched-chain amino acid transaminases in Saccharomyces cerevisiae isobutanol biosynthesis" [Metab. Eng. 44 (2017) 302-312]. Metab Eng 61:438 PMID:32417202
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  • Hammer SK, et al. (2020) Mitochondrial Compartmentalization Confers Specificity to the 2-Ketoacid Recursive Pathway: Increasing Isopentanol Production in Saccharomyces cerevisiae. ACS Synth Biol 9(3):546-555 PMID:32049515
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  • Lane S, et al. (2020) Xylose assimilation enhances the production of isobutanol in engineered Saccharomyces cerevisiae. Biotechnol Bioeng 117(2):372-381 PMID:31631318
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  • Zhao EM, et al. (2020) Design and Characterization of Rapid Optogenetic Circuits for Dynamic Control in Yeast Metabolic Engineering. ACS Synth Biol 9(12):3254-3266 PMID:33232598
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  • Kuroda K, et al. (2019) Critical Roles of the Pentose Phosphate Pathway and GLN3 in Isobutanol-Specific Tolerance in Yeast. Cell Syst 9(6):534-547.e5 PMID:31734159
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  • Zhang Y, et al. (2019) Xylose utilization stimulates mitochondrial production of isobutanol and 2-methyl-1-butanol in Saccharomyces cerevisiae. Biotechnol Biofuels 12:223 PMID:31548865
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  • Zhao EM, et al. (2018) Optogenetic regulation of engineered cellular metabolism for microbial chemical production. Nature 555(7698):683-687 PMID:29562237
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  • Hammer SK and Avalos JL (2017) Harnessing yeast organelles for metabolic engineering. Nat Chem Biol 13(8):823-832 PMID:28853733
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  • Hammer SK and Avalos JL (2017) Uncovering the role of branched-chain amino acid transaminases in Saccharomyces cerevisiae isobutanol biosynthesis. Metab Eng 44:302-312 PMID:29037781
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  • Avalos JL, et al. (2013) Compartmentalization of metabolic pathways in yeast mitochondria improves the production of branched-chain alcohols. Nat Biotechnol 31(4):335-41 PMID:23417095
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  • Cosgrove MS, et al. (2006) The structural basis of sirtuin substrate affinity. Biochemistry 45(24):7511-21 PMID:16768447
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  • Avalos JL, et al. (2005) Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme. Mol Cell 17(6):855-68 PMID:15780941
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  • Avalos JL, et al. (2002) Structure of a Sir2 enzyme bound to an acetylated p53 peptide. Mol Cell 10(3):523-35 PMID:12408821
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  • Smith JS, et al. (2000) A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family. Proc Natl Acad Sci U S A 97(12):6658-63 PMID:10841563
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