Elizabeth Vierling

Affiliations: 
University of Arizona, Tucson, AZ 
Area:
Biochemistry
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"Elizabeth Vierling"
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Randall S. Alberte grad student 1982 Chicago
 (STRUCTURE AND BIOSYNTHESIS OF THE P700 CHLOROPHYLL A-PROTEIN)
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Publications

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Zhu L, Scafaro AP, Vierling E, et al. (2023) Heat tolerance of a tropical-subtropical rainforest tree species Polyscias elegans: time-dependent dynamic responses of physiological thermostability and biochemistry. The New Phytologist
Waters ER, Bezanilla M, Vierling E. (2023) ATAD3 Proteins: Unique Mitochondrial Proteins Essential for Life in Diverse Eukaryotic Lineages. Plant & Cell Physiology
Kim M, Swenson J, McLoughlin F, et al. (2022) Mutation of the polyadenylation complex subunit CstF77 reveals that mRNA 3' end formation and HSP101 levels are critical for a robust heat stress response. The Plant Cell
Kim M, Schulz V, Brings L, et al. (2021) mTERF18 and ATAD3 are required for mitochondrial nucleoid structure and their disruption confers heat tolerance in Arabidopsis thaliana. The New Phytologist
Liu T, Arsenault J, Vierling E, et al. (2021) Mitochondrial ATP Synthase Subunit d, a Component of the Peripheral Stalk, is Essential for Growth and Heat Stress Tolerance in Arabidopsis thaliana. The Plant Journal : For Cell and Molecular Biology
Waters ER, Vierling E. (2020) Plant small heat shock proteins - evolutionary and functional diversity. The New Phytologist
McLoughlin F, Kim M, Marshall RS, et al. (2019) HSP101 Interacts with the Proteasome and Promotes the Clearance of Ubiquitylated Protein Aggregates. Plant Physiology
Carra S, Alberti S, Benesch JLP, et al. (2019) Small heat shock proteins: multifaceted proteins with important implications for life. Cell Stress & Chaperones
Wang X, Hou L, Lu Y, et al. (2018) Metabolic adaptation of wheat grain contributes to a stable filling rate under heat stress. Journal of Experimental Botany. 69: 5531-5545
Santhanagopalan I, Degiacomi MT, Shepherd DA, et al. (2018) It takes a dimer to tango: Oligomeric small heat shock proteins dissociate to capture substrate. The Journal of Biological Chemistry
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