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The NADH oxidase of Streptococcus pneumoniae : its involvement in competence and virulence

Molecular microbiology, 1999-12, Vol.34 (5), p.1018-1028

1999

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Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPγS

The EMBO journal, 1997-09, Vol.16 (18), p.5582-5591

1997

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Mechanism of renaturation of a large protein, aspartokinase-homoserine dehydrogenase

Biochemistry (Easton), 1987-05, Vol.26 (10), p.2785-2790

1987

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Urea-induced inactivation, dissociation and unfolding of the allosteric phosphofructokinase from Escherichia coli

Biochemistry (Easton), 1989-08, Vol.28 (17), p.6836-6841

1989

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Regulation of the Biosynthesis of Amino Acids of the Aspartate Family in Coliform Bacteria and Pseudomonads

Journal of Bacteriology, 1969-09, Vol.99 (3), p.791-801

1969

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The role of Glu187 in the regulation of phosphofructokinase by phosphoenolpyruvate

Journal of molecular biology, 1994, Vol.235 (1), p.68-72

1994

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Tetramer-Dimer Equilibrium of Phosphofructokinase and Formation of Hybrid Tetramers

Biochemistry (Easton), 1995-10, Vol.34 (40), p.13203-13210

1995

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Allosteric activation increases the maximum velocity of E. coli phosphofructokinase 1 1Edited by A. R. Fersht

Journal of molecular biology, 1997-04, Vol.267 (3), p.476-480

1997

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Allosteric activation increases the maximum velocity of E. coli phosphofructokinase

Journal of molecular biology, 1997-04, Vol.267 (3), p.476-480

1997

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Hypercooperativity Induced by Interface Mutations in the Phosphofructokinase fromEscherichia coli

Journal of molecular biology, 1995-02, Vol.246 (2), p.248-253

1995

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The primary structure of Escherichia coli K 12 aspartokinase I-homoserine dehydrogenase I

Biochimie, 1979, Vol.61 (5), p.733-738

1979

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Hypercooperativity induced by interface mutations in the phosphofructokinase from Escherichia coli

Journal of molecular biology, 1995-02, Vol.246 (2), p.248-253

1995

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Crystallization of d-lactate dehydrogenase from Lactobacillus bulgaricus

Journal of molecular biology, 1994-01, Vol.235 (1), p.370-371

1994

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Ordered disruption of subunit interfaces during the stepwise reversible dissociation of Escherichia coli phosphofructokinase with KSCN

Biochemistry (Easton), 1989-02, Vol.28 (4), p.1917-1922

1989

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Rétro-inhibition et répression de l'homosérine déshydrogénase d' Escherichia coli

Biochimica et biophysica acta, 1963, Vol.67, p.16-30

1963

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Rétro-inhibition et répression de l'homosérine déshydrogénase d'Escherichia coli

Biochimica et biophysica acta. Specialized section on enzymological subjects, 1963, Vol.67, p.16-30

1963

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Limited proteolysis at the carboxy end modifies interactions between the subunits of Escherichia phosphofructokinase

Biochemistry (Easton), 1986-05, Vol.25 (9), p.2490-2493

1986

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Ordered disruption of subunit interfaces during the stepwise reversible dissociation of Escherichia coli phosphofructokinase with potassium thiocyanate

Biochemistry (Easton), 1989-02, Vol.28 (4), p.1917-1922

1989

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A proteolyzed derivative of E. coli phosphofructokinase is no longer sensitive to allosteric effectors and still shows cooperativity in substrate binding

Biochemistry (Easton), 1982-12, Vol.21 (26), p.6656-6660

1982

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The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Isolation and characterisation of the peptides produced by cyanogen bromide

Biochimica et biophysica acta, 1978-08, Vol.535 (2), p.206-215

1978

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A proteolyzed derivative of Escherichia coli phosphofructokinase is no longer sensitive to allosteric effectors and still shows cooperativity in substrate binding

Biochemistry (Easton), 1982-12, Vol.21 (26), p.6656-6660

1982

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Limited proteolysis at the carboxy end modifies interactions between the subunits of Escherichia coli phosphofructokinase

Biochemistry (Easton), 1986-05, Vol.25 (9), p.2490-2493

1986

Volltextzugriff (PDF)

The primary structure of Escherichia coli K 12 aspartokinase I-homoserine dehydrogenase I

Biochimie, 1979-09, Vol.61 (5-6), p.733-738

1979

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The primary structure of Escherichia coli K 12 aspartokinase I-homoserine dehydrogenase I

Biochimie, 1979-09, Vol.61 (5), p.739-739

1979

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Enzymatic and genetic regulation of glycolysis in Lactobacillus delbrueckii subsp. bulgaricus

Lait, 1998, Vol.78 (1), p.85-90

1998

Volltextzugriff (PDF)

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The NADH oxidase of Streptococcus pneumoniae : its involvement in competence and virulence

Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPγS

Mechanism of renaturation of a large protein, aspartokinase-homoserine dehydrogenase

Urea-induced inactivation, dissociation and unfolding of the allosteric phosphofructokinase from Escherichia coli

Regulation of the Biosynthesis of Amino Acids of the Aspartate Family in Coliform Bacteria and Pseudomonads

The role of Glu187 in the regulation of phosphofructokinase by phosphoenolpyruvate

Tetramer-Dimer Equilibrium of Phosphofructokinase and Formation of Hybrid Tetramers

Allosteric activation increases the maximum velocity of E. coli phosphofructokinase 1 1Edited by A. R. Fersht

Allosteric activation increases the maximum velocity of E. coli phosphofructokinase

Hypercooperativity Induced by Interface Mutations in the Phosphofructokinase fromEscherichia coli

The primary structure of Escherichia coli K 12 aspartokinase I-homoserine dehydrogenase I

Hypercooperativity induced by interface mutations in the phosphofructokinase from Escherichia coli

Crystallization of d-lactate dehydrogenase from Lactobacillus bulgaricus

Ordered disruption of subunit interfaces during the stepwise reversible dissociation of Escherichia coli phosphofructokinase with KSCN

Rétro-inhibition et répression de l'homosérine déshydrogénase d' Escherichia coli

Rétro-inhibition et répression de l'homosérine déshydrogénase d'Escherichia coli

Limited proteolysis at the carboxy end modifies interactions between the subunits of Escherichia phosphofructokinase

Ordered disruption of subunit interfaces during the stepwise reversible dissociation of Escherichia coli phosphofructokinase with potassium thiocyanate

A proteolyzed derivative of E. coli phosphofructokinase is no longer sensitive to allosteric effectors and still shows cooperativity in substrate binding

The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Isolation and characterisation of the peptides produced by cyanogen bromide

A proteolyzed derivative of Escherichia coli phosphofructokinase is no longer sensitive to allosteric effectors and still shows cooperativity in substrate binding

Limited proteolysis at the carboxy end modifies interactions between the subunits of Escherichia coli phosphofructokinase

The primary structure of Escherichia coli K 12 aspartokinase I-homoserine dehydrogenase I

The primary structure of Escherichia coli K 12 aspartokinase I-homoserine dehydrogenase I

Enzymatic and genetic regulation of glycolysis in Lactobacillus delbrueckii subsp. bulgaricus

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