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Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals

Enzyme and microbial technology, 2011-10, Vol.49 (5), p.429-440

2011

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α-Amylase: an enzyme specificity found in various families of glycoside hydrolases

Cellular and molecular life sciences : CMLS, 2014-04, Vol.71 (7), p.1149-1170

2014

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Starch-binding domains as CBM families–history, occurrence, structure, function and evolution

Biotechnology advances, 2019-12, Vol.37 (8), p.107451-107451, Article 107451

2019

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A new clan of CBM families based on bioinformatics of starch‐binding domains from families CBM20 and CBM21

The FEBS journal, 2005-11, Vol.272 (21), p.5497-5513

2005

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A remote but significant sequence homology between glycoside hydrolase clan GH-H and family GH31

FEBS letters, 2007-04, Vol.581 (7), p.1261-1268

2007

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The starch‐binding domain family CBM41—An in silico analysis of evolutionary relationships

Proteins, structure, function, and bioinformatics, 2017-08, Vol.85 (8), p.1480-1492

2017

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The proteinaceous inhibitor of limit dextrinase in barley and malt

BBA - Proteins and Proteomics, 2004-02, Vol.1696 (2), p.165-170

MacGregor, E.Ann

2004

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Relation between domain evolution, specificity, and taxonomy of the α‐amylase family members containing a C‐terminal starch‐binding domain

European journal of biochemistry, 2003-02, Vol.270 (4), p.635-645

2003

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[alpha]-Amylase: an enzyme specificity found in various families of glycoside hydrolases

Cellular and molecular life sciences : CMLS, 2014-04, Vol.71 (7), p.1149

2014

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In the clinic. Migraine

Annals of internal medicine, 2013-11, Vol.159 (9), p.ITC5

MacGregor, E Ann

2013

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Possible structure and active site residues of starch, glycogen, and sucrose synthases

Journal of protein chemistry, 2002-05, Vol.21 (4), p.297-306

MacGregor, E Ann

2002

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Relationship of sequence and structure to specificity in the α-amylase family of enzymes

Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology, 2001-03, Vol.1546 (1), p.1-20

2001

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A circularly permuted α-amylase-type α/β-barrel structure in glucan-synthesizing glucosyltransferases

FEBS letters, 1996-01, Vol.378 (3), p.263-266

1996

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Substrate Binding and Catalytic Mechanism of a Barley β-d-Glucosidase/(1,4)-β-d-Glucan Exohydrolase

The Journal of biological chemistry, 1998-05, Vol.273 (18), p.11134-11143

1998

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Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (beta/alpha)8-barrel domain and evolutionary relationship to other amylolytic enzymes

Journal of protein chemistry, 1993-12, Vol.12 (6), p.791-805

1993

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Models for the action of barley alpha-amylase isozymes on linear substrates

Carbohydrate research, 1994-05, Vol.257 (2), p.249-268

1994

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Relationships Between Structure and Activity in the α-Amylase Family of Starch-metabolising Enzymes

Starch - Stärke, 1993, Vol.45 (7), p.232-237

MacGregor, E. Ann

1993

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The action of germinated barley alpha-amylases on linear maltodextrins

Carbohydrate research, 1992-04, Vol.227, p.301-313

1992

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Substrate Binding and Catalytic Mechanism of a Barley Î²-d-Glucosidase/(1,4)-Î²-d-Glucan Exohydrolase

The Journal of biological chemistry, 1998-05, Vol.273 (18), p.11134

1998

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Influence of pH on the hydrolysis of p-nitrophenyl maltodextrins by alpha-amylase 2 from malted barley

Carbohydrate research, 1998, Vol.313 (2), p.139-143

1998

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Models for the action of barley alpha-amylase isozymes on linear substrates: Carbohydrate Research

Carbohydrate research, 1994-11, Vol.264 (1), p.C7-C7

1994

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Models for the action of barley alpha-amylase isozymes on linear substrates

Carbohydrate research, 1994-11, Vol.264 (1), p.C7

1994

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Structure and activity of some starch-metabolising enzymes

Progress in Biotechnology, 1996, Vol.12, p.109-124

Ann MacGregor, E.

1996

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α-amylase structure and activity

Journal of protein chemistry, 1988-08, Vol.7 (4), p.399-415

MACGREGOR, E. A

1988

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24-Hour Urinary Sodium and Potassium Excretion and Cardiovascular Risk

The New England journal of medicine, 2022-01, Vol.386 (3), p.252-263

2022

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Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals

α-Amylase: an enzyme specificity found in various families of glycoside hydrolases

Starch-binding domains as CBM families–history, occurrence, structure, function and evolution

A new clan of CBM families based on bioinformatics of starch‐binding domains from families CBM20 and CBM21

A remote but significant sequence homology between glycoside hydrolase clan GH-H and family GH31

The starch‐binding domain family CBM41—An in silico analysis of evolutionary relationships

The proteinaceous inhibitor of limit dextrinase in barley and malt

Relation between domain evolution, specificity, and taxonomy of the α‐amylase family members containing a C‐terminal starch‐binding domain

[alpha]-Amylase: an enzyme specificity found in various families of glycoside hydrolases

In the clinic. Migraine

Possible structure and active site residues of starch, glycogen, and sucrose synthases

Relationship of sequence and structure to specificity in the α-amylase family of enzymes

A circularly permuted α-amylase-type α/β-barrel structure in glucan-synthesizing glucosyltransferases

Substrate Binding and Catalytic Mechanism of a Barley β-d-Glucosidase/(1,4)-β-d-Glucan Exohydrolase

Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (beta/alpha)8-barrel domain and evolutionary relationship to other amylolytic enzymes

Models for the action of barley alpha-amylase isozymes on linear substrates

Relationships Between Structure and Activity in the α-Amylase Family of Starch-metabolising Enzymes

The action of germinated barley alpha-amylases on linear maltodextrins

Substrate Binding and Catalytic Mechanism of a Barley Î²-d-Glucosidase/(1,4)-Î²-d-Glucan Exohydrolase

Influence of pH on the hydrolysis of p-nitrophenyl maltodextrins by alpha-amylase 2 from malted barley

Models for the action of barley alpha-amylase isozymes on linear substrates: Carbohydrate Research

Models for the action of barley alpha-amylase isozymes on linear substrates

Structure and activity of some starch-metabolising enzymes

α-amylase structure and activity

24-Hour Urinary Sodium and Potassium Excretion and Cardiovascular Risk

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