asparagine and imipenem, anhydrous

asparagine has been researched along with imipenem, anhydrous 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
Nakae, T; Ono, T; Yoneyama, H; Yoshihara, E	1
Beadle, BM; Shoichet, BK; Trehan, I	1

Other Studies

2 other study(ies) available for asparagine and imipenem, anhydrous

Article	Year
Identification of the catalytic triad of the protein D2 protease in Pseudomonas aeruginosa. Biochemical and biophysical research communications, 1998, Jun-09, Volume: 247, Issue:1 Topics: Alanine; Amino Acid Substitution; Asparagine; Aspartic Acid; Carbapenems; Catalysis; Endopeptidases; Glutamine; Histidine; Imipenem; Ion Channels; Microbial Sensitivity Tests; Mutagenesis, Site-Directed; Porins; Pseudomonas aeruginosa; Serine	1998
Inhibition of AmpC beta-lactamase through a destabilizing interaction in the active site. Biochemistry, 2001, Jul-10, Volume: 40, Issue:27 Topics: Alanine; Amino Acid Substitution; Asparagine; Bacterial Proteins; beta-Lactamase Inhibitors; beta-Lactamases; Binding Sites; Crystallization; Crystallography, X-Ray; Enzyme Stability; Escherichia coli; Imipenem; Kinetics; Moxalactam; Mutagenesis, Site-Directed; Protein Denaturation; Thermodynamics	2001

Article

Year

Identification of the catalytic triad of the protein D2 protease in Pseudomonas aeruginosa.

Biochemical and biophysical research communications, 1998, Jun-09, Volume: 247, Issue:1

Topics: Alanine; Amino Acid Substitution; Asparagine; Aspartic Acid; Carbapenems; Catalysis; Endopeptidases; Glutamine; Histidine; Imipenem; Ion Channels; Microbial Sensitivity Tests; Mutagenesis, Site-Directed; Porins; Pseudomonas aeruginosa; Serine

1998

Inhibition of AmpC beta-lactamase through a destabilizing interaction in the active site.

Biochemistry, 2001, Jul-10, Volume: 40, Issue:27

Topics: Alanine; Amino Acid Substitution; Asparagine; Bacterial Proteins; beta-Lactamase Inhibitors; beta-Lactamases; Binding Sites; Crystallization; Crystallography, X-Ray; Enzyme Stability; Escherichia coli; Imipenem; Kinetics; Moxalactam; Mutagenesis, Site-Directed; Protein Denaturation; Thermodynamics

2001