Publications by authors named "Jonathan D Monroe"

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Functional Characterization of Arabidopsis α-Amylase3 (AMY3): Amylose Specificity and Structural Insights into Its Duplex Carbohydrate-Binding Module.
Ruhi Rahman, Sara E Scanlan, Fady Sidarous, Jonathan D Monroe, Christopher E Berndsen

bioRxiv· September 2025

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The Pseudoenzyme β-Amylase9 From Arabidopsis Activates α-Amylase3: A Possible Mechanism to Promote Stress-Induced Starch Degradation.
Christopher E Berndsen, Amanda R Storm, Angelina M Sardelli, Sheikh R Hossain, Kristen R Clermont, Jonathan D Monroe

Proteins· June 2025

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Malate dehydrogenase in plants: evolution, structure, and a myriad of functions.
Lisa M Baird, Christopher E Berndsen, Jonathan D Monroe

Essays Biochem· October 2024

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The pseudoenzyme β-amylase9 from Arabidopsis binds to and enhances the activity of α-amylase3: A possible mechanism to promote stress-induced starch degradation.
Christopher E Berndsen, Amanda R Storm, Angelina M Sardelli, Sheikh R Hossain, Kristen R Clermont, Jonathan D Monroe

bioRxiv· August 2024

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Maize β-amylase7 encodes 2 proteins using alternative transcriptional start sites: Nuclear BAM7 and plastidic BAM2.
Kenan E Ozcan, Jonathan D Monroe

Plant Physiol· August 2023

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The BAM7 gene in Zea mays encodes a protein with similar structural and catalytic properties to Arabidopsis BAM2.
Claire M Ravenburg, McKayla B Riney, Jonathan D Monroe, Christopher E Berndsen

Acta Crystallogr D Struct Biol· May 2022

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Solution structure and assembly of β-amylase 2 from Arabidopsis thaliana.
Nithesh P Chandrasekharan, Claire M Ravenburg, Ian R Roy, Jonathan D Monroe, Christopher E Berndsen

Acta Crystallogr D Struct Biol· April 2020

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Involvement of five catalytically active Arabidopsis β-amylases in leaf starch metabolism and plant growth.
Jonathan D Monroe

Plant Direct· February 2020

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Review: The Arabidopsis β-amylase (BAM) gene family: Diversity of form and function.
Jonathan D Monroe, Amanda R Storm

Plant Sci· November 2018

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Quaternary Structure, Salt Sensitivity, and Allosteric Regulation of β-AMYLASE2 From .
Jonathan D Monroe, Lauren E Pope, Jillian S Breault, Christopher E Berndsen, Amanda R Storm

Front Plant Sci· August 2018

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Glutathionylation Inhibits the Catalytic Activity of Arabidopsis β-Amylase3 but Not That of Paralog β-Amylase1.
Amanda R Storm, Matthew R Kohler, Christopher E Berndsen, Jonathan D Monroe

Biochemistry· February 2018

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Arabidopsis β-Amylase2 Is a K-Requiring, Catalytic Tetramer with Sigmoidal Kinetics.
Jonathan D Monroe, Jillian S Breault, Lauren E Pope, Catherine E Torres, Tewaldemedhine B Gebrejesus

Plant Physiol· December 2017

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β-Amylase1 and β-amylase3 are plastidic starch hydrolases in Arabidopsis That Seem to Be Adapted for Different Thermal, pH, and stress conditions.
Jonathan D Monroe, Amanda R Storm, Elizabeth M Badley, Michael D Lehman, Samantha M Platt

Plant Physiol· December 2014

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β-amylase-like proteins function as transcription factors in Arabidopsis, controlling shoot growth and development.
Heike Reinhold, Sebastian Soyk, Klára Simková, Carmen Hostettler, John Marafino, Jonathan D Monroe

Plant Cell· April 2011

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Genomics and bioinformatics in undergraduate curricula: Contexts for hybrid laboratory/lecture courses for entering and advanced science students.
Louise Temple, Steven G Cresawn, Jonathan D Monroe

Biochem Mol Biol Educ· January 2010

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An alpha-amylase (At4g25000) in Arabidopsis leaves is secreted and induced by biotic and abiotic stress.
Elizabeth A Doyle, Ashleigh M Lane, James M Sides, Mary Beth Mudgett, Jonathan D Monroe

Plant Cell Environ· April 2007

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