thiamine pyrophosphate and acrolein

thiamine pyrophosphate has been researched along with acrolein in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Baburina, I; Dikdan, G; Guo, F; Jordan, F; Root, B; Tous, GI	1
Chakraborty, S; Jordan, F; Kenyon, GL; McLeish, MJ; Nemeria, N; Yep, A	1

Other Studies

2 other study(ies) available for thiamine pyrophosphate and acrolein

Article	Year
Reactivity at the substrate activation site of yeast pyruvate decarboxylase: inhibition by distortion of domain interactions. Biochemistry, 1998, Feb-03, Volume: 37, Issue:5 Topics: Acrolein; Amino Acid Sequence; Carbon Radioisotopes; Chromatography, High Pressure Liquid; Cysteine; Enzyme Activation; Fatty Acids, Monounsaturated; Glyoxylates; Kinetics; Maleates; Malonates; Molecular Sequence Data; Peptides; Protein Structure, Tertiary; Pyruvate Decarboxylase; Saccharomyces cerevisiae; Substrate Specificity; Sulfhydryl Reagents; Thiamine Pyrophosphate; Tritium	1998
Mechanism of benzaldehyde lyase studied via thiamin diphosphate-bound intermediates and kinetic isotope effects. Biochemistry, 2008, Mar-25, Volume: 47, Issue:12 Topics: Acrolein; Aldehyde-Lyases; Benzaldehydes; Benzoin; Butyrates; Circular Dichroism; Deuterium Exchange Measurement; Glyoxylates; Kinetics; Mandelic Acids; Models, Chemical; Phenylpyruvic Acids; Pseudomonas fluorescens; Pyridines; Thiamine Pyrophosphate	2008

Article

Year

Reactivity at the substrate activation site of yeast pyruvate decarboxylase: inhibition by distortion of domain interactions.

Biochemistry, 1998, Feb-03, Volume: 37, Issue:5

Topics: Acrolein; Amino Acid Sequence; Carbon Radioisotopes; Chromatography, High Pressure Liquid; Cysteine; Enzyme Activation; Fatty Acids, Monounsaturated; Glyoxylates; Kinetics; Maleates; Malonates; Molecular Sequence Data; Peptides; Protein Structure, Tertiary; Pyruvate Decarboxylase; Saccharomyces cerevisiae; Substrate Specificity; Sulfhydryl Reagents; Thiamine Pyrophosphate; Tritium

1998

Mechanism of benzaldehyde lyase studied via thiamin diphosphate-bound intermediates and kinetic isotope effects.

Biochemistry, 2008, Mar-25, Volume: 47, Issue:12

Topics: Acrolein; Aldehyde-Lyases; Benzaldehydes; Benzoin; Butyrates; Circular Dichroism; Deuterium Exchange Measurement; Glyoxylates; Kinetics; Mandelic Acids; Models, Chemical; Phenylpyruvic Acids; Pseudomonas fluorescens; Pyridines; Thiamine Pyrophosphate

2008