Published in Acta Crystallogr D Biol Crystallogr on July 01, 1994
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Serine-53 at the tip of the glycine-rich loop of cAMP-dependent protein kinase: role in catalysis, P-site specificity, and interaction with inhibitors. Biochemistry (2000) 1.23
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Identification of aspartate-184 as an essential residue in the catalytic subunit of cAMP-dependent protein kinase. Biochemistry (1988) 1.19
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A point mutation abolishes binding of cAMP to site A in the regulatory subunit of cAMP-dependent protein kinase. J Biol Chem (1988) 1.18
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Conserved water molecules contribute to the extensive network of interactions at the active site of protein kinase A. Proc Natl Acad Sci U S A (1998) 1.18
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DNA complexed structure of the key transcription factor initiating development in sporulating bacteria. Structure (2002) 1.16
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DdPK3, which plays essential roles during Dictyostelium development, encodes the catalytic subunit of cAMP-dependent protein kinase. Proc Natl Acad Sci U S A (1992) 1.13