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phosphoglycolohydroxamate and glutamic acid

phosphoglycolohydroxamate has been researched along with glutamic acid 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
Eritja, R; Schliebs, W; Thanki, N; Wierenga, R	1
Bates, MA; Berry, A; Plater, AR; Thomson, GJ; Zgiby, S	1

Other Studies

2 other study(ies) available for phosphoglycolohydroxamate and glutamic acid

Article	Year
Active site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies. Protein science : a publication of the Protein Society, 1996, Volume: 5, Issue:2 Topics: Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Catalysis; Chickens; Circular Dichroism; Enzyme Inhibitors; Fungal Proteins; Glutamic Acid; Glycolates; Histidine; Hydroxamic Acids; Kinetics; Lysine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Conformation; Protozoan Proteins; Saccharomyces cerevisiae; Species Specificity; Structure-Activity Relationship; Substrate Specificity; Triose-Phosphate Isomerase; Trypanosoma	1996
A functional role for a flexible loop containing Glu182 in the class II fructose-1,6-bisphosphate aldolase from Escherichia coli. Journal of molecular biology, 2002, Jan-11, Volume: 315, Issue:2 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

Article

Year

Active site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies.

Protein science : a publication of the Protein Society, 1996, Volume: 5, Issue:2

Topics: Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Catalysis; Chickens; Circular Dichroism; Enzyme Inhibitors; Fungal Proteins; Glutamic Acid; Glycolates; Histidine; Hydroxamic Acids; Kinetics; Lysine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Conformation; Protozoan Proteins; Saccharomyces cerevisiae; Species Specificity; Structure-Activity Relationship; Substrate Specificity; Triose-Phosphate Isomerase; Trypanosoma

1996

A functional role for a flexible loop containing Glu182 in the class II fructose-1,6-bisphosphate aldolase from Escherichia coli.

Journal of molecular biology, 2002, Jan-11, Volume: 315, Issue:2

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