phosphoglycolohydroxamate has been researched along with dihydroxyacetone phosphate in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (25.00) | 18.2507 |
| 2000's | 3 (37.50) | 29.6817 |
| 2010's | 3 (37.50) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Fonvielle, M; Hemery, M; Therisod, H; Therisod, M | 1 |
| Knowles, JR; Sampson, NS | 1 |
| Berry, A; Hall, DR; Hunter, WN; Leonard, GA; Reed, CD; Watt, CI | 1 |
| Bates, MA; Berry, A; Plater, AR; Thomson, GJ; Zgiby, S | 1 |
| Doruker, P; Jernigan, RL; Kurkcuoglu, O | 1 |
| Alahuhta, M; Wierenga, RK | 1 |
| Baker, EA; Capodagli, GC; Franzblau, SG; Krasnykh, O; Mesecar, AD; Pegan, SD; Rukseree, K | 1 |
| Gunasekaran, K; Jeyakanthan, J; Karthik, L; Nachiappan, M; Velmurugan, D | 1 |
8 other study(ies) available for phosphoglycolohydroxamate and dihydroxyacetone phosphate
| Article | Year |
|---|---|
New competitive inhibitors of cytosolic (NADH-dependent) rabbit muscle glycerophosphate dehydrogenase.
Topics: Animals; Cytosol; Enzyme Inhibitors; Glycerolphosphate Dehydrogenase; Humans; Hydrogen Bonding; Hydroxamic Acids; Kinetics; Magnetic Resonance Spectroscopy; Molecular Conformation; Muscle, Skeletal; NAD; Rabbits; Spectrometry, Mass, Electrospray Ionization | 2007 |
Segmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase.
Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Catalysis; Dihydroxyacetone Phosphate; Escherichia coli; Hydrogen Bonding; Hydroxamic Acids; Kinetics; Ligands; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Conformation; Saccharomyces cerevisiae; Structure-Activity Relationship; Triose-Phosphate Isomerase | 1992 |
The crystal structure of Escherichia coli class II fructose-1, 6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity.
Topics: Binding Sites; Catalysis; Dihydroxyacetone Phosphate; Dimerization; Enzyme Inhibitors; Escherichia coli; Fructose-Bisphosphate Aldolase; Hydrogen Bonding; Hydroxamic Acids; Models, Molecular; X-Ray Diffraction; Zinc | 1999 |
A functional role for a flexible loop containing Glu182 in the class II fructose-1,6-bisphosphate aldolase from Escherichia coli.
Topics: Amino Acid Substitution; Binding Sites; Catalysis; Circular Dichroism; Deuterium; Dihydroxyacetone Phosphate; Escherichia coli; Fructose-Bisphosphate Aldolase; Glutamic Acid; Hydroxamic Acids; Kinetics; Models, Molecular; Oxidation-Reduction; Pliability; Protein Conformation; Protons; Structure-Activity Relationship; Zinc | 2002 |
Loop motions of triosephosphate isomerase observed with elastic networks.
Topics: Anisotropy; Binding Sites; Computer Simulation; Crystallography; Databases, Protein; Dihydroxyacetone Phosphate; Hydroxamic Acids; Ligands; Models, Theoretical; Motion; Protein Conformation; Structure-Activity Relationship; Triose-Phosphate Isomerase | 2006 |
Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: new insight in the proton transfer reaction mechanism.
Topics: Anisotropy; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Dihydroxyacetone Phosphate; Hydroxamic Acids; Leishmania mexicana; Protons; Static Electricity; Substrate Specificity; Triose-Phosphate Isomerase | 2010 |
Active site loop dynamics of a class IIa fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis.
Topics: Amino Acid Sequence; Catalytic Domain; Dihydroxyacetone Phosphate; Fructose-Bisphosphate Aldolase; Hydroxamic Acids; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mycobacterium tuberculosis; Protein Binding; Sequence Alignment; Substrate Specificity | 2013 |
Crystal structure analysis of L-fuculose-1-phosphate aldolase from Thermus thermophilus HB8 and its catalytic action: as explained through in silico.
Topics: Aldehyde-Lyases; Amino Acid Sequence; Bacterial Proteins; Catalysis; Catalytic Domain; Computer Simulation; Crystallography, X-Ray; Dihydroxyacetone Phosphate; Escherichia coli; Hydroxamic Acids; Models, Molecular; Molecular Sequence Data; Protein Conformation; Thermus thermophilus | 2013 |