phenylalanine and 2-(n-morpholino)ethanesulfonic acid

phenylalanine has been researched along with 2-(n-morpholino)ethanesulfonic acid in 2 studies

Research

Studies (2)

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

Authors

Authors	Studies
Almo, SC; Fedorov, AA; Guo, XL; Lawrence, DS; Lee, SY; Shen, K; Sun, JP; Zhang, ZY	1
Anant, A; Biswal, BK; Nasir, N; Vyas, R	1

Other Studies

2 other study(ies) available for phenylalanine and 2-(n-morpholino)ethanesulfonic acid

Article	Year
Crystal structure of PTP1B complexed with a potent and selective bidentate inhibitor. The Journal of biological chemistry, 2003, Apr-04, Volume: 278, Issue:14 Topics: Alkanesulfonic Acids; Binding Sites; Crystallography; Humans; Kinetics; Morpholines; Mutagenesis, Site-Directed; Phenylalanine; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Tyrosine Phosphatase, Non-Receptor Type 1; Protein Tyrosine Phosphatases; Vanadates	2003
Crystal structures of Mycobacterium tuberculosis HspAT and ArAT reveal structural basis of their distinct substrate specificities. Scientific reports, 2016, Jan-07, Volume: 6 Topics: Alkanesulfonic Acids; Amino Acid Sequence; Bacterial Proteins; Catalytic Domain; Crystallography, X-Ray; Enzyme Inhibitors; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Kinetics; Models, Molecular; Morpholines; Mycobacterium tuberculosis; Phenylalanine; Protein Binding; Protein Conformation, alpha-Helical; Structural Homology, Protein; Substrate Specificity; Succinic Acid; Transaminases	2016

Article

Year

Crystal structure of PTP1B complexed with a potent and selective bidentate inhibitor.

The Journal of biological chemistry, 2003, Apr-04, Volume: 278, Issue:14

Topics: Alkanesulfonic Acids; Binding Sites; Crystallography; Humans; Kinetics; Morpholines; Mutagenesis, Site-Directed; Phenylalanine; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Tyrosine Phosphatase, Non-Receptor Type 1; Protein Tyrosine Phosphatases; Vanadates

2003

Crystal structures of Mycobacterium tuberculosis HspAT and ArAT reveal structural basis of their distinct substrate specificities.

Scientific reports, 2016, Jan-07, Volume: 6

Topics: Alkanesulfonic Acids; Amino Acid Sequence; Bacterial Proteins; Catalytic Domain; Crystallography, X-Ray; Enzyme Inhibitors; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Kinetics; Models, Molecular; Morpholines; Mycobacterium tuberculosis; Phenylalanine; Protein Binding; Protein Conformation, alpha-Helical; Structural Homology, Protein; Substrate Specificity; Succinic Acid; Transaminases

2016