5'-methylthioadenosine and formycin

5'-methylthioadenosine has been researched along with formycin 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
Horvatin-Mrakovcic, C; Howell, PL; Lee, JE; Siu, KK; Smith, GD	1
Banco, MT; Evans, GB; Kovalevsky, A; Mishra, V; Ostermann, A; Ronning, DR; Schrader, TE	1

Other Studies

2 other study(ies) available for 5'-methylthioadenosine and formycin

Article	Year
Structure of Staphylococcus aureus 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase. Acta crystallographica. Section F, Structural biology and crystallization communications, 2008, May-01, Volume: 64, Issue:Pt 5 Topics: Amino Acid Sequence; Binding Sites; Catalysis; Crystallization; Deoxyadenosines; Drug Design; Enzyme Inhibitors; Escherichia coli; Formycins; Hydrogen Bonding; Kinetics; Molecular Sequence Data; N-Glycosyl Hydrolases; Protein Binding; Protein Conformation; S-Adenosylhomocysteine; Sequence Homology, Amino Acid; Staphylococcus aureus; Thionucleosides	2008
Neutron structures of the Helicobacter pylori 5'-methylthioadenosine nucleosidase highlight proton sharing and protonation states. Proceedings of the National Academy of Sciences of the United States of America, 2016, 11-29, Volume: 113, Issue:48 Topics: Adenine; Catalytic Domain; Crystallography, X-Ray; Deoxyadenosines; Formycins; Helicobacter pylori; Hydrogen Bonding; Models, Molecular; Neutrons; Protein Binding; Protons; Purine-Nucleoside Phosphorylase; Pyrrolidines; S-Adenosylhomocysteine; Substrate Specificity; Thionucleosides	2016

Article

Year

Structure of Staphylococcus aureus 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase.

Acta crystallographica. Section F, Structural biology and crystallization communications, 2008, May-01, Volume: 64, Issue:Pt 5

Topics: Amino Acid Sequence; Binding Sites; Catalysis; Crystallization; Deoxyadenosines; Drug Design; Enzyme Inhibitors; Escherichia coli; Formycins; Hydrogen Bonding; Kinetics; Molecular Sequence Data; N-Glycosyl Hydrolases; Protein Binding; Protein Conformation; S-Adenosylhomocysteine; Sequence Homology, Amino Acid; Staphylococcus aureus; Thionucleosides

2008

Neutron structures of the Helicobacter pylori 5'-methylthioadenosine nucleosidase highlight proton sharing and protonation states.

Proceedings of the National Academy of Sciences of the United States of America, 2016, 11-29, Volume: 113, Issue:48

Topics: Adenine; Catalytic Domain; Crystallography, X-Ray; Deoxyadenosines; Formycins; Helicobacter pylori; Hydrogen Bonding; Models, Molecular; Neutrons; Protein Binding; Protons; Purine-Nucleoside Phosphorylase; Pyrrolidines; S-Adenosylhomocysteine; Substrate Specificity; Thionucleosides

2016