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Review: The Arabidopsis β-amylase (BAM) gene family: Diversity of form and function

Plant science (Limerick), 2018-11, Vol.276, p.163-170

2018

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Weak Measurement of a Superconducting Qubit Reconciles Incompatible Operators

Physical review letters, 2021-03, Vol.126 (10), p.100403-100403, Article 100403

2021

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Maize β-amylase7 encodes 2 proteins using alternative transcriptional start sites: Nuclear BAM7 and plastidic BAM2

Plant physiology (Bethesda), 2023-08, Vol.192 (4), p.2871-2882

2023

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A Poverty of Objects: The Prose Poem and the Politics of Genre

Monroe, Jonathan

1, 1987

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Involvement of five catalytically active Arabidopsis β‐amylases in leaf starch metabolism and plant growth

Plant direct, 2020-02, Vol.4 (2), p.e00199-n/a

Monroe, Jonathan D.

2020

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Homologs of PROTEIN TARGETING TO STARCH Control Starch Granule Initiation in Arabidopsis Leaves

The Plant cell, 2017-07, Vol.29 (7), p.1657-1677

2017

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The BAM7 gene in Zea mays encodes a protein with similar structural and catalytic properties to Arabidopsis BAM2

Acta crystallographica. Section D, Biological crystallography., 2022-05, Vol.78 (5), p.560-570

2022

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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

Plant physiology (Bethesda), 2014-12, Vol.166 (4), p.1748-1763

2014

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Solution structure and assembly of β‐amylase 2 from Arabidopsis thaliana

Acta crystallographica. Section D, Biological crystallography., 2020-04, Vol.76 (4), p.357-365

2020

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Arabidopsis β-Amylase2 Is a K + -Requiring, Catalytic Tetramer with Sigmoidal Kinetics

Plant physiology (Bethesda), 2017-12, Vol.175 (4), p.1525-1535

2017

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β-Amylase–Like Proteins Function as Transcription Factors in Arabidopsis, Controlling Shoot Growth and Development

The Plant cell, 2011-04, Vol.23 (4), p.1391-1403

2011

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Glutathionylation Inhibits the Catalytic Activity of Arabidopsis β‑Amylase3 but Not That of Paralog β‑Amylase1

Biochemistry (Easton), 2018-02, Vol.57 (5), p.711-721

2018

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Quaternary Structure, Salt Sensitivity, and Allosteric Regulation of β-AMYLASE2 From Arabidopsis thaliana

Frontiers in plant science, 2018-08, Vol.9, p.1176-1176

2018

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SG1120-1202: Mass-quenching as Tracked by UV Emission in the Group Environment at z = 0.37

The Astrophysical journal, 2017-02, Vol.836 (1), p.7

2017

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Dynamic gating of substrate binding in β‐amylase2 from Arabidopsis thaliana

The FASEB journal, 2022-05, Vol.36 (S1), p.n/a

2022

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Abstract 1948 Complex formation of Arabidopsis thaliana alpha-amylase 3 with beta-amylase 9

The Journal of biological chemistry, 2024-03, Vol.300 (3), p.106210, Article 106210

2024

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α-amylase (At4g25000) in Arabidopsis leaves is secreted and induced by biotic and abiotic stress

Plant, cell and environment, 2007-04, Vol.30 (4), p.388-398

2007

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Abstract 2103: X-Ray Scattering of Carbohydrate Chains in Solution

The Journal of biological chemistry, 2023, Vol.299 (3), p.103758, Article 103758

2023

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Abstract 1802 A Colorimetric Assay to Determine Substrate Specificity of Beta-Amylases

The Journal of biological chemistry, 2024-03, Vol.300 (3), p.106193, Article 106193

2024

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Investigation into the Redox Regulation of the Arabidopsis β‐amylase BAM1

The FASEB journal, 2021-05, Vol.35 (S1), p.n/a, Article fasebj.2021.35.S1.03449

2021

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Abstract 2059: Structural Modeling and Analysis of [beta]-amylase9

The Journal of biological chemistry, 2023, Vol.299 (3), p.104107, Article 104107

2023

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Abstract 2213: Arabidopsis β-amylase9 interacts with and enhances the activity of α-amylase3

The Journal of biological chemistry, 2023, Vol.299 (3), p.104134, Article 104134

2023

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A Continuous Fluorescent Assay for β‐Amylase Activity

The FASEB journal, 2020-04, Vol.34 (S1), p.1-1

2020

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Investigation into the Structure and Activity of the Arabidopsis β‐amylase BAM1

The FASEB journal, 2022-05, Vol.36 (S1), p.n/a

2022

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Structural comparison of the Arabidopsis thaliana family of β‐amylases

The FASEB journal, 2018-04, Vol.32 (S1), p.792.12-792.12

2018

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Review: The Arabidopsis β-amylase (BAM) gene family: Diversity of form and function

Weak Measurement of a Superconducting Qubit Reconciles Incompatible Operators

Maize β-amylase7 encodes 2 proteins using alternative transcriptional start sites: Nuclear BAM7 and plastidic BAM2

A Poverty of Objects: The Prose Poem and the Politics of Genre

Involvement of five catalytically active Arabidopsis β‐amylases in leaf starch metabolism and plant growth

Homologs of PROTEIN TARGETING TO STARCH Control Starch Granule Initiation in Arabidopsis Leaves

The BAM7 gene in Zea mays encodes a protein with similar structural and catalytic properties to Arabidopsis BAM2

β-Amylase1 and β-Amylase3 Are Plastidic Starch Hydrolases in Arabidopsis That Seem to Be Adapted for Different Thermal, pH, and Stress Conditions

Solution structure and assembly of β‐amylase 2 from Arabidopsis thaliana

Arabidopsis β-Amylase2 Is a K + -Requiring, Catalytic Tetramer with Sigmoidal Kinetics

β-Amylase–Like Proteins Function as Transcription Factors in Arabidopsis, Controlling Shoot Growth and Development

Glutathionylation Inhibits the Catalytic Activity of Arabidopsis β‑Amylase3 but Not That of Paralog β‑Amylase1

Quaternary Structure, Salt Sensitivity, and Allosteric Regulation of β-AMYLASE2 From Arabidopsis thaliana

SG1120-1202: Mass-quenching as Tracked by UV Emission in the Group Environment at z = 0.37

Dynamic gating of substrate binding in β‐amylase2 from Arabidopsis thaliana

Abstract 1948 Complex formation of Arabidopsis thaliana alpha-amylase 3 with beta-amylase 9

α-amylase (At4g25000) in Arabidopsis leaves is secreted and induced by biotic and abiotic stress

Abstract 2103: X-Ray Scattering of Carbohydrate Chains in Solution

Abstract 1802 A Colorimetric Assay to Determine Substrate Specificity of Beta-Amylases

Investigation into the Redox Regulation of the Arabidopsis β‐amylase BAM1

Abstract 2059: Structural Modeling and Analysis of [beta]-amylase9

Abstract 2213: Arabidopsis β-amylase9 interacts with and enhances the activity of α-amylase3

A Continuous Fluorescent Assay for β‐Amylase Activity

Investigation into the Structure and Activity of the Arabidopsis β‐amylase BAM1

Structural comparison of the Arabidopsis thaliana family of β‐amylases

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