alanine and methylthio-adp

alanine has been researched along with methylthio-adp 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
Bandivadekar, KR; Ding, Z; Jin, J; Kunapuli, SP; Tuluc, F; Zhang, L	1
Almo, SC; Burgos, ES; Cameron, SA; Gulab, SA; Schramm, VL; Thomas, K	1

Other Studies

2 other study(ies) available for alanine and methylthio-adp

Article	Year
Arg333 and Arg334 in the COOH terminus of the human P2Y1 receptor are crucial for Gq coupling. American journal of physiology. Cell physiology, 2005, Volume: 288, Issue:3 Topics: Adenosine Diphosphate; Alanine; Amino Acid Sequence; Animals; Arginine; CHO Cells; Cricetinae; GTP-Binding Protein alpha Subunits, Gq-G11; Humans; Molecular Sequence Data; Protein Structure, Tertiary; Receptors, Purinergic P2; Receptors, Purinergic P2Y1; Recombinant Fusion Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Thionucleotides	2005
Active site and remote contributions to catalysis in methylthioadenosine nucleosidases. Biochemistry, 2015, Apr-21, Volume: 54, Issue:15 Topics: Adenosine Diphosphate; Alanine; Amino Acid Substitution; Catalysis; Catalytic Domain; Crystallography, X-Ray; Escherichia coli; Escherichia coli Proteins; Mutation, Missense; N-Glycosyl Hydrolases; Thionucleotides; Valine; Vibrio cholerae	2015

Article

Year

Arg333 and Arg334 in the COOH terminus of the human P2Y1 receptor are crucial for Gq coupling.

American journal of physiology. Cell physiology, 2005, Volume: 288, Issue:3

Topics: Adenosine Diphosphate; Alanine; Amino Acid Sequence; Animals; Arginine; CHO Cells; Cricetinae; GTP-Binding Protein alpha Subunits, Gq-G11; Humans; Molecular Sequence Data; Protein Structure, Tertiary; Receptors, Purinergic P2; Receptors, Purinergic P2Y1; Recombinant Fusion Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Thionucleotides

2005

Active site and remote contributions to catalysis in methylthioadenosine nucleosidases.

Biochemistry, 2015, Apr-21, Volume: 54, Issue:15

Topics: Adenosine Diphosphate; Alanine; Amino Acid Substitution; Catalysis; Catalytic Domain; Crystallography, X-Ray; Escherichia coli; Escherichia coli Proteins; Mutation, Missense; N-Glycosyl Hydrolases; Thionucleotides; Valine; Vibrio cholerae

2015