Page last updated: 2024-08-25

n-acetylhistamine and 1-benzylimidazole

n-acetylhistamine has been researched along with 1-benzylimidazole 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
Cheng, WJ; Huang, KF; Ko, TP; Liu, YL; Wang, AH	1
Chen, YL; Chia, CY; Huang, KF; Huang, WL; Liaw, SS; Lo, YC; Wang, AH	1

Other Studies

2 other study(ies) available for n-acetylhistamine and 1-benzylimidazole

Article	Year
Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation. Proceedings of the National Academy of Sciences of the United States of America, 2005, Sep-13, Volume: 102, Issue:37 Topics: Aminoacyltransferases; Binding Sites; Catalysis; Crystallography, X-Ray; Enzyme Inhibitors; Humans; Imidazoles; Kinetics; Molecular Structure; Mutation; Protein Binding; Protein Structure, Secondary; Water; Zinc	2005
Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding. The Journal of biological chemistry, 2011, Apr-08, Volume: 286, Issue:14 Topics: Amino Acid Sequence; Aminoacyltransferases; Crystallography, X-Ray; Enzyme Inhibitors; Golgi Apparatus; Humans; Molecular Sequence Data; Protein Binding; Protein Structure, Secondary; Sequence Homology, Amino Acid	2011

Article

Year

Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation.

Proceedings of the National Academy of Sciences of the United States of America, 2005, Sep-13, Volume: 102, Issue:37

Topics: Aminoacyltransferases; Binding Sites; Catalysis; Crystallography, X-Ray; Enzyme Inhibitors; Humans; Imidazoles; Kinetics; Molecular Structure; Mutation; Protein Binding; Protein Structure, Secondary; Water; Zinc

2005

Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding.

The Journal of biological chemistry, 2011, Apr-08, Volume: 286, Issue:14

Topics: Amino Acid Sequence; Aminoacyltransferases; Crystallography, X-Ray; Enzyme Inhibitors; Golgi Apparatus; Humans; Molecular Sequence Data; Protein Binding; Protein Structure, Secondary; Sequence Homology, Amino Acid

2011