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Thermal stability and heat transfer in the reservoir low-temperature network

Journal of physics. Conference series, 2019-11, Vol.1343 (1), p.12113

2019

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Spontaneous Deamidation and Isomerization of Asn108 in Prion Peptide 106–126 and in Full-Length Prion Protein

Biochemical and biophysical research communications, 1999-08, Vol.261 (3), p.578-583

1999

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Neurotoxicity of prion peptide 106-126 not confirmed

FEBS letters, 1999-09, Vol.458 (1), p.65-68

1999

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The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system

Journal of molecular biology, 1997-06, Vol.269 (5), p.757-768

1997

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Control of the DnaK Chaperone Cycle by Substoichiometric Concentrations of the Co-chaperones DnaJ and GrpE

The Journal of biological chemistry, 1998-03, Vol.273 (12), p.6643-6649

1998

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Structural Studies of the Catalytic Reaction Pathway of a Hyperthermophilic Histidinol-phosphate Aminotransferase

The Journal of biological chemistry, 2004-05, Vol.279 (20), p.21478-21488

2004

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Modulation of the activity of mitochondrial aspartate aminotransferase H352C by the redox state of the engineered interdomain disulfide bond

The Journal of biological chemistry, 1994-10, Vol.269 (41), p.25432-25436

1994

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Mitochondrial aspartate aminotransferase 27/32-410. Partially active enzyme derivative produced by limited proteolytic cleavage of native enzyme

The Journal of biological chemistry, 1980-11, Vol.255 (21), p.10284-10289

1980

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Chemical modification of a functional arginyl residue (Arg 292) of mitochondrial aspartate aminotransferase. Identification as the binding site for the distal carboxylate group of the substrate

The Journal of biological chemistry, 1982-06, Vol.257 (12), p.6745-6750

1982

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Conformational changes in aspartate aminotransferase. Effect of active site ligands on peptide hydrogen-deuterium exchange

The Journal of biological chemistry, 1985-09, Vol.260 (21), p.11414-11421

1985

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Reported channel formation by prion protein fragment 106–126 in planar lipid bilayers cannot be reproduced

FEBS letters, 2000-06, Vol.474 (2), p.255-256

2000

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Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes : regio-specific α, β and γ families

European journal of biochemistry, 1994-02, Vol.219 (3), p.953-960

1994

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Multiple evolutionary origin of pyridoxal‐5′‐phosphate‐dependent amino acid decarboxylases

European journal of biochemistry, 1994-05, Vol.221 (3), p.997-1002

1994

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Active-site Arg → Lys Substitutions Alter Reaction and Substrate Specificity of Aspartate Aminotransferase

The Journal of biological chemistry, 1997-08, Vol.272 (35), p.21932-21937

1997

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Rates of Evolution of Pyridoxal-5′- Phosphate-Dependent Enzymes

Biochemical and biophysical research communications, 2000-04, Vol.270 (2), p.576-580

2000

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Analysis of globin transition in Xenopus laevis and identification of globins by in vitro translation of hybrid-selected mRNA

FEBS letters, 1986-09, Vol.205 (2), p.219-222

1986

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Measurement and Control of Dissolved Oxygen below 100 ppb

Annals of the New York Academy of Sciences, 1986-05, Vol.469 (1), p.178-189

1986

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Developmental pattern and molecular identification of globin chains in Xenopus laevis

Roux's Archives of Developmental Biology, 1988-12, Vol.197 (7), p.406-412

1988

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Conformational changes in mitochondrial aspartate aminotransferase detected by a covalently attached fluorescent probe

Progress in clinical and biological research, 1984, Vol.144B, p.117

1984

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Reply by the authors(1)

FEBS letters, 2000-01, Vol.466 (1), p.207

2000

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Active-site ARG arrow right Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase

The Journal of biological chemistry, 1997-08, Vol.272 (35), p.21932-21937

1997

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Reply by the authors

FEBS letters, 1999-11, Vol.460 (3), p.561

1999

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Correlation of structure and catalysis by aspartate aminotransferase isoenzymes

Biochemical Society transactions, 1984-06, Vol.12 (3), p.427-430

1984

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Aspartate aminotransferase: studies on conformational adaptions and 3H-transfer during transamination

Progress in clinical and biological research, 1984, Vol.144B, p.223

1984

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Potassium Ions and the Molecular‐Chaperone Activity of DnaK

European journal of biochemistry, 1996-04, Vol.237 (1), p.318-321

1996

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Thermal stability and heat transfer in the reservoir low-temperature network

Spontaneous Deamidation and Isomerization of Asn108 in Prion Peptide 106–126 and in Full-Length Prion Protein

Neurotoxicity of prion peptide 106-126 not confirmed

The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system

Control of the DnaK Chaperone Cycle by Substoichiometric Concentrations of the Co-chaperones DnaJ and GrpE

Structural Studies of the Catalytic Reaction Pathway of a Hyperthermophilic Histidinol-phosphate Aminotransferase

Modulation of the activity of mitochondrial aspartate aminotransferase H352C by the redox state of the engineered interdomain disulfide bond

Mitochondrial aspartate aminotransferase 27/32-410. Partially active enzyme derivative produced by limited proteolytic cleavage of native enzyme

Chemical modification of a functional arginyl residue (Arg 292) of mitochondrial aspartate aminotransferase. Identification as the binding site for the distal carboxylate group of the substrate

Conformational changes in aspartate aminotransferase. Effect of active site ligands on peptide hydrogen-deuterium exchange

Reported channel formation by prion protein fragment 106–126 in planar lipid bilayers cannot be reproduced

Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes : regio-specific α, β and γ families

Multiple evolutionary origin of pyridoxal‐5′‐phosphate‐dependent amino acid decarboxylases

Active-site Arg → Lys Substitutions Alter Reaction and Substrate Specificity of Aspartate Aminotransferase

Rates of Evolution of Pyridoxal-5′- Phosphate-Dependent Enzymes

Analysis of globin transition in Xenopus laevis and identification of globins by in vitro translation of hybrid-selected mRNA

Measurement and Control of Dissolved Oxygen below 100 ppb

Developmental pattern and molecular identification of globin chains in Xenopus laevis

Conformational changes in mitochondrial aspartate aminotransferase detected by a covalently attached fluorescent probe

Reply by the authors(1)

Active-site ARG arrow right Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase

Reply by the authors

Correlation of structure and catalysis by aspartate aminotransferase isoenzymes

Aspartate aminotransferase: studies on conformational adaptions and 3H-transfer during transamination

Potassium Ions and the Molecular‐Chaperone Activity of DnaK

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