The Ligand Specificity of the (Adenosine 3',5'-Monophosphate)-Binding Site of Yeast Glyceraldehyde-3-Phosphate Dehydrogenase. Interaction with Adenosine Derivatives and Pharmacologically-Active Compounds
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1980.tb04766.x/fullpdf
Reference44 articles.
1. Purification and Characterization of Two High-Affinity (Adenosine 3',5'-Monophosphate)-Binding Proteins from Yeast. Identification as Multiple Forms of Glyceraldehyde-3-Phosphate Dehydrogenase
2. An adenosine 3':5'-monophosphate-adenosine binding protein from mouse liver.
3. An adenosine 3′:5′-monophosphate adenosine-binding protein from mouse liver
4. DIRECT PHOTO-AFFINITY LABELING OF CYCLIC NUCLEOTIDE BINDING PROTEINS WITH GUANOSINE-3‘,5’-MONOPHOSPHATE
5. The binding of adenosine-3′,5′-monophosphate by messenger ribonucleoprotein-like particles
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